UniProtKB - Q864U1 (BRCA1_BOVIN)
Breast cancer type 1 susceptibility protein homolog
BRCA1
Functioni
Catalytic activityi
- S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.By similarity EC:2.3.2.27
: protein ubiquitination Pathwayi
This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 24 – 65 | RING-typePROSITE-ProRule annotationAdd BLAST | 42 |
GO - Molecular functioni
- DNA binding Source: UniProtKB-KW
- RNA polymerase binding Source: UniProtKB
- transcription coactivator activity Source: UniProtKB
- ubiquitin-protein transferase activity Source: UniProtKB
- zinc ion binding Source: InterPro
GO - Biological processi
- cell cycle Source: UniProtKB-KW
- DNA recombination Source: UniProtKB-KW
- DNA repair Source: UniProtKB-KW
- fatty acid biosynthetic process Source: UniProtKB-KW
- negative regulation of fatty acid biosynthetic process Source: UniProtKB
- positive regulation of transcription, DNA-templated Source: UniProtKB
- protein autoubiquitination Source: UniProtKB
- protein K6-linked ubiquitination Source: UniProtKB
- regulation of transcription by RNA polymerase II Source: UniProtKB
Keywordsi
Molecular function | Activator, DNA-binding, Transferase |
Biological process | Cell cycle, DNA damage, DNA recombination, DNA repair, Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Transcription, Transcription regulation, Ubl conjugation pathway |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
UniPathwayi | UPA00143 |
Names & Taxonomyi
Protein namesi | Recommended name: Breast cancer type 1 susceptibility protein homolog (EC:2.3.2.27By similarity)Alternative name(s): RING-type E3 ubiquitin transferase BRCA1Curated |
Gene namesi | Name:BRCA1 |
Organismi | Bos taurus (Bovine) |
Taxonomic identifieri | 9913 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Proteomesi |
|
Subcellular locationi
Cytoplasm and Cytosol
- Cytoplasm By similarity
Nucleus
- Nucleus By similarity
Other locations
- Chromosome By similarity
Note: Localizes at sites of DNA damage at double-strand breaks (DSBs); recruitment to DNA damage sites is mediated by the BRCA1-A complex. Translocated to the cytoplasm during UV-induced apoptosis.By similarity
Nucleus
- BRCA1-BARD1 complex Source: UniProtKB
- nucleus Source: UniProtKB
Other locations
- chromosome Source: UniProtKB
- cytoplasm Source: UniProtKB
Keywords - Cellular componenti
Chromosome, Cytoplasm, NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000055827 | 1 – 1849 | Breast cancer type 1 susceptibility protein homologAdd BLAST | 1849 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1 | N-acetylmethionineBy similarity | 1 | |
Modified residuei | 114 | PhosphoserineBy similarity | 1 | |
Cross-linki | 301 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Cross-linki | 339 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 395 | PhosphoserineBy similarity | 1 | |
Modified residuei | 398 | PhosphoserineBy similarity | 1 | |
Modified residuei | 423 | PhosphoserineBy similarity | 1 | |
Modified residuei | 434 | PhosphoserineBy similarity | 1 | |
Cross-linki | 457 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Cross-linki | 517 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 691 | PhosphoserineBy similarity | 1 | |
Modified residuei | 711 | PhosphoserineBy similarity | 1 | |
Modified residuei | 720 | PhosphoserineBy similarity | 1 | |
Cross-linki | 981 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 982 | Phosphoserine; by CHEK2By similarity | 1 | |
Modified residuei | 1002 | PhosphoserineBy similarity | 1 | |
Cross-linki | 1073 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity | ||
Modified residuei | 1138 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1184 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1211 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1212 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1274 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1323 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1330 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1336 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1382 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1389 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 1418 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1452 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1518 | PhosphoserineBy similarity | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
PaxDbi | Q864U1 |
PRIDEi | Q864U1 |
Interactioni
Subunit structurei
Heterodimer with BARD1. Part of the BRCA1-associated genome surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the MRE11-RAD50-NBN protein (MRN) complex. This association could be a dynamic process changing throughout the cell cycle and within subnuclear domains.
Component of the BRCA1-A complex, at least composed of BRCA1, BARD1, UIMC1/RAP80, ABRAXAS1, BRCC3/BRCC36, BABAM2 and BABAM1/NBA1.
Interacts (via the BRCT domains) with ABRAXAS1 (phosphorylated form); this is important for recruitment to sites of DNA damage. Can form a heterotetramer with two molecules of ABRAXAS1 (phosphorylated form).
Component of the BRCA1-RBBP8 complex.
Interacts (via the BRCT domains) with RBBP8 ('Ser-327' phosphorylated form); the interaction ubiquitinates RBBP8, regulates CHEK1 activation, and involves RBBP8 in BRCA1-dependent G2/M checkpoint control on DNA damage. Associates with RNA polymerase II holoenzyme.
Interacts with SMC1A, NELFB, DCLRE1C, CLSPN. CHEK1, CHEK2, BAP1, BRCC3, UBXN1 and PCLAF.
Interacts (via BRCT domains) with BRIP1 (phosphorylated form).
Interacts with FANCD2 (ubiquitinated form).
Interacts with H2AX (phosphorylated on 'Ser-140').
Interacts (via the BRCT domains) with ACACA (phosphorylated form); the interaction prevents dephosphorylation of ACACA.
Part of a BRCA complex containing BRCA1, BRCA2 and PALB2.
Interacts directly with PALB2; the interaction is essential for its function in HRR.
Interacts directly with BRCA2; the interaction occurs only in the presence of PALB2 which serves as the bridging protein.
Interacts (via the BRCT domains) with LMO4; the interaction represses the transcriptional activity of BRCA1.
Interacts (via the BRCT domains) with CCAR2 (via N-terminus); the interaction represses the transcriptional activator activity of BRCA1 (By similarity).
Interacts with EXD2 (By similarity).
Interacts (via C-terminus) with DHX9; this interaction is direct and links BRCA1 to the RNA polymerase II holoenzyme (By similarity).
By similarity1 PublicationGO - Molecular functioni
- RNA polymerase binding Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 160259, 2 interactors |
STRINGi | 9913.ENSBTAP00000011616 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 1642 – 1729 | BRCT 1PROSITE-ProRule annotationAdd BLAST | 88 | |
Domaini | 1749 – 1848 | BRCT 2PROSITE-ProRule annotationAdd BLAST | 100 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1392 – 1419 | Interaction with PALB2By similarityAdd BLAST | 28 |
Domaini
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 24 – 65 | RING-typePROSITE-ProRule annotationAdd BLAST | 42 |
Keywords - Domaini
Repeat, Zinc-fingerPhylogenomic databases
eggNOGi | KOG4362, Eukaryota |
InParanoidi | Q864U1 |
OrthoDBi | 496760at2759 |
Family and domain databases
Gene3Di | 3.30.40.10, 1 hit 3.40.50.10190, 2 hits |
InterProi | View protein in InterPro IPR011364, BRCA1 IPR031099, BRCA1-associated IPR025994, BRCA1_serine_dom IPR001357, BRCT_dom IPR036420, BRCT_dom_sf IPR018957, Znf_C3HC4_RING-type IPR001841, Znf_RING IPR013083, Znf_RING/FYVE/PHD IPR017907, Znf_RING_CS |
PANTHERi | PTHR13763, PTHR13763, 1 hit |
Pfami | View protein in Pfam PF00533, BRCT, 2 hits PF12820, BRCT_assoc, 1 hit PF00097, zf-C3HC4, 1 hit |
PIRSFi | PIRSF001734, BRCA1, 1 hit |
PRINTSi | PR00493, BRSTCANCERI |
SMARTi | View protein in SMART SM00292, BRCT, 2 hits SM00184, RING, 1 hit |
SUPFAMi | SSF52113, SSF52113, 2 hits |
PROSITEi | View protein in PROSITE PS50172, BRCT, 2 hits PS00518, ZF_RING_1, 1 hit PS50089, ZF_RING_2, 1 hit |
i Sequence
Sequence statusi: Complete.
10 20 30 40 50
MDLSADHVEE VQNVLNAMQK ILECPICLEL IKEPVSTKCD HIFCKFCMLK
60 70 80 90 100
LLNQKKGPSQ CPLCKNDITK RSLQESTRFS QLVEELLKII HAFELDTGLQ
110 120 130 140 150
FANSYNFSRK EDNSPEHLKE EVSIIQSMGY RNRAKRLWQS EPENPTLQET
160 170 180 190 200
SLTVELSNLG IVRSLRTKQQ TQSQNKSVYI ELGSDSSEDT VNKASYFSVG
210 220 230 240 250
DHELLEITPQ GAKAKTNLNP AEKAACEFSE KDITNTEHHQ LSIKDLITTQ
260 270 280 290 300
KHATETHPEK YQGISVSDFH VEPCGTDTHA SSLQHENSSL LLTENRLNVE
310 320 330 340 350
KAEFCNKSKQ PVLVKSQQSR WAESKGTCKD RQIPSTEKKI VLNTDPLYRR
360 370 380 390 400
KELRKQKPAC PDSPGDSQDV PWVTLNNSIQ KVNDWFSRSD EILTSDDSCD
410 420 430 440 450
GGSESNNEVA GAVEIPNKVD GYSGSSEKIN LMASDPHGTL IHERVHSKPV
460 470 480 490 500
ESNIEDKIFG KTYRRKSSLP NFSHIAEDLI LGAFTVEPQI TQEQPLTNKL
510 520 530 540 550
KCKRRGTSGL QPEDFIKKVD LTIVPKTPEK MTEGTDQTEQ KCHGMNITSD
560 570 580 590 600
GHENKTKRDY VQKEQNANPA ESLEKESVFR TEAEPISISI SNMELELNIH
610 620 630 640 650
RSKAPKNRLK RKSSTRKIPE LELVVSRNPS LPNHTELPID SSSSNEEMKK
660 670 680 690 700
KHSSQMPVRQ SQKLQLIGDK ELTAGAKNNK TYEQINKRLA SDAFPELKLT
710 720 730 740 750
NTPGYFTNCS SKPEEFVHPS LQREENLGTI QVSNSTKDPK DLILREGKAL
760 770 780 790 800
QIERSVESTN ISLVPDTDYS TQDSISLLEA KTPEKAKTAP NPCVSLCTAT
810 820 830 840 850
KNLKELIHRD FKDTKNNTEG FQDLLGHDIN YVIQETSREM EDSELDTQYL
860 870 880 890 900
QNTFKASKRQ TFALFSNPGN PQKECATVFA HSGSLRDQSP RDPLKCRQKE
910 920 930 940 950
DSQGKSESKS QHVQAICTTV HFPVADQQDR TPGDDAKCSA KEVTRVCQSS
960 970 980 990 1000
QLRGHKTELV FANKQGVSEK PNLIPSLSPI KSSVKTICKK SPSEKFEEPV
1010 1020 1030 1040 1050
TSPEKTLGSE SIIQSAVSTI SQNNIQESTF KEVSSNSVNE VGSSTNEVGS
1060 1070 1080 1090 1100
SVNEVGSSGE NIQAEPGRNR EPKLRALLGL GLTQPEVYKQ SLPVSNCHHP
1110 1120 1130 1140 1150
EIKRQGENED MPQAVKADFS PCLISDNLEQ PTGSRHASQV CSETPDNLLN
1160 1170 1180 1190 1200
DDEIKENSHF AESDIKERSA VFSESVQKGE FRGSPGPFTH THLAQGHQRG
1210 1220 1230 1240 1250
AGKLESEETV SSEDEELPCF QQLLFGKVTS TLSPSTGCNT VATEGLSKET
1260 1270 1280 1290 1300
EGNLESLKSG LNDCSGQVTS AKVSQEHHLN EEARCSGSLF SSQCSAMEDL
1310 1320 1330 1340 1350
TTNTNTQDPF LMFERPSKQV YQSESEEVLS DKELVSDDEE RETGLEEDSC
1360 1370 1380 1390 1400
QEEQSVDSDL GEAVSDHVSE TSLSEDGVGL SSQSDILTTQ QRDTMQDNLL
1410 1420 1430 1440 1450
KLQQEMAELE AVLERHGSQP SHSSASLTAD SRGPEHLLNL EQDTSERAIL
1460 1470 1480 1490 1500
TSEKSRDYSR SQNPESLSAD KFPVSLDSST NKNKEPGMER SSASKFQLSY
1510 1520 1530 1540 1550
NRWYMHSSRS LQDRNCPSQK EPINVADMEE QQLAKREAQD LMGSFLPRQD
1560 1570 1580 1590 1600
QEGTPYLKSG ISLFSHEPES DPSEDRAAEP AHVHSMPPSA SALKLSQFRV
1610 1620 1630 1640 1650
EESTKNPAAA HIANTTRCNL REESMSKEKP EVISSTERSK KRLSMVASGL
1660 1670 1680 1690 1700
TPKELMLVQK FARKHHVTLT NLITEETTHV IMKTDPEFVC ERTLKYFLGI
1710 1720 1730 1740 1750
AGGKWVVSYF WVTQSIKEGK MLDEHDFEVR GDVVNGRNHQ GPKRARESRD
1760 1770 1780 1790 1800
KKIFKGLEIC CYGPFTNMPT DQLEWMVQLC GASVVKEPSS FTPDQGTHPV
1810 1820 1830 1840
VVVQPDAWTE DAGFHVIGQM CEAPVVTREW VLDSVALYQC QELDTYLVP
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AY077732 mRNA Translation: AAL76094.1 |
RefSeqi | NP_848668.1, NM_178573.1 |
Genome annotation databases
GeneIDi | 353120 |
KEGGi | bta:353120 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AY077732 mRNA Translation: AAL76094.1 |
RefSeqi | NP_848668.1, NM_178573.1 |
3D structure databases
SMRi | Q864U1 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 160259, 2 interactors |
STRINGi | 9913.ENSBTAP00000011616 |
Proteomic databases
PaxDbi | Q864U1 |
PRIDEi | Q864U1 |
Genome annotation databases
GeneIDi | 353120 |
KEGGi | bta:353120 |
Organism-specific databases
CTDi | 672 |
Phylogenomic databases
eggNOGi | KOG4362, Eukaryota |
InParanoidi | Q864U1 |
OrthoDBi | 496760at2759 |
Enzyme and pathway databases
UniPathwayi | UPA00143 |
Family and domain databases
Gene3Di | 3.30.40.10, 1 hit 3.40.50.10190, 2 hits |
InterProi | View protein in InterPro IPR011364, BRCA1 IPR031099, BRCA1-associated IPR025994, BRCA1_serine_dom IPR001357, BRCT_dom IPR036420, BRCT_dom_sf IPR018957, Znf_C3HC4_RING-type IPR001841, Znf_RING IPR013083, Znf_RING/FYVE/PHD IPR017907, Znf_RING_CS |
PANTHERi | PTHR13763, PTHR13763, 1 hit |
Pfami | View protein in Pfam PF00533, BRCT, 2 hits PF12820, BRCT_assoc, 1 hit PF00097, zf-C3HC4, 1 hit |
PIRSFi | PIRSF001734, BRCA1, 1 hit |
PRINTSi | PR00493, BRSTCANCERI |
SMARTi | View protein in SMART SM00292, BRCT, 2 hits SM00184, RING, 1 hit |
SUPFAMi | SSF52113, SSF52113, 2 hits |
PROSITEi | View protein in PROSITE PS50172, BRCT, 2 hits PS00518, ZF_RING_1, 1 hit PS50089, ZF_RING_2, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | BRCA1_BOVIN | |
Accessioni | Q864U1Primary (citable) accession number: Q864U1 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 23, 2004 |
Last sequence update: | June 1, 2003 | |
Last modified: | April 7, 2021 | |
This is version 127 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways