| General information | | DisProt: | DP00238 | | Name: | Breast cancer type 1 susceptibility protein | | Synonym(s): | BRCA1_HUMAN
RING finger protein 53
BRCA1
| | First appeared in release: | Release 2.2 (04/14/2005) | | UniProt: | P38398 | | UniGene: | Hs.194143 | | SwissProt: | BRCA1_HUMAN | | TrEMBL: | | | NCBI (GI): | 728984 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 1863 | | Percent disordered: | 81% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MDLSALRVEE VQNVINAMQK ILECPICLEL IKEPVSTKCD HIFCKFCMLK LLNQKKGPSQ - 60
CPLCKNDITK RSLQESTRFS QLVEELLKII CAFQLDTGLE YANSYNFAKK ENNSPEHLKD - 120
EVSIIQSMGY RNRAKRLLQS EPENPSLQET SLSVQLSNLG TVRTLRTKQR IQPQKTSVYI - 180
ELGSDSSEDT VNKATYCSVG DQELLQITPQ GTRDEISLDS AKKAACEFSE TDVTNTEHHQ - 240
PSNNDLNTTE KRAAERHPEK YQGSSVSNLH VEPCGTNTHA SSLQHENSSL LLTKDRMNVE - 300
KAEFCNKSKQ PGLARSQHNR WAGSKETCND RRTPSTEKKV DLNADPLCER KEWNKQKLPC - 360
SENPRDTEDV PWITLNSSIQ KVNEWFSRSD ELLGSDDSHD GESESNAKVA DVLDVLNEVD - 420
EYSGSSEKID LLASDPHEAL ICKSERVHSK SVESNIEDKI FGKTYRKKAS LPNLSHVTEN - 480
LIIGAFVTEP QIIQERPLTN KLKRKRRPTS GLHPEDFIKK ADLAVQKTPE MINQGTNQTE - 540
QNGQVMNITN SGHENKTKGD SIQNEKNPNP IESLEKESAF KTKAEPISSS ISNMELELNI - 600
HNSKAPKKNR LRRKSSTRHI HALELVVSRN LSPPNCTELQ IDSCSSSEEI KKKKYNQMPV - 660
RHSRNLQLME GKEPATGAKK SNKPNEQTSK RHDSDTFPEL KLTNAPGSFT KCSNTSELKE - 720
FVNPSLPREE KEEKLETVKV SNNAEDPKDL MLSGERVLQT ERSVESSSIS LVPGTDYGTQ - 780
ESISLLEVST LGKAKTEPNK CVSQCAAFEN PKGLIHGCSK DNRNDTEGFK YPLGHEVNHS - 840
RETSIEMEES ELDAQYLQNT FKVSKRQSFA PFSNPGNAEE ECATFSAHSG SLKKQSPKVT - 900
FECEQKEENQ GKNESNIKPV QTVNITAGFP VVGQKDKPVD NAKCSIKGGS RFCLSSQFRG - 960
NETGLITPNK HGLLQNPYRI PPLFPIKSFV KTKCKKNLLE ENFEEHSMSP EREMGNENIP - 1020
STVSTISRNN IRENVFKEAS SSNINEVGSS TNEVGSSINE IGSSDENIQA ELGRNRGPKL - 1080
NAMLRLGVLQ PEVYKQSLPG SNCKHPEIKK QEYEEVVQTV NTDFSPYLIS DNLEQPMGSS - 1140
HASQVCSETP DDLLDDGEIK EDTSFAENDI KESSAVFSKS VQKGELSRSP SPFTHTHLAQ - 1200
GYRRGAKKLE SSEENLSSED EELPCFQHLL FGKVNNIPSQ STRHSTVATE CLSKNTEENL - 1260
LSLKNSLNDC SNQVILAKAS QEHHLSEETK CSASLFSSQC SELEDLTANT NTQDPFLIGS - 1320
SKQMRHQSES QGVGLSDKEL VSDDEERGTG LEENNQEEQS MDSNLGEAAS GCESETSVSE - 1380
DCSGLSSQSD ILTTQQRDTM QHNLIKLQQE MAELEAVLEQ HGSQPSNSYP SIISDSSALE - 1440
DLRNPEQSTS EKAVLTSQKS SEYPISQNPE GLSADKFEVS ADSSTSKNKE PGVERSSPSK - 1500
CPSLDDRWYM HSCSGSLQNR NYPSQEELIK VVDVEEQQLE ESGPHDLTET SYLPRQDLEG - 1560
TPYLESGISL FSDDPESDPS EDRAPESARV GNIPSSTSAL KVPQLKVAES AQSPAAAHTT - 1620
DTAGYNAMEE SVSREKPELT ASTERVNKRM SMVVSGLTPE EFMLVYKFAR KHHITLTNLI - 1680
TEETTHVVMK TDAEFVCERT LKYFLGIAGG KWVVSYFWVT QSIKERKMLN EHDFEVRGDV - 1740
VNGRNHQGPK RARESQDRKI FRGLEICCYG PFTNMPTDQL EWMVQLCGAS VVKELSSFTL - 1800
GTGVHPIVVV QPDAWTEDNG FHAIGQMCEA PVVTREWVLD SVALYQCQEL DTYLIPQIPH - 1860
SHY
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| Functional narrative |
The BRCA1 tumor suppressor gene is implicated in many cellular pathways including transcription, cell-cycle, checkpoint control, apoptosis and DNA repair. The central disordered region may act as a scaffold for intermolecular interactions crucial for DNA damage reponse.
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| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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| Region 1 | | Type: | Disordered | | Name: | | | Location: | 170 - 1649 | | Length: | 1480 | | Region sequence: |
RIQPQKTSVYIELGSDSSEDTVNKATYCSVGDQELLQITPQGTRDEISLDSAKKAACEFS
ETDVTNTEHHQPSNNDLNTTEKRAAERHPEKYQGSSVSNLHVEPCGTNTHASSLQHENSS
LLLTKDRMNVEKAEFCNKSKQPGLARSQHNRWAGSKETCNDRRTPSTEKKVDLNADPLCE
RKEWNKQKLPCSENPRDTEDVPWITLNSSIQKVNEWFSRSDELLGSDDSHDGESESNAKV
ADVLDVLNEVDEYSGSSEKIDLLASDPHEALICKSERVHSKSVESNIEDKIFGKTYRKKA
SLPNLSHVTENLIIGAFVTEPQIIQERPLTNKLKRKRRPTSGLHPEDFIKKADLAVQKTP
EMINQGTNQTEQNGQVMNITNSGHENKTKGDSIQNEKNPNPIESLEKESAFKTKAEPISS
SISNMELELNIHNSKAPKKNRLRRKSSTRHIHALELVVSRNLSPPNCTELQIDSCSSSEE
IKKKKYNQMPVRHSRNLQLMEGKEPATGAKKSNKPNEQTSKRHDSDTFPELKLTNAPGSF
TKCSNTSELKEFVNPSLPREEKEEKLETVKVSNNAEDPKDLMLSGERVLQTERSVESSSI
SLVPGTDYGTQESISLLEVSTLGKAKTEPNKCVSQCAAFENPKGLIHGCSKDNRNDTEGF
KYPLGHEVNHSRETSIEMEESELDAQYLQNTFKVSKRQSFAPFSNPGNAEEECATFSAHS
GSLKKQSPKVTFECEQKEENQGKNESNIKPVQTVNITAGFPVVGQKDKPVDNAKCSIKGG
SRFCLSSQFRGNETGLITPNKHGLLQNPYRIPPLFPIKSFVKTKCKKNLLEENFEEHSMS
PEREMGNENIPSTVSTISRNNIRENVFKEASSSNINEVGSSTNEVGSSINEIGSSDENIQ
AELGRNRGPKLNAMLRLGVLQPEVYKQSLPGSNCKHPEIKKQEYEEVVQTVNTDFSPYLI
SDNLEQPMGSSHASQVCSETPDDLLDDGEIKEDTSFAENDIKESSAVFSKSVQKGELSRS
PSPFTHTHLAQGYRRGAKKLESSEENLSSEDEELPCFQHLLFGKVNNIPSQSTRHSTVAT
ECLSKNTEENLLSLKNSLNDCSNQVILAKASQEHHLSEETKCSASLFSSQCSELEDLTAN
TNTQDPFLIGSSKQMRHQSESQGVGLSDKELVSDDEERGTGLEENNQEEQSMDSNLGEAA
SGCESETSVSEDCSGLSSQSDILTTQQRDTMQHNLIKLQQEMAELEAVLEQHGSQPSNSY
PSIISDSSALEDLRNPEQSTSEKAVLTSQKSSEYPISQNPEGLSADKFEVSADSSTSKNK
EPGVERSSPSKCPSLDDRWYMHSCSGSLQNRNYPSQEELIKVVDVEEQQLEESGPHDLTE
TSYLPRQDLEGTPYLESGISLFSDDPESDPSEDRAPESARVGNIPSSTSALKVPQLKVAE
SAQSPAAAHTTDTAGYNAMEESVSREKPELTASTERVNKR | | Modification type: | Fragment
Native
| | PDB: | | | Structural/functional type: | Relationship to function unknown
| | Functional classes: | Molecular recognition effectors
| | Functional subclasses: | Protein-protein binding
| Detection methods:
- Circular dichroism (CD) spectroscopy, far-UV
- Nuclear magnetic resonance (NMR)
| References:
- Mark WY, Liao JC, Lu Y, Ayed A, Laister R, Szymczyna B, Chakrabartty A, Arrowsmith CH. "Characterization of segments from the central region of BRCA1: an intrinsically disordered scaffold for multiple protein-protein and protein-DNA interactions?" J Mol Biol. 2005; 345(2): 275-87. PubMed: 15571721
| Comments:The structure of the 1480 residue central region was investigated by characterizing 21 different fragments.
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| Region 2 | | Type: | Disordered | | Name: | | | Location: | 1755 - 1758 | | Length: | 4 | | Region sequence: |
SQDR | | Modification type: | | | PDB: | | | Structural/functional type: | | | Functional classes: | | | Functional subclasses: | | Detection methods:
- Nuclear magnetic resonance (NMR) (296 K; pH: 6.8; DTT 10 mM; K2HPO4 10 mM; KCl 5 mM; KH2PO4 10 mM)
| References:
- Gaiser OJ, Ball LJ, Schmieder P, Leitner D, Strauss H, Wahl M, Kuhne R, Oschkinat H, Heinemann U. "Solution structure, backbone dynamics, and association behavior of the C-terminal BRCT domain from the breast cancer-associated protein BRCA1." Biochemistry. 2004; 43(51): 15983-95. PubMed: 15609993
| Comments:
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| Region 3 | | Type: | Disordered | | Name: | | | Location: | 1773 - 1777 | | Length: | 5 | | Region sequence: |
TNMPT | | Modification type: | | | PDB: | | | Structural/functional type: | | | Functional classes: | | | Functional subclasses: | | Detection methods:
- Nuclear magnetic resonance (NMR) (296 K; pH: 6.8; DTT 10 mM; K2HPO4 10 mM; KCl 5 mM; KH2PO4 10 mM)
| References:
- Gaiser OJ, Ball LJ, Schmieder P, Leitner D, Strauss H, Wahl M, Kuhne R, Oschkinat H, Heinemann U. "Solution structure, backbone dynamics, and association behavior of the C-terminal BRCT domain from the breast cancer-associated protein BRCA1." Biochemistry. 2004; 43(51): 15983-95. PubMed: 15609993
| Comments:
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| Region 4 | | Type: | Disordered | | Name: | | | Location: | 1799 - 1804 | | Length: | 6 | | Region sequence: |
TLGTGV | | Modification type: | | | PDB: | | | Structural/functional type: | | | Functional classes: | | | Functional subclasses: | | Detection methods:
- Nuclear magnetic resonance (NMR) (296 K; pH: 6.8; DTT 10 mM; K2HPO4 10 mM; KCl 5 mM; KH2PO4 10 mM)
| References:
- Gaiser OJ, Ball LJ, Schmieder P, Leitner D, Strauss H, Wahl M, Kuhne R, Oschkinat H, Heinemann U. "Solution structure, backbone dynamics, and association behavior of the C-terminal BRCT domain from the breast cancer-associated protein BRCA1." Biochemistry. 2004; 43(51): 15983-95. PubMed: 15609993
| Comments:
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| Region 5 | | Type: | Disordered | | Name: | | | Location: | 1812 - 1823 | | Length: | 12 | | Region sequence: |
PDAWTEDNGFHA | | Modification type: | | | PDB: | | | Structural/functional type: | | | Functional classes: | | | Functional subclasses: | | Detection methods:
- Nuclear magnetic resonance (NMR) (296 K; pH: 6.8; DTT 10 mM; K2HPO4 10 mM; KCl 5 mM; KH2PO4 10 mM)
| References:
- Gaiser OJ, Ball LJ, Schmieder P, Leitner D, Strauss H, Wahl M, Kuhne R, Oschkinat H, Heinemann U. "Solution structure, backbone dynamics, and association behavior of the C-terminal BRCT domain from the breast cancer-associated protein BRCA1." Biochemistry. 2004; 43(51): 15983-95. PubMed: 15609993
| Comments:
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| If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us. |
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