KR102637287B1 - 유비퀴틴 및 유비퀴틴-유사 효소 활성의 확인 방법 - Google Patents
유비퀴틴 및 유비퀴틴-유사 효소 활성의 확인 방법 Download PDFInfo
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Abstract
본 발명은 생물학적 샘플의 세포에서 SUMO/유비퀴틴/Nedd8 단백질의 컨쥬게이션에 관여된 단백질/효소의 활성을 정량화하는 방법에 관한 것으로서, 이 방법은 하기를 포함한다:
a) 적어도 3개의 단백질의 하위그룹의 각 단백질과 세포의 세포 추출물을 접촉시키는 단계로서, 상기 적어도 3개의 단백질은 서열 SEQ ID NO: 1 내지 3으로 본질적으로 이루어지거나 이루어진 단백질에 상응하는, 단계,
b) 유비퀴틴, SUMO 및 Nedd8에 대한 제1의 값을 수득하기 위해 상기 적어도 3개의 단백질 각각의 유비퀴틴화(ubiquitination), SUMO화(SUMOylation) 및 NEDD화(NEDDylation) 수준을 동시에 측정하는 단계.
a) 적어도 3개의 단백질의 하위그룹의 각 단백질과 세포의 세포 추출물을 접촉시키는 단계로서, 상기 적어도 3개의 단백질은 서열 SEQ ID NO: 1 내지 3으로 본질적으로 이루어지거나 이루어진 단백질에 상응하는, 단계,
b) 유비퀴틴, SUMO 및 Nedd8에 대한 제1의 값을 수득하기 위해 상기 적어도 3개의 단백질 각각의 유비퀴틴화(ubiquitination), SUMO화(SUMOylation) 및 NEDD화(NEDDylation) 수준을 동시에 측정하는 단계.
Description
본 발명은 유비퀴틴 및 유비퀴틴-유사 효소 활성, 특히 나아가 약물 치료에 대한 효소 활성에 대한 확인 방법에 관한 것이다.
전구체 단백질은 활성이 아니며 그러므로 기능적 성숙 단백질이 되기 위한 추가 프로세싱이 필요하다. 번역후 단백질 변형(modification)은 단백질 생합성 이전 또는 이후 단백질의 화학적 변형이며, 인산화, 유비퀴틸화(ubiquitylation), 메틸화, 아세틸화 및 유비퀴틴-유사 변형자(UBL)에 의한 변형을 포함한다.
유비퀴틴이 가장 잘 이해되는 번역 후 변형자이지만, 유비퀴틴 프로테아좀 경로와 평행하지만 구별되는 경로에서 세포 표적을 변형시키는 유비퀴틴-유사 단백질(UBL)의 패밀리가 증가하고 있다. 이들 대체 변형자는 하기를 포함한다: SUMO(Sentrin, 효모에서 Smt3), NEDD8(효모에서 Rub1), ISG15(UCRP), APG8, APG12, FAT10, Ufm1, URM1 및 Hub1.
이들 관련 분자는 신규한 기능을 갖고 다양한 생물학적 과정에 영향을 미친다. 또한 일부 단백질은 하나 초과의 UBL에 의해 변형될 수 있고 때때로 동일한 리신 잔기에서도 변형될 수 있기 때문에 다양한 컨쥬게이션(conjugation) 경로들 사이에서 교차-조절이 존재한다. 예를 들어, SUMO 변형은 유비퀴틴화(ubiquitination)의 것에 대해 길항적으로 작용할 수 있고, 단백질 기질을 안정화시키는 역할을 할 수 있다. UBL에 대해 컨쥬게이션된 단백질은 전형적으로 프로테아좀에 의한 분해를 위해 표적화되지는 않지만, 오히려 다양한 조절 활성에서 기능한다. UBL의 부착은 기질 입체구조(conformation)를 변경시키고, 리간드 또는 기타 상호작용 분자에 대한 친화성에 영향을 끼치고, 기질 위치를 바꾸고 단백질 안정성에 영향을 미칠 수 있다.
UBL은 구조적으로 유비퀴틴과 유사하고, 유비퀴틴에 대한 상응하는 메카니즘과 유사한 효소적 단계에 의해 컨쥬게이트(conjugate)로부터 프로세싱, 활성화, 컨쥬게이션 및 방출된다. UBL은 또한 불변 C-말단 GG 모티프를 노출하도록 프로세싱된 C-말단 확장으로 번역된다. 이들 변형자는 UBL을 세포내 표적에 컨쥬게이션시키는 이들 고유의 특이적 E1(활성화), E2(컨쥬게이션) 및 E3(결찰) 효소를 갖는다. 이들 컨쥬게이트는 탈유비퀴틴화 효소의 것과 유사한 메카니즘을 가진 UBL-특이적 이소펩티다아제에 의해 역전될 수 있다.
따라서, UBL은 많은 세포 과정에서 중심 기능을 하며, 그리하여 이의 규제가 완화될 수 있고, 이러한 규제 완화(deregulation)는 많은 질병 및 증후군에 관여된다.
따라서, 유비퀴틴 및 UBL 변형을 제어하고 비정상적인 변이를 평가할 필요가 있다.
그러나, 현재까지, 질병 결과 또는 나아가 저해제로의 치료에 대한 유비퀴틴 및 UBL 변형에 대한 전반적인 평가를 수행하는 것은 용이하지 않다. 실제로, 기존의 기술은 개별 단백질의 변형 수준을 정량화하고 효소의 활성을 직접적으로 정량화하지 않는다.
따라서, 유비퀴틴 및 UBL 변형에 관여하는 효소 활성을 모니터링할 수 있게 하는 방법을 제공할 필요가 있다.
본 발명의 한 목적은 이러한 방법 및 이러한 방법을 수행하기 쉬운 키트를 제안하는 것이다.
본 발명은 생물학적 샘플의 세포에서 SUMO/유비퀴틴/Nedd8 단백질의 컨쥬게이션에 관여된 단백질 또는 효소의 활성을 정량화하는 방법에 관한 것으로서, 이 방법은 하기를 포함한다:
a) 적어도 세포의 세포 추출물을, 10개의 단백질의 그룹 중에서 선택된 적어도 3개의 단백질의 하위그룹의 각 단백질과 접촉시키는 단계로서, 상기 10개의 단백질의 그룹은 46개의 단백질의 세트에 속하고,
상기 적어도 3개의 단백질은 지지체 상에 고정되고,
상기 적어도 3개의 단백질은 상기 세포 추출물과 접촉되기 전 SUMO/유비퀴틴/Nedd8 단백질에 의해 실질적으로 컨쥬게이션되지 않으며,
상기 적어도 3개의 단백질은 서열 SEQ ID NO: 1 내지 3으로 본질적으로 이루어지거나 이루어진 단백질에 상응하고, 상기 10개의 단백질은 서열 SEQ ID NO: 1 내지 10으로 본질적으로 이루어지거나 이루어진 단백질에 상응하고, 상기 46개의 단백질의 그룹은 서열 SEQ ID NO: 1 내지 46으로 본질적으로 이루어지거나 이루어진 단백질에 상응하고,
SEQ ID NO: 1은 ZMYM5 단백질에 상응하고; SEQ ID NO: 2은 BEAN 단백질에 상응하고, SEQ ID NO: 3은 OTUD6B에 상응하는, 단계; 및
b) 유비퀴틴, SUMO 및 Nedd8에 대한 제1의 값을 수득하기 위해 상기 적어도 3개의 단백질 각각의 유비퀴틴화, SUMO화(SUMOylation) 및 NEDD화(NEDDylation) 수준을 동시에 측정하는 단계.
본 발명은 46개의 단백질의 그룹에 속하는 적어도 3개의 특정 단백질의 유비퀴틴, SUMO 및 NEDD8에 의한 변형의 평가가 상기 경로의 활성을 측정하고 이들 경로를 표적으로 하는 약물의 효과를 모니터링하는데 매우 중요하다는 본 발명자들의 예상하지 못한 관찰을 기초로 한다.
실제로, 본 발명자들은 상기 3개의 단백질 상 유비퀴틴 및/또는 SUMO 및/또는 NEDD8의 첨가에 의해 유도된 변형을 평가하는 것이 이들의 컨쥬게이션에 관여된 특정 효소의 활성 및 Ubl 경로를 변형하는 화합물의 능력에 대한 양호한 정보를 제공한다고 논평했다.
유비퀴틴이나 SUMO 또는 NEDD8에 의해 변형되지 않은 정제된 결정된 단백질(상기 적어도 3개의 단백질)을 이용함으로써, 본 발명자들은 SUMO/유비퀴틴/Nedd8 경로의 활성을 용이하게 정량화할 수 있다.
더욱이, SUMO/유비퀴틴/Nedd8 단백질의 컨쥬게이션에 관여된 단백질/효소의 활성을 결정하는데 사용된 세포 추출물이 이러한 활성을 변형하기 쉬운 결정된 상태에 있는 경우(예를 들어, 특정 환경에 놓인, 결정된 온도 및/또는 압력에 놓인, 약물 또는 화합물로 처리), 이때에는 이것은 이 결정된 상태에 있지 않은 세포, 즉 대조군 세포의 변형 수준과 변형 수준을 비교하는 것과 관련있다.
유비퀴틴(Ub)은 76개의 아미노산 잔기로 이루어진 구형의 단백질이고, UPS(유비퀴틴-프로테아좀 시스템)는 세포 내 단백질의 80% 내지 90%를 분해하는 것을 담당한다. Ub는 유비퀴틴-활성화 효소 E1, 유비퀴틴-컨쥬게이션 효소 E2 및 유비퀴틴 E3 리가아제를 포함한 일련의 효소에 의해 표적 단백질의 리신 잔기에 결합한다. 후속해서, 이들 유비퀴틴화 단백질은 일반적으로 26S 프로테아좀에 의해 인식되고 분해된다.
3가지 SUMO1, SUMO2 및 SUMO3 파라로그(paralogue) 모두의 구조는 구형의 조밀한 Ub-유사 폴드와 유사하다. SUMO1과 SUMO2의 차이는 대개 두 단백질의 두번째 β-가닥 및 α-나선에서 발견된다. 세포에서, 상이한 SUMO 파라로그는 공통의 특성을 공유하는 것처럼 보이나 일부 구별되는 기능을 가진다. 예를 들어, 전골수구성 백혈병 단백질은 세 모두의 SUMO 파라로그에 컨쥬게이션하는 반면 RanGAP1은 유사분열 동안 우선적으로 SUMO1으로 변형되고, 토포이소머라아제 II는 SUMO2/3으로 변형된다. 더욱이, SUMO1 및 SUMO2/3 양자 모두가 핵질에서 대개 발견되지만, SUMO1은 핵소체, 핵 외피 및 세포질 병소 내에서 독특하게 발견되는 반면, SUMO2/3은 핵 개질 과정에서 초기 지점에서 염색체에 축적된다. 흥미롭게도, SUMO1보다 더 큰 자유의 비-컨쥬게이션된 SUMO2/3의 풀(pool)이 존재한다.
NEDD8은 9 kDa 상대 분자 질량을 가진 81-아미노산 단백질이며, 유비퀴틴과 60% 동일하고 80% 상동성이다. NEDD8은 전용 E1-활성화 효소(AppBp1/UBA3, 또는 NAE) 및 E2-컨쥬게이션 효소(UBC12, UBE2F)를 가지며, 퀄린 스캐폴드(cullin scaffold)와의 컨쥬게이션을 통해 E3 리가아제의 CRL 패밀리의 효소적 활성에 필수적이다. Nedd화 경로의 기타 성분에는 NEDD8을 이것의 성숙한 76-아미노산 형태로 프로세싱하는 DEN1 및 퀄린 단백질로부터 NEDD8을 제거하는 담당을 하는 COP9 시그널로솜 복합체가 포함된다. CAND1(cullin-associated and neddylation-dissociated)는 NEDD8 활성화의 부재 하에서 퀄린과의 결합에 의해 CRL 복합체 어셈블리를 조절하는 추가적인 성분이다.
본 발명에서, 46개의 단백질의 세트(즉, 46개의 단백질로 이루어진 세트)는 하기의 단백질로 구성된다:
상기 언급된 방법에서, SEQ ID NO: 1 내지 3에 기재된 바와 같은 적어도 3개의 단백질은 지지체 상에 침착된 다음 비교될 세포(UBL 경로를 저해하기 쉬운 화합물로 처리되었거나 그렇지 않은 세포)의 세포 추출물과 접촉된다.
이 방법으로, 본 발명자들은 세포 추출물에 함유된 모든 단백질이 아닌 단백질 SEQ ID NO: 1 내지 3의 유비퀴틴/SUMO/NEDD8에 의한 변형을 구체적으로 평가한다.
접촉 기간 동안, 추출물에 함유된 유비퀴틴/SUMO/NEDD8의 첨가를 담당하는 효소는 단백질 SEQ ID NO: 1 내지 3을 변형할 것이다. 그러므로, 유비퀴틴화, SUMO화 및 NEDD화 양이 효소의 활성에 따라 좌우될 것이며, 분석될 조건의 효과(세포 유형, 저해제...)와 직접적으로 상관 관계가 있다.
단백질과 세포 추출물 사이의 접촉에 더하여, 유비퀴틴/SUMO/NEDD8에 의한 변형은 유비퀴틴 또는 SUMO 또는 NEDD8에 대항해 지시된 특이적 항체를 이용한 면역학적 기술에 의해 측정된다.
예를 들어, 유비퀴틴 및/또는 SUMO 및/또는 NEDD8 단백질에 의해 변형된 단백질은 그에 따라 유비퀴틴 및/또는 SUMO 및/또는 NEED8 단백질에 대항해 지시된 항체와 상호작용하여 분자 복합체를 형성할 것이다. 복합체는 유비퀴틴 및/또는 SUMO 및/또는 NEDD8 단백질에 대항해 지시된 상기 항체의 불변부 FC 사슬을 인식 (및 상호작용)하는 2차 항체에 의해 검출될 수 있다.
상기 복합체는 2차 항체가 리포터 분자, 예컨대 형광 단백질, 퍼옥시다아제, 형광 염료 등으로 표지될 때 식별될 수 있다.
당업자는 복합체 단백질/항 유비퀴틴, 항 SUMO 또는 항 NEDD8 항체를 특히 유세포분석기를 이용하여 정량화하는 방법을 알고 있다.
이어서, 유비퀴틴, SUMO 및 NEDD8 각각에 대해 각 단백질 SEQ ID NO: 1 내지 3에 대한 변형 값이 수득된다.
단백질 SEQ ID NO: 1은 SUMO1 및 SUMO2에 의해 변형될 수 있는 반면, 단백질 SEQ ID NO: 2는 바람직하게 유비퀴틴에 의해 변형되고, 단백질 SEQ ID NO: 3은 NEDD8에 의해 변형될 수 있음을 주목해야 한다.
따라서, 상기 적어도 단백질을 평가할 때 간섭 없이 UBL 경로 활성을 결정하고 세포에서 UBL 경로의 정량적 활성을 수득하는 것이 가능하다.
도 9는 이들 단백질의 특이성을 나타낸다.
유리하게도, 본 발명은 상기 기술된 방법에 관한 것으로서, 여기서 상기 방법은 46개의 단백질의 세트에 속하는 10개의 단백질의 그룹의 각 단백질과 세포 추출물을 접촉시키는 단계를 포함한다.
즉, 본 발명은 유리하게도 상기 언급된 방법에 관한 것으로서, 상기 방법은 하기를 포함한다:
a) 46개의 단백질의 세트 중에서 선택된 적어도 10개의 단백질의 하위그룹의 각 단백질과 세포의 세포 추출물을 접촉시키는 단계로서;
상기 적어도 3개의 단백질은 지지체 상에 고정되고,
상기 적어도 10개의 단백질은 상기 세포 추출물과 접촉되기 전 SUMO/유비퀴틴/Nedd8 단백질에 의해 실질적으로 컨쥬게이션되지 않으며,
상기 10개의 단백질은 서열 SEQ ID NO: 1 내지 10으로 본질적으로 이루어지거나 이루어진 단백질에 상응하고, 상기 46개의 단백질의 세트는 서열 SEQ ID NO: 1 내지 46으로 본질적으로 이루어지거나 이루어진 단백질에 상응하는, 단계,
및
b) 유비퀴틴, SUMO 및 Nedd8에 대한 제1의 값을 수득하기 위해 상기 적어도 3개의 단백질 각각의 유비퀴틴화, SUMO화 및 NEDD화 수준을 동시에 측정하는 단계.
더욱 유리하게도, 본 발명은 상기 정의된 방법에 관한 것으로서, 여기서 상기 방법은 상기 46개의 단백질의 세트의 각 단백질과 세포 추출물을 접촉시키는 단계를 포함한다.
즉, 본 발명은 유리하게도 상기 언급된 방법에 관한 것으로서, 상기 방법은 하기를 포함한다:
a) 세포의 세포 추출물을 46개의 단백질의 각 단백질과 접촉시키는 단계로서;
상기 46개의 단백질은 지지체 상 고정되고,
상기 46개의 단백질은 상기 세포 추출물과 접촉되기 전 SUMO/유비퀴틴/Nedd8 단백질에 의해 실질적으로 컨쥬게이션되지 않으며,
상기 46개의 단백질의 세트는 서열 SEQ ID NO: 1 내지 46으로 본질적으로 이루어지거나 이루어진 단백질에 상응하는, 단계,
b) 유비퀴틴, SUMO 및 Nedd8에 대한 제1의 값을 수득하기 위해 상기 46개의 단백질 각각의 유비퀴틴화, SUMO화 및 NEDD화 수준을 동시에 측정하는 단계;
더욱 유리하게도, 본 발명은 상기 정의된 방법에 관한 것으로서, 여기서 상기 적어도 3개의 단백질은 비즈에 의해 지지된다.
유리하게도, 본 발명은 상기 정의된 방법에 관한 것으로서, 여기서 상기 비즈는 형광 비즈이다.
유리하게도, 본 발명은 상기 정의된 방법에 관한 것으로서, 여기서 상기 적어도 3개의 단백질 각각은 다른 비즈의 형광 특성과 상이한 형광 특성을 가진 결정된 비즈에 의해 지지되고,
동일한 형광 특성을 가진 모든 비즈는 동일한 단백질을 지지한다.
예를 들어, 상기 방법은 Luminex에 의해 개발된 XMap 기술로 수행될 수 있다. 이것은 고유 색상의 Mag-Plex 금속-기반 미소구체(2가지의 상이한 염료의 다양한 수준을 가진 500개의 상이한 색상)에 있다. 이들은 카르보이미드 커플링 기술을 이용하여 특정 단백질로 커플링될 수 있다. 단백질-커플링된 비즈는 이후의 실시예에 기술된 바와 같이 다중화될 수 있고 세포 추출물로 사용될 수 있다. 상이한 비즈는 전용 분석기 또는 유세포 분석기를 이용하여 구별될 수 있다.
본 발명에 따른 단백질은 당업계에 익히 공지되어 있는 임의의 수단에 의해 형광 비즈 상에 공유적으로 그래프팅된다.
일 양태에서, 본 발명은 예를 들어, UBL 단백질 변형에 대한 약물의 효과를 확인하기 위해, 생물학적 샘플의 세포에서 SUMO/유비퀴틴/Nedd8 단백질의 컨쥬게이션에 의한 단백질 변형에 대한 약물의 효과를 확인하는 것과 관련된 단백질/효소의 활성을 정량화하는 방법에 관한 것으로서, 상기 방법은 하기를 포함한다:
a) (예를 들어, 상기 약물로 처리된 세포의) 시험될 세포 추출물을 10개의 단백질의 그룹 중 선택된 적어도 3개의 단백질의 하위그룹의 각 단백질과 접촉하는 단계로서, 상기 10개의 단백질의 그룹은 46개의 단백질의 세트에 속하고;
상기 적어도 3개의 단백질은 지지체 상에 고정되고,
상기 적어도 3개의 단백질은 상기 세포 추출물과 접촉되기 전 SUMO/유비퀴틴/Nedd8 단백질에 의해 실질적으로 컨쥬게이션되지 않으며,
상기 적어도 3개의 단백질은 서열 SEQ ID NO: 1 내지 3으로 본질적으로 이루어지거나 이루어진 단백질에 상응하고, 상기 10개의 단백질은 서열 SEQ ID NO: 1 내지 10으로 본질적으로 이루어지거나 이루어진 단백질에 상응하고, 상기 46개의 단백질의 그룹은 서열 SEQ ID NO: 1 내지 46으로 본질적으로 이루어지거나 이루어진 단백질에 상응하고,
SEQ ID NO: 1은 ZMYM5 단백질에 상응하고; SEQ ID NO: 2는 BEAN 단백질에 상응하고, SEQ ID NO: 3은 OTUD6B에 상응하는, 단계,
b) 유비퀴틴, SUMO 및 Nedd8에 대한 제1의 값을 수득하기 위해 상기 적어도 3개의 단백질 각각의 유비퀴틴화, SUMO화 및 NEDD화 수준을 동시에 측정하는 단계;
c) 이전 단계에서 수득된 제1의 값을, (예를 들어 상기 약물로 처리하지 않은 세포의) 상기 대조군 세포 추출물과 상기 적어도 단백질을 접촉시 수득된 상기 적어도 3개의 단백질의 유비퀴틴화, SUMO화 및 NEDD화의 제2의 값과 비교하여; 제1의 값과 제2의 값 사이의 비율을 수득하는 단계; 및
d) 하기를 결정하는 단계:
i- 상기 적어도 3개의 단백질 각각의 유비퀴틴화, SUMO화 및 NEDD화의 비율이 1과 유의미하게 상이하지 않은 경우, 이때에는 상기 시험된 약물 조건(예, 약물 처리)이 SUMO/유비퀴틴/Nedd8 단백질에 의한 단백질 변형에 영향을 미치지 않는지 여부, 및
ii- 상기 적어도 3개의 단백질의 적어도 하나의 유비퀴틴화, SUMO화 및 NEDD화의 비율이 1보다 현저히 낮거나 높은 경우, 이때에는 상기 시험된 약물 조건(예, 약물 처리)이 SUMO/유비퀴틴/Nedd8 단백질에 의한 단백질 변형에 영향을 미치는지 여부.
유리하게도, 본 발명은 유리하게도 상기 언급된 방법에 관한 것으로서, 상기 방법은 하기를 포함한다:
a) (예를 들어, 상기 약물로 처리된 세포의) 시험될 세포 추출물을, 그룹의 적어도 10개의 단백질의 하위그룹의 각 단백질과 접촉시키는 단계로서, 상기 10개의 단백질의 그룹은 46개의 단백질의 세트에 속하고;
상기 적어도 10개의 단백질은 지지체 상에 고정되고,
상기 적어도 10개의 단백질은 상기 세포 추출물과 접촉되기 전 SUMO/유비퀴틴/Nedd8 단백질에 의해 실질적으로 컨쥬게이션되지 않으며,
상기 10개의 단백질은 서열 SEQ ID NO: 1 내지 10으로 본질적으로 이루어지거나 이루어진 단백질에 상응하고, 상기 46개 단백질의 그룹은 서열 SEQ ID NO: 1 내지 46으로 본질적으로 이루어지거나 이루어진 단백질에 상응하는, 단계,
b) 유비퀴틴, SUMO 및 Nedd8에 대한 제1의 값을 수득하기 위해 상기 적어도 10개의 단백질 각각의 유비퀴틴화, SUMO화 및 NEDD화 수준을 동시에 측정하는 단계;
c) 이전 단계에서 수득된 제1의 값을, (예를 들어, 상기 약물로 처리하지 않은 세포의) 상기 대조군 세포 추출물과 상기 적어도 단백질을 접촉시 수득된 상기 적어도 10개의 단백질의 유비퀴틴화, SUMO화 및 NEDD화의 제2의 값과 비교하여; 제1의 값과 제2의 값 사이의 비율을 수득하는 단계; 및
d) 하기를 결정하는 단계:
i. 상기 적어도 10개의 단백질 각각의 유비퀴틴화, SUMO화 및 NEDD화의 비율이 1과 유의미하게 상이하지 않은 경우, 이때에는 상기 시험된 조건(예, 약물 처리) 약물이 SUMO/유비퀴틴/Nedd8 단백질에 의한 단백질 변형에 영향을 미치지 않는지 여부, 및
ii. 상기 적어도 10개의 단백질의 적어도 하나의 유비퀴틴화, SUMO화 및 NEDD화의 비율이 1보다 현저히 낮거나 높은 경우, 이때에는 상기 시험된 약물 조건(예, 약물 처리)이 SUMO/유비퀴틴/Nedd8 단백질에 의한 단백질 변형에 영향을 미치는지 여부.
더욱 유리하게도, 본 발명은 상기 언급된 방법에 관한 것으로서, 상기 방법은 하기를 포함한다:
a) (예를 들어, 상기 약물로 처리된) 시험될 세포의 세포 추출물을, 46개의 단백질의 각 단백질 세트와 접촉시키는 단계로서;
상기 46개의 단백질은 지지체 상 고정되고,
상기 46개의 단백질은 상기 세포 추출물과 접촉되기 전 SUMO/유비퀴틴/Nedd8 단백질에 의해 실질적으로 컨쥬게이션되지 않으며,
상기 46개는 서열 SEQ ID NO: 1 내지 46으로 본질적으로 이루어지거나 이루어진, 단계,
b) 유비퀴틴, SUMO 및 Nedd8에 대한 제1의 값을 수득하기 위해 상기 46개의 단백질 각각의 유비퀴틴화, SUMO화 및 NEDD화 수준을 동시에 측정하는 단계;
c) 이전 단계에서 수득된 제1의 값을, (예를 들어, 상기 약물로 처리하지 않은 세포의) 상기 대조군 세포 추출물과 상기 적어도 단백질을 접촉시 수득된 상기 46개의 단백질의 유비퀴틴화, SUMO화 및 NEDD화의 제2의 값과 비교하여; 제1의 값과 제2의 값 사이의 비율을 수득하는 단계; 및
d) 하기를 결정하는 단계:
i. 상기 46개의 단백질 각각의 유비퀴틴화, SUMO화 및 NEDD화의 비율이 1과 유의미하게 상이하지 않은 경우, 이때에는 상기 시험된 조건(예, 약물 처리)이 SUMO/유비퀴틴/Nedd8 단백질에 의한 단백질 변형에 영향을 미치지 않는지 여부, 및
ii. 상기 46개의 단백질의 적어도 하나의 유비퀴틴화, SUMO화 및 NEDD화의 비율이 1보다 현저히 낮거나 높은 경우, 이때에는 상기 시험된 조건(예, 약물 처리)이 SUMO/유비퀴틴/Nedd8 단백질에 의한 단백질 변형에 영향을 미치는지 여부.
본 발명은 생물학적 샘플의 세포에서 SUMO/유비퀴틴/Nedd8 단백질에 의한 단백질 변형에 대한 약물의 효과를 확인하는 방법에 관한 것으로서, 상기 방법은 하기를 포함한다:
a) 상기 약물로 처리된 세포의 세포 추출물을 10개의 단백질의 그룹 중 선택된 적어도 3개의 단백질의 하위그룹의 각 단백질과 접촉하는 단계로서, 상기 10개의 단백질의 그룹은 46개의 단백질의 세트에 속하고;
상기 적어도 3개의 단백질은 지지체 상에 고정되고,
상기 적어도 3개의 단백질은 상기 세포 추출물과 접촉되기 전 SUMO/유비퀴틴/Nedd8 단백질에 의해 실질적으로 컨쥬게이션되지 않으며,
상기 적어도 3개의 단백질은 서열 SEQ ID NO: 1 내지 3으로 본질적으로 이루어지거나 이루어진 단백질에 상응하고, 상기 10개의 단백질은 서열 SEQ ID NO: 1 내지 10으로 본질적으로 이루어지거나 이루어진 단백질에 상응하고, 상기 46개의 단백질의 그룹은 서열 SEQ ID NO: 1 내지 46으로 본질적으로 이루어지거나 이루어진 단백질에 상응하고,
SEQ ID NO: 1은 ZMYM5 단백질에 상응하고; SEQ ID NO: 2는 BEAN 단백질에 상응하고, SEQ ID NO: 3은 OTUD6B에 상응하는, 단계,
a) 유비퀴틴, SUMO 및 Nedd8에 대한 제1의 값을 수득하기 위해 상기 적어도 3개의 단백질 각각의 유비퀴틴화, SUMO화 및 NEDD화 수준을 동시에 측정하는 단계;
b) 이전 단계에서 수득된 제1의 값을, 상기 약물로 처리하지 않은 세포의 상기 세포 추출물과 상기 적어도 단백질을 접촉시 수득된 상기 적어도 3개의 단백질의 유비퀴틴화, SUMO화 및 NEDD화의 제2의 값과 비교하여; 제1의 값과 제2의 값 사이의 비율을 수득하는 단계; 및
c) 하기를 결정하는 단계:
i- 상기 적어도 3개의 단백질 각각의 유비퀴틴화, SUMO화 및 NEDD화의 비율이 1과 유의미하게 상이하지 않은 경우, 이때에는 상기 약물이 SUMO/유비퀴틴/Nedd8 단백질에 의한 단백질 변형에 영향을 미치지 않는지 여부, 및
ii- 상기 적어도 3개의 단백질의 적어도 하나의 유비퀴틴화, SUMO화 및 NEDD화의 비율이 1보다 현저히 낮거나 높은 경우, 이때에는 상기 약물이 SUMO/유비퀴틴/Nedd8 단백질에 의한 단백질 변형에 영향을 미치는지 여부.
상기에 기술된 단계 a) 및 b)에 대한 상기 조건은 여기서 필요한 부분만 약간만 수정하여 적용된다.
시험된 조건(예, 약물 처리)은 유비퀴틴화, SUMO화 및 NEDD화의 과정에 영향을 미치지 않을 때, 이때에는 단백질 SEQ ID NO:1 내지 3은 동일한 성질의 대조군 세포 추출물(예를 들어, 저해제로 처리되지 않은 세포)로 수득된 변형과 유사한 수준으로 변형된다.
반대로, 시험된 조건(예, 약물 처리)이 UBL 경로에 영향을 미친다면, 단백질 SEQ ID NO:1 내지 3의 유비퀴틴/SUMO/NEDD8에 의한 변형의 양은 대조군 조건(예, 비처리된 세포)에서 관찰된 변형의 양에 비해 증가 또는 감소될 것이다.
단백질과 세포 추출물 사이의 접촉에 더하여, 유비퀴틴/SUMO/NEDD8에 의한 변형은 유비퀴틴 또는 SUMO 또는 NEDD8에 대항해 지시된 특이적 항체를 이용한 면역학적 기술에 의해 측정된다.
예를 들어, 유비퀴틴 및/또는 SUMO 및/또는 NEDD8 단백질에 의해 변형된 단백질은 그에 따라 유비퀴틴 및/또는 SUMO 및/또는 NEED8 단백질에 대항해 지시된 항체와 상호작용하여 분자 복합체를 형성할 것이다. 복합체는 유비퀴틴 및/또는 SUMO 및/또는 NEDD8 단백질에 대항해 지시된 상기 항체의 불변부 FC 사슬을 인식 (및 상호작용)하는 2차 항체에 의해 검출될 수 있다.
상기 복합체는 2차 항체가 리포터 분자, 예컨대 형광 단백질, 퍼옥시다아제, 형광 염료 등으로 표지될 때 식별될 수 있다.
당업자는 복합체 단백질/항 유비퀴틴, 항 SUMO 또는 항 NEDD8 항체를 특히 유세포분석기를 이용하여 정량화하는 방법을 알고 있다.
이어서, 유비퀴틴, SUMO 및 NEDD8 각각에 대해 각 단백질 SEQ ID NO: 1 내지 3에 대한 변형 값이 수득된다.
이어서, 이 값은 대조군 세포 추출물(예, 저해제로 처리된 것과 동일한 성질을 가지나 상기 저해제로 처리되지 않은 세포)로 접촉된 동일한 단백질에 대해 수득된 참조 값과 비교된다.
제1의 값, 즉 시험될 세포 추출물(예, 저해제로 처리됨)로 수득된 값과 제2의 값, 즉 대조군 세포 추출물(예, 저해제로 처리되지 않음)로 수득된 값 사이의 비율이 확립된다.
이어서, 하나의 단백질에 대해, 세 가지의 상이한 비율이 수득된다: 유비퀴틴에 대한 것, SUMO에 대한 것, 및 NEDD8에 대한 것:
R유비퀴틴 (i) = 시험될 세포(예, 저해제로 처리됨)의 세포 추출물로 단백질 SEQ ID NO: i의 유비퀴틴에 대한 값/ 대조군 세포(예, 저해제로 처리되지 않음)의 세포 추출물로 단백질 SEQ ID NO: i의 유비퀴틴에 대한 값;
RSUMO (i) = 시험될 세포(예, 저해제로 처리됨)의 세포 추출물로 단백질 SEQ ID NO: i의 SUMO에 대한 값/ 대조군 세포(예, 저해제로 처리되지 않음)의 세포 추출물로 단백질 SEQ ID NO: i의 SUMO에 대한 값;
RNEDD8 (i) = 시험될 세포(예, 저해제로 처리됨)의 세포 추출물로 단백질 SEQ ID NO: i의 NEDD8에 대한 값/ 대조군 세포(예, 저해제로 처리되지 않음)의 세포 추출물로 단백질 SEQ ID NO: i의 NEDD8에 대한 값.
상기 실시예에서, i는 1, 2 또는 3이다.
비율이 확립되면, 시험된 조건(예, 약물 처리)이 각 유비퀴틴, SUMO 및 NEDD8에 대한 각 단백질에 대해 계산된 모든 비율이 약 1과 같을 때 UBL 경로에 영향을 미치지 않는다는 결론이 내려진다. 이는 단백질 SEQ ID NO:1 내지 3에서 발생된 변형이 시험될 세포 추출물(예, 상기 약물로의 처리)과 대조군(예, 비처리) 간에 유사하다는 점을 의미한다.
반대로, 상기에서 언급된 비율 중 적어도 하나가 1과 상이한 경우, 이때에는 시험된 조건(예, 약물 처리)이 UBL 경로에 영향을 미친다는 결론을 내릴 수 있다.
단백질 SEQ ID NO: 1은 SUMO1 및 SUMO2에 의해 변형될 수 있는 반면, 단백질 SEQ ID NO: 2는 바람직하게 유비퀴틴에 의해 변형되고, 단백질 SEQ ID NO: 3은 NEDD8에 의해 변형될 수 있음을 주목해야 한다.
따라서, 적어도 상기 단백질을 평가할 때 시험된 조건(예, 저해제 처리)에 의해 어떤 UBL 경로가 영향을 받는지를 확인하는 것이 가능하다.
도 9는 이들 단백질의 특이성을 나타낸다.
유리하게도, 본 발명은 상기 기술된 방법에 대한 것으로, 여기서 상기 방법은 (예, 상기 약물로 처리된 세포의) 시험될 세포 추출물을 10개의 단백질의 그룹의 각 단백질과 접촉하는 단계로서, 상기 10개의 단백질의 그룹은 46개의 단백질의 세트에 속하는 단계를 포함한다.
즉, 본 발명은 유리하게도 상기 언급된 방법에 관한 것으로서, 상기 방법은 하기를 포함한다:
a) (예를 들어, 상기 약물로 처리된 세포의) 시험될 세포 추출물을, 그룹의 적어도 10개의 단백질의 하위그룹의 각 단백질과 접촉시키는 단계로서, 상기 10개의 단백질의 그룹은 46개의 단백질의 세트에 속하고;
상기 적어도 10개의 단백질은 지지체 상에 고정되고,
상기 적어도 10개의 단백질은 상기 세포 추출물과 접촉되기 전 SUMO/유비퀴틴/Nedd8 단백질에 의해 실질적으로 컨쥬게이션되지 않으며,
상기 10개의 단백질은 서열 SEQ ID NO: 1 내지 10으로 본질적으로 이루어지거나 이루어진 단백질에 상응하고, 상기 46개 단백질의 그룹은 서열 SEQ ID NO: 1 내지 46으로 본질적으로 이루어지거나 이루어진 단백질에 상응하는, 단계,
b) 유비퀴틴, SUMO 및 Nedd8에 대한 제1의 값을 수득하기 위해 상기 적어도 10개의 단백질 각각의 유비퀴틴화, SUMO화 및 NEDD화 수준을 동시에 측정하는 단계;
c) 이전 단계에서 수득된 제1의 값을, 상기 대조군 세포 추출물(예를 들어, 상기 약물로 처리하지 않은 세포)과 상기 적어도 단백질을 접촉시 수득된 상기 적어도 10개의 단백질의 유비퀴틴화, SUMO화 및 NEDD화의 제2의 값과 비교하여; 제1의 값과 제2의 값 사이의 비율을 수득하는 단계; 및
d) 하기를 결정하는 단계:
a. 상기 적어도 10개의 단백질 각각의 유비퀴틴화, SUMO화 및 NEDD화의 비율이 1과 유의미하게 상이하지 않은 경우, 이때에는 상기 시험된 조건(예, 약물 처리)이 SUMO/유비퀴틴/Nedd8 단백질에 의한 단백질 변형에 영향을 미치지 않는지 여부, 및
b. 상기 적어도 10개의 단백질의 적어도 하나의 유비퀴틴화, SUMO화 및 NEDD화의 비율이 1보다 현저히 낮거나 높은 경우, 이때에는 상기 시험된 조건(예, 약물 처리)이 SUMO/유비퀴틴/Nedd8 단백질에 의한 단백질 변형에 영향을 미치는지 여부.
더욱 유리하게도, 본 발명은 상기 정의된 방법에 관한 것으로서, 여기서 상기 방법은 46개의 단백질의 세트의 각 단백질과 (예, 상기 약물로 처리된 세포의) 시험될 세포 추출물을 접촉시키는 단계를 포함한다.
즉, 본 발명은 유리하게도 상기 언급된 방법에 관한 것으로서, 상기 방법은 하기를 포함한다:
a) (예를 들어, 상기 약물로 처리된) 시험될 세포의 세포 추출물을, 46개의 단백질의 각 단백질 세트와 접촉시키는 단계로서;
상기 46개의 단백질은 지지체 상 고정되고,
상기 46개의 단백질은 상기 세포 추출물과 접촉되기 전 SUMO/유비퀴틴/Nedd8 단백질에 의해 실질적으로 컨쥬게이션되지 않으며,
상기 46개는 서열 SEQ ID NO: 1 내지 46으로 본질적으로 이루어지거나 이루어진, 단계,
b) 유비퀴틴, SUMO 및 Nedd8에 대한 제1의 값을 수득하기 위해 상기 46개의 단백질 각각의 유비퀴틴화, SUMO화 및 NEDD화 수준을 동시에 측정하는 단계;
c) 이전 단계에서 수득된 제1의 값을, (예를 들어, 상기 약물로 처리하지 않은 세포의) 상기 대조군 세포 추출물과 상기 적어도 단백질을 접촉시 수득된 상기 46개의 단백질의 유비퀴틴화, SUMO화 및 NEDD화의 제2의 값과 비교하여; 제1의 값과 제2의 값 사이의 비율을 수득하는 단계; 및
d) 하기를 결정하는 단계:
a. 상기 46개의 단백질 각각의 유비퀴틴화, SUMO화 및 NEDD화의 비율이 1과 유의미하게 상이하지 않은 경우, 이때에는 상기 시험된 조건(예, 약물 처리)이 SUMO/유비퀴틴/Nedd8 단백질에 의한 단백질 변형에 영향을 미치지 않는지 여부, 및
b. 상기 46개의 단백질의 적어도 하나의 유비퀴틴화, SUMO화 및 NEDD화의 비율이 1보다 현저히 낮거나 높은 경우, 이때에는 상기 시험된 조건(예, 약물 처리)이 SUMO/유비퀴틴/Nedd8 단백질에 의한 단백질 변형에 영향을 미치는지 여부.
더욱 유리하게도, 본 발명은 상기 정의된 방법에 관한 것으로서, 여기서 상기 적어도 3개의 단백질은 비즈에 의해 지지되고, 상기 비즈는 유리하게도 형광 비즈이다.
유리하게도, 본 발명은 상기 정의된 방법에 관한 것으로서, 여기서 상기 적어도 3개의 단백질 각각은 다른 비즈의 형광 특성과 상이한 형광 특성을 가진 결정된 비즈에 의해 지지되고,
동일한 형광 특성을 가진 모든 비즈는 동일한 단백질을 지지한다.
본 발명은 또한 10개의 단백질의 그룹 중에서 선택된 적어도 3개의 단백질을 포함하는 조성물에 관한 것으로서, 상기 10개의 단백질의 그룹은 46개의 단백질의 세트에 속하고;
상기 적어도 3개의 단백질은 서열 SEQ ID NO: 1 내지 3으로 본질적으로 이루어지거나 이루어진 단백질에 상응하고, 상기 10개의 단백질은 서열 SEQ ID NO: 1 내지 10으로 본질적으로 이루어지거나 이루어진 단백질에 상응하고, 상기 46개의 단백질의 그룹은 서열 SEQ ID NO: 1 내지 46으로 본질적으로 이루어지거나 이루어진 단백질에 상응하고,
상기 적어도 3개의 단백질은 형광 비즈 상 지지되고,
상기 적어도 3개의 단백질 각각은 결정된 형광 특성을 가진 비즈에 의해 지지되어 적어도 3개의 구별된 단백질-지지 비즈가 수득되고,
상기 적어도 3개의 단백질 중 하나를 지지하는 비즈는 적어도 2개의 다른 단백질-지지 비즈의 형광 특성과는 상이한 결정된 형광 특성을 갖고,
동일한 형광 특성을 가진 모든 형광 비즈는 동일한 단백질을 지지한다.
따라서, 상기 언급된 조성물은 상기 언급된 단백질 SEQ ID NO: 1 내지 3을 지지하는 적어도 비즈, 또는 상기 기재된 세트의 46개의 단백질까지의 그 이상의 단백질을 포함하고, 상기 단백질의 유비퀴틴화, SUMO화, NEDD화를 평가하는데 사용될 수 있다.
유리하게도, 본 발명은 10개의 단백질의 적어도 10개의 단백질의 그룹을 포함하는, 상기 언급된 바와 같은 조성물에 관한 것으로서, 상기 그룹은 46개의 단백질의 세트에 속하고;
상기 적어도 10개의 단백질은 형광 비즈 상 지지되고,
상기 적어도 10개의 단백질 각각은 결정된 형광 특성을 가진 비즈에 의해 지지되어 적어도 10개의 구별된 단백질-지지 비즈가 수득되고,
상기 적어도 10개의 단백질 중 하나를 지지하는 비즈는 적어도 9개의 다른 단백질-지지 비즈의 형광 특성과는 상이한 결정된 형광 특성을 갖고,
동일한 형광 특성을 가진 모든 형광 비즈는 동일한 단백질을 지지한다.
다시 말하면, 본 발명은 유리하게는 상기 기재된 세트의 46개의 단백질까지 SEQ ID NO: 1 내지 10으로 나타낸 적어도 10개의 단백질을 지지하는 비즈를 포함하는 상기에서 언급된 바와 같은 조성물에 관한 것이다.
REV14
유리하게도, 본 발명은 46개의 단백질을 포함하는 상기 언급된 바와 같은 조성물에 관한 것으로서;
상기 46개의 단백질은 형광 비즈 상 지지되고,
상기 46개의 단백질 각각은 결정된 형광 특성을 가진 비즈에 의해 지지되어 46개의 구별된 단백질-지지 비즈가 수득되고,
상기 46개의 단백질 중 하나를 지지하는 비즈는 적어도 45개의 다른 단백질-지지 비즈의 형광 특성과는 상이한 결정된 형광 특성을 갖고,
동일한 형광 특성을 가진 모든 형광 비즈는 동일한 단백질을 지지한다.
기타의 한 양태에서, 본 발명은 UBL 경로 활성을 정량화하기 위한, 생물학적 샘플의 세포에서 SUMO/유비퀴틴/Nedd8 단백질에 의한 변형에 대한 약물의 시험관 내 효과를 확인하기 위한 상기 정의된 조성물의 용도에 관한 것이다.
본 발명에 따른 조성물은 예를 들어 상기 정의된 방법을 수행하는데 사용될 수 있다.
본 발명은 하기의 도면 및 실시예를 참조하여 잘 설명 및 예시될 것이다.
도 1은 UBC9 shRNA로 처리된 세포(B, C 및 D) 대 대조군 shRNA로 처리된 세포(A)에서 SUMO화 활성의 변형을 나타내는 그래프를 나타낸다. Y-축은 대조군 양에 대한 UBC9 mRNA의 양을 나타낸다. N.S.:유의하지 않음. **: p<0.01
도 2은 UBC9 shRNA로 처리된 세포(B, C 및 D) 대 대조군 shRNA로 처리된 세포(A)에서 ZMYM5 단백질에 대한 SUMO화 활성을 나타내는 그래프를 나타낸다. 세포 추출물을 또한 NEM(N-에틸말레이미드)로 처리하여 모든 SUMO 컨쥬게이션을 저해하였다(음성 대조군)(N). Y-축은 ZMYM5에 대한 SUMO의 양을 나타낸다. N.S.:유의하지 않음. *: p<0.05 **: p<0.01
도 3은 UBC9 shRNA로 처리된 세포(B, C 및 D) 대 대조군 shRNA로 처리된 세포(A)에서 BIRC7 단백질에 대한 유비퀴티닐화(Ubiquitinylation) 활성을 나타내는 그래프를 나타낸다. 세포 추출물을 또한 NEM(N-에틸말레이미드)로 처리하여 모든 SUMO 컨쥬게이션을 저해하였다(음성 대조군)(N). Y-축은 BIRC7에 대한 유비퀴틴의 양을 나타낸다. N.S.:유의하지 않음. *: p<0.05 **: p<0.01
도 4는 UBC9 shRNA로 처리된 세포 추출물(B, B', C, C', D 및 D') 대 대조군 세포 추출물(A, A')의 웨스턴 블롯 결과를 나타낸다. 블롯은 항-SUMO1(A) 및 항-SUMO2(B) 항체로 표지되었다.
도 5는 아나카르드산(C) 또는 2D08(D)으로 처리된 세포의 HL60 세포 추출물 대 디메틸술폭시드(DMSO- B)로 처리된 세포 또는 N-에틸말레이미드(NEM) 처리된 세포(음성 대조군)(A)의 추출물에서 ZMYM5 단백질에 대한 SUMO화 활성 조정을 보여주는 그래프를 나타낸다. Y-축은 ZMYM5에 대한 SUMO의 양을 나타낸다. N.S.:유의하지 않음. *: p<0.05
도 6은 항-SUMO1 항체로 표지된, DMSO(A), 아나카르드산(B) 또는 2D08(C) 저해제로 처리된 세포에 상응하는 세포 추출물의 면역블롯을 나타낸다. 1.은 SUMO화된 단백질을 나타내고, 2.는 유리 SUMO를 나타낸다.
도 7은 MLN4924 저해제(C)로 처리된 HL60의 세포 추출물 대 DMSO(B)로 처리된 세포 또는 N-에틸말레이미드(NEM) 처리된 세포(A)의 세포 추출물에 대한 NEDD화 활성 조정을 보여주는 그래프를 나타낸다.
도 8은 TMEM92(1), BEAN1(2), WBP2(3) 단백질로 코팅된 비즈 상 유비퀴틴 첨가, ZMYM5(4)로 코팅된 비즈 상 SUMO1 첨가, 또는 OTUD6B(5)로 코팅된 비즈 상 NEDD8 첨가를 평가하는 그래프를 나타낸다. HL60 세포는 6시간 동안 0(B), 5(C), 10(D), 50(E), 100(F) 및 500 nM(G) MLN7243로 처리되었다. 대조군으로서, N-에틸말레이미드(NEM) 처리된 세포 추출물을 이용했다(A).
도 9는 SUMO1(A), SUMO2(B), 유비퀴틴(C) 또는 NEDD8(D)과 함께 인큐베이션되고 세포 추출물과 접촉된 형광 비즈 상 코팅된 10개의 단백질의 형광 수준을 보여주는 그래프를 나타낸다. 1.은 ZMYM5 단백질(SEQ ID NO: 1)을 나타내고; 2.는 BEAN 단백질(SEQ ID NO: 2)을 나타내고, 3.은 OTUD6B 단백질(SEQ ID NO: 3)을 나타낸다. Y-축은 세포 카운트를 나타내고, X-축은 형광 강도(임의 단위)를 나타낸다. T는 대조군 비즈(세포 추출물로 처리되지 않음)를 나타낸다.
도 2은 UBC9 shRNA로 처리된 세포(B, C 및 D) 대 대조군 shRNA로 처리된 세포(A)에서 ZMYM5 단백질에 대한 SUMO화 활성을 나타내는 그래프를 나타낸다. 세포 추출물을 또한 NEM(N-에틸말레이미드)로 처리하여 모든 SUMO 컨쥬게이션을 저해하였다(음성 대조군)(N). Y-축은 ZMYM5에 대한 SUMO의 양을 나타낸다. N.S.:유의하지 않음. *: p<0.05 **: p<0.01
도 3은 UBC9 shRNA로 처리된 세포(B, C 및 D) 대 대조군 shRNA로 처리된 세포(A)에서 BIRC7 단백질에 대한 유비퀴티닐화(Ubiquitinylation) 활성을 나타내는 그래프를 나타낸다. 세포 추출물을 또한 NEM(N-에틸말레이미드)로 처리하여 모든 SUMO 컨쥬게이션을 저해하였다(음성 대조군)(N). Y-축은 BIRC7에 대한 유비퀴틴의 양을 나타낸다. N.S.:유의하지 않음. *: p<0.05 **: p<0.01
도 4는 UBC9 shRNA로 처리된 세포 추출물(B, B', C, C', D 및 D') 대 대조군 세포 추출물(A, A')의 웨스턴 블롯 결과를 나타낸다. 블롯은 항-SUMO1(A) 및 항-SUMO2(B) 항체로 표지되었다.
도 5는 아나카르드산(C) 또는 2D08(D)으로 처리된 세포의 HL60 세포 추출물 대 디메틸술폭시드(DMSO- B)로 처리된 세포 또는 N-에틸말레이미드(NEM) 처리된 세포(음성 대조군)(A)의 추출물에서 ZMYM5 단백질에 대한 SUMO화 활성 조정을 보여주는 그래프를 나타낸다. Y-축은 ZMYM5에 대한 SUMO의 양을 나타낸다. N.S.:유의하지 않음. *: p<0.05
도 6은 항-SUMO1 항체로 표지된, DMSO(A), 아나카르드산(B) 또는 2D08(C) 저해제로 처리된 세포에 상응하는 세포 추출물의 면역블롯을 나타낸다. 1.은 SUMO화된 단백질을 나타내고, 2.는 유리 SUMO를 나타낸다.
도 7은 MLN4924 저해제(C)로 처리된 HL60의 세포 추출물 대 DMSO(B)로 처리된 세포 또는 N-에틸말레이미드(NEM) 처리된 세포(A)의 세포 추출물에 대한 NEDD화 활성 조정을 보여주는 그래프를 나타낸다.
도 8은 TMEM92(1), BEAN1(2), WBP2(3) 단백질로 코팅된 비즈 상 유비퀴틴 첨가, ZMYM5(4)로 코팅된 비즈 상 SUMO1 첨가, 또는 OTUD6B(5)로 코팅된 비즈 상 NEDD8 첨가를 평가하는 그래프를 나타낸다. HL60 세포는 6시간 동안 0(B), 5(C), 10(D), 50(E), 100(F) 및 500 nM(G) MLN7243로 처리되었다. 대조군으로서, N-에틸말레이미드(NEM) 처리된 세포 추출물을 이용했다(A).
도 9는 SUMO1(A), SUMO2(B), 유비퀴틴(C) 또는 NEDD8(D)과 함께 인큐베이션되고 세포 추출물과 접촉된 형광 비즈 상 코팅된 10개의 단백질의 형광 수준을 보여주는 그래프를 나타낸다. 1.은 ZMYM5 단백질(SEQ ID NO: 1)을 나타내고; 2.는 BEAN 단백질(SEQ ID NO: 2)을 나타내고, 3.은 OTUD6B 단백질(SEQ ID NO: 3)을 나타낸다. Y-축은 세포 카운트를 나타내고, X-축은 형광 강도(임의 단위)를 나타낸다. T는 대조군 비즈(세포 추출물로 처리되지 않음)를 나타낸다.
실시예
단백질은 하기의 프로토콜에 따라 비즈에 코팅/그래프팅된다.
1. 제조업체의 지침에 따라 스톡 비결합 비즈 현탁물을 재현탁한다.
2. 5.0x106개의 스톡 비즈를 권장되는 미세원심분리 튜브로 옮긴다.
3. 튜브를 자기 분리기에 넣고, 30 내지 60초 동안 분리가 발생되게 한다.
4. 튜브가 여전히 자기 분리기에 있는 상태에서, 상청액을 제거한다. 비즈를 방해하지 않도록 주의한다.
5. 튜브를 자기 분리기에서 제거하고, 약 20초 동안 100 μL dH2O 중 보텍스 및 초음파에 의해 재현탁한다.
6. 튜브를 자기 분리기에 넣고, 30 내지 60초 동안 분리가 발생되게 한다.
7. 튜브가 여전히 자기 분리기에 있는 상태에서, 상청액을 제거한다. 비즈를 방해하지 않도록 주의한다.
8. 튜브를 자기 분리기에서 제거하고, 80 μL 0.1 M 나트륨 포스페이트(단염기성), pH 6.2에 세척된 비즈를 약 20초 동안 보텍스 및 초음파에 의해 재현탁한다. 참고: 비즈는 이 절차 전반에 걸쳐 빛에 장기간 노출되지 않도록 보호되어야 한다.
9. 10 μL의 50 mg/mL 술포-NHS(dH20 중 희석)를 비즈에 첨가하고, 보텍스로 부드럽게 혼합한다.
10. 10 μL의 50 mg/mL EDC(dH20 중 희석)를 비즈에 첨가하고, 보텍스로 부드럽게 혼합한다.
11. 10분의 간격으로 보텍스에 의해 부드럽게 혼합하면서 20분 동안 실온에서 인큐베이션한다.
12. 튜브를 자기 분리기에 넣고, 30 내지 60초 동안 분리가 발생되게 한다.
13. 튜브가 여전히 자기 분리기에 있는 상태에서, 상청액을 제거한다. 비즈를 방해하지 않도록 주의한다.
14. 튜브를 자기 분리기에서 제거하고, 약 20초 동안 250 μL의 50 mM MES, pH 5.0 중 보텍스 및 초음파에 의해 재현탁한다.
15. 50 mM MES, pH 5.0로 총 2회의 세척을 위해 단계 12 및 13을 반복한다.
16. 튜브를 자기 분리기에서 분리하고, 약 20초 동안 100 μL의 50 mM MES, pH 5.0 중 보텍스 및 초음파에 의해 활성화되고 세척된 비즈를 재현탁한다.
17. 25 μg 단백질을 재현탁된 비즈에 첨가한다(즉, 5 μg/1 백만 비즈). (참고: 1 백만 비즈당 5 μg 단백질은 전형적으로 잘 수행된다. 최적의 어세이 성능을 달성하는데 필요에 따라 위 및/또는 아래로 적정하는 것이 권고된다.)
18. 50 mM MES, pH 5.0로 총 부피를 500 μL로 만든다.
19. 보텍스에 의해 커플링 반응을 혼합한다.
20. 실온에서 (회전에 의해) 혼합하면서 2시간 동안 인큐베이션한다.
21. 튜브를 자기 분리기에 넣고, 30 내지 60초 동안 분리가 발생되게 한다.
22. 튜브가 여전히 자기 분리기에 있는 상태에서, 상청액을 제거한다. 비즈를 방해하지 않도록 주의한다.
23. 튜브를 자기 분리기에서 제거하고, 약 20초 동안 보텍스 및 초음파에 의해 500 μL의 PBS-TBN 중 커플링된 비즈를 재현탁한다.
24. 선택적인 블로킹 단계 - 실온에서 (회전에 의해) 혼합하면서 30분 동안 인큐베이션한다. (참고: 비즈를 동일한 날에 이용하는 경우 이 단계를 수행한다.)
25. 튜브를 자기 분리기에 넣고, 30 내지 60초 동안 분리가 발생되게 한다.
26. 튜브가 여전히 자기 분리기에 있는 상태에서, 상청액을 제거한다. 비즈를 방해하지 않도록 주의한다.
27. 튜브를 자기 분리기에서 제거하고, 약 20초 동안 보텍스 및 초음파에 의해 1 mL의 PBS-TBN 중 비즈를 재현탁한다.
28. 단계 25 및 26을 반복한다. 이는 1 mL PBS-TBN로 총 2회의 세척이다.
29. 튜브를 자기 분리기에서 제거하고, 250 내지 1000 μL의 PBS-TBN 중 커플링되고 세척된 비즈를 재현탁한다.
30. 세포 카운터 또는 혈구계를 사용하여 커플링 반응 후 회수된 비즈의 개수를 카운트한다.
31. 커플링된 비즈를 암실에서 2 내지 8℃에서 냉장 보관한다.
실시예 1: 활성 유비퀴틴-유사 시스템의 측정
본 발명자들은 세포 추출물에서 유비퀴티닐화, SUMO화, 및 NEDD화 활성의 정량적 측정이 가능하게 MagPlex Xmap 비즈를 이용하여 방법을 최적화하였다.
따라서 본 발명자들은 유비퀴틴-유사 시스템의 효소를 표적으로 하는 화합물의 저해 활성을 평가하기 위해 이 방법을 이용하고자 하였다.
이 방법을 실시하기 위해, 본 발명자들은 형광 비즈 상 그래프팅된, 유비퀴틴/SUMO/NEDD8에 의해 매우 변형된 10개의 단백질을 이용했다. 10개의 선택된 단백질은 4개의 상이한 경로, 즉 유비퀴틴, SUMO 1 및 2, 및 NEDD8을 나타낸다. 선택된 단백질 일부는 상이한 효소에 의해 동시에 변형될 수 있다.
이 표는 UbL 시스템의 저해 활성의 측정을 위해 선택된 단백질을 나타낸다.
제1의 단계는 단백질이 본 발명자의 방법에 따라 변형될 수 있는지 검토하는 것이었다. 이어서, 단백질을 박테리아에서 생성시킨 다음 상이한 형광 특성을 가진 비즈와 커플링시키고, 약물에 민감한 HL60 세포 추출물을 이용했다.
ZMYM5은 SUMO화의 마커로서 이용하고, OTUD6B는 NEDD화의 마커로서 이용하고, TMEM92, BEAN 및 WBP2은 유비퀴티닐화의 마커로서 이용했다.
실시예 2: SUMO 경로의 저해
본 발명자들은 SUMO화 저해를 평가함으로써 이들의 방법을 검증하기를 원했다.
첫 번째 접근에서, 본 발명자들은 SUMO의 E2 효소인 UBC9의 발현을 저해하는 shRNA를 발현하는 HL60 세포주를 이용했다. 상이한 shRNA를 가진 세 가지 상이한 세포주를 이용하고, 대조군 세포주를 대조군으로서 이용했다. UBC9 발현 저해는, UBC9 RNA의 상대량을 정량화함으로써 RT-qPCR에 의해 평가되었다.
shRNA1은 Ubc9 발현의 제한적인 감소(유의하지 않음)을 유도했고, shRNA2는 약 20%의 감소를 유도하며, shRNA3은 50%의 감소를 유도했다.
따라서, 본 발명자들은 상기 언급된 shRNA로 처리된 세포 추출물에 이들의 방법을 적용한다. 동일한 반응에서, 본 발명자들은 유비퀴티닐화를 측정하였고, SUMO1 및 SUMO2에 의한 SUMO화를 웨스턴 블롯으로써 측정하였다. (도 1 내지 4)
놀랍게도, 웨스턴 블롯에 의해 측정된 SUMO화 수준은 Ubc9 RNA의 50%의 감소가 있는 세포에서 비롯해 유의미하게 변형되지 않는다.
이는 면역블롯에 의해 검출된 단백질이 SUMO화에 의해 유의미하게 변형된 것으로, Ubc9의 양 감소에 덜 민감한 단백질에 상응한다는 사실에 의해 설명될 수 있다.
그러나, 본 발명에 따른 방법은 실험에서 문서화된 세포에서 전반적인 SUMO화의 검출을 허용한다. 실제로, 본 발명에 따른 방법에 의해 측정된 SUMO화 활성은 qPCR에 의해 평가된 UBC9 발현과 직접적으로 상관관계가 있다.
두 번째로, 본 발명자들은 본 발명의 방법이 UbL 경로의 저해제의 효과를 측정하는데 사용될 수 있는지 평가하였다. 이를 위해, 본 발명자들은 두 개의 공지된 SUMO화 저해제(SUMO의 E1 효소를 저해하는 아나카르드산, 및 SUMO의 E2 효소를 저해하는 2D08)를 이용함으로써 방법을 평가했다.
HL60 세포를, 6시간 동안 50μM의 이들 화합물로 처리한 다음, 세포 추출물을 제조하여 본 발명에 따른 방법을 실시하는데 이용하였다.
이어서 세포를 Laemmli 버퍼 중 용해시키고, 샘플을 SDS-PAGE 분리를 위해 아크릴아미드-비스아크릴아미드 겔 상에 로딩하였다. 이어서 단백질을 PVDF 막 상으로 옮기고, 항-SUMO1 항체로 표지하였다.
결과를 도 5 및 6에 나타낸다.
본 발명에 따른 방법을 이용함으로써, 세포 추출물에서 50%의 SUMO화 감소를 검출하는 것이 가능하지만, 면역블롯은 이러한 감소를 나타내지 않는다. 이는 웨스턴 블롯에서 SUMO에 의해 변형되기 쉬운 모든 단백질, 특히 유의미하게 변형된 것이 검출된다는 점에 의해 설명될 수 있다.
약물로 처리된 샘플에서, SUMO화의 감소의 특징인 유리 SUMO1을 검출하는 것이 가능하다. 따라서 본 발명에 따른 방법이 웨스턴 블롯 기반 방법보다 보다 효율적이다.
실시예 3: 약제학적 저해제를 이용한 유비퀴틴-유사 경로의 저해
이 실시예에서, 본 발명자들은 유비퀴틴 및 Nedd8 경로에 대해 치료학적으로 효율적인 것으로 입증되어진 상업용 저해제, 즉 MLN7243(유비퀴틴), 및 MLN4924(NEDD8)로 치료된 환자들의 샘플에 대한 방법을 검증하고자 하였다.
MLN7243(TAK-243)은 유비퀴틴-활성화 효소(UAE, 또한 E1 효소로도 공지됨)를 표적으로 하는 세포 투과성 소분자 저해제이다. 정상의, 건강한 세포에서보다 암세포에서 보다 활성인 것으로 밝혀진 효소는 프로테아좀을 통한 분해를 위한 단백질을 표적으로 하여 유비퀴틴화 반응의 제1 단계를 촉매작용시킨다. 표적화된 단백질에 대한 유비퀴틴 또는 유비퀴틴-유사 단백질의 이 공유 부착은 진핵 유기체에서 단백질 작용을 조절하기 위한 주요 메커니즘이다. 효소의 저해는 단백질 유비퀴틴화와 후속의 유비퀴틴-매개 프로테아좀 분해 모두를 방해하여 세포에서 과량의 단백질을 초래해 소포체(ER) 스트레스-매개 세포자멸사를 초래할 수 있어, 따라서 종양(암) 세포 증식 및 생존을 저해시킬 수 있다. MLN7243은 임상적으로 연구된 이러한 부류의 효소를 특이적으로 표적으로 하는 혁신 신약 저해제이다.
MLN7243은 하기의 화학식을 가진다:
[화학식 1]
.
MLN4924(또한 페보네디스타트(Pevonedistat)로 지칭됨)은 단백질 항상성 경로의 핵심 성분인 NEDD8-활성화 효소(NAE)의 소분자 저해제이다. 이것은 임상적으로 연구될 이 부류의 효소를 특이적으로 표적화하는 제1의 소분자로, 현재 임상 I 상 시험에서 조사되고 있다.
MLN4924은 하기의 화학식을 가진다:
[화학식 2]
.
HL60 세포는 먼저 1 μM의 MLN4924, DMSO로 처리하거나, 세포 배지만으로 6시간 동안 처리하였다. UBC12(NEDD8에 의해 변형된 것으로 이전에 보고된 NEDD화 E2 효소)를 지지하는 비즈를 상기 세포 추출물과 접촉시키고, NEDD8 수준을 평가하였다.
결과를 도 7에 나타낸다.
대조군 샘플에서 측정된 NEDD화는 낮았지만, 1 μM MLN4924로의 처리는 UBC12 단백질 NEDD화의 감소를 보인다.
그 후 본 발명자들은 유비퀴틴 경로의 E1 효소인 MLN7243의 상이한 양의 효과를 평가했다.
이어서, 세포를 0, 5, 10, 50, 100 또는 500 nM MLN7243로 6시간 동안 처리했다. 세포 추출물을 제조하고, TMEM92, BEAN1 또는 WBP2로 코팅된 비즈와 접촉시켰다.
결과를 도 8에 나타낸다.
이들 결과는, 10 nM 이상의 MLN7243으로 유비퀴틴화 활성의 50% 초과가 저해됨을 보여준다(시험관 내 IC50: 1 nM; 급성 골수성 백혈병 세포주에 대한 시험관 내 독성 IC50: 20 내지 40 nM).
500 nM MLN7243으로, TMEM92 NEDD화 저해가 최대이고, WBP2 및 BEAN1은 잔류 수준에서 유비퀴틸화된 채로 존재한다.
MLN7243 저해제는 또한 SUMO화 활성에 영향을 끼치지만, 850 nM의 시험관 내 IC50과 일치하는 다량의 저해제를 사용한 것이다.
NEDD화와 관련하여, MLN7243 시험관 내 IC50은 OTUD6B 단백질에 있어서 28 nM이지만, 데이터는 약간 상이한 감소를 보인다.
재료 및 방법
세포 배양
HL-60(DSMZ, 독일)을 5 % CO2의 존재 하에서 10% 소태아 혈청(FBS) 및 스트렙토마이신/페니실린으로 보충된 RPMI 배지에서 37℃에서 배양하였다. HL-60은 쇼트-탠덤-리피트(Short-Tandem-Repeat) 분석을 이용하여 ATCC에 의해 인증되었다. 모든 세포는 정기적으로 마이코플라스마에 대해 음성으로 테스트되었다. 해동 후, 세포를 10회 이하의 계대 동안 2 내지 3일마다 3.105/ml의 밀도로 계대하였다.
세포 추출물
5 내지 8.105/mL 밀도로 성장된 세포를 5분 동안 4℃에서 스핀 다운(300 g)하고, PBS로 1회 세척하였다. 1 mL의 PBS 중 펠릿 재현탁 후, 이것들을 다시 4℃에서 5분간 다시 원심분리하였다(16,000 g). 펠릿을 재현탁시키고, 2.106 세포당 25 μL의 부피로 저장성 버퍼(20 mM HEPES pH 7.5, 1.5 mM MgCl2, 5 mM KCl, 1 mM DTT 및 1 mg/L의 아프로티닌, 류펩틴 및 펩스타틴) 중 30분 동안 4℃에서 인큐베이션하였다. 액체 질소를 이용해 4회의 동결/해동 사이클을 통해 세포 용해를 달성하였고, DNA를 20-1/2G 니들을 통해 10회의 계대로 전단하였다. 추출물을 마지막으로 4℃에서 20분 동안 2회 원심분리하고(16000 g), 상청액을 분취하고, 급속-냉동하고 -80℃에서 사용할 때까지 유지시켰다.
재조합 단백질의 생성
관심 단백질을 인코딩하는 cDNA를 Ultimate ORF 라이브러리(Thermofisher)로부터 회수하고, 제조업체 프로토콜(Life Technologies)에 따라 Gateway 기술을 이용하여 박테리아 발현 벡터 pGGWA 벡터에서 클로닝하였다. 이어서, 구축물을 BL21(DE3) E.coli 균주에서 형질전환하였다. 단백질 생성은 25℃에서 기하급수적으로 성장하는 박테리아에서 6시간 동안 1 mM 이소프로필 β-D-1-티오갈락토피라노시드(IPTG)로 유도하였다.
박테리아 펠릿을, 500 mM NaCl 및 50 mM MgSO4을 함유하는 50 mM Tris-HCl pH 8.6에서 재현탁하고, 액체 N2에서 급속 동결하였다. 해동 후, 박테리아 현탁물을 1 mg/mL 리소자임(Sigma-Aldrich), 8 mM β-메르캅토에탄올, 1 mg/L 아프로티닌, 류펩틴 및 펩스타틴으로 보충하고, 1시간 동안 4℃에서 인큐베이션하였다. 박테리아 부스러기를 스핀다운하였다(1시간 동안 100 000 g). 이어서, 추출물을 Tris 50 mM pH 8.6, NaCl 500 mM, MgSO4 50 mM, 8 mM β-메르캅토에탄올, 1 mg/L 아프로티닌, 류펩틴, 펩스타틴 중 평형화된 글루타티온 아가로오스 비즈(Generon)에 결합시켰다. 이어서, 컬럼을 Tris 50 mM pH 8.6, NaCl 150 mM, MgSO4 50 mM, 8 mM β-메르캅토에탄올, 1 mg/L 아프로티닌, 류펩틴, 펩스타틴으로 광범위하게 세척하고, 20 mM 환원 글루타티온(Sigma-Aldrich)의 첨가로써 용리하였다.
XMap과의 단백질 커플링
Luminex의 2.105 자기 MagPlex XMap 비즈(저농도)를, 저 결합 마이크로튜브(Eppendor)로 옮기고, 500 mM NaCl을 이용하여 세척하였다. 이어서, 이것들을 50 μL의 50 mM MES pH 6.1중 재현탁하고, 5 mg/mL 1-에틸-3-(3-디메틸아미노프로필)카르보디이미드 히드로클로라이드(EDC, Pierce) 및 5 mg/mL Sulfo-NHS(Pierce)의 존재 하에서 실온에서 20분 동안 인큐베이션하였다. 이어서, 비즈를 500 mM NaCl을 함유하는 PBS 중 세척하고, 2시간 동안 실온에서 100 μL PBS중 결합될 7 μg의 재조합 단백질과 인큐베이션하였다. 이어서 이것들을 0.1 % BSA, 0.02 % Tween 20, 0.05 % 나트륨 아지드 및 500 mM NaCl을 함유하는 PBS로 2회 세척하고, 0.1 % BSA, 0.02 % Tween-20, 0.05 % 나트륨 아지드를 함유하는 PBS에서 4℃에서 저장하였다.
XMap 비즈와 커플링된 단백질에 대한 UbL 컨쥬게이션
SUMO-1-, SUMO-2-, NEDD8 및 유비퀴틴 비닐 술폰(0.5 μM 각각)을 세포 추출물(10 μL)에 첨가하고, 이를 15분 동안 4℃에서 인큐베이션하였다. 대조군 추출물을 또한 50 mM NEM으로 인큐베이션하였다. 이어서, 본 발명자들은 20 mM HEPES pH 7.3, 110 mM KOAc, 2 mM Mg(OAc)2, 0.05 % Tween-20, 0.5 mM EGTA, 0.2 mg/mL 오브알부민, 1 mM DTT, 1 mg/L 아프로티닌, 류펩틴 및 펩스타틴, 1 mM ATP, 30 μM 플래그-유비퀴틴, 15 μM NEDD8, 15 μM SUMO-1 및 15 μM SUMO-2을 함유하는 반응 버퍼 10μL 중 함유된 103 단백질-커플링된 XMap 비즈에 첨가하였다. 반응을 45분 동안 30℃에서 수행하였다. 비즈를 0.05 % Tween-20 및 0.5 % SDS를 함유하는 PBS로 2회 5분 동안 및 0.05 % Tween-20을 함유하는 PBS로 3회 5분 동안 세척하였다. 이어서, 이것들을 1 μg/mL의 항-SUMO-1(21C7) 및 항-Flag 항체 또는 항-SUMO-2(8A2) 및 항-NEDD8과 1시간 동안 실온에서 교반 하 인큐베이션하였다. 0.05% Tween-20을 함유하는 PBS 중 5분 동안 세척 후, 이것들을 실온에서 30분 동안 항-마우스 Alexa Fluor 488- 및 항-래빗 Alexa Fluor 405 항체와 0.05% Tween-20 함유 100 μL의 PBS 중 인큐베이션하였다. 비즈를 0.05 % Tween-20을 함유하는 PBS로 5분 동안 다시 세척하였다. 이어서, 이것들을 200 μL PBS 중 재현탁하고, BD Biosciences의 LSR Fortessa 장치를 이용하여 유세포분석의 분석을 하였다. 결과를 FlowJow 소프트웨어를 이용하여 분석하였다.
관심 단백질의 선택
HL-60 또는 U937의 추출물을 UbL-비닐-술폰 및 재조합 UbL로 보충하고, Protoarrays(Life Technologies) 상 인큐베이션하였다. 광범위한 세척 후, 어레이를 1차 마우스 항-SUMO-1 및 래빗 항-Flag(반응에 첨가된 재조합 유비퀴틴 상에 존재하는 태그) 항체 후 형광 커플링된 2차 항체와 인큐베이션하고, 형광에 대해 스캔하였다. 이어서, 항체를 제거하고, 1차 마우스 항-SUMO-2 및 래빗 항-NEDD8 항체 다음 형광 커플링된 2차 항체와 어레이-인큐베이션한 후 형광에 대해 스캔하였다. 강력하게 변형된, 단백질을 확인하기 위해 모든 어레이 상 모든 변형자에 대해 수득된 정규화된 형광 데이터를 대조군 어레이(NEM)의 평균 신호와 비교했다. Welch 및 Wilcoxon-Mann-Whitney 모두를 이용하고 Protoarray 상 평균 형광 강도값이 800보다 높은 두 그룹 사이의 유의미한 차이를 보이는 46개의 단백질을 선택했다.
SEQUENCE LISTING
<110> Centre National de la Recherche Scientifique
Universite de Montpellier
<120> Method for identifying ubiquitin and ubiquitin-like enzyme
activities
<130> BR112490/RIM
<150> EP19305690.0
<151> 2019-05-29
<160> 46
<170> PatentIn version 3.5
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Ala Cys Pro Lys Gly Phe Lys Cys Cys Gly Asp Ser Cys Cys Gln Glu
35 40 45
Asn Glu Leu Phe Pro Gly Pro Val Arg Ile Phe Val Ile Ile Phe Leu
50 55 60
Val Ile Leu Ser Val Phe Cys Ile Cys Gly Leu Ala Lys Cys Phe Cys
65 70 75 80
Arg Asn Cys Arg Glu Pro Glu Pro Asp Thr Pro Val Asp Cys Arg Gly
85 90 95
Pro Leu Glu Leu Pro Ser Ile Ile Pro Pro Glu Arg Val Arg Val Ser
100 105 110
Leu Ser Ala Pro Pro Pro Pro Tyr Ser Glu Val Ile Leu Lys Pro Ser
115 120 125
Leu Gly Pro Thr Pro Thr Glu Pro Pro Pro Pro Tyr Ser Phe Arg Pro
130 135 140
Glu Glu Tyr Thr Gly Asp Gln Arg Gly Ile Asp Asn Pro Ala Phe
145 150 155
<210> 9
<211> 872
<212> PRT
<213> Homo sapiens
<400> 9
Met Ala Thr Ala Cys Lys Arg Ser Gly Glu Pro Gln Ser Asp Asp Ile
1 5 10 15
Glu Ala Ser Arg Met Lys Arg Ala Ala Ala Lys His Leu Ile Glu Arg
20 25 30
Tyr Tyr His Gln Leu Thr Glu Gly Cys Gly Asn Glu Ala Cys Thr Asn
35 40 45
Glu Phe Cys Ala Ser Cys Pro Thr Phe Leu Arg Met Asp Asn Asn Ala
50 55 60
Ala Ala Ile Lys Ala Leu Glu Leu Tyr Lys Ile Asn Ala Lys Leu Cys
65 70 75 80
Asp Pro His Pro Ser Lys Lys Gly Ala Ser Ser Ala Tyr Leu Glu Asn
85 90 95
Ser Lys Gly Ala Pro Asn Asn Ser Cys Ser Glu Ile Lys Met Asn Lys
100 105 110
Lys Gly Ala Arg Ile Asp Phe Lys Asp Val Thr Tyr Leu Thr Glu Glu
115 120 125
Lys Val Tyr Glu Ile Leu Glu Leu Cys Arg Glu Arg Glu Asp Tyr Ser
130 135 140
Pro Leu Ile Arg Val Ile Gly Arg Val Phe Ser Ser Ala Glu Ala Leu
145 150 155 160
Val Gln Ser Phe Arg Lys Val Lys Gln His Thr Lys Glu Glu Leu Lys
165 170 175
Ser Leu Gln Ala Lys Asp Glu Asp Lys Asp Glu Asp Glu Lys Glu Lys
180 185 190
Ala Ala Cys Ser Ala Ala Ala Met Glu Glu Asp Ser Glu Ala Ser Ser
195 200 205
Ser Arg Ile Gly Asp Ser Ser Gln Gly Asp Asn Asn Leu Gln Lys Leu
210 215 220
Gly Pro Asp Asp Val Ser Val Asp Ile Asp Ala Ile Arg Arg Val Tyr
225 230 235 240
Thr Arg Leu Leu Ser Asn Glu Lys Ile Glu Thr Ala Phe Leu Asn Ala
245 250 255
Leu Val Tyr Leu Ser Pro Asn Val Glu Cys Asp Leu Thr Tyr His Asn
260 265 270
Val Tyr Ser Arg Asp Pro Asn Tyr Leu Asn Leu Phe Ile Ile Val Met
275 280 285
Glu Asn Arg Asn Leu His Ser Pro Glu Tyr Leu Glu Met Ala Leu Pro
290 295 300
Leu Phe Cys Lys Ala Met Ser Lys Leu Pro Leu Ala Ala Gln Gly Lys
305 310 315 320
Leu Ile Arg Leu Trp Ser Lys Tyr Asn Ala Asp Gln Ile Arg Arg Met
325 330 335
Met Glu Thr Phe Gln Gln Leu Ile Thr Tyr Lys Val Ile Ser Asn Glu
340 345 350
Phe Asn Ser Arg Asn Leu Val Asn Asp Asp Asp Ala Ile Val Ala Ala
355 360 365
Ser Lys Cys Leu Lys Met Val Tyr Tyr Ala Asn Val Val Gly Gly Glu
370 375 380
Val Asp Thr Asn His Asn Glu Glu Asp Asp Glu Glu Pro Ile Pro Glu
385 390 395 400
Ser Ser Glu Leu Thr Leu Gln Glu Leu Leu Gly Glu Glu Arg Arg Asn
405 410 415
Lys Lys Gly Pro Arg Val Asp Pro Leu Glu Thr Glu Leu Gly Val Lys
420 425 430
Thr Leu Asp Cys Arg Lys Pro Leu Ile Pro Phe Glu Glu Phe Ile Asn
435 440 445
Glu Pro Leu Asn Glu Val Leu Glu Met Asp Lys Asp Tyr Thr Phe Phe
450 455 460
Lys Val Glu Thr Glu Asn Lys Phe Ser Phe Met Thr Cys Pro Phe Ile
465 470 475 480
Leu Asn Ala Val Thr Lys Asn Leu Gly Leu Tyr Tyr Asp Asn Arg Ile
485 490 495
Arg Met Tyr Ser Glu Arg Arg Ile Thr Val Leu Tyr Ser Leu Val Gln
500 505 510
Gly Gln Gln Leu Asn Pro Tyr Leu Arg Leu Lys Val Arg Arg Asp His
515 520 525
Ile Ile Asp Asp Ala Leu Val Arg Leu Glu Met Ile Ala Met Glu Asn
530 535 540
Pro Ala Asp Leu Lys Lys Gln Leu Tyr Val Glu Phe Glu Gly Glu Gln
545 550 555 560
Gly Val Asp Glu Gly Gly Val Ser Lys Glu Phe Phe Gln Leu Val Val
565 570 575
Glu Glu Ile Phe Asn Pro Asp Ile Gly Met Phe Thr Tyr Asp Glu Ser
580 585 590
Thr Lys Leu Phe Trp Phe Asn Pro Ser Ser Phe Glu Thr Glu Gly Gln
595 600 605
Phe Thr Leu Ile Gly Ile Val Leu Gly Leu Ala Ile Tyr Asn Asn Cys
610 615 620
Ile Leu Asp Val His Phe Pro Met Val Val Tyr Arg Lys Leu Met Gly
625 630 635 640
Lys Lys Gly Thr Phe Arg Asp Leu Gly Asp Ser His Pro Val Leu Tyr
645 650 655
Gln Ser Leu Lys Asp Leu Leu Glu Tyr Glu Gly Asn Val Glu Asp Asp
660 665 670
Met Met Ile Thr Phe Gln Ile Ser Gln Thr Asp Leu Phe Gly Asn Pro
675 680 685
Met Met Tyr Asp Leu Lys Glu Asn Gly Asp Lys Ile Pro Ile Thr Asn
690 695 700
Glu Asn Arg Lys Glu Phe Val Asn Leu Tyr Ser Asp Tyr Ile Leu Asn
705 710 715 720
Lys Ser Val Glu Lys Gln Phe Lys Ala Phe Arg Arg Gly Phe His Met
725 730 735
Val Thr Asn Glu Ser Pro Leu Lys Tyr Leu Phe Arg Pro Glu Glu Ile
740 745 750
Glu Leu Leu Ile Cys Gly Ser Arg Asn Leu Gly Phe Gln Ala Leu Glu
755 760 765
Glu Thr Thr Glu Tyr Asp Gly Gly Tyr Thr Arg Asp Ser Val Leu Ile
770 775 780
Arg Glu Phe Trp Glu Ile Val His Ser Phe Thr Asp Glu Gln Lys Arg
785 790 795 800
Leu Phe Leu Gln Phe Thr Thr Gly Thr Asp Arg Ala Pro Val Gly Gly
805 810 815
Leu Gly Lys Leu Lys Met Ile Ile Ala Lys Asn Gly Pro Asp Thr Glu
820 825 830
Arg Leu Pro Thr Ser His Thr Cys Phe Asn Val Leu Leu Leu Pro Glu
835 840 845
Tyr Ser Ser Lys Glu Lys Leu Lys Glu Arg Leu Leu Lys Ala Ile Thr
850 855 860
Tyr Ala Lys Gly Phe Gly Met Leu
865 870
<210> 10
<211> 261
<212> PRT
<213> Homo sapiens
<400> 10
Met Ala Leu Asn Lys Asn His Ser Glu Gly Gly Gly Val Ile Val Asn
1 5 10 15
Asn Thr Glu Ser Ile Leu Met Ser Tyr Asp His Val Glu Leu Thr Phe
20 25 30
Asn Asp Met Lys Asn Val Pro Glu Ala Phe Lys Gly Thr Lys Lys Gly
35 40 45
Thr Val Tyr Leu Thr Pro Tyr Arg Val Ile Phe Leu Ser Lys Gly Lys
50 55 60
Asp Ala Met Gln Ser Phe Met Met Pro Phe Tyr Leu Met Lys Asp Cys
65 70 75 80
Glu Ile Lys Gln Pro Val Phe Gly Ala Asn Tyr Ile Lys Gly Thr Val
85 90 95
Lys Ala Glu Ala Gly Gly Gly Trp Glu Gly Ser Ala Ser Tyr Lys Leu
100 105 110
Thr Phe Thr Ala Gly Gly Ala Ile Glu Phe Gly Gln Arg Met Leu Gln
115 120 125
Val Ala Ser Gln Ala Ser Arg Gly Glu Val Pro Ser Gly Ala Tyr Gly
130 135 140
Tyr Ser Tyr Met Pro Ser Gly Ala Tyr Val Tyr Pro Pro Pro Val Ala
145 150 155 160
Asn Gly Met Tyr Pro Cys Pro Pro Gly Tyr Pro Tyr Pro Pro Pro Pro
165 170 175
Pro Glu Phe Tyr Pro Gly Pro Pro Met Met Asp Gly Ala Met Gly Tyr
180 185 190
Val Gln Pro Pro Pro Pro Pro Tyr Pro Gly Pro Met Glu Pro Pro Val
195 200 205
Ser Gly Pro Asp Val Pro Ser Thr Pro Ala Ala Glu Ala Lys Ala Ala
210 215 220
Glu Ala Ala Ala Ser Ala Tyr Tyr Asn Pro Gly Asn Pro His Asn Val
225 230 235 240
Tyr Met Pro Thr Ser Gln Pro Pro Pro Pro Pro Tyr Tyr Pro Pro Glu
245 250 255
Asp Lys Lys Thr Gln
260
<210> 11
<211> 433
<212> PRT
<213> Homo sapiens
<400> 11
Met Gly Arg Val Gln Leu Phe Glu Ile Ser Leu Ser His Gly Arg Val
1 5 10 15
Val Tyr Ser Pro Gly Glu Pro Leu Ala Gly Thr Val Arg Val Arg Leu
20 25 30
Gly Ala Pro Leu Pro Phe Arg Ala Ile Arg Val Thr Cys Ile Gly Ser
35 40 45
Cys Gly Val Ser Asn Lys Ala Asn Asp Thr Ala Trp Val Val Glu Glu
50 55 60
Gly Tyr Phe Asn Ser Ser Leu Ser Leu Ala Asp Lys Gly Ser Leu Pro
65 70 75 80
Ala Gly Glu His Ser Phe Pro Phe Gln Phe Leu Leu Pro Ala Thr Ala
85 90 95
Pro Thr Ser Phe Glu Gly Pro Phe Gly Lys Ile Val His Gln Val Arg
100 105 110
Ala Ala Ile His Thr Pro Arg Phe Ser Lys Asp His Lys Cys Ser Leu
115 120 125
Val Phe Tyr Ile Leu Ser Pro Leu Asn Leu Asn Ser Ile Pro Asp Ile
130 135 140
Glu Gln Pro Asn Val Ala Ser Ala Thr Lys Lys Phe Ser Tyr Lys Leu
145 150 155 160
Val Lys Thr Gly Ser Val Val Leu Thr Ala Ser Thr Asp Leu Arg Gly
165 170 175
Tyr Val Val Gly Gln Ala Leu Gln Leu His Ala Asp Val Glu Asn Gln
180 185 190
Ser Gly Lys Asp Thr Ser Pro Val Val Ala Ser Leu Leu Gln Lys Val
195 200 205
Ser Tyr Lys Ala Lys Arg Trp Ile His Asp Val Arg Thr Ile Ala Glu
210 215 220
Val Glu Gly Ala Gly Val Lys Ala Trp Arg Arg Ala Gln Trp His Glu
225 230 235 240
Gln Ile Leu Val Pro Ala Leu Pro Gln Ser Ala Leu Pro Gly Cys Ser
245 250 255
Leu Ile His Ile Asp Tyr Tyr Leu Gln Val Ser Leu Lys Ala Pro Glu
260 265 270
Ala Thr Val Thr Leu Pro Val Phe Ile Gly Asn Ile Ala Val Asn His
275 280 285
Ala Pro Val Ser Pro Arg Pro Gly Leu Gly Leu Pro Pro Gly Ala Pro
290 295 300
Pro Leu Val Val Pro Ser Ala Pro Pro Gln Glu Glu Ala Glu Ala Glu
305 310 315 320
Ala Ala Ala Gly Gly Pro His Phe Leu Asp Pro Val Phe Leu Ser Thr
325 330 335
Lys Ser His Ser Gln Arg Gln Pro Leu Leu Ala Thr Leu Ser Ser Val
340 345 350
Pro Gly Ala Pro Glu Pro Cys Pro Gln Asp Gly Ser Pro Ala Ser His
355 360 365
Pro Leu His Pro Pro Leu Cys Ile Ser Thr Gly Ala Thr Val Pro Tyr
370 375 380
Phe Ala Glu Gly Ser Gly Gly Pro Val Pro Thr Thr Ser Thr Leu Ile
385 390 395 400
Leu Pro Pro Glu Tyr Ser Ser Trp Gly Tyr Pro Tyr Glu Ala Pro Pro
405 410 415
Ser Tyr Glu Gln Ser Cys Gly Gly Val Glu Pro Ser Leu Thr Pro Glu
420 425 430
Ser
<210> 12
<211> 414
<212> PRT
<213> Homo sapiens
<400> 12
Met Val Leu Gly Lys Val Lys Ser Leu Thr Ile Ser Phe Asp Cys Leu
1 5 10 15
Asn Asp Ser Asn Val Pro Val Tyr Ser Ser Gly Asp Thr Val Ser Gly
20 25 30
Arg Val Asn Leu Glu Val Thr Gly Glu Ile Arg Val Lys Ser Leu Lys
35 40 45
Ile His Ala Arg Gly His Ala Lys Val Arg Trp Thr Glu Ser Arg Asn
50 55 60
Ala Gly Ser Asn Thr Ala Tyr Thr Gln Asn Tyr Thr Glu Glu Val Glu
65 70 75 80
Tyr Phe Asn His Lys Asp Ile Leu Ile Gly His Glu Arg Asp Asp Asp
85 90 95
Asn Ser Glu Glu Gly Phe His Thr Ile His Ser Gly Arg His Glu Tyr
100 105 110
Ala Phe Ser Phe Glu Leu Pro Gln Thr Pro Leu Ala Thr Ser Phe Glu
115 120 125
Gly Arg His Gly Ser Val Arg Tyr Trp Val Lys Ala Glu Leu His Arg
130 135 140
Pro Trp Leu Leu Pro Val Lys Leu Lys Lys Glu Phe Thr Val Phe Glu
145 150 155 160
His Ile Asp Ile Asn Thr Pro Ser Leu Leu Ser Pro Gln Ala Gly Thr
165 170 175
Lys Glu Lys Thr Leu Cys Cys Trp Phe Cys Thr Ser Gly Pro Ile Ser
180 185 190
Leu Ser Ala Lys Ile Glu Arg Lys Gly Tyr Thr Pro Gly Glu Ser Ile
195 200 205
Gln Ile Phe Ala Glu Ile Glu Asn Cys Ser Ser Arg Met Val Val Pro
210 215 220
Lys Ala Ala Ile Tyr Gln Thr Gln Ala Phe Tyr Ala Lys Gly Lys Met
225 230 235 240
Lys Glu Val Lys Gln Leu Val Ala Asn Leu Arg Gly Glu Ser Leu Ser
245 250 255
Ser Gly Lys Thr Glu Thr Trp Asn Gly Lys Leu Leu Lys Ile Pro Pro
260 265 270
Val Ser Pro Ser Ile Leu Asp Cys Ser Ile Ile Arg Val Glu Tyr Ser
275 280 285
Leu Met Val Tyr Val Asp Ile Pro Gly Ala Met Asp Leu Phe Leu Asn
290 295 300
Leu Pro Leu Val Ile Gly Thr Ile Pro Leu His Pro Phe Gly Ser Arg
305 310 315 320
Thr Ser Ser Val Ser Ser Gln Cys Ser Met Asn Met Asn Trp Leu Ser
325 330 335
Leu Ser Leu Pro Glu Arg Pro Glu Ala Pro Pro Ser Tyr Ala Glu Val
340 345 350
Val Thr Glu Glu Gln Arg Arg Asn Asn Leu Ala Pro Val Ser Ala Cys
355 360 365
Asp Asp Phe Glu Arg Ala Leu Gln Gly Pro Leu Phe Ala Tyr Ile Gln
370 375 380
Glu Phe Arg Phe Leu Pro Pro Pro Leu Tyr Ser Glu Ile Asp Pro Asn
385 390 395 400
Pro Asp Gln Ser Ala Asp Asp Arg Pro Ser Cys Pro Ser Arg
405 410
<210> 13
<211> 255
<212> PRT
<213> Homo sapiens
<400> 13
Met Ser Cys Gly Arg Leu Gly Arg Phe Lys Ala Thr Leu Trp Leu Ser
1 5 10 15
Glu Glu His Pro Leu Ser Leu Gly Asp Gln Val Thr Pro Ile Ile Asp
20 25 30
Leu Met Ala Ile Ser Asn Ala His Phe Ala Lys Leu Arg Asp Phe Ile
35 40 45
Thr Leu Arg Leu Pro Pro Gly Phe Pro Val Lys Ile Glu Ile Pro Leu
50 55 60
Phe His Val Leu Asn Ala Arg Ile Thr Phe Ser Asn Leu Cys Gly Cys
65 70 75 80
Asp Glu Pro Leu Ser Ser Val Trp Val Pro Ala Pro Ser Ser Ala Val
85 90 95
Ala Ala Ser Gly Asn Pro Phe Pro Cys Glu Val Asp Pro Thr Val Phe
100 105 110
Glu Val Pro Asn Gly Tyr Ser Val Leu Gly Met Glu Arg Asn Glu Pro
115 120 125
Leu Arg Asp Glu Asp Asp Asp Leu Leu Gln Phe Ala Ile Gln Gln Ser
130 135 140
Leu Leu Glu Ala Gly Thr Glu Ala Glu Gln Val Thr Val Trp Glu Ala
145 150 155 160
Leu Thr Asn Thr Arg Pro Gly Ala Arg Pro Pro Pro Gln Ala Thr Val
165 170 175
Tyr Glu Glu Gln Leu Gln Leu Glu Arg Ala Leu Gln Glu Ser Leu Gln
180 185 190
Leu Ser Thr Glu Pro Arg Gly Pro Gly Ser Pro Pro Arg Thr Pro Pro
195 200 205
Ala Pro Gly Pro Pro Ser Phe Glu Glu Gln Leu Arg Leu Ala Leu Glu
210 215 220
Leu Ser Ser Arg Glu Gln Glu Glu Arg Glu Arg Arg Gly Gln Gln Glu
225 230 235 240
Glu Glu Asp Leu Gln Arg Ile Leu Gln Leu Ser Leu Thr Glu His
245 250 255
<210> 14
<211> 497
<212> PRT
<213> Homo sapiens
<400> 14
Met Thr Phe Asn Ser Phe Glu Gly Ser Lys Thr Cys Val Pro Ala Asp
1 5 10 15
Ile Asn Lys Glu Glu Glu Phe Val Glu Glu Phe Asn Arg Leu Lys Thr
20 25 30
Phe Ala Asn Phe Pro Ser Gly Ser Pro Val Ser Ala Ser Thr Leu Ala
35 40 45
Arg Ala Gly Phe Leu Tyr Thr Gly Glu Gly Asp Thr Val Arg Cys Phe
50 55 60
Ser Cys His Ala Ala Val Asp Arg Trp Gln Tyr Gly Asp Ser Ala Val
65 70 75 80
Gly Arg His Arg Lys Val Ser Pro Asn Cys Arg Phe Ile Asn Gly Phe
85 90 95
Tyr Leu Glu Asn Ser Ala Thr Gln Ser Thr Asn Ser Gly Ile Gln Asn
100 105 110
Gly Gln Tyr Lys Val Glu Asn Tyr Leu Gly Ser Arg Asp His Phe Ala
115 120 125
Leu Asp Arg Pro Ser Glu Thr His Ala Asp Tyr Leu Leu Arg Thr Gly
130 135 140
Gln Val Val Asp Ile Ser Asp Thr Ile Tyr Pro Arg Asn Pro Ala Met
145 150 155 160
Tyr Ser Glu Glu Ala Arg Leu Lys Ser Phe Gln Asn Trp Pro Asp Tyr
165 170 175
Ala His Leu Thr Pro Arg Glu Leu Ala Ser Ala Gly Leu Tyr Tyr Thr
180 185 190
Gly Ile Gly Asp Gln Val Gln Cys Phe Cys Cys Gly Gly Lys Leu Lys
195 200 205
Asn Trp Glu Pro Cys Asp Arg Ala Trp Ser Glu His Arg Arg His Phe
210 215 220
Pro Asn Cys Phe Phe Val Leu Gly Arg Asn Leu Asn Ile Arg Ser Glu
225 230 235 240
Ser Asp Ala Val Ser Ser Asp Arg Asn Phe Pro Asn Ser Thr Asn Leu
245 250 255
Pro Arg Asn Pro Ser Met Ala Asp Tyr Glu Ala Arg Ile Phe Thr Phe
260 265 270
Gly Thr Trp Ile Tyr Ser Val Asn Lys Glu Gln Leu Ala Arg Ala Gly
275 280 285
Phe Tyr Ala Leu Gly Glu Gly Asp Lys Val Lys Cys Phe His Cys Gly
290 295 300
Gly Gly Leu Thr Asp Trp Lys Pro Ser Glu Asp Pro Trp Glu Gln His
305 310 315 320
Ala Lys Trp Tyr Pro Gly Cys Lys Tyr Leu Leu Glu Gln Lys Gly Gln
325 330 335
Glu Tyr Ile Asn Asn Ile His Leu Thr His Ser Leu Glu Glu Cys Leu
340 345 350
Val Arg Thr Thr Glu Lys Thr Pro Ser Leu Thr Arg Arg Ile Asp Asp
355 360 365
Thr Ile Phe Gln Asn Pro Met Val Gln Glu Ala Ile Arg Met Gly Phe
370 375 380
Ser Phe Lys Asp Ile Lys Lys Ile Met Glu Glu Lys Ile Gln Ile Ser
385 390 395 400
Gly Ser Asn Tyr Lys Ser Leu Glu Val Leu Val Ala Asp Leu Val Asn
405 410 415
Ala Gln Lys Asp Ser Met Gln Asp Glu Ser Ser Gln Thr Ser Leu Gln
420 425 430
Lys Glu Ile Ser Thr Glu Glu Gln Leu Arg Arg Leu Gln Glu Glu Lys
435 440 445
Leu Cys Lys Ile Cys Met Asp Arg Asn Ile Ala Ile Val Phe Val Pro
450 455 460
Cys Gly His Leu Val Thr Cys Lys Gln Cys Ala Glu Ala Val Asp Lys
465 470 475 480
Cys Pro Met Cys Tyr Thr Val Ile Thr Phe Lys Gln Lys Ile Phe Met
485 490 495
Ser
<210> 15
<211> 298
<212> PRT
<213> Homo sapiens
<400> 15
Met Gly Pro Lys Asp Ser Ala Lys Cys Leu His Arg Gly Pro Gln Pro
1 5 10 15
Ser His Trp Ala Ala Gly Asp Gly Pro Thr Gln Glu Arg Cys Gly Pro
20 25 30
Arg Ser Leu Gly Ser Pro Val Leu Gly Leu Asp Thr Cys Arg Ala Trp
35 40 45
Asp His Val Asp Gly Gln Ile Leu Gly Gln Leu Arg Pro Leu Thr Glu
50 55 60
Glu Glu Glu Glu Glu Gly Ala Gly Ala Thr Leu Ser Arg Gly Pro Ala
65 70 75 80
Phe Pro Gly Met Gly Ser Glu Glu Leu Arg Leu Ala Ser Phe Tyr Asp
85 90 95
Trp Pro Leu Thr Ala Glu Val Pro Pro Glu Leu Leu Ala Ala Ala Gly
100 105 110
Phe Phe His Thr Gly His Gln Asp Lys Val Arg Cys Phe Phe Cys Tyr
115 120 125
Gly Gly Leu Gln Ser Trp Lys Arg Gly Asp Asp Pro Trp Thr Glu His
130 135 140
Ala Lys Trp Phe Pro Ser Cys Gln Phe Leu Leu Arg Ser Lys Gly Arg
145 150 155 160
Asp Phe Val His Ser Val Gln Glu Thr His Ser Gln Leu Leu Gly Ser
165 170 175
Trp Asp Pro Trp Glu Glu Pro Glu Asp Ala Ala Pro Val Ala Pro Ser
180 185 190
Val Pro Ala Ser Gly Tyr Pro Glu Leu Pro Thr Pro Arg Arg Glu Val
195 200 205
Gln Ser Glu Ser Ala Gln Glu Pro Gly Gly Val Ser Pro Ala Glu Ala
210 215 220
Gln Arg Ala Trp Trp Val Leu Glu Pro Pro Gly Ala Arg Asp Val Glu
225 230 235 240
Ala Gln Leu Arg Arg Leu Gln Glu Glu Arg Thr Cys Lys Val Cys Leu
245 250 255
Asp Arg Ala Val Ser Ile Val Phe Val Pro Cys Gly His Leu Val Cys
260 265 270
Ala Glu Cys Ala Pro Gly Leu Gln Leu Cys Pro Ile Cys Arg Ala Pro
275 280 285
Val Arg Ser Arg Val Arg Thr Phe Leu Ser
290 295
<210> 16
<211> 306
<212> PRT
<213> Homo sapiens
<400> 16
Met Pro Glu Ala Gly Phe Gln Ala Thr Asn Ala Phe Thr Glu Cys Lys
1 5 10 15
Phe Thr Cys Thr Ser Gly Lys Cys Leu Tyr Leu Gly Ser Leu Val Cys
20 25 30
Asn Gln Gln Asn Asp Cys Gly Asp Asn Ser Asp Glu Glu Asn Cys Leu
35 40 45
Leu Val Thr Glu His Pro Pro Pro Gly Ile Phe Asn Ser Glu Leu Glu
50 55 60
Phe Ala Gln Ile Ile Ile Ile Val Val Val Val Thr Val Met Val Val
65 70 75 80
Val Ile Val Cys Leu Leu Asn His Tyr Lys Val Ser Thr Arg Ser Phe
85 90 95
Ile Asn Arg Pro Asn Gln Ser Arg Arg Arg Glu Asp Gly Leu Pro Gln
100 105 110
Glu Gly Cys Leu Trp Pro Ser Asp Ser Ala Ala Pro Arg Leu Gly Ala
115 120 125
Ser Glu Ile Met His Ala Pro Arg Ser Arg Asp Arg Phe Thr Ala Pro
130 135 140
Ser Phe Ile Gln Arg Asp Arg Phe Ser Arg Phe Gln Pro Thr Tyr Pro
145 150 155 160
Tyr Val Gln His Glu Ile Asp Leu Pro Pro Thr Ile Ser Leu Ser Asp
165 170 175
Gly Glu Glu Pro Pro Pro Tyr Gln Gly Pro Cys Thr Leu Gln Leu Arg
180 185 190
Asp Pro Glu Gln Gln Met Glu Leu Asn Arg Glu Ser Val Arg Ala Pro
195 200 205
Pro Asn Arg Thr Ile Phe Asp Ser Asp Leu Ile Asp Ile Ala Met Tyr
210 215 220
Ser Gly Gly Pro Cys Pro Pro Ser Ser Asn Ser Gly Ile Ser Ala Ser
225 230 235 240
Thr Cys Ser Ser Asn Gly Arg Met Glu Gly Pro Pro Pro Thr Tyr Ser
245 250 255
Glu Val Met Gly His His Pro Gly Ala Ser Phe Leu His His Gln Arg
260 265 270
Ser Asn Ala His Arg Gly Ser Arg Leu Gln Phe Gln Gln Asn Asn Ala
275 280 285
Glu Ser Thr Ile Val Pro Ile Lys Gly Lys Asp Arg Lys Pro Gly Asn
290 295 300
Leu Val
305
<210> 17
<211> 170
<212> PRT
<213> Homo sapiens
<400> 17
Met Gln Asn Arg Thr Gly Leu Ile Leu Cys Ala Leu Ala Leu Leu Met
1 5 10 15
Gly Phe Leu Met Val Cys Leu Gly Ala Phe Phe Ile Ser Trp Gly Ser
20 25 30
Ile Phe Asp Cys Gln Gly Ser Leu Ile Ala Ala Tyr Leu Leu Leu Pro
35 40 45
Leu Gly Phe Val Ile Leu Leu Ser Gly Ile Phe Trp Ser Asn Tyr Arg
50 55 60
Gln Val Thr Glu Ser Lys Gly Val Leu Arg His Met Leu Arg Gln His
65 70 75 80
Leu Ala His Gly Ala Leu Pro Val Ala Thr Val Asp Arg Pro Asp Phe
85 90 95
Tyr Pro Pro Ala Tyr Glu Glu Ser Leu Glu Val Glu Lys Gln Ser Cys
100 105 110
Pro Ala Glu Arg Glu Ala Ser Gly Ile Pro Pro Pro Leu Tyr Thr Glu
115 120 125
Thr Gly Leu Glu Phe Gln Asp Gly Asn Asp Ser His Pro Glu Ala Pro
130 135 140
Pro Ser Tyr Arg Glu Ser Ile Ala Gly Leu Val Val Thr Ala Ile Ser
145 150 155 160
Glu Asp Ala Gln Arg Arg Gly Gln Glu Cys
165 170
<210> 18
<211> 386
<212> PRT
<213> Homo sapiens
<400> 18
Met Thr Ser Leu Phe Arg Arg Ser Ser Ser Gly Ser Gly Gly Gly Gly
1 5 10 15
Thr Ala Gly Ala Arg Gly Gly Gly Gly Gly Thr Ala Ala Pro Gln Glu
20 25 30
Leu Asn Asn Ser Arg Pro Ala Arg Gln Val Arg Arg Leu Glu Phe Asn
35 40 45
Gln Ala Met Asp Asp Phe Lys Thr Met Phe Pro Asn Met Asp Tyr Asp
50 55 60
Ile Ile Glu Cys Val Leu Arg Ala Asn Ser Gly Ala Val Asp Ala Thr
65 70 75 80
Ile Asp Gln Leu Leu Gln Met Asn Leu Glu Gly Gly Gly Ser Ser Gly
85 90 95
Gly Val Tyr Glu Asp Ser Ser Asp Ser Glu Asp Ser Ile Pro Pro Glu
100 105 110
Ile Leu Glu Arg Thr Leu Glu Pro Asp Ser Ser Asp Glu Glu Pro Pro
115 120 125
Pro Val Tyr Ser Pro Pro Ala Tyr His Met His Val Phe Asp Arg Pro
130 135 140
Tyr Pro Leu Ala Pro Pro Thr Pro Pro Pro Arg Ile Asp Ala Leu Gly
145 150 155 160
Ser Gly Ala Pro Thr Ser Gln Arg Arg Tyr Arg Asn Trp Asn Pro Pro
165 170 175
Leu Leu Gly Asn Leu Pro Asp Asp Phe Leu Arg Ile Leu Pro Gln Gln
180 185 190
Leu Asp Ser Ile Gln Gly Asn Ala Gly Gly Pro Lys Pro Gly Ser Gly
195 200 205
Glu Gly Cys Pro Pro Ala Met Ala Gly Pro Gly Pro Gly Asp Gln Glu
210 215 220
Ser Arg Trp Lys Gln Tyr Leu Glu Asp Glu Arg Ile Ala Leu Phe Leu
225 230 235 240
Gln Asn Glu Glu Phe Met Lys Glu Leu Gln Arg Asn Arg Asp Phe Leu
245 250 255
Leu Ala Leu Glu Arg Asp Arg Leu Lys Tyr Glu Ser Gln Lys Ser Lys
260 265 270
Ser Ser Ser Val Ala Val Gly Asn Asp Phe Gly Phe Ser Ser Pro Val
275 280 285
Pro Gly Thr Gly Asp Ala Asn Pro Ala Val Ser Glu Asp Ala Leu Phe
290 295 300
Arg Asp Lys Leu Lys His Met Gly Lys Ser Thr Arg Arg Lys Leu Phe
305 310 315 320
Glu Leu Ala Arg Ala Phe Ser Glu Lys Thr Lys Met Arg Lys Ser Lys
325 330 335
Arg Lys His Leu Leu Lys His Gln Ser Leu Gly Ala Ala Ala Ser Thr
340 345 350
Ala Asn Leu Leu Asp Asp Val Glu Gly His Ala Cys Asp Glu Asp Phe
355 360 365
Arg Gly Arg Arg Gln Glu Ala Pro Lys Val Glu Glu Gly Leu Arg Glu
370 375 380
Gly Gln
385
<210> 19
<211> 168
<212> PRT
<213> Homo sapiens
<400> 19
Met Asn Ser Lys Gly Gln Tyr Pro Thr Gln Pro Thr Tyr Pro Val Gln
1 5 10 15
Pro Pro Gly Asn Pro Val Tyr Pro Gln Thr Leu His Leu Pro Gln Ala
20 25 30
Pro Pro Tyr Thr Asp Ala Pro Pro Ala Tyr Ser Glu Leu Tyr Arg Pro
35 40 45
Ser Phe Val His Pro Gly Ala Ala Thr Val Pro Thr Met Ser Ala Ala
50 55 60
Phe Pro Gly Ala Ser Leu Tyr Leu Pro Met Ala Gln Ser Val Ala Val
65 70 75 80
Gly Pro Leu Gly Ser Thr Ile Pro Met Ala Tyr Tyr Pro Val Gly Pro
85 90 95
Ile Tyr Pro Pro Gly Ser Thr Val Leu Val Glu Gly Gly Tyr Asp Ala
100 105 110
Gly Ala Arg Phe Gly Ala Gly Ala Thr Ala Gly Asn Ile Pro Pro Pro
115 120 125
Pro Pro Gly Cys Pro Pro Asn Ala Ala Gln Leu Ala Val Met Gln Gly
130 135 140
Ala Asn Val Leu Val Thr Gln Arg Lys Gly Asn Phe Phe Met Gly Gly
145 150 155 160
Ser Asp Gly Gly Tyr Thr Ile Trp
165
<210> 20
<211> 396
<212> PRT
<213> Homo sapiens
<400> 20
Met Leu Ile Thr Val Tyr Cys Val Arg Arg Asp Leu Ser Glu Val Thr
1 5 10 15
Phe Ser Leu Gln Val Ser Pro Asp Phe Glu Leu Arg Asn Phe Lys Val
20 25 30
Leu Cys Glu Ala Glu Ser Arg Val Pro Val Glu Glu Ile Gln Ile Ile
35 40 45
His Met Glu Arg Leu Leu Ile Glu Asp His Cys Ser Leu Gly Ser Tyr
50 55 60
Gly Leu Lys Asp Gly Asp Ile Val Val Leu Leu Gln Lys Asp Asn Val
65 70 75 80
Gly Pro Arg Ala Pro Gly Arg Ala Pro Asn Gln Pro Arg Val Asp Phe
85 90 95
Ser Gly Ile Ala Val Pro Gly Thr Ser Ser Ser Arg Pro Gln His Pro
100 105 110
Gly Gln Gln Gln Gln Arg Thr Pro Ala Ala Gln Arg Ser Gln Gly Leu
115 120 125
Ala Ser Gly Glu Lys Val Ala Gly Leu Gln Gly Leu Gly Ser Pro Ala
130 135 140
Leu Ile Arg Ser Met Leu Leu Ser Asn Pro His Asp Leu Ser Leu Leu
145 150 155 160
Lys Glu Arg Asn Pro Pro Leu Ala Glu Ala Leu Leu Ser Gly Ser Leu
165 170 175
Glu Thr Phe Ser Gln Val Leu Met Glu Gln Gln Arg Glu Lys Ala Leu
180 185 190
Arg Glu Gln Glu Arg Leu Arg Leu Tyr Thr Ala Asp Pro Leu Asp Arg
195 200 205
Glu Ala Gln Ala Lys Ile Glu Glu Glu Ile Arg Gln Gln Asn Ile Glu
210 215 220
Glu Asn Met Asn Ile Ala Ile Glu Glu Ala Pro Glu Ser Phe Gly Gln
225 230 235 240
Val Thr Met Leu Tyr Ile Asn Cys Lys Val Asn Gly His Pro Leu Lys
245 250 255
Ala Phe Val Asp Ser Gly Ala Gln Met Thr Ile Met Ser Gln Ala Cys
260 265 270
Ala Glu Arg Cys Asn Ile Met Arg Leu Val Asp Arg Arg Trp Ala Gly
275 280 285
Val Ala Lys Gly Val Gly Thr Gln Arg Ile Ile Gly Arg Val His Leu
290 295 300
Ala Gln Ile Gln Ile Glu Gly Asp Phe Leu Gln Cys Ser Phe Ser Ile
305 310 315 320
Leu Glu Asp Gln Pro Met Asp Met Leu Leu Gly Leu Asp Met Leu Arg
325 330 335
Arg His Gln Cys Ser Ile Asp Leu Lys Lys Asn Val Leu Val Ile Gly
340 345 350
Thr Thr Gly Thr Gln Thr Tyr Phe Leu Pro Glu Gly Glu Leu Pro Leu
355 360 365
Cys Ser Arg Met Val Ser Gly Gln Asp Glu Ser Ser Asp Lys Glu Ile
370 375 380
Thr His Ser Val Met Asp Ser Gly Arg Lys Glu His
385 390 395
<210> 21
<211> 650
<212> PRT
<213> Homo sapiens
<400> 21
Met Ala Glu Gly Thr Ala Glu Ala Pro Leu Glu Asn Gly Gly Gly Gly
1 5 10 15
Asp Ser Gly Ala Gly Ala Leu Glu Arg Gly Val Ala Pro Ile Lys Arg
20 25 30
Gln Tyr Leu Thr Thr Lys Glu Gln Phe His Gln Phe Leu Glu Ala Lys
35 40 45
Gly Gln Glu Lys Thr Cys Arg Glu Thr Glu Val Gly Asp Pro Ala Gly
50 55 60
Asn Glu Leu Ala Glu Pro Glu Ala Lys Arg Ile Arg Leu Glu Asp Gly
65 70 75 80
Gln Thr Ala Asp Gly Gln Thr Glu Glu Ala Ala Glu Pro Gly Glu Gln
85 90 95
Leu Gln Thr Gln Lys Arg Ala Arg Gly Gln Asn Lys Gly Arg Pro His
100 105 110
Val Lys Pro Thr Asn Tyr Asp Lys Asn Arg Leu Cys Pro Ser Leu Ile
115 120 125
Gln Glu Ser Ala Ala Lys Cys Phe Phe Gly Asp Arg Cys Arg Phe Leu
130 135 140
His Asp Val Gly Arg Tyr Leu Glu Thr Lys Pro Ala Asp Leu Gly Pro
145 150 155 160
Arg Cys Val Leu Phe Glu Thr Phe Gly Arg Cys Pro Tyr Gly Val Thr
165 170 175
Cys Arg Phe Ala Gly Ala His Leu Gly Pro Glu Gly Gln Asn Leu Val
180 185 190
Gln Glu Glu Leu Ala Ala Arg Gly Thr Gln Pro Pro Ser Ile Arg Asn
195 200 205
Gly Leu Asp Lys Ala Leu Gln Gln Gln Leu Arg Lys Arg Glu Val Arg
210 215 220
Phe Glu Arg Ala Glu Gln Ala Leu Arg Arg Phe Ser Gln Gly Pro Thr
225 230 235 240
Pro Ala Ala Ala Val Pro Glu Gly Thr Ala Ala Glu Gly Ala Pro Arg
245 250 255
Gln Glu Asn Cys Gly Ala Gln Gln Val Pro Ala Gly Pro Gly Thr Ser
260 265 270
Thr Pro Pro Ser Ser Pro Val Arg Thr Cys Gly Pro Leu Thr Asp Glu
275 280 285
Asp Val Val Arg Leu Arg Pro Cys Glu Lys Lys Arg Leu Asp Ile Arg
290 295 300
Gly Lys Leu Tyr Leu Ala Pro Leu Thr Thr Cys Gly Asn Leu Pro Phe
305 310 315 320
Arg Arg Ile Cys Lys Arg Phe Gly Ala Asp Val Thr Cys Gly Glu Met
325 330 335
Ala Val Cys Thr Asn Leu Leu Gln Gly Gln Met Ser Glu Trp Ala Leu
340 345 350
Leu Lys Arg His Gln Cys Glu Asp Ile Phe Gly Val Gln Leu Glu Gly
355 360 365
Ala Phe Pro Asp Thr Met Thr Lys Cys Ala Glu Leu Leu Ser Arg Thr
370 375 380
Val Glu Val Asp Phe Val Asp Ile Asn Val Gly Cys Pro Ile Asp Leu
385 390 395 400
Val Tyr Lys Lys Gly Gly Gly Cys Ala Leu Met Asn Arg Ser Thr Lys
405 410 415
Phe Gln Gln Ile Val Arg Gly Met Asn Gln Val Leu Asp Val Pro Leu
420 425 430
Thr Val Lys Ile Arg Thr Gly Val Gln Glu Arg Val Asn Leu Ala His
435 440 445
Arg Leu Leu Pro Glu Leu Arg Asp Trp Gly Val Ala Leu Val Thr Leu
450 455 460
His Gly Arg Ser Arg Glu Gln Arg Tyr Thr Lys Leu Ala Asp Trp Gln
465 470 475 480
Tyr Ile Glu Glu Cys Val Gln Ala Ala Ser Pro Met Pro Leu Phe Gly
485 490 495
Asn Gly Asp Ile Leu Ser Phe Glu Asp Ala Asn Arg Ala Met Gln Thr
500 505 510
Gly Val Thr Gly Ile Met Ile Ala Arg Gly Ala Leu Leu Lys Pro Trp
515 520 525
Leu Phe Thr Glu Ile Lys Glu Gln Arg His Trp Asp Ile Ser Ser Ser
530 535 540
Glu Arg Leu Asp Ile Leu Arg Asp Phe Thr Asn Tyr Gly Leu Glu His
545 550 555 560
Trp Gly Ser Asp Thr Gln Gly Val Glu Lys Thr Arg Arg Phe Leu Leu
565 570 575
Glu Trp Leu Ser Phe Leu Cys Arg Tyr Val Pro Val Gly Leu Leu Glu
580 585 590
Arg Leu Pro Gln Arg Ile Asn Glu Arg Pro Pro Tyr Tyr Leu Gly Arg
595 600 605
Asp Tyr Leu Glu Thr Leu Met Ala Ser Gln Lys Ala Ala Asp Trp Ile
610 615 620
Arg Ile Ser Glu Met Leu Leu Gly Pro Val Pro Pro Ser Phe Ala Phe
625 630 635 640
Leu Pro Lys His Lys Ala Asn Ala Tyr Lys
645 650
<210> 22
<211> 326
<212> PRT
<213> Homo sapiens
<400> 22
Met Gln Pro Pro Val Pro Gly Pro Leu Gly Leu Leu Asp Pro Ala Glu
1 5 10 15
Gly Leu Ser Arg Arg Lys Lys Thr Ser Leu Trp Phe Val Gly Ser Leu
20 25 30
Leu Leu Val Ser Val Leu Ile Val Thr Val Gly Leu Ala Ala Thr Thr
35 40 45
Arg Thr Glu Asn Val Thr Val Gly Gly Tyr Tyr Pro Gly Ile Ile Leu
50 55 60
Gly Phe Gly Ser Phe Leu Gly Ile Ile Gly Ile Asn Leu Val Glu Asn
65 70 75 80
Arg Arg Gln Met Leu Val Ala Ala Ile Val Phe Ile Ser Phe Gly Val
85 90 95
Val Ala Ala Phe Cys Cys Ala Ile Val Asp Gly Val Phe Ala Ala Gln
100 105 110
His Ile Glu Pro Arg Pro Leu Thr Thr Gly Arg Cys Gln Phe Tyr Ser
115 120 125
Ser Gly Val Gly Tyr Leu Tyr Asp Val Tyr Gln Thr Glu Val Thr Cys
130 135 140
His Ser Leu Asp Gly Lys Cys Gln Leu Lys Val Arg Ser Asn Thr Cys
145 150 155 160
Tyr Cys Cys Asp Leu Tyr Ala Cys Gly Ser Ala Glu Pro Ser Pro Ala
165 170 175
Tyr Tyr Glu Phe Ile Gly Val Ser Gly Cys Gln Asp Val Leu His Leu
180 185 190
Tyr Arg Leu Leu Trp Ala Ser Ala Val Leu Asn Val Leu Gly Leu Phe
195 200 205
Leu Gly Ile Ile Thr Ala Ala Val Leu Gly Ala Phe Lys Asp Met Val
210 215 220
Pro Leu Ser Gln Leu Ala Tyr Gly Pro Ala Val Pro Pro Gln Thr Leu
225 230 235 240
Tyr Asn Pro Ala Gln Gln Ile Leu Ala Tyr Ala Gly Phe Arg Leu Thr
245 250 255
Pro Glu Pro Val Pro Thr Cys Ser Ser Tyr Pro Leu Pro Leu Gln Pro
260 265 270
Cys Ser Arg Phe Pro Val Ala Pro Ser Ser Ala Leu Ala Ser Ser Glu
275 280 285
Asp Leu Gln Pro Pro Ser Pro Ser Ser Ser Gly Ser Gly Leu Pro Gly
290 295 300
Gln Ala Pro Pro Cys Tyr Ala Pro Thr Tyr Phe Pro Pro Gly Glu Lys
305 310 315 320
Pro Pro Pro Tyr Ala Pro
325
<210> 23
<211> 521
<212> PRT
<213> Homo sapiens
<400> 23
Met Glu Phe Gly Leu Ser Trp Val Leu Leu Val Val Phe Leu Gln Gly
1 5 10 15
Val Gln Cys Glu Val Gln Leu Val Asp Ser Gly Gly Gly Leu Val Gln
20 25 30
Pro Gly Gly Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Ile Val
35 40 45
Ser Asp His Tyr Val Glu Trp Val Arg Gln Ala Pro Gly Lys Gly Pro
50 55 60
Glu Trp Val Gly Cys Phe Arg Ser Lys Ala His Lys Ser Thr Thr Glu
65 70 75 80
Tyr Ala Ala Ser Val Lys Gly Arg Phe Thr Ile Leu Arg Asp Asp Ser
85 90 95
Lys Asn Ser Val His Leu Gln Met Asn Ser Leu Lys Thr Asp Asp Thr
100 105 110
Ala Val Tyr Tyr Cys Val Arg Asp Leu Glu Gly Ala Gly Lys Tyr Asp
115 120 125
Trp Tyr Phe Asp Ile Trp Gly Arg Gly Ile Leu Val Thr Val Ser Ser
130 135 140
Ala Ser Thr Lys Gly Pro Ser Val Phe Pro Leu Ala Pro Cys Ser Arg
145 150 155 160
Ser Thr Ser Gly Gly Thr Ala Ala Leu Gly Cys Leu Val Lys Asp Tyr
165 170 175
Phe Pro Glu Pro Val Thr Val Ser Trp Asn Ser Gly Ala Leu Thr Ser
180 185 190
Gly Val His Thr Phe Pro Ala Val Leu Gln Ser Ser Gly Leu Tyr Ser
195 200 205
Leu Ser Ser Val Val Thr Val Pro Ser Ser Ser Leu Gly Thr Gln Thr
210 215 220
Tyr Thr Cys Asn Val Asn His Lys Pro Ser Asn Thr Lys Val Asp Lys
225 230 235 240
Arg Val Glu Leu Lys Thr Pro Leu Gly Asp Thr Thr His Thr Cys Pro
245 250 255
Arg Cys Pro Glu Pro Lys Ser Cys Asp Thr Pro Pro Pro Cys Pro Arg
260 265 270
Cys Pro Glu Pro Lys Ser Cys Asp Thr Pro Pro Pro Cys Pro Arg Cys
275 280 285
Pro Glu Pro Lys Ser Cys Asp Thr Pro Pro Pro Cys Pro Arg Cys Pro
290 295 300
Ala Pro Glu Leu Leu Gly Gly Pro Ser Val Phe Leu Phe Pro Pro Lys
305 310 315 320
Pro Lys Asp Thr Leu Met Ile Ser Arg Thr Pro Glu Val Thr Cys Val
325 330 335
Val Val Asp Val Ser His Glu Asp Pro Glu Val Gln Phe Lys Trp Tyr
340 345 350
Val Asp Gly Val Glu Val His Asn Ala Lys Thr Lys Pro Arg Glu Glu
355 360 365
Gln Phe Asn Ser Thr Phe Arg Val Val Ser Val Leu Thr Val Leu His
370 375 380
Gln Asp Trp Leu Asn Gly Lys Glu Tyr Lys Cys Lys Val Ser Asn Lys
385 390 395 400
Ala Leu Pro Ala Pro Ile Glu Lys Thr Ile Ser Lys Thr Lys Gly Gln
405 410 415
Pro Arg Glu Pro Gln Val Tyr Thr Leu Pro Pro Ser Arg Glu Glu Met
420 425 430
Thr Lys Asn Gln Val Ser Leu Thr Cys Leu Val Lys Gly Phe Tyr Pro
435 440 445
Ser Asp Ile Ala Val Glu Trp Glu Ser Ser Gly Gln Pro Glu Asn Asn
450 455 460
Tyr Asn Thr Thr Pro Pro Met Leu Asp Ser Asp Gly Ser Phe Phe Leu
465 470 475 480
Tyr Ser Lys Leu Thr Val Asp Lys Ser Arg Trp Gln Gln Gly Asn Ile
485 490 495
Phe Ser Cys Ser Val Met His Glu Ala Leu His Asn Arg Phe Thr Gln
500 505 510
Lys Ser Leu Ser Leu Ser Pro Gly Lys
515 520
<210> 24
<211> 303
<212> PRT
<213> Homo sapiens
<400> 24
Met Cys His Gly Arg Ile Ala Pro Lys Ser Thr Ser Val Phe Ala Val
1 5 10 15
Ala Ser Val Gly His Gly Val Phe Leu Pro Leu Val Ile Leu Cys Thr
20 25 30
Leu Leu Gly Asp Gly Leu Ala Ser Val Cys Pro Leu Pro Pro Glu Pro
35 40 45
Glu Asn Gly Gly Tyr Ile Cys His Pro Arg Pro Cys Arg Asp Pro Leu
50 55 60
Thr Ala Gly Ser Val Ile Glu Tyr Leu Cys Ala Glu Gly Tyr Met Leu
65 70 75 80
Lys Gly Asp Tyr Lys Tyr Leu Thr Cys Lys Asn Gly Glu Trp Lys Pro
85 90 95
Ala Met Glu Ile Ser Cys Arg Leu Asn Glu Asp Lys Asp Thr His Thr
100 105 110
Ser Leu Gly Val Pro Thr Leu Ser Ile Val Ala Ser Thr Ala Ser Ser
115 120 125
Val Ala Leu Ile Leu Leu Leu Val Val Leu Phe Val Leu Leu Gln Pro
130 135 140
Lys Leu Lys Ser Phe His His Ser Arg Arg Asp Gln Gly Val Ser Gly
145 150 155 160
Asp Gln Val Ser Ile Met Val Asp Gly Val Gln Val Ala Leu Pro Ser
165 170 175
Tyr Glu Glu Ala Val Tyr Gly Ser Ser Gly His Cys Val Pro Pro Ala
180 185 190
Asp Pro Arg Val Gln Ile Val Leu Ser Glu Gly Ser Gly Pro Ser Gly
195 200 205
Arg Ser Val Pro Arg Glu Gln Gln Leu Pro Asp Gln Gly Ala Cys Ser
210 215 220
Ser Ala Gly Gly Glu Asp Glu Ala Pro Gly Gln Ser Gly Leu Cys Glu
225 230 235 240
Ala Trp Gly Ser Arg Ala Ser Glu Thr Val Met Val His Gln Ala Thr
245 250 255
Thr Ser Ser Trp Val Ala Gly Ser Gly Asn Arg Gln Leu Ala His Lys
260 265 270
Glu Thr Ala Asp Ser Glu Asn Ser Asp Ile Gln Ser Leu Leu Ser Leu
275 280 285
Thr Ser Glu Glu Tyr Thr Asp Asp Ile Pro Leu Leu Lys Glu Ala
290 295 300
<210> 25
<211> 262
<212> PRT
<213> Homo sapiens
<400> 25
Met Asp Pro Arg Leu Ser Thr Val Arg Gln Thr Cys Cys Cys Phe Asn
1 5 10 15
Val Arg Ile Ala Thr Thr Ala Leu Ala Ile Tyr His Val Ile Met Ser
20 25 30
Val Leu Leu Phe Ile Glu His Ser Val Glu Val Ala His Gly Lys Ala
35 40 45
Ser Cys Lys Leu Ser Gln Met Gly Tyr Leu Arg Ile Ala Asp Leu Ile
50 55 60
Ser Ser Phe Leu Leu Ile Thr Met Leu Phe Ile Ile Ser Leu Ser Leu
65 70 75 80
Leu Ile Gly Val Val Lys Asn Arg Glu Lys Tyr Leu Leu Pro Phe Leu
85 90 95
Ser Leu Gln Ile Met Asp Tyr Leu Leu Cys Leu Leu Thr Leu Leu Gly
100 105 110
Ser Tyr Ile Glu Leu Pro Ala Tyr Leu Lys Leu Ala Ser Arg Ser Arg
115 120 125
Ala Ser Ser Ser Lys Phe Pro Leu Met Thr Leu Gln Leu Leu Asp Phe
130 135 140
Cys Leu Ser Ile Leu Thr Leu Cys Ser Ser Tyr Met Glu Val Pro Thr
145 150 155 160
Tyr Leu Asn Phe Lys Ser Met Asn His Met Asn Tyr Leu Pro Ser Gln
165 170 175
Glu Asp Met Pro His Asn Gln Phe Ile Lys Met Met Ile Ile Phe Ser
180 185 190
Ile Ala Phe Ile Thr Val Leu Ile Phe Lys Val Tyr Met Phe Lys Cys
195 200 205
Val Trp Arg Cys Tyr Arg Leu Ile Lys Cys Met Asn Ser Val Glu Glu
210 215 220
Lys Arg Asn Ser Lys Met Leu Gln Lys Val Val Leu Pro Ser Tyr Glu
225 230 235 240
Glu Ala Leu Ser Leu Pro Ser Lys Thr Pro Glu Gly Gly Pro Ala Pro
245 250 255
Pro Pro Tyr Ser Glu Val
260
<210> 26
<211> 251
<212> PRT
<213> Homo sapiens
<400> 26
Met Ser Ser Asp His Leu Asn Asn Ser Thr Leu Lys Glu Ala Gln Phe
1 5 10 15
Lys Asp Leu Phe Leu Lys Lys Ala Glu Leu Glu Phe Ala Gln Ile Ile
20 25 30
Ile Ile Val Val Val Val Thr Val Met Val Val Val Ile Val Cys Leu
35 40 45
Leu Asn His Tyr Lys Val Ser Thr Arg Ser Phe Ile Asn Arg Pro Asn
50 55 60
Gln Ser Arg Arg Arg Glu Asp Gly Leu Pro Gln Ile Met His Ala Pro
65 70 75 80
Arg Ser Arg Asp Arg Phe Thr Ala Pro Ser Phe Ile Gln Arg Asp Arg
85 90 95
Phe Ser Arg Phe Gln Pro Thr Tyr Pro Tyr Val Gln His Glu Ile Asp
100 105 110
Leu Pro Pro Thr Ile Ser Leu Ser Asp Gly Glu Glu Pro Pro Pro Tyr
115 120 125
Gln Gly Pro Cys Thr Leu Gln Leu Arg Asp Pro Glu Gln Gln Met Glu
130 135 140
Leu Asn Arg Glu Ser Val Arg Ala Pro Pro Asn Arg Thr Ile Phe Asp
145 150 155 160
Ser Asp Leu Ile Asp Ile Ala Met Tyr Ser Gly Gly Pro Cys Pro Pro
165 170 175
Ser Ser Asn Ser Gly Ile Ser Ala Ser Thr Cys Ser Ser Asn Gly Arg
180 185 190
Met Glu Gly Pro Pro Pro Thr Tyr Ser Glu Val Met Gly His His Pro
195 200 205
Gly Ala Ser Phe Leu His His Gln Arg Ser Asn Ala His Arg Gly Ser
210 215 220
Arg Leu Gln Phe Gln Gln Asn Asn Ala Glu Ser Thr Ile Val Pro Ile
225 230 235 240
Lys Gly Lys Asp Arg Lys Pro Gly Asn Leu Val
245 250
<210> 27
<211> 161
<212> PRT
<213> Homo sapiens
<400> 27
Met Ser Val Pro Gly Pro Tyr Gln Ala Ala Thr Gly Pro Ser Ser Ala
1 5 10 15
Pro Ser Ala Pro Pro Ser Tyr Glu Glu Thr Val Ala Val Asn Ser Tyr
20 25 30
Tyr Pro Thr Pro Pro Ala Pro Met Pro Gly Pro Thr Thr Gly Leu Val
35 40 45
Thr Gly Pro Asp Gly Lys Gly Met Asn Pro Pro Ser Tyr Tyr Thr Gln
50 55 60
Pro Ala Pro Ile Pro Asn Asn Asn Pro Ile Thr Val Gln Thr Val Tyr
65 70 75 80
Val Gln His Pro Ile Thr Phe Leu Asp Arg Pro Ile Gln Met Cys Cys
85 90 95
Pro Ser Cys Asn Lys Met Ile Val Ser Gln Leu Ser Tyr Asn Ala Gly
100 105 110
Ala Leu Thr Trp Leu Ser Cys Gly Ser Leu Cys Leu Leu Gly Cys Ile
115 120 125
Ala Gly Cys Cys Phe Ile Pro Phe Cys Val Asp Ala Leu Gln Asp Val
130 135 140
Asp His Tyr Cys Pro Asn Cys Arg Ala Leu Leu Gly Thr Tyr Lys Arg
145 150 155 160
Leu
<210> 28
<211> 118
<212> PRT
<213> Homo sapiens
<400> 28
Met Pro Arg Glu Asp Ala His Phe Ile Tyr Gly Tyr Pro Lys Lys Gly
1 5 10 15
His Gly His Ser Tyr Thr Thr Ala Glu Glu Ala Ala Gly Ile Gly Ile
20 25 30
Leu Thr Val Ile Leu Gly Val Leu Leu Leu Ile Gly Cys Trp Tyr Cys
35 40 45
Arg Arg Arg Asn Gly Tyr Arg Ala Leu Met Asp Lys Ser Leu His Val
50 55 60
Gly Thr Gln Cys Ala Leu Thr Arg Arg Cys Pro Gln Glu Gly Phe Asp
65 70 75 80
His Arg Asp Ser Lys Val Ser Leu Gln Glu Lys Asn Cys Glu Pro Val
85 90 95
Val Pro Asn Ala Pro Pro Ala Tyr Glu Lys Leu Ser Ala Glu Gln Ser
100 105 110
Pro Pro Pro Tyr Ser Pro
115
<210> 29
<211> 242
<212> PRT
<213> Homo sapiens
<400> 29
Met Asp His His Gln Pro Gly Thr Gly Arg Tyr Gln Val Leu Leu Asn
1 5 10 15
Glu Glu Asp Asn Ser Glu Ser Ser Ala Ile Glu Gln Pro Pro Thr Ser
20 25 30
Asn Pro Ala Pro Gln Ile Val Gln Ala Ala Ser Ser Ala Pro Ala Leu
35 40 45
Glu Thr Asp Ser Ser Pro Pro Pro Tyr Ser Ser Ile Thr Val Glu Val
50 55 60
Pro Thr Thr Ser Asp Thr Glu Val Tyr Gly Glu Phe Tyr Pro Val Pro
65 70 75 80
Pro Pro Tyr Ser Val Ala Thr Ser Leu Pro Thr Tyr Asp Glu Ala Glu
85 90 95
Lys Ala Lys Ala Ala Ala Met Ala Ala Ala Ala Ala Glu Thr Ser Gln
100 105 110
Arg Ile Gln Glu Glu Glu Cys Pro Pro Arg Asp Asp Phe Ser Asp Ala
115 120 125
Asp Gln Leu Arg Val Gly Asn Asp Gly Ile Phe Met Leu Ala Phe Phe
130 135 140
Met Ala Phe Ile Phe Asn Trp Leu Gly Phe Cys Leu Ser Phe Cys Ile
145 150 155 160
Thr Asn Thr Ile Ala Gly Arg Tyr Gly Ala Ile Cys Gly Phe Gly Leu
165 170 175
Ser Leu Ile Lys Trp Ile Leu Ile Val Arg Phe Ser Asp Tyr Phe Thr
180 185 190
Gly Tyr Phe Asn Gly Gln Tyr Trp Leu Trp Trp Ile Phe Leu Val Leu
195 200 205
Gly Leu Leu Leu Phe Phe Arg Gly Phe Val Asn Tyr Leu Lys Val Arg
210 215 220
Asn Met Ser Glu Ser Met Ala Ala Ala His Arg Thr Arg Tyr Phe Phe
225 230 235 240
Leu Leu
<210> 30
<211> 252
<212> PRT
<213> Homo sapiens
<400> 30
Met Ala Glu Leu Glu Phe Val Gln Ile Ile Ile Ile Val Val Val Met
1 5 10 15
Met Val Met Val Val Val Ile Thr Cys Leu Leu Ser His Tyr Lys Leu
20 25 30
Ser Ala Arg Ser Phe Ile Ser Arg His Ser Gln Gly Arg Arg Arg Glu
35 40 45
Asp Ala Leu Ser Ser Glu Gly Cys Leu Trp Pro Ser Glu Ser Thr Val
50 55 60
Ser Gly Asn Gly Ile Pro Glu Pro Gln Val Tyr Ala Pro Pro Arg Pro
65 70 75 80
Thr Asp Arg Leu Ala Val Pro Pro Phe Ala Gln Arg Glu Arg Phe His
85 90 95
Arg Phe Gln Pro Thr Tyr Pro Tyr Leu Gln His Glu Ile Asp Leu Pro
100 105 110
Pro Thr Ile Ser Leu Ser Asp Gly Glu Glu Pro Pro Pro Tyr Gln Gly
115 120 125
Pro Cys Thr Leu Gln Leu Arg Asp Pro Glu Gln Gln Leu Glu Leu Asn
130 135 140
Arg Glu Ser Val Arg Ala Pro Pro Asn Arg Thr Ile Phe Asp Ser Asp
145 150 155 160
Leu Met Asp Ser Ala Arg Leu Gly Gly Pro Cys Pro Pro Ser Ser Asn
165 170 175
Ser Gly Ile Ser Ala Thr Cys Tyr Gly Ser Gly Gly Arg Met Glu Gly
180 185 190
Pro Pro Pro Thr Tyr Ser Glu Val Ile Gly His Tyr Pro Gly Ser Ser
195 200 205
Phe Gln His Gln Gln Ser Ser Gly Pro Pro Ser Leu Leu Glu Gly Thr
210 215 220
Arg Leu His His Thr His Ile Ala Pro Leu Glu Ser Ala Ala Ile Trp
225 230 235 240
Ser Lys Glu Lys Asp Lys Gln Lys Gly His Pro Leu
245 250
<210> 31
<211> 377
<212> PRT
<213> Homo sapiens
<400> 31
Met Val Leu Glu Ser Thr Met Val Cys Val Asp Asn Ser Glu Tyr Met
1 5 10 15
Arg Asn Gly Asp Phe Leu Pro Thr Arg Leu Gln Ala Gln Gln Asp Ala
20 25 30
Val Asn Ile Val Cys His Ser Lys Thr Arg Ser Asn Pro Glu Asn Asn
35 40 45
Val Gly Leu Ile Thr Leu Ala Asn Asp Cys Glu Val Leu Thr Thr Leu
50 55 60
Thr Pro Asp Thr Gly Arg Ile Leu Ser Lys Leu His Thr Val Gln Pro
65 70 75 80
Lys Gly Lys Ile Thr Phe Cys Thr Gly Ile Arg Val Ala His Leu Ala
85 90 95
Leu Lys His Arg Gln Gly Lys Asn His Lys Met Arg Ile Ile Ala Phe
100 105 110
Val Gly Ser Pro Val Glu Asp Asn Glu Lys Asp Leu Val Lys Leu Ala
115 120 125
Lys Arg Leu Lys Lys Glu Lys Val Asn Val Asp Ile Ile Asn Phe Gly
130 135 140
Glu Glu Glu Val Asn Thr Glu Lys Leu Thr Ala Phe Val Asn Thr Leu
145 150 155 160
Asn Gly Lys Asp Gly Thr Gly Ser His Leu Val Thr Val Pro Pro Gly
165 170 175
Pro Ser Leu Ala Asp Ala Leu Ile Ser Ser Pro Ile Leu Ala Gly Glu
180 185 190
Gly Gly Ala Met Leu Gly Leu Gly Ala Ser Asp Phe Glu Phe Gly Val
195 200 205
Asp Pro Ser Ala Asp Pro Glu Leu Ala Leu Ala Leu Arg Val Ser Met
210 215 220
Glu Glu Gln Arg Gln Arg Gln Glu Glu Glu Ala Arg Arg Ala Ala Ala
225 230 235 240
Ala Ser Ala Ala Glu Ala Gly Ile Ala Thr Thr Gly Thr Glu Asp Ser
245 250 255
Asp Asp Ala Leu Leu Lys Met Thr Ile Ser Gln Gln Glu Phe Gly Arg
260 265 270
Thr Gly Leu Pro Asp Leu Ser Ser Met Thr Glu Glu Glu Gln Ile Ala
275 280 285
Tyr Ala Met Gln Met Ser Leu Gln Gly Ala Glu Phe Gly Gln Ala Glu
290 295 300
Ser Ala Asp Ile Asp Ala Ser Ser Ala Met Asp Thr Ser Glu Pro Ala
305 310 315 320
Lys Glu Glu Asp Asp Tyr Asp Val Met Gln Asp Pro Glu Phe Leu Gln
325 330 335
Ser Val Leu Glu Asn Leu Pro Gly Val Asp Pro Asn Asn Glu Ala Ile
340 345 350
Arg Asn Ala Met Gly Ser Leu Ala Ser Gln Ala Thr Lys Asp Gly Lys
355 360 365
Lys Asp Lys Lys Glu Glu Asp Lys Lys
370 375
<210> 32
<211> 621
<212> PRT
<213> Homo sapiens
<400> 32
Met Ala Asp Phe Glu Glu Leu Arg Asn Met Val Ser Ser Phe Arg Val
1 5 10 15
Ser Glu Leu Gln Val Leu Leu Gly Phe Ala Gly Arg Asn Lys Ser Gly
20 25 30
Arg Lys His Asp Leu Leu Met Arg Ala Leu His Leu Leu Lys Ser Gly
35 40 45
Cys Ser Pro Ala Val Gln Ile Lys Ile Arg Glu Leu Tyr Arg Arg Arg
50 55 60
Tyr Pro Arg Thr Leu Glu Gly Leu Ser Asp Leu Ser Thr Ile Lys Ser
65 70 75 80
Ser Val Phe Ser Leu Asp Gly Gly Ser Ser Pro Val Glu Pro Asp Leu
85 90 95
Ala Val Ala Gly Ile His Ser Leu Pro Ser Thr Ser Val Thr Pro His
100 105 110
Ser Pro Ser Ser Pro Val Gly Ser Val Leu Leu Gln Asp Thr Lys Pro
115 120 125
Thr Phe Glu Met Gln Gln Pro Ser Pro Pro Ile Pro Pro Val His Pro
130 135 140
Asp Val Gln Leu Lys Asn Leu Pro Phe Tyr Asp Val Leu Asp Val Leu
145 150 155 160
Ile Lys Pro Thr Ser Leu Val Gln Ser Ser Ile Gln Arg Phe Gln Glu
165 170 175
Lys Phe Phe Ile Phe Ala Leu Thr Pro Gln Gln Val Arg Glu Ile Cys
180 185 190
Ile Ser Arg Asp Phe Leu Pro Gly Gly Arg Arg Asp Tyr Thr Val Gln
195 200 205
Val Gln Leu Arg Leu Cys Leu Ala Glu Thr Ser Cys Pro Gln Glu Asp
210 215 220
Asn Tyr Pro Asn Ser Leu Cys Ile Lys Val Asn Gly Lys Leu Phe Pro
225 230 235 240
Leu Pro Gly Tyr Ala Pro Pro Pro Lys Asn Gly Ile Glu Gln Lys Arg
245 250 255
Pro Gly Arg Pro Leu Asn Ile Thr Ser Leu Val Arg Leu Ser Ser Ala
260 265 270
Val Pro Asn Gln Ile Ser Ile Ser Trp Ala Ser Glu Ile Gly Lys Asn
275 280 285
Tyr Ser Met Ser Val Tyr Leu Val Arg Gln Leu Thr Ser Ala Met Leu
290 295 300
Leu Gln Arg Leu Lys Met Lys Gly Ile Arg Asn Pro Asp His Ser Arg
305 310 315 320
Ala Leu Ile Lys Glu Lys Leu Thr Ala Asp Pro Asp Ser Glu Ile Ala
325 330 335
Thr Thr Ser Leu Arg Val Ser Leu Met Cys Pro Leu Gly Lys Met Arg
340 345 350
Leu Thr Ile Pro Cys Arg Ala Val Thr Cys Thr His Leu Gln Cys Phe
355 360 365
Asp Ala Ala Leu Tyr Leu Gln Met Asn Glu Lys Lys Pro Thr Trp Ile
370 375 380
Cys Pro Val Cys Asp Lys Lys Ala Ala Tyr Glu Ser Leu Ile Leu Asp
385 390 395 400
Gly Leu Phe Met Glu Ile Leu Asn Asp Cys Ser Asp Val Asp Glu Ile
405 410 415
Lys Phe Gln Glu Asp Gly Ser Trp Cys Pro Met Arg Pro Lys Lys Glu
420 425 430
Ala Met Lys Val Ser Ser Gln Pro Cys Thr Lys Ile Glu Ser Ser Ser
435 440 445
Val Leu Ser Lys Pro Cys Ser Val Thr Val Ala Ser Glu Ala Ser Lys
450 455 460
Lys Lys Val Asp Val Ile Asp Leu Thr Ile Glu Ser Ser Ser Asp Glu
465 470 475 480
Glu Glu Asp Pro Pro Ala Lys Arg Lys Cys Ile Phe Met Ser Glu Thr
485 490 495
Gln Ser Ser Pro Thr Lys Gly Val Leu Met Tyr Gln Pro Ser Ser Val
500 505 510
Arg Val Pro Ser Val Thr Ser Val Asp Pro Ala Ala Ile Pro Pro Ser
515 520 525
Leu Thr Asp Tyr Ser Val Pro Phe His His Thr Pro Ile Ser Ser Met
530 535 540
Ser Ser Asp Leu Pro Gly Leu Asp Phe Leu Ser Leu Ile Pro Val Asp
545 550 555 560
Pro Gln Tyr Cys Pro Pro Met Phe Leu Asp Ser Leu Thr Ser Pro Leu
565 570 575
Thr Ala Ser Ser Thr Ser Val Thr Thr Thr Ser Ser His Glu Ser Ser
580 585 590
Thr His Val Ser Ser Ser Ser Ser Arg Ser Glu Thr Gly Val Ile Thr
595 600 605
Ser Ser Gly Ser Asn Ile Pro Asp Ile Ile Ser Leu Asp
610 615 620
<210> 33
<211> 715
<212> PRT
<213> Homo sapiens
<400> 33
Met Glu Leu Ala Asp Val Gly Ala Ala Ala Ser Ser Gln Gly Val His
1 5 10 15
Asp Gln Val Leu Pro Thr Pro Asn Ala Ser Ser Arg Val Ile Val His
20 25 30
Val Asp Leu Asp Cys Phe Tyr Ala Gln Val Glu Met Ile Ser Asn Pro
35 40 45
Glu Leu Lys Asp Lys Pro Leu Gly Val Gln Gln Lys Tyr Leu Val Val
50 55 60
Thr Cys Asn Tyr Glu Ala Arg Lys Leu Gly Val Lys Lys Leu Met Asn
65 70 75 80
Val Arg Asp Ala Lys Glu Lys Cys Pro Gln Leu Val Leu Val Asn Gly
85 90 95
Glu Asp Leu Thr Arg Tyr Arg Glu Met Ser Tyr Lys Val Thr Glu Leu
100 105 110
Leu Glu Glu Phe Ser Pro Val Val Glu Arg Leu Gly Phe Asp Glu Asn
115 120 125
Phe Val Asp Leu Thr Glu Met Val Glu Lys Arg Leu Gln Gln Leu Gln
130 135 140
Ser Asp Glu Leu Ser Ala Val Thr Val Ser Gly His Val Tyr Asn Asn
145 150 155 160
Gln Ser Ile Asn Leu Leu Asp Val Leu His Ile Arg Leu Leu Val Gly
165 170 175
Ser Gln Ile Ala Ala Glu Met Arg Glu Ala Met Tyr Asn Gln Leu Gly
180 185 190
Leu Thr Gly Cys Ala Gly Val Ala Ser Asn Lys Leu Leu Ala Lys Leu
195 200 205
Val Ser Gly Val Phe Lys Pro Asn Gln Gln Thr Val Leu Leu Pro Glu
210 215 220
Ser Cys Gln His Leu Ile His Ser Leu Asn His Ile Lys Glu Ile Pro
225 230 235 240
Gly Ile Gly Tyr Lys Thr Ala Lys Cys Leu Glu Ala Leu Gly Ile Asn
245 250 255
Ser Val Arg Asp Leu Gln Thr Phe Ser Pro Lys Ile Leu Glu Lys Glu
260 265 270
Leu Gly Ile Ser Val Ala Gln Arg Ile Gln Lys Leu Ser Phe Gly Glu
275 280 285
Asp Asn Ser Pro Val Ile Leu Ser Gly Pro Pro Gln Ser Phe Ser Glu
290 295 300
Glu Asp Ser Phe Lys Lys Cys Ser Ser Glu Val Glu Ala Lys Asn Lys
305 310 315 320
Ile Glu Glu Leu Leu Ala Ser Leu Leu Asn Arg Val Cys Gln Asp Gly
325 330 335
Arg Lys Pro His Thr Val Arg Leu Ile Ile Arg Arg Tyr Ser Ser Glu
340 345 350
Lys His Tyr Gly Arg Glu Ser Arg Gln Cys Pro Ile Pro Ser His Val
355 360 365
Ile Gln Lys Leu Gly Thr Gly Asn Tyr Asp Val Met Thr Pro Met Val
370 375 380
Asp Ile Leu Met Lys Leu Phe Arg Asn Met Val Asn Val Lys Met Pro
385 390 395 400
Phe His Leu Thr Leu Leu Ser Val Cys Phe Cys Asn Leu Lys Ala Leu
405 410 415
Asn Thr Ala Lys Lys Gly Leu Ile Asp Tyr Tyr Leu Met Pro Ser Leu
420 425 430
Ser Thr Thr Ser Arg Ser Gly Lys His Ser Phe Lys Met Lys Asp Thr
435 440 445
His Met Glu Asp Phe Pro Lys Asp Lys Glu Thr Asn Arg Asp Phe Leu
450 455 460
Pro Ser Gly Arg Ile Glu Ser Thr Arg Thr Arg Glu Ser Pro Leu Asp
465 470 475 480
Thr Thr Asn Phe Ser Lys Glu Lys Asp Ile Asn Glu Phe Pro Leu Cys
485 490 495
Ser Leu Pro Glu Gly Val Asp Gln Glu Val Phe Lys Gln Leu Pro Val
500 505 510
Asp Ile Gln Glu Glu Ile Leu Ser Gly Lys Ser Arg Glu Lys Phe Gln
515 520 525
Gly Lys Gly Ser Val Ser Cys Pro Leu His Ala Ser Arg Gly Val Leu
530 535 540
Ser Phe Phe Ser Lys Lys Gln Met Gln Asp Ile Pro Ile Asn Pro Arg
545 550 555 560
Asp His Leu Ser Ser Ser Lys Gln Val Ser Ser Val Ser Pro Cys Glu
565 570 575
Pro Gly Thr Ser Gly Phe Asn Ser Ser Ser Ser Ser Tyr Met Ser Ser
580 585 590
Gln Lys Asp Tyr Ser Tyr Tyr Leu Asp Asn Arg Leu Lys Asp Glu Arg
595 600 605
Ile Ser Gln Gly Pro Lys Glu Pro Gln Gly Phe His Phe Thr Asn Ser
610 615 620
Asn Pro Ala Val Ser Ala Phe His Ser Phe Pro Asn Leu Gln Ser Glu
625 630 635 640
Gln Leu Phe Ser Arg Asn His Thr Thr Asp Ser His Lys Gln Thr Val
645 650 655
Ala Thr Asp Ser His Glu Gly Leu Thr Glu Asn Arg Glu Pro Asp Ser
660 665 670
Val Asp Glu Lys Ile Thr Phe Pro Ser Asp Ile Asp Pro Gln Val Phe
675 680 685
Tyr Glu Leu Pro Glu Ala Val Gln Lys Glu Leu Leu Ala Glu Trp Lys
690 695 700
Arg Ala Gly Ser Asp Phe His Ile Gly His Lys
705 710 715
<210> 34
<211> 696
<212> PRT
<213> Homo sapiens
<400> 34
Met Asp Ala Asp Met Asp Tyr Glu Arg Pro Asn Val Glu Thr Ile Lys
1 5 10 15
Cys Val Val Val Gly Asp Asn Ala Val Gly Lys Thr Arg Leu Ile Cys
20 25 30
Ala Arg Ala Cys Asn Thr Thr Leu Thr Gln Tyr Gln Leu Leu Ala Thr
35 40 45
His Val Pro Thr Val Trp Ala Ile Asp Gln Tyr Arg Val Cys Gln Glu
50 55 60
Val Leu Glu Arg Ser Arg Asp Val Val Asp Glu Val Ser Val Ser Leu
65 70 75 80
Arg Leu Trp Asp Thr Phe Gly Asp His His Lys Asp Arg Arg Phe Ala
85 90 95
Tyr Gly Arg Ser Asp Val Val Val Leu Cys Phe Ser Ile Ala Asn Pro
100 105 110
Asn Ser Leu Asn His Val Lys Ser Met Trp Tyr Pro Glu Ile Lys His
115 120 125
Phe Cys Pro Arg Thr Pro Val Ile Leu Val Gly Cys Gln Leu Asp Leu
130 135 140
Arg Tyr Ala Asp Leu Glu Ala Val Asn Arg Ala Arg Arg Pro Leu Ala
145 150 155 160
Arg Pro Ile Lys Arg Gly Asp Ile Leu Pro Pro Glu Lys Gly Arg Glu
165 170 175
Val Ala Lys Glu Leu Gly Leu Pro Tyr Tyr Glu Thr Ser Val Phe Asp
180 185 190
Gln Phe Gly Ile Lys Asp Val Phe Asp Asn Ala Ile Arg Ala Ala Leu
195 200 205
Ile Ser Arg Arg His Leu Gln Phe Trp Lys Ser His Leu Lys Lys Val
210 215 220
Gln Lys Pro Leu Leu Gln Ala Pro Phe Leu Pro Pro Lys Ala Pro Pro
225 230 235 240
Pro Val Ile Lys Ile Pro Glu Cys Pro Ser Met Gly Thr Asn Glu Ala
245 250 255
Ala Cys Leu Leu Asp Asn Pro Leu Cys Ala Asp Val Leu Phe Ile Leu
260 265 270
Gln Asp Gln Glu His Ile Phe Ala His Arg Ile Tyr Leu Ala Thr Ser
275 280 285
Ser Ser Lys Phe Tyr Asp Leu Phe Leu Met Glu Cys Glu Glu Ser Pro
290 295 300
Asn Gly Ser Glu Gly Ala Cys Glu Lys Glu Lys Gln Ser Arg Asp Phe
305 310 315 320
Gln Gly Arg Ile Leu Ser Val Asp Pro Glu Glu Glu Arg Glu Glu Gly
325 330 335
Pro Pro Arg Ile Pro Gln Ala Asp Gln Trp Lys Ser Ser Asn Lys Ser
340 345 350
Leu Val Glu Ala Leu Gly Leu Glu Ala Glu Gly Ala Val Pro Glu Thr
355 360 365
Gln Thr Leu Thr Gly Trp Ser Lys Gly Phe Ile Gly Met His Arg Glu
370 375 380
Met Gln Val Asn Pro Ile Ser Lys Arg Met Gly Pro Met Thr Val Val
385 390 395 400
Arg Met Asp Ala Ser Val Gln Pro Gly Pro Phe Arg Thr Leu Leu Gln
405 410 415
Phe Leu Tyr Thr Gly Gln Leu Asp Glu Lys Glu Lys Asp Leu Val Gly
420 425 430
Leu Ala Gln Ile Ala Glu Val Leu Glu Met Phe Asp Leu Arg Met Met
435 440 445
Val Glu Asn Ile Met Asn Lys Glu Ala Phe Met Asn Gln Glu Ile Thr
450 455 460
Lys Ala Phe His Val Arg Lys Ala Asn Arg Ile Lys Glu Cys Leu Ser
465 470 475 480
Lys Gly Thr Phe Ser Asp Val Thr Phe Lys Leu Asp Asp Gly Ala Ile
485 490 495
Ser Ala His Lys Pro Leu Leu Ile Cys Ser Cys Glu Trp Met Ala Ala
500 505 510
Met Phe Gly Gly Ser Phe Val Glu Ser Ala Asn Ser Glu Val Tyr Leu
515 520 525
Pro Asn Ile Asn Lys Ile Ser Met Gln Ala Val Leu Asp Tyr Leu Tyr
530 535 540
Thr Lys Gln Leu Ser Pro Asn Leu Asp Leu Asp Pro Leu Glu Leu Ile
545 550 555 560
Ala Leu Ala Asn Arg Phe Cys Leu Pro His Leu Val Ala Leu Ala Glu
565 570 575
Gln His Ala Val Gln Glu Leu Thr Lys Ala Ala Thr Ser Gly Val Gly
580 585 590
Ile Asp Gly Glu Val Leu Ser Tyr Leu Glu Leu Ala Gln Phe His Asn
595 600 605
Ala His Gln Leu Ala Ala Trp Cys Leu His His Ile Cys Thr Asn Tyr
610 615 620
Asn Ser Val Cys Ser Lys Phe Arg Lys Glu Ile Lys Ser Lys Ser Ala
625 630 635 640
Asp Asn Gln Glu Tyr Phe Glu Arg His Arg Trp Pro Pro Val Trp Tyr
645 650 655
Leu Lys Glu Glu Asp His Tyr Gln Arg Val Lys Arg Glu Arg Glu Lys
660 665 670
Glu Asp Ile Ala Leu Asn Lys His Arg Ser Arg Arg Lys Trp Cys Phe
675 680 685
Trp Asn Ser Ser Pro Ala Val Ala
690 695
<210> 35
<211> 180
<212> PRT
<213> Homo sapiens
<400> 35
Met Ile Thr Lys Phe Val Gln Asp Arg His Arg Ala Arg Arg Asn Arg
1 5 10 15
Leu Arg Lys Asp Gln Leu Lys Lys Leu Pro Val His Lys Phe Lys Lys
20 25 30
Gly Asp Glu Tyr Asp Val Cys Ala Ile Cys Leu Asp Glu Tyr Glu Asp
35 40 45
Gly Asp Lys Leu Arg Ile Leu Pro Cys Ser His Ala Tyr His Cys Lys
50 55 60
Cys Val Asp Pro Trp Leu Thr Lys Thr Lys Lys Thr Cys Pro Val Cys
65 70 75 80
Lys Gln Lys Val Val Pro Ser Gln Gly Asp Ser Asp Ser Asp Thr Asp
85 90 95
Ser Ser Gln Glu Glu Asn Glu Val Thr Glu His Thr Pro Leu Leu Arg
100 105 110
Pro Leu Ala Ser Val Ser Ala Gln Ser Phe Gly Ala Leu Ser Glu Ser
115 120 125
Arg Ser His Gln Asn Met Thr Glu Ser Ser Asp Tyr Glu Glu Asp Asp
130 135 140
Asn Glu Asp Thr Asp Ser Ser Asp Ala Glu Asn Glu Ile Asn Glu His
145 150 155 160
Asp Val Val Val Gln Leu Gln Pro Asn Gly Glu Arg Asp Tyr Asn Ile
165 170 175
Ala Asn Thr Val
180
<210> 36
<211> 190
<212> PRT
<213> Homo sapiens
<400> 36
Met Ser Thr Arg Lys Arg Arg Gly Gly Ala Ile Asn Ser Arg Gln Ala
1 5 10 15
Gln Lys Arg Thr Arg Glu Ala Thr Ser Thr Pro Glu Ile Ser Leu Glu
20 25 30
Ala Glu Pro Ile Glu Leu Val Glu Thr Ala Gly Asp Glu Ile Val Asp
35 40 45
Leu Thr Cys Glu Ser Leu Glu Pro Val Val Val Asp Leu Thr His Asn
50 55 60
Asp Ser Val Val Ile Val Asp Glu Arg Arg Arg Pro Arg Arg Asn Ala
65 70 75 80
Arg Arg Leu Pro Gln Asp His Ala Asp Ser Cys Val Val Ser Ser Asp
85 90 95
Asp Glu Glu Leu Ser Arg Asp Arg Asp Val Tyr Val Thr Thr His Thr
100 105 110
Pro Arg Asn Ala Arg Asp Glu Gly Ala Thr Gly Leu Arg Pro Ser Gly
115 120 125
Thr Val Ser Cys Pro Ile Cys Met Asp Gly Tyr Ser Glu Ile Val Gln
130 135 140
Asn Gly Arg Leu Ile Val Ser Thr Glu Cys Gly His Val Phe Cys Ser
145 150 155 160
Gln Cys Leu Arg Asp Ser Leu Lys Asn Ala Asn Thr Cys Pro Thr Cys
165 170 175
Arg Lys Lys Ile Asn His Lys Arg Tyr His Pro Ile Tyr Ile
180 185 190
<210> 37
<211> 372
<212> PRT
<213> Homo sapiens
<400> 37
Met Lys Ala Gly Ala Thr Ser Met Trp Ala Ser Cys Cys Gly Leu Leu
1 5 10 15
Asn Glu Val Met Gly Thr Gly Ala Val Arg Gly Gln Gln Ser Ala Phe
20 25 30
Ala Gly Ala Thr Gly Pro Phe Arg Phe Thr Pro Asn Pro Glu Phe Ser
35 40 45
Thr Tyr Pro Pro Ala Ala Thr Glu Gly Pro Asn Ile Val Cys Lys Ala
50 55 60
Cys Gly Leu Ser Phe Ser Val Phe Arg Lys Lys His Val Cys Cys Asp
65 70 75 80
Cys Lys Lys Asp Phe Cys Ser Val Cys Ser Val Leu Gln Glu Asn Leu
85 90 95
Arg Arg Cys Ser Thr Cys His Leu Leu Gln Glu Thr Ala Phe Gln Arg
100 105 110
Pro Gln Leu Met Arg Leu Lys Val Lys Asp Leu Arg Gln Tyr Leu Ile
115 120 125
Leu Arg Asn Ile Pro Ile Asp Thr Cys Arg Glu Lys Glu Asp Leu Val
130 135 140
Asp Leu Val Leu Cys His His Gly Leu Gly Ser Glu Asp Asp Met Asp
145 150 155 160
Thr Ser Ser Leu Asn Ser Ser Arg Ser Gln Thr Ser Ser Phe Phe Thr
165 170 175
Arg Ser Phe Phe Ser Asn Tyr Thr Ala Pro Ser Ala Thr Met Ser Ser
180 185 190
Phe Gln Gly Glu Leu Met Asp Gly Asp Gln Thr Ser Arg Ser Gly Val
195 200 205
Pro Ala Gln Val Gln Ser Glu Ile Thr Ser Ala Asn Thr Glu Asp Asp
210 215 220
Asp Asp Asp Asp Asp Glu Asp Asp Asp Asp Glu Glu Glu Asn Ala Glu
225 230 235 240
Asp Arg Asn Pro Gly Leu Ser Lys Glu Arg Val Arg Ala Ser Leu Ser
245 250 255
Asp Leu Ser Ser Leu Asp Asp Val Glu Gly Met Ser Val Arg Gln Leu
260 265 270
Lys Glu Ile Leu Ala Arg Asn Phe Val Asn Tyr Ser Gly Cys Cys Glu
275 280 285
Lys Trp Glu Leu Val Glu Lys Val Asn Arg Leu Tyr Lys Glu Asn Glu
290 295 300
Glu Asn Gln Lys Ser Tyr Gly Glu Arg Leu Gln Leu Gln Asp Glu Glu
305 310 315 320
Asp Asp Ser Leu Cys Arg Ile Cys Met Asp Ala Val Ile Asp Cys Val
325 330 335
Leu Leu Glu Cys Gly His Met Val Thr Cys Thr Lys Cys Gly Lys Arg
340 345 350
Met Ser Glu Cys Pro Ile Cys Arg Gln Tyr Val Val Arg Ala Val His
355 360 365
Val Phe Lys Ser
370
<210> 38
<211> 640
<212> PRT
<213> Homo sapiens
<400> 38
Met Ala Leu Ser Arg Gly Leu Pro Arg Glu Leu Ala Glu Ala Val Ala
1 5 10 15
Gly Gly Arg Val Leu Val Val Gly Ala Gly Gly Ile Gly Cys Glu Leu
20 25 30
Leu Lys Asn Leu Val Leu Thr Gly Phe Ser His Ile Asp Leu Ile Asp
35 40 45
Leu Asp Thr Ile Asp Val Ser Asn Leu Asn Arg Gln Phe Leu Phe Gln
50 55 60
Lys Lys His Val Gly Arg Ser Lys Ala Gln Val Ala Lys Glu Ser Val
65 70 75 80
Leu Gln Phe Tyr Pro Lys Ala Asn Ile Val Ala Tyr His Asp Ser Ile
85 90 95
Met Asn Pro Asp Tyr Asn Val Glu Phe Phe Arg Gln Phe Ile Leu Val
100 105 110
Met Asn Ala Leu Asp Asn Arg Ala Ala Arg Asn His Val Asn Arg Met
115 120 125
Cys Leu Ala Ala Asp Val Pro Leu Ile Glu Ser Gly Thr Ala Gly Tyr
130 135 140
Leu Gly Gln Val Thr Thr Ile Lys Lys Gly Val Thr Glu Cys Tyr Glu
145 150 155 160
Cys His Pro Lys Pro Thr Gln Arg Thr Phe Pro Gly Cys Thr Ile Arg
165 170 175
Asn Thr Pro Ser Glu Pro Ile His Cys Ile Val Trp Ala Lys Tyr Leu
180 185 190
Phe Asn Gln Leu Phe Gly Glu Glu Asp Ala Asp Gln Glu Val Ser Pro
195 200 205
Asp Arg Ala Asp Pro Glu Ala Ala Trp Glu Pro Thr Glu Ala Glu Ala
210 215 220
Arg Ala Arg Ala Ser Asn Glu Asp Gly Asp Ile Lys Arg Ile Ser Thr
225 230 235 240
Lys Glu Trp Ala Lys Ser Thr Gly Tyr Asp Pro Val Lys Leu Phe Thr
245 250 255
Lys Leu Phe Lys Asp Asp Ile Arg Tyr Leu Leu Thr Met Asp Lys Leu
260 265 270
Trp Arg Lys Arg Lys Pro Pro Val Pro Leu Asp Trp Ala Glu Val Gln
275 280 285
Ser Gln Gly Glu Glu Thr Asn Ala Ser Asp Gln Gln Asn Glu Pro Gln
290 295 300
Leu Gly Leu Lys Asp Gln Gln Val Leu Asp Val Lys Ser Tyr Ala Arg
305 310 315 320
Leu Phe Ser Lys Ser Ile Glu Thr Leu Arg Val His Leu Ala Glu Lys
325 330 335
Gly Asp Gly Ala Glu Leu Ile Trp Asp Lys Asp Asp Pro Ser Ala Met
340 345 350
Asp Phe Val Thr Ser Ala Ala Asn Leu Arg Met His Ile Phe Ser Met
355 360 365
Asn Met Lys Ser Arg Phe Asp Ile Lys Ser Met Ala Gly Asn Ile Ile
370 375 380
Pro Ala Ile Ala Thr Thr Asn Ala Val Ile Ala Gly Leu Ile Val Leu
385 390 395 400
Glu Gly Leu Lys Ile Leu Ser Gly Lys Ile Asp Gln Cys Arg Thr Ile
405 410 415
Phe Leu Asn Lys Gln Pro Asn Pro Arg Lys Lys Leu Leu Val Pro Cys
420 425 430
Ala Leu Asp Pro Pro Asn Pro Asn Cys Tyr Val Cys Ala Ser Lys Pro
435 440 445
Glu Val Thr Val Arg Leu Asn Val His Lys Val Thr Val Leu Thr Leu
450 455 460
Gln Asp Lys Ile Val Lys Glu Lys Phe Ala Met Val Ala Pro Asp Val
465 470 475 480
Gln Ile Glu Asp Gly Lys Gly Thr Ile Leu Ile Ser Ser Glu Glu Gly
485 490 495
Glu Thr Glu Ala Asn Asn His Lys Lys Leu Ser Glu Phe Gly Ile Arg
500 505 510
Asn Gly Ser Arg Leu Gln Ala Asp Asp Phe Leu Gln Asp Tyr Thr Leu
515 520 525
Leu Ile Asn Ile Leu His Ser Glu Asp Leu Gly Lys Asp Val Glu Phe
530 535 540
Glu Val Val Gly Asp Ala Pro Glu Lys Val Gly Pro Lys Gln Ala Glu
545 550 555 560
Asp Ala Ala Lys Ser Ile Thr Asn Gly Ser Asp Asp Gly Ala Gln Pro
565 570 575
Ser Thr Ser Thr Ala Gln Glu Gln Asp Asp Val Leu Ile Val Asp Ser
580 585 590
Asp Glu Glu Asp Ser Ser Asn Asn Ala Asp Val Ser Glu Glu Glu Arg
595 600 605
Ser Arg Lys Arg Lys Leu Asp Glu Lys Glu Asn Leu Ser Ala Lys Arg
610 615 620
Ser Arg Ile Glu Gln Lys Glu Glu Leu Asp Asp Val Ile Ala Leu Asp
625 630 635 640
<210> 39
<211> 731
<212> PRT
<213> Homo sapiens
<400> 39
Met Lys Leu Arg Ser Ser His Asn Ala Ser Lys Thr Leu Asn Ala Asn
1 5 10 15
Asn Met Glu Thr Leu Ile Glu Cys Gln Ser Glu Gly Asp Ile Lys Glu
20 25 30
His Pro Leu Leu Ala Ser Cys Glu Ser Glu Asp Ser Ile Cys Gln Leu
35 40 45
Ile Glu Val Lys Lys Arg Lys Lys Val Leu Ser Trp Pro Phe Leu Met
50 55 60
Arg Arg Leu Ser Pro Ala Ser Asp Phe Ser Gly Ala Leu Glu Thr Asp
65 70 75 80
Leu Lys Ala Ser Leu Phe Asp Gln Pro Leu Ser Ile Ile Cys Gly Asp
85 90 95
Ser Asp Thr Leu Pro Arg Pro Ile Gln Asp Ile Leu Thr Ile Leu Cys
100 105 110
Leu Lys Gly Pro Ser Thr Glu Gly Ile Phe Arg Arg Ala Ala Asn Glu
115 120 125
Lys Ala Arg Lys Glu Leu Lys Glu Glu Leu Asn Ser Gly Asp Ala Val
130 135 140
Asp Leu Glu Arg Leu Pro Val His Leu Leu Ala Val Val Phe Lys Asp
145 150 155 160
Phe Leu Arg Ser Ile Pro Arg Lys Leu Leu Ser Ser Asp Leu Phe Glu
165 170 175
Glu Trp Met Gly Ala Leu Glu Met Gln Asp Glu Glu Asp Arg Ile Glu
180 185 190
Ala Leu Lys Gln Val Ala Asp Lys Leu Pro Arg Pro Asn Leu Leu Leu
195 200 205
Leu Lys His Leu Val Tyr Val Leu His Leu Ile Ser Lys Asn Ser Glu
210 215 220
Val Asn Arg Met Asp Ser Ser Asn Leu Ala Ile Cys Ile Gly Pro Asn
225 230 235 240
Met Leu Thr Leu Glu Asn Asp Gln Ser Leu Ser Phe Glu Ala Gln Lys
245 250 255
Asp Leu Asn Asn Lys Val Lys Thr Leu Val Glu Phe Leu Ile Asp Asn
260 265 270
Cys Phe Glu Ile Phe Gly Glu Asn Ile Pro Val His Ser Ser Ile Thr
275 280 285
Ser Asp Asp Ser Leu Glu His Thr Asp Ser Ser Asp Val Ser Thr Leu
290 295 300
Gln Asn Asp Ser Ala Tyr Asp Ser Asn Asp Pro Asp Val Glu Ser Asn
305 310 315 320
Ser Ser Ser Gly Ile Ser Ser Pro Ser Arg Gln Pro Gln Val Pro Met
325 330 335
Ala Thr Ala Ala Gly Leu Asp Ser Ala Gly Pro Gln Asp Ala Arg Glu
340 345 350
Val Ser Pro Glu Pro Ile Val Ser Thr Val Ala Arg Leu Lys Ser Ser
355 360 365
Leu Ala Gln Pro Asp Arg Arg Tyr Ser Glu Pro Ser Met Pro Ser Ser
370 375 380
Gln Glu Cys Leu Glu Ser Arg Val Thr Asn Gln Thr Leu Thr Lys Ser
385 390 395 400
Glu Gly Asp Phe Pro Val Pro Arg Val Gly Ser Arg Leu Glu Ser Glu
405 410 415
Glu Ala Glu Asp Pro Phe Pro Glu Glu Val Phe Pro Ala Val Gln Gly
420 425 430
Lys Thr Lys Arg Pro Val Asp Leu Lys Ile Lys Asn Leu Ala Pro Gly
435 440 445
Ser Val Leu Pro Arg Ala Leu Val Leu Lys Ala Phe Ser Ser Ser Ser
450 455 460
Leu Asp Ala Ser Ser Asp Ser Ser Pro Val Ala Ser Pro Ser Ser Pro
465 470 475 480
Lys Arg Asn Phe Phe Ser Arg His Gln Ser Phe Thr Thr Lys Thr Glu
485 490 495
Lys Gly Lys Pro Ser Arg Glu Ile Lys Lys His Ser Met Ser Phe Thr
500 505 510
Phe Ala Pro His Lys Lys Val Leu Thr Lys Asn Leu Ser Ala Gly Ser
515 520 525
Gly Lys Ser Gln Asp Phe Thr Arg Asp His Val Pro Arg Gly Val Arg
530 535 540
Lys Glu Ser Gln Leu Ala Gly Arg Ile Val Gln Glu Asn Gly Cys Glu
545 550 555 560
Thr His Asn Gln Thr Ala Arg Gly Phe Cys Leu Arg Pro His Ala Leu
565 570 575
Ser Val Asp Asp Val Phe Gln Gly Ala Asp Trp Glu Arg Pro Gly Ser
580 585 590
Pro Pro Ser Tyr Glu Glu Ala Met Gln Gly Pro Ala Ala Arg Leu Val
595 600 605
Ala Ser Glu Ser Gln Thr Val Gly Ser Met Thr Val Gly Ser Met Arg
610 615 620
Ala Arg Met Leu Glu Ala His Cys Leu Leu Pro Pro Leu Pro Pro Ala
625 630 635 640
His His Val Glu Asp Ser Arg His Arg Gly Ser Lys Glu Pro Leu Pro
645 650 655
Gly His Gly Leu Ser Pro Leu Pro Glu Arg Trp Lys Gln Ser Arg Thr
660 665 670
Val His Ala Ser Gly Asp Ser Leu Gly His Val Ser Gly Pro Gly Arg
675 680 685
Pro Glu Leu Leu Pro Leu Arg Thr Val Ser Glu Ser Val Gln Arg Asn
690 695 700
Lys Arg Asp Cys Leu Val Arg Arg Cys Ser Gln Pro Val Phe Glu Ala
705 710 715 720
Asp Gln Phe Gln Tyr Ala Lys Glu Ser Tyr Ile
725 730
<210> 40
<211> 216
<212> PRT
<213> Homo sapiens
<400> 40
Met Val Pro Met His Leu Leu Gly Arg Leu Glu Lys Pro Leu Leu Leu
1 5 10 15
Leu Cys Cys Ala Ser Phe Leu Leu Gly Leu Ala Leu Leu Gly Ile Lys
20 25 30
Thr Asp Ile Thr Pro Val Ala Tyr Phe Phe Leu Thr Leu Gly Gly Phe
35 40 45
Phe Leu Phe Ala Tyr Leu Leu Val Arg Phe Leu Glu Trp Gly Leu Arg
50 55 60
Ser Gln Leu Gln Ser Met Gln Thr Glu Ser Pro Gly Pro Ser Gly Asn
65 70 75 80
Ala Arg Asp Asn Glu Ala Phe Glu Val Pro Val Tyr Glu Glu Ala Val
85 90 95
Val Gly Leu Glu Ser Gln Cys Arg Pro Gln Glu Leu Asp Gln Pro Pro
100 105 110
Pro Tyr Ser Thr Val Val Ile Pro Pro Ala Pro Glu Glu Glu Gln Pro
115 120 125
Ser His Pro Glu Gly Ser Arg Arg Ala Lys Leu Glu Gln Arg Arg Met
130 135 140
Ala Ser Glu Gly Ser Met Ala Gln Glu Gly Ser Pro Gly Arg Ala Pro
145 150 155 160
Ile Asn Leu Arg Leu Arg Gly Pro Arg Ala Val Ser Thr Ala Pro Asp
165 170 175
Leu Gln Ser Leu Ala Ala Val Pro Thr Leu Glu Pro Leu Thr Pro Pro
180 185 190
Pro Ala Tyr Asp Val Cys Phe Gly His Pro Asp Asp Asp Ser Val Phe
195 200 205
Tyr Glu Asp Asn Trp Ala Pro Pro
210 215
<210> 41
<211> 243
<212> PRT
<213> Homo sapiens
<400> 41
Met Glu Gln Gly Ser Gly Arg Leu Glu Asp Phe Pro Val Asn Val Phe
1 5 10 15
Ser Val Thr Pro Tyr Thr Pro Ser Thr Ala Asp Ile Gln Val Ser Asp
20 25 30
Asp Asp Lys Ala Gly Ala Thr Leu Leu Phe Ser Gly Ile Phe Leu Gly
35 40 45
Leu Val Gly Ile Thr Phe Thr Val Met Gly Trp Ile Lys Tyr Gln Gly
50 55 60
Val Ser His Phe Glu Trp Thr Gln Leu Leu Gly Pro Val Leu Leu Ser
65 70 75 80
Val Gly Val Thr Phe Ile Leu Ile Ala Val Cys Lys Phe Lys Met Leu
85 90 95
Ser Cys Gln Leu Cys Lys Glu Ser Glu Glu Arg Val Pro Asp Ser Glu
100 105 110
Gln Thr Pro Gly Gly Pro Ser Phe Val Phe Thr Gly Ile Asn Gln Pro
115 120 125
Ile Thr Phe His Gly Ala Thr Val Val Gln Tyr Ile Pro Pro Pro Tyr
130 135 140
Gly Ser Pro Glu Pro Met Gly Ile Asn Thr Ser Tyr Leu Gln Ser Val
145 150 155 160
Val Ser Pro Cys Gly Leu Ile Thr Ser Gly Gly Ala Ala Ala Ala Met
165 170 175
Ser Ser Pro Pro Gln Tyr Tyr Thr Ile Tyr Pro Gln Asp Asn Ser Ala
180 185 190
Phe Val Val Asp Glu Gly Cys Leu Ser Phe Thr Asp Gly Gly Asn His
195 200 205
Arg Pro Asn Pro Asp Val Asp Gln Leu Glu Glu Thr Gln Leu Glu Glu
210 215 220
Glu Ala Cys Ala Cys Phe Ser Pro Pro Pro Tyr Glu Glu Ile Tyr Ser
225 230 235 240
Leu Pro Arg
<210> 42
<211> 277
<212> PRT
<213> Homo sapiens
<400> 42
Met Ala Ala Asp Gly Glu Arg Ser Pro Leu Leu Ser Glu Pro Ile Asp
1 5 10 15
Gly Gly Ala Gly Gly Asn Gly Leu Val Gly Pro Gly Gly Ser Gly Ala
20 25 30
Gly Pro Gly Gly Gly Leu Thr Pro Ser Ala Pro Pro Tyr Gly Ala Ala
35 40 45
Phe Pro Pro Phe Pro Glu Gly His Pro Ala Val Leu Pro Gly Glu Asp
50 55 60
Pro Pro Pro Tyr Ser Pro Leu Thr Ser Pro Asp Ser Gly Ser Ala Pro
65 70 75 80
Met Ile Thr Cys Arg Val Cys Gln Ser Leu Ile Asn Val Glu Gly Lys
85 90 95
Met His Gln His Val Val Lys Cys Gly Val Cys Asn Glu Ala Thr Pro
100 105 110
Ile Lys Asn Ala Pro Pro Gly Lys Lys Tyr Val Arg Cys Pro Cys Asn
115 120 125
Cys Leu Leu Ile Cys Lys Val Thr Ser Gln Arg Ile Ala Cys Pro Arg
130 135 140
Pro Tyr Cys Lys Arg Ile Ile Asn Leu Gly Pro Val His Pro Gly Pro
145 150 155 160
Leu Ser Pro Glu Pro Gln Pro Met Gly Val Arg Val Ile Cys Gly His
165 170 175
Cys Lys Asn Thr Phe Leu Trp Thr Glu Phe Thr Asp Arg Thr Leu Ala
180 185 190
Arg Cys Pro His Cys Arg Lys Val Ser Ser Ile Gly Arg Arg Tyr Pro
195 200 205
Arg Lys Arg Cys Ile Cys Cys Phe Leu Leu Gly Leu Leu Leu Ala Val
210 215 220
Thr Ala Thr Gly Leu Ala Phe Gly Thr Trp Lys His Ala Arg Arg Tyr
225 230 235 240
Gly Gly Ile Tyr Ala Ala Trp Ala Phe Val Ile Leu Leu Ala Val Leu
245 250 255
Cys Leu Gly Arg Ala Leu Tyr Trp Ala Cys Met Lys Val Ser His Pro
260 265 270
Val Gln Asn Phe Ser
275
<210> 43
<211> 287
<212> PRT
<213> Homo sapiens
<400> 43
Met His Arg Leu Met Gly Val Asn Ser Thr Ala Ala Ala Ala Ala Gly
1 5 10 15
Gln Pro Asn Val Ser Cys Thr Cys Asn Cys Lys Arg Ser Leu Phe Gln
20 25 30
Ser Met Glu Ile Thr Glu Leu Glu Phe Val Gln Ile Ile Ile Ile Val
35 40 45
Val Val Met Met Val Met Val Val Val Ile Thr Cys Leu Leu Ser His
50 55 60
Tyr Lys Leu Ser Ala Arg Ser Phe Ile Ser Arg His Ser Gln Gly Arg
65 70 75 80
Arg Arg Glu Asp Ala Leu Ser Ser Glu Gly Cys Leu Trp Pro Ser Glu
85 90 95
Ser Thr Val Ser Gly Asn Gly Ile Pro Glu Pro Gln Val Tyr Ala Pro
100 105 110
Pro Arg Pro Thr Asp Arg Leu Ala Val Pro Pro Phe Ala Gln Arg Glu
115 120 125
Arg Phe His Arg Phe Gln Pro Thr Tyr Pro Tyr Leu Gln His Glu Ile
130 135 140
Asp Leu Pro Pro Thr Ile Ser Leu Ser Asp Gly Glu Glu Pro Pro Pro
145 150 155 160
Tyr Gln Gly Pro Cys Thr Leu Gln Leu Arg Asp Pro Glu Gln Gln Leu
165 170 175
Glu Leu Asn Arg Glu Ser Val Arg Ala Pro Pro Asn Arg Thr Ile Phe
180 185 190
Asp Ser Asp Leu Met Asp Ser Ala Arg Leu Gly Gly Pro Cys Pro Pro
195 200 205
Ser Ser Asn Ser Gly Ile Ser Ala Thr Cys Tyr Gly Ser Gly Gly Arg
210 215 220
Met Glu Gly Pro Pro Pro Thr Tyr Ser Glu Val Ile Gly His Tyr Pro
225 230 235 240
Gly Ser Ser Phe Gln His Gln Gln Ser Ser Gly Pro Pro Ser Leu Leu
245 250 255
Glu Gly Thr Arg Leu His His Thr His Ile Ala Pro Leu Glu Ser Ala
260 265 270
Ala Ile Trp Ser Lys Glu Lys Asp Lys Gln Lys Gly His Pro Leu
275 280 285
<210> 44
<211> 158
<212> PRT
<213> Homo sapiens
<400> 44
Met Ser Gly Ile Ala Leu Ser Arg Leu Ala Gln Glu Arg Lys Ala Trp
1 5 10 15
Arg Lys Asp His Pro Phe Gly Phe Val Ala Val Pro Thr Lys Asn Pro
20 25 30
Asp Gly Thr Met Asn Leu Met Asn Trp Glu Cys Ala Ile Pro Gly Lys
35 40 45
Lys Gly Thr Pro Trp Glu Gly Gly Leu Phe Lys Leu Arg Met Leu Phe
50 55 60
Lys Asp Asp Tyr Pro Ser Ser Pro Pro Lys Cys Lys Phe Glu Pro Pro
65 70 75 80
Leu Phe His Pro Asn Val Tyr Pro Ser Gly Thr Val Cys Leu Ser Ile
85 90 95
Leu Glu Glu Asp Lys Asp Trp Arg Pro Ala Ile Thr Ile Lys Gln Ile
100 105 110
Leu Leu Gly Ile Gln Glu Leu Leu Asn Glu Pro Asn Ile Gln Asp Pro
115 120 125
Ala Gln Ala Glu Ala Tyr Thr Ile Tyr Cys Gln Asn Arg Val Glu Tyr
130 135 140
Glu Lys Arg Val Arg Ala Gln Ala Lys Lys Phe Ala Pro Ser
145 150 155
<210> 45
<211> 146
<212> PRT
<213> Homo sapiens
<400> 45
Met Ser Arg Ser Arg Leu Phe Ser Val Thr Ser Ala Ile Ser Thr Ile
1 5 10 15
Gly Ile Leu Cys Leu Pro Leu Phe Gln Leu Val Leu Ser Asp Leu Pro
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35 40 45
Gly Trp Tyr Ile Trp Ile Leu Leu Leu Leu Val Leu Val Ala Ala Leu
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Leu Cys Gly Ala Val Val Leu Cys Leu Gln Cys Trp Leu Arg Arg Pro
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Arg Ile Asp Ser His Arg Arg Thr Met Ala Val Phe Ala Val Gly Asp
85 90 95
Leu Asp Ser Ile Tyr Gly Thr Glu Ala Ala Val Ser Pro Thr Val Gly
100 105 110
Ile His Leu Gln Thr Gln Thr Pro Asp Leu Tyr Pro Val Pro Ala Pro
115 120 125
Cys Phe Gly Pro Leu Gly Ser Pro Pro Pro Tyr Glu Glu Ile Val Lys
130 135 140
Thr Thr
145
<210> 46
<211> 304
<212> PRT
<213> Homo sapiens
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Met Ala Glu Ala Ser Ala Ala Gly Ala Asp Ser Gly Ala Ala Val Ala
1 5 10 15
Ala His Arg Phe Phe Cys His Phe Cys Lys Gly Glu Val Ser Pro Lys
20 25 30
Leu Pro Glu Tyr Ile Cys Pro Arg Cys Glu Ser Gly Phe Ile Glu Glu
35 40 45
Val Thr Asp Asp Ser Ser Phe Leu Gly Gly Gly Gly Ser Arg Ile Asp
50 55 60
Asn Thr Thr Thr Thr His Phe Ala Glu Leu Trp Gly His Leu Asp His
65 70 75 80
Thr Met Phe Phe Gln Asp Phe Arg Pro Phe Leu Ser Ser Ser Pro Leu
85 90 95
Asp Gln Asp Asn Arg Ala Asn Glu Arg Gly His Gln Thr His Thr Asp
100 105 110
Phe Trp Gly Ala Arg Pro Pro Arg Leu Pro Leu Gly Arg Arg Tyr Arg
115 120 125
Ser Arg Gly Ser Ser Arg Pro Asp Arg Ser Pro Ala Ile Glu Gly Ile
130 135 140
Leu Gln His Ile Phe Ala Gly Phe Phe Ala Asn Ser Ala Ile Pro Gly
145 150 155 160
Ser Pro His Pro Phe Ser Trp Ser Gly Met Leu His Ser Asn Pro Gly
165 170 175
Asp Tyr Ala Trp Gly Gln Thr Gly Leu Asp Ala Ile Val Thr Gln Leu
180 185 190
Leu Gly Gln Leu Glu Asn Thr Gly Pro Pro Pro Ala Asp Lys Glu Lys
195 200 205
Ile Thr Ser Leu Pro Thr Val Thr Val Thr Gln Glu Gln Val Asp Met
210 215 220
Gly Leu Glu Cys Pro Val Cys Lys Glu Asp Tyr Thr Val Glu Glu Glu
225 230 235 240
Val Arg Gln Leu Pro Cys Asn His Phe Phe His Ser Ser Cys Ile Val
245 250 255
Pro Trp Leu Glu Leu His Asp Thr Cys Pro Val Cys Arg Lys Ser Leu
260 265 270
Asn Gly Glu Asp Ser Thr Arg Gln Ser Gln Ser Thr Glu Ala Ser Ala
275 280 285
Ser Asn Arg Phe Ser Asn Asp Ser Gln Leu His Asp Arg Trp Thr Phe
290 295 300
Claims (16)
- 생물학적 샘플의 세포에서 SUMO/유비퀴틴/Nedd8 단백질의 컨쥬게이션에 관여된 단백질 또는 효소의 활성을 정량화하는 방법으로서, 상기 방법은 하기를 포함하는, 방법:
a) 세포의 세포 추출물을, 10개의 단백질의 그룹 중에서 선택된 적어도 3개의 단백질의 하위그룹의 각 단백질과 접촉시키는 단계로서, 상기 10개의 단백질의 그룹은 46개의 단백질의 세트에 속하고;
상기 적어도 3개의 단백질은 지지체 상에 고정되고,
상기 적어도 3개의 단백질은 상기 세포 추출물과 접촉되기 전 SUMO/유비퀴틴/Nedd8 단백질에 의해 컨쥬게이션되지 않으며,
상기 적어도 3개의 단백질은 서열 SEQ ID NO: 1 내지 3으로 이루어진 단백질에 상응하고, 상기 10개의 단백질은 서열 SEQ ID NO: 1 내지 10으로 이루어진 단백질에 상응하고, 상기 46개의 단백질의 그룹은 서열 SEQ ID NO: 1 내지 46으로 이루어진 단백질에 상응하고,
SEQ ID NO: 1은 ZMYM5 단백질에 상응하고; SEQ ID NO: 2은 BEAN 단백질에 상응하고, SEQ ID NO: 3은 OTUD6B에 상응하는, 단계, 및
b) 유비퀴틴, SUMO 및 Nedd8에 대한 제1의 값을 수득하기 위해 상기 적어도 3개의 단백질 각각의 유비퀴틴화(ubiquitination), SUMO화(SUMOylation) 및 NEDD화(NEDDylation) 수준을 동시에 측정하는 단계. - 제1항에 있어서, 상기 방법은 10개의 단백질의 그룹의 각 단백질과 세포 추출물을 접촉시키는 단계를 포함하고, 상기 10개의 단백질의 그룹은 상기 46개의 단백질의 세트에 속하는, 방법.
- 제1항 또는 제2항에 있어서, 상기 방법은 46개의 단백질의 세트의 각 단백질과 세포 추출물을 접촉시키는 단계를 포함하는, 방법.
- 제1항에 있어서, 상기 적어도 3개의 단백질은 비즈에 의해 지지되는, 방법.
- 제4항에 있어서, 상기 비즈는 형광 비즈인, 방법.
- 제4항 또는 제5항에 있어서, 상기 적어도 3개의 단백질 각각은 다른 비즈의 형광 특성과 상이한 형광 특성을 가진 결정된 비즈에 의해 지지되고,
동일한 형광 특성을 가진 모든 비즈는 동일한 단백질을 지지하는, 방법. - 생물학적 샘플의 세포에서 SUMO/유비퀴틴/Nedd8 단백질에 의한 단백질 변형에 대한 약물의 효과를 확인하는 방법으로서, 상기 방법은 하기를 포함하는, 방법:
a) 상기 약물로 처리된 세포의 세포 추출물을 10개의 단백질의 그룹 중 선택된 적어도 3개의 단백질의 하위그룹의 각 단백질과 접촉하는 단계로서, 상기 10개의 단백질의 그룹은 46개의 단백질의 세트에 속하고;
상기 적어도 3개의 단백질은 지지체 상에 고정되고,
상기 적어도 3개의 단백질은 상기 세포 추출물과 접촉되기 전 SUMO/유비퀴틴/Nedd8 단백질에 의해 컨쥬게이션되지 않으며,
상기 적어도 3개의 단백질은 서열 SEQ ID NO: 1 내지 3으로 이루어진 단백질에 상응하고, 상기 10개의 단백질은 서열 SEQ ID NO: 1 내지 10으로 이루어진 단백질에 상응하고, 상기 46개의 단백질의 그룹은 서열 SEQ ID NO: 1 내지 46으로 이루어진 단백질에 상응하고,
SEQ ID NO: 1은 ZMYM5 단백질에 상응하고; SEQ ID NO: 2는 BEAN 단백질에 상응하고, SEQ ID NO: 3은 OTUD6B에 상응하는, 단계,
b) 유비퀴틴, SUMO 및 Nedd8에 대한 제1의 값을 수득하기 위해 상기 적어도 3개의 단백질 각각의 유비퀴틴화, SUMO화 및 NEDD화 수준을 동시에 측정하는 단계;
c) 이전 단계에서 수득된 제1의 값을, 상기 약물로 처리하지 않은 세포의 상기 세포 추출물과 상기 적어도 3개의 단백질을 접촉시 수득된 상기 적어도 3개의 단백질의 유비퀴틴화, SUMO화 및 NEDD화의 제2의 값과 비교하여; 제1의 값과 제2의 값 사이의 비율을 수득하는 단계; 및
d) 하기를 결정하는 단계:
a. 상기 적어도 3개의 단백질 각각의 유비퀴틴화, SUMO화 및 NEDD화의 비율이 1과 상이하지 않은 경우, 이때에는 상기 약물이 SUMO/유비퀴틴/Nedd8 단백질에 의한 단백질 변형에 영향을 미치지 않는지 여부, 및
b. 상기 적어도 3개의 단백질의 적어도 하나의 유비퀴틴화, SUMO화 및 NEDD화의 비율이 1보다 낮거나 높은 경우, 이때에는 상기 약물이 SUMO/유비퀴틴/Nedd8 단백질에 의한 단백질 변형에 영향을 미치는지 여부. - 제7항에 있어서, 상기 방법은 상기 약물로 처리된 세포의 세포 추출물을 46개의 단백질 세트에 속하는 10개의 단백질 그룹의 각 단백질과 접촉시키는 단계를 포함하는, 방법.
- 제8항에 있어서, 상기 방법은 상기 약물로 처리된 세포의 세포 추출물을 46개의 단백질의 세트의 각 단백질과 접촉시키는 단계를 포함하는, 방법.
- 제7항 내지 제9항 중 어느 한 항에 있어서, 상기 적어도 3개의 단백질은 비즈에 의해 지지되는, 방법.
- 제10항에 있어서, 상기 비즈는 형광 비즈인, 방법.
- 제11항에 있어서, 상기 적어도 3개의 단백질 각각은 다른 비즈의 형광 특성과 상이한 형광 특성을 가진 결정된 비즈에 의해 지지되고,
동일한 형광 특성을 가진 모든 비즈는 동일한 단백질을 지지하는, 방법. - 10개의 단백질의 그룹 중에서 선택된 적어도 3개의 단백질을 포함하는 조성물로서, 상기 10개의 단백질의 그룹은 46개의 단백질의 세트에 속하고;
상기 적어도 3개의 단백질은 서열 SEQ ID NO: 1 내지 3으로 이루어진 단백질에 상응하고, 상기 10개의 단백질은 서열 SEQ ID NO: 1 내지 10으로 이루어진 단백질에 상응하고, 상기 46개의 단백질의 그룹은 서열 SEQ ID NO: 1 내지 46으로 이루어진 단백질에 상응하고,
상기 적어도 3개의 단백질은 형광 비즈 상 지지되고,
상기 적어도 3개의 단백질 각각은 결정된 형광 특성을 가진 비즈에 의해 지지되어 적어도 3개의 구별된 단백질-지지 비즈가 수득되고,
상기 적어도 3개의 단백질 중 하나를 지지하는 비즈는 적어도 2개의 다른 단백질-지지 비즈의 형광 특성과는 상이한 결정된 형광 특성을 갖고,
동일한 형광 특성을 가진 모든 형광 비즈는 동일한 단백질을 지지하는, 조성물. - 제13항에 있어서, 10개의 단백질의 적어도 10개의 단백질의 그룹을 포함하는 조성물로서, 상기 그룹은 46개의 단백질의 세트에 속하고;
상기 적어도 10개의 단백질은 형광 비즈 상 지지되고,
상기 적어도 10개의 단백질 각각은 결정된 형광 특성을 가진 비즈에 의해 지지되어 적어도 10개의 구별된 단백질-지지 비즈가 수득되고,
상기 적어도 10개의 단백질 중 하나를 지지하는 비즈는 적어도 9개의 다른 단백질-지지 비즈의 형광 특성과는 상이한 결정된 형광 특성을 갖고,
동일한 형광 특성을 가진 모든 형광 비즈는 동일한 단백질을 지지하는, 조성물. - 제13항 또는 제14항에 있어서, 46개의 단백질을 포함하는 조성물로서;
상기 46개의 단백질은 형광 비즈 상 지지되고,
상기 46개의 단백질 각각은 결정된 형광 특성을 가진 비즈에 의해 지지되어 46개의 구별된 단백질-지지 비즈가 수득되고,
상기 46개의 단백질 중 하나를 지지하는 비즈는 적어도 45개의 다른 단백질-지지 비즈의 형광 특성과는 상이한 결정된 형광 특성을 갖고,
동일한 형광 특성을 가진 모든 형광 비즈는 동일한 단백질을 지지하는, 조성물. - 제13항에 있어서, UBL 경로 활성을 정량화 또는 생물학적 샘플의 세포에서 SUMO/유비퀴틴/Nedd8 단백질에 의한 변형에 대한 약물의 시험관 내 효과 확인용, 조성물.
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| EP1820024B1 (en) | 2004-12-01 | 2012-06-13 | Proteologics, Ltd | Ubiquitin ligase assays and related reagents |
| WO2016034895A1 (en) | 2014-09-04 | 2016-03-10 | The University Court Of The University Of Edinburgh | Method and systems for investigating the ubiquitin-proteasome system |
| US20160209414A1 (en) | 2014-11-07 | 2016-07-21 | University Of Washington Through Its Center For Commercialization | Compositions and methods for the diagnosis and treatment of breast cancer |
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| WO2004020458A2 (en) | 2002-08-30 | 2004-03-11 | Rigel Pharmaceuticals, Inc. | Assays and compositions for identifying agents that modulate the activity of deubiquitinating agents |
| EP1820024B1 (en) | 2004-12-01 | 2012-06-13 | Proteologics, Ltd | Ubiquitin ligase assays and related reagents |
| WO2016034895A1 (en) | 2014-09-04 | 2016-03-10 | The University Court Of The University Of Edinburgh | Method and systems for investigating the ubiquitin-proteasome system |
| US20160209414A1 (en) | 2014-11-07 | 2016-07-21 | University Of Washington Through Its Center For Commercialization | Compositions and methods for the diagnosis and treatment of breast cancer |
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