FKBP1A

FKBP1A
사용 가능한 구조
PDB	Ortholog 검색: PDBe RCSB
PDB ID 코드 목록
	1A7X, 1B6C, 1BKF, 1BL4, 1D6O, 1D7H, 1D7I, 1D7J, 1EYM, 1F40, 1FAP, 1FKB, 1FKHD, 1FKHF, 1KHF, 1KHF, 1KF, 1KF, 1KF, 1KF, 1KF
식별자
에일리어스	FKBP1A, FKBP-12, FKBP-1A, FKBP1, FKBP12, PKC12, PKCI2, PPIase, FK506 결합단백질1A, FKBP프롤릴화효소1A
외부 ID	OMIM : 186945 MGI : 95541 HomoloGene : 105139 GenCard : FKBP1A
유전자 위치(인간)
크르.	20번 염색체(인간)
끝.	1,393,128 bp
유전자 위치(마우스)
크르.	2번 염색체(마우스)
끝.	151,403,612 bp
RNA발현패턴
	상단 표시 위치:
	오른쪽 폐; ; 단구; ; 좌폐 상엽; ; 갑상선 우엽; ; 갑상선 좌엽; ; 핵액컴벤스; ; 직장; ; 좌측 자궁관; ; 평활근 조직; ; 자궁내막간질세포;
	추가 참조 표현식 데이터
	; ; ; ;
	추가 참조 표현식 데이터
유전자 존재론
분자 함수	칼슘채널억제활성; 액티빈 결합; 이성질화효소활성; 마크로라이드 결합; 펩티딜프로릴시스트랜스 이성질화효소; 신호 변환기 활성; GO:0001948 단백질 결합; SMAD 바인딩; 형질전환성장인자β수용체결합; FK506 바인딩; 효소결합; Hsp70 단백질 결합; I형변환성장인자β수용체결합; 단백질 호모다이머화; 막전송체결합;
셀룰러 컴포넌트	세포질; 종말 시스테나; Z디스크; 세포외 엑소좀; 유기막 외인성 성분; 막세포질측; 리아노딘수용체복합체; 세포; 막; 석소체망; 석소체망막; 세포막내소기관; 축삭 종단;
생물학적 과정	SMAD단백질복합체조립체; 아밀로이드 섬유 형성; 액티빈수용체신호경로조절; 단백질 접힘에 의한 단백질 성숙; 아밀로이드 전구체 단백질 이화 과정 조절; 단백질펩티딜프로릴이성체화; 리아노딘 감수성 칼슘 방출 채널 활성 음성 조절; 단백질 국재 조절; 칼슘 이온 막 통과 수송; 단백질 리폴딩; 면역 반응 조절; I-kappaB인산화효소/NF-kappaB신호의 양성조절; 세포에 격리된 칼슘 이온 방출의 음성 조절; 단백질 결합의 양성 조절; 단백질 유비퀴티네이션의 양성 조절; 'de novo' 단백질 접힘; 형질전환성장인자β수용체신호경로; T세포활성화; 샤페론결합단백질접힘; 초분자 섬유 조직; 인단백인산가수분해효소활성음성조절; 단백질 접힘; 단백질인산화부정조절; 심장 형태 형성; 근육 수축; 철이온에 대한 반응; 사이토카인결합신호경로; 카페인에 대한 반응; T세포증식; 세포에 격리된 칼슘 이온 방출; 심실심근조직형태형성; 리아노딘 감수성 칼슘 방출 채널 활성 조절; 심장 사시 형성;
	출처:아미고 / QuickGO
맞춤법
	2280
	14225
	ENSG00008832
	ENSMUSG000032966
	P62942
	P26883
	NM_054014; NM_000801; NM_001199786
NM_001302077; NM_001302078; NM_001302079; NM_001302080; NM_008019;
	NM_001355077; NM_001355078
	NP_000792; NP_001186715; NP_463460
NP_001289006; NP_001289007; NP_001289008; NP_001289009; NP_032045;
	NP_001342006; NP_001342007
	위키데이터
인간 보기/편집	마우스 표시/편집

펩티딜-프롤릴시스-트랜스 이성질화효소 FKBP1A는 FKBP1A ^[5]유전자에 의해 인체 내에서 부호화되는 효소이다.

기능.

이 유전자에 의해 코드된 단백질은 면역 조절과 단백질 접힘과 밀매를 수반하는 기본적인 세포 과정에 역할을 하는 면역필린 단백질 패밀리의 구성원이다.이 암호화된 단백질은 면역억제제 FK506(타크로리머스)과 라파마이신(시롤리머스)을 결합하는 시스-트랜스 프로릴 이성질체이다.Type I TGF-β 수용체를 포함한 여러 세포 내 신호 전달 단백질과 상호작용합니다.또한 사분자 골격근 리아노딘 수용체를 포함한 여러 세포 내 칼슘 방출 채널과 상호작용합니다.생쥐에서, 이 상동 유전자의 결실은 좌심실 심근의 비압축으로 알려진 선천성 심장 장애를 일으킨다.이 유전자에 대해 여러 개의 대체 결합 전사 변형이 있다는 증거가 있지만, 일부 변종의 전체 길이 특성은 ^[6]결정되지 않았다.

상호 작용

FKBP1A는 다음과 상호작용하는 것으로 나타났습니다.

GLMN,^[7]^[8]
ITPR1^[9]^[10]
KIAA1303,^[11]^[12]
포유류의 라파마이신 ^[11]^[12]^[13]^[14]^[15]^[16]표적은
RYR1,^[17]^[18]^[19] 및
TGF 베타 수용체 ^[20]^[21]1

레퍼런스

^ ^a ^b ^c GRCh38: 앙상블 릴리즈 89: ENSG00008832 - 앙상블, 2017년 5월
^ ^a ^b ^c GRCm38: 앙상블 릴리즈 89: ENSMUSG000032966 - 앙상블, 2017년 5월
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ DiLella AG (Sep 1991). "Chromosomal assignment of the human immunophilin FKBP-12 gene". Biochemical and Biophysical Research Communications. 179 (3): 1427–33. doi:10.1016/0006-291X(91)91732-R. PMID 1930186.
^ "Entrez Gene: FKBP1A FK506 binding protein 1A, 12kDa".
^ Chambraud B, Radanyi C, Camonis JH, Shazand K, Rajkowski K, Baulieu EE (Dec 1996). "FAP48, a new protein that forms specific complexes with both immunophilins FKBP59 and FKBP12. Prevention by the immunosuppressant drugs FK506 and rapamycin". The Journal of Biological Chemistry. 271 (51): 32923–9. doi:10.1074/jbc.271.51.32923. PMID 8955134.
^ Neye H (Mar 2001). "Mutation of FKBP associated protein 48 (FAP48) at proline 219 disrupts the interaction with FKBP12 and FKBP52". Regulatory Peptides. 97 (2–3): 147–52. doi:10.1016/s0167-0115(00)00206-8. PMID 11164950. S2CID 20617551.
^ MacMillan D, Currie S, Bradley KN, Muir TC, McCarron JG (Dec 2005). "In smooth muscle, FK506-binding protein modulates IP3 receptor-evoked Ca2+ release by mTOR and calcineurin". Journal of Cell Science. 118 (Pt 23): 5443–51. doi:10.1242/jcs.02657. PMID 16278292.
^ Cameron AM, Nucifora FC, Fung ET, Livingston DJ, Aldape RA, Ross CA, Snyder SH (Oct 1997). "FKBP12 binds the inositol 1,4,5-trisphosphate receptor at leucine-proline (1400-1401) and anchors calcineurin to this FK506-like domain". The Journal of Biological Chemistry. 272 (44): 27582–8. doi:10.1074/jbc.272.44.27582. PMID 9346894.
^ ^a ^b Jacinto E, Loewith R, Schmidt A, Lin S, Rüegg MA, Hall A, Hall MN (Nov 2004). "Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive". Nature Cell Biology. 6 (11): 1122–8. doi:10.1038/ncb1183. PMID 15467718. S2CID 13831153.
^ ^a ^b Sarbassov DD, Ali SM, Kim DH, Guertin DA, Latek RR, Erdjument-Bromage H, Tempst P, Sabatini DM (Jul 2004). "Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton". Current Biology. 14 (14): 1296–302. doi:10.1016/j.cub.2004.06.054. PMID 15268862. S2CID 4658268.
^ Choi J, Chen J, Schreiber SL, Clardy J (Jul 1996). "Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP". Science. 273 (5272): 239–42. Bibcode:1996Sci...273..239C. doi:10.1126/science.273.5272.239. PMID 8662507. S2CID 27706675.
^ Luker KE, Smith MC, Luker GD, Gammon ST, Piwnica-Worms H, Piwnica-Worms D (Aug 2004). "Kinetics of regulated protein-protein interactions revealed with firefly luciferase complementation imaging in cells and living animals". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12288–93. Bibcode:2004PNAS..10112288L. doi:10.1073/pnas.0404041101. PMC 514471. PMID 15284440.
^ Banaszynski LA, Liu CW, Wandless TJ (Apr 2005). "Characterization of the FKBP.rapamycin.FRB ternary complex". Journal of the American Chemical Society. 127 (13): 4715–21. doi:10.1021/ja043277y. PMID 15796538.
^ Sabers CJ, Martin MM, Brunn GJ, Williams JM, Dumont FJ, Wiederrecht G, Abraham RT (Jan 1995). "Isolation of a protein target of the FKBP12-rapamycin complex in mammalian cells". The Journal of Biological Chemistry. 270 (2): 815–22. doi:10.1074/jbc.270.2.815. PMID 7822316.
^ Avila G, Lee EH, Perez CF, Allen PD, Dirksen RT (Jun 2003). "FKBP12 binding to RyR1 modulates excitation-contraction coupling in mouse skeletal myotubes". The Journal of Biological Chemistry. 278 (25): 22600–8. doi:10.1074/jbc.M205866200. PMID 12704193.
^ Bultynck G, De Smet P, Rossi D, Callewaert G, Missiaen L, Sorrentino V, De Smedt H, Parys JB (Mar 2001). "Characterization and mapping of the 12 kDa FK506-binding protein (FKBP12)-binding site on different isoforms of the ryanodine receptor and of the inositol 1,4,5-trisphosphate receptor". The Biochemical Journal. 354 (Pt 2): 413–22. doi:10.1042/bj3540413. PMC 1221670. PMID 11171121.
^ Gaburjakova M, Gaburjakova J, Reiken S, Huang F, Marx SO, Rosemblit N, Marks AR (May 2001). "FKBP12 binding modulates ryanodine receptor channel gating". The Journal of Biological Chemistry. 276 (20): 16931–5. doi:10.1074/jbc.M100856200. PMID 11279144.
^ Wang T, Donahoe PK, Zervos AS (Jul 1994). "Specific interaction of type I receptors of the TGF-beta family with the immunophilin FKBP-12". Science. 265 (5172): 674–6. Bibcode:1994Sci...265..674W. doi:10.1126/science.7518616. PMID 7518616.
^ Liu F, Ventura F, Doody J, Massagué J (Jul 1995). "Human type II receptor for bone morphogenic proteins (BMPs): extension of the two-kinase receptor model to the BMPs". Molecular and Cellular Biology. 15 (7): 3479–86. doi:10.1128/mcb.15.7.3479. PMC 230584. PMID 7791754.

추가 정보

Schiene-Fischer C, Yu C (Apr 2001). "Receptor accessory folding helper enzymes: the functional role of peptidyl prolyl cis/trans isomerases". FEBS Letters. 495 (1–2): 1–6. doi:10.1016/S0014-5793(01)02326-2. PMID 11322937. S2CID 42263861.
DiLella AG, Hawkins A, Craig RJ, Schreiber SL, Griffin CA (Dec 1992). "Chromosomal band assignments of the genes encoding human FKBP12 and FKBP13". Biochemical and Biophysical Research Communications. 189 (2): 819–23. doi:10.1016/0006-291X(92)92276-4. PMID 1281998.
Jayaraman T, Brillantes AM, Timerman AP, Fleischer S, Erdjument-Bromage H, Tempst P, Marks AR (May 1992). "FK506 binding protein associated with the calcium release channel (ryanodine receptor)". The Journal of Biological Chemistry. 267 (14): 9474–7. doi:10.1016/S0021-9258(19)50114-4. PMID 1374404.
Lepre CA, Thomson JA, Moore JM (May 1992). "Solution structure of FK506 bound to FKBP-12". FEBS Letters. 302 (1): 89–96. doi:10.1016/0014-5793(92)80292-O. PMID 1375171. S2CID 41469360.
Maki N, Sekiguchi F, Nishimaki J, Miwa K, Hayano T, Takahashi N, Suzuki M (Jul 1990). "Complementary DNA encoding the human T-cell FK506-binding protein, a peptidylprolyl cis-trans isomerase distinct from cyclophilin". Proceedings of the National Academy of Sciences of the United States of America. 87 (14): 5440–3. Bibcode:1990PNAS...87.5440M. doi:10.1073/pnas.87.14.5440. PMC 54340. PMID 1695378.
Standaert RF, Galat A, Verdine GL, Schreiber SL (Aug 1990). "Molecular cloning and overexpression of the human FK506-binding protein FKBP". Nature. 346 (6285): 671–4. Bibcode:1990Natur.346..671S. doi:10.1038/346671a0. PMID 1696686. S2CID 4368221.
Siekierka JJ, Wiederrecht G, Greulich H, Boulton D, Hung SH, Cryan J, Hodges PJ, Sigal NH (Dec 1990). "The cytosolic-binding protein for the immunosuppressant FK-506 is both a ubiquitous and highly conserved peptidyl-prolyl cis-trans isomerase". The Journal of Biological Chemistry. 265 (34): 21011–5. doi:10.1016/S0021-9258(17)45319-1. PMID 1701173.
Michnick SW, Rosen MK, Wandless TJ, Karplus M, Schreiber SL (May 1991). "Solution structure of FKBP, a rotamase enzyme and receptor for FK506 and rapamycin". Science. 252 (5007): 836–9. Bibcode:1991Sci...252..836M. doi:10.1126/science.1709301. PMID 1709301. S2CID 28289138.
Van Duyne GD, Standaert RF, Karplus PA, Schreiber SL, Clardy J (May 1991). "Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant complex". Science. 252 (5007): 839–42. Bibcode:1991Sci...252..839V. doi:10.1126/science.1709302. PMID 1709302. S2CID 32539611.
Rosen MK, Michnick SW, Karplus M, Schreiber SL (May 1991). "Proton and nitrogen sequential assignments and secondary structure determination of the human FK506 and rapamycin binding protein". Biochemistry. 30 (19): 4774–89. CiteSeerX 10.1.1.559.2890. doi:10.1021/bi00233a020. PMID 1709363.
Jin YJ, Albers MW, Lane WS, Bierer BE, Schreiber SL, Burakoff SJ (Aug 1991). "Molecular cloning of a membrane-associated human FK506- and rapamycin-binding protein, FKBP-13". Proceedings of the National Academy of Sciences of the United States of America. 88 (15): 6677–81. Bibcode:1991PNAS...88.6677J. doi:10.1073/pnas.88.15.6677. PMC 52151. PMID 1713687.
DiLella AG, Craig RJ (Sep 1991). "Exon organization of the human FKBP-12 gene: correlation with structural and functional protein domains". Biochemistry. 30 (35): 8512–7. doi:10.1021/bi00099a002. PMID 1716149.
Harding MW, Galat A, Uehling DE, Schreiber SL (Oct 1989). "A receptor for the immunosuppressant FK506 is a cis-trans peptidyl-prolyl isomerase". Nature. 341 (6244): 758–60. Bibcode:1989Natur.341..758H. doi:10.1038/341758a0. PMID 2477715. S2CID 4349152.
Wang T, Donahoe PK, Zervos AS (Jul 1994). "Specific interaction of type I receptors of the TGF-beta family with the immunophilin FKBP-12". Science. 265 (5172): 674–6. Bibcode:1994Sci...265..674W. doi:10.1126/science.7518616. PMID 7518616.
Peattie DA, Hsiao K, Benasutti M, Lippke JA (Dec 1994). "Three distinct messenger RNAs can encode the human immunosuppressant-binding protein FKBP12". Gene. 150 (2): 251–7. doi:10.1016/0378-1119(94)90434-0. PMID 7529739.
Yang WM, Inouye CJ, Seto E (Jun 1995). "Cyclophilin A and FKBP12 interact with YY1 and alter its transcriptional activity". The Journal of Biological Chemistry. 270 (25): 15187–93. doi:10.1074/jbc.270.25.15187. PMID 7541038.
Kawamura A, Su MS (Jun 1995). "Interaction of FKBP12-FK506 with calcineurin A at the B subunit-binding domain". The Journal of Biological Chemistry. 270 (26): 15463–6. doi:10.1074/jbc.270.26.15463. PMID 7541044.
Griffith JP, Kim JL, Kim EE, Sintchak MD, Thomson JA, Fitzgibbon MJ, Fleming MA, Caron PR, Hsiao K, Navia MA (Aug 1995). "X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex". Cell. 82 (3): 507–22. doi:10.1016/0092-8674(95)90439-5. PMID 7543369. S2CID 15502270.
Van Duyne GD, Standaert RF, Karplus PA, Schreiber SL, Clardy J (Jan 1993). "Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin". Journal of Molecular Biology. 229 (1): 105–24. doi:10.1006/jmbi.1993.1012. PMID 7678431.

[refGRCh38Ensembl-1] GRCh38: 앙상블 릴리즈 89: ENSG00008832 - 앙상블, 2017년 5월

[refGRCm38Ensembl-2] GRCm38: 앙상블 릴리즈 89: ENSMUSG000032966 - 앙상블, 2017년 5월

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid1930186-5] DiLella AG (Sep 1991). "Chromosomal assignment of the human immunophilin FKBP-12 gene". Biochemical and Biophysical Research Communications. 179 (3): 1427–33. doi:10.1016/0006-291X(91)91732-R. PMID 1930186.

[6] "Entrez Gene: FKBP1A FK506 binding protein 1A, 12kDa".

[pmid8955134-7] Chambraud B, Radanyi C, Camonis JH, Shazand K, Rajkowski K, Baulieu EE (Dec 1996). "FAP48, a new protein that forms specific complexes with both immunophilins FKBP59 and FKBP12. Prevention by the immunosuppressant drugs FK506 and rapamycin". The Journal of Biological Chemistry. 271 (51): 32923–9. doi:10.1074/jbc.271.51.32923. PMID 8955134.

[pmid11164950-8] Neye H (Mar 2001). "Mutation of FKBP associated protein 48 (FAP48) at proline 219 disrupts the interaction with FKBP12 and FKBP52". Regulatory Peptides. 97 (2–3): 147–52. doi:10.1016/s0167-0115(00)00206-8. PMID 11164950. S2CID 20617551.

[pmid16278292-9] MacMillan D, Currie S, Bradley KN, Muir TC, McCarron JG (Dec 2005). "In smooth muscle, FK506-binding protein modulates IP3 receptor-evoked Ca2+ release by mTOR and calcineurin". Journal of Cell Science. 118 (Pt 23): 5443–51. doi:10.1242/jcs.02657. PMID 16278292.

[pmid9346894-10] Cameron AM, Nucifora FC, Fung ET, Livingston DJ, Aldape RA, Ross CA, Snyder SH (Oct 1997). "FKBP12 binds the inositol 1,4,5-trisphosphate receptor at leucine-proline (1400-1401) and anchors calcineurin to this FK506-like domain". The Journal of Biological Chemistry. 272 (44): 27582–8. doi:10.1074/jbc.272.44.27582. PMID 9346894.

[pmid15467718-11] Jacinto E, Loewith R, Schmidt A, Lin S, Rüegg MA, Hall A, Hall MN (Nov 2004). "Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive". Nature Cell Biology. 6 (11): 1122–8. doi:10.1038/ncb1183. PMID 15467718. S2CID 13831153.

[pmid15268862-12] Sarbassov DD, Ali SM, Kim DH, Guertin DA, Latek RR, Erdjument-Bromage H, Tempst P, Sabatini DM (Jul 2004). "Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton". Current Biology. 14 (14): 1296–302. doi:10.1016/j.cub.2004.06.054. PMID 15268862. S2CID 4658268.

[pmid8662507-13] Choi J, Chen J, Schreiber SL, Clardy J (Jul 1996). "Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP". Science. 273 (5272): 239–42. Bibcode:1996Sci...273..239C. doi:10.1126/science.273.5272.239. PMID 8662507. S2CID 27706675.

[pmid15284440-14] Luker KE, Smith MC, Luker GD, Gammon ST, Piwnica-Worms H, Piwnica-Worms D (Aug 2004). "Kinetics of regulated protein-protein interactions revealed with firefly luciferase complementation imaging in cells and living animals". Proceedings of the National Academy of Sciences of the United States of America. 101 (33): 12288–93. Bibcode:2004PNAS..10112288L. doi:10.1073/pnas.0404041101. PMC 514471. PMID 15284440.

[pmid15796538-15] Banaszynski LA, Liu CW, Wandless TJ (Apr 2005). "Characterization of the FKBP.rapamycin.FRB ternary complex". Journal of the American Chemical Society. 127 (13): 4715–21. doi:10.1021/ja043277y. PMID 15796538.

[pmid7822316-16] Sabers CJ, Martin MM, Brunn GJ, Williams JM, Dumont FJ, Wiederrecht G, Abraham RT (Jan 1995). "Isolation of a protein target of the FKBP12-rapamycin complex in mammalian cells". The Journal of Biological Chemistry. 270 (2): 815–22. doi:10.1074/jbc.270.2.815. PMID 7822316.

[pmid12704193-17] Avila G, Lee EH, Perez CF, Allen PD, Dirksen RT (Jun 2003). "FKBP12 binding to RyR1 modulates excitation-contraction coupling in mouse skeletal myotubes". The Journal of Biological Chemistry. 278 (25): 22600–8. doi:10.1074/jbc.M205866200. PMID 12704193.

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v t 효소
활동	활성 사이트 바인딩 사이트 촉매 삼합체 옥시 음이온 홀 효소 문란성 확산제한효소 코엔자임 보조인자 효소 촉매 작용
규정	알로스테릭 조절 협동성 효소억제제 효소활성화제
분류	EC 번호 효소 슈퍼 패밀리 효소족 효소 목록
동력학	효소역학 Eadie-Hofstee 다이어그램 하네스-울프 그림 Lineweaver-Burk 그림 미카엘리스 멘텐 동역학
종류들	EC1 산화환원효소(목록) EC2 전송효소(리스트) EC3 가수분해효소 (리스트) EC4 리아제 (리스트) EC5 이성질화효소 (리스트) EC6 연결효소(리스트) EC7 트랜스로케이스 (리스트)

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