Tag |
Content |
dbPAF ID |
dbPAF-0001888 |
Uniprot Accession |
O54952; BRCA1_RAT; P97951; |
Genbank Protein ID |
NP_036646.1; |
Genbank Nucleotide ID |
NM_012514.1; |
Protein Name |
Breast cancer type 1 susceptibility protein homolog |
Protein Synonyms/Alias |
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Gene Name |
Brca1 |
Gene Synonyms/Alias |
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Organism |
Rattus norvegicus(Rat) |
NCBI Taxa ID |
10116 |
Functional Description (View all) |
E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. It is unclear whether it also mediates the formation of other types of polyubiquitin chains. The E3 ubiquitin-protein ligase activity is required for its tumor suppressor function. The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Regulates centrosomal microtubule nucleation. Required for normal cell cycle progression from G2 to mitosis. Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle. Involved in transcriptional regulation of P21 in response to DNA damage. Required for FANCD2 targeting to sites of DNA damage. May function as a transcriptional regulator. Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation. Contributes to homologous recombination repair (HRR) via its direct interaction with PALB2, fine-tunes recombinational repair partly through its modulatory role in the PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks. Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage via BRCA1-mediated ubiquitination of RBBP8. Acts as a transcriptional activator (By similarity).Functional Description
E3 ubiquitin-protein ligase that specifically mediates the formation of 'Lys-6'-linked polyubiquitin chains and plays a central role in DNA repair by facilitating cellular responses to DNA damage. It is unclear whether it also mediates the formation of other types of polyubiquitin chains. The E3 ubiquitin-protein ligase activity is required for its tumor suppressor function. The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Regulates centrosomal microtubule nucleation. Required for normal cell cycle progression from G2 to mitosis. Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle. Involved in transcriptional regulation of P21 in response to DNA damage. Required for FANCD2 targeting to sites of DNA damage. May function as a transcriptional regulator. Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation. Contributes to homologous recombination repair (HRR) via its direct interaction with PALB2, fine-tunes recombinational repair partly through its modulatory role in the PALB2-dependent loading of BRCA2-RAD51 repair machinery at DNA breaks. Component of the BRCA1-RBBP8 complex which regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage via BRCA1-mediated ubiquitination of RBBP8. Acts as a transcriptional activator (By similarity).
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Phosphorylation Sites
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dbPAF PTMs: 7 |
Sequence (Fasta) | MDLSAVRIQE VQNVLHAMQK ILECPICLEL IKEPVSTQCD HIFCKFCMLK LLNQKKGPSQ 60 CPLCKNEITK RSLQGSARFS QLVEELLKII DAFELDTGMQ CANGFSFSKK KNSSSELLNE 120 DASIIQSVGY RNRVKKLQQI ESGSATLKDS LSVQLSNLGI VRSMKKNRQT QPQNKSVYIA 180 LESDSSEERV NAPDGCSVRD QELFQIAPGG AGDEGKLNSA KKAACDFSEG IRNIEHHQCS 240 DKDLNPTENH ATERHPEKCP RISVANVHVE PCGTDARASS LQRGTRSLLF TEDRLDAEKA 300 EFCDRSKQSG AAVSQQSRWA DSKETCNGRP VPRTEGKADP NVDSLCGRKQ WNHPKSLCPE 360 NSGATTDVPW ITLNSSIQKV NEWFSRTGEM LTSDNASDRR PASNAEAAVV LEVSNEVDGC 420 FSSSKKIDLV APDPDNAVMC TSGRDFSKPV ENIINDKIFG KTYQRKGSRP HLNHVTEIIG 480 TFTTEPQIIQ EQPFTNKLKR KRSTCLHPED FIKKADLTVV QRISENLNQG TDQMEPNDQA 540 MSITSNGQEN RATGNDLQRG RNAHPIESLR KEPAFTAKAK SISNSISDLE VELNVHSSKA 600 PKKNRLRRKS TRCVLPLEPI SRNPSPPTCA ELQIESCGSS EETKKNNSNQ TPAGHIREPQ 660 LIEDTEPAAD AKKNEPNEHI RKRSASDAFP EEKLMNKAGL LTSCSSPRKP QGPVNPSPER 720 KGIEQLEMCQ MPDNNKELGD LVLGGEPSGK PTEPSEESTS VSLVPDTDYD TQNSVSILEA 780 NTVRYARTGS VQCMTQFVAS ENPKELVHGS NNAGSGSECF KHPLRHELNH NQETIEMEDS 840 ELDTQYLQNT FQVSKRQSFA LFSKLRSPQK DCTLVGARSV PSREPSPKVT SRGEQKERQG 900 QEESEISHVQ AVTVTVGLPV PCQEGKPGAV TMCADVSRLC PSSHYRSCEN GLNTTDKSGI 960 SQNSHFRQSV SPLRSSIKTD NRKTLTEGRF EKHTERGMGN ETAVQSTIHT ISLNNRGDAC 1020 LEASSGSVIE VHSTGENVQG QLDRNRGPKV NTVSLLDSTQ PGVSKQSAPV SDKYLEIKQE 1080 SKAVSADFSP CLFSDHLEKP MRSDKTFQVC SETPDDLLDD VEIQENASFG EGGITEKSAI 1140 FNGSVLRRES SRSPSPVTHA SKSRSLHRGS RKLEFSEESD STEDEDLPCF QHLLSRVSST 1200 PELTRCSSVV TQRVPEKAKG TQAPRKSSIS DCNNEVILGE ASQEYQFSED AKCSGSMFSS 1260 QHSAALGSPA NALSQDPDFN PPSKQRRHQA ENEEAFLSDK ELISDHEDMA ACLEEASDQE 1320 EDSIIPDSVA SGYESEANLS EDCSQSDILT TQQRATMKDN LIKLQQEMAQ LEAVLEQHGS 1380 QPSGHPPCLP ADPCALEDLP DPEQNRSGTA ILTSKNINEN PVSQNPKRAC DDKSQPQPPD 1440 GLPSGDKESG MRRPSPFKSP LTSSRCSARG HSRSLQNRNS TSQEELLQPA XLEKSCEPHN 1500 LTGRSCLPRQ DLEGTPYPES GIRLVSSRDP DSESPKVSAL VCTAPASTSA LKISQGQVAG 1560 SCRSPAAGGA DTAVVEIVSK IKPEVTSPKE RAERDISMVV SGLTPKEVMI VQKFAEKYRL 1620 ALTDVITEET THVIIKTDAE FVCERTLKYF LGIAGGKWIV SYSWVIKSIQ ERKLLSVHEF 1680 EVKGDVVTGS NHQGPRRSRE SQEKLFEGLQ IYCCEPFTNM PKDELERMLQ LCGASVVKEL 1740 PLLTRDTGAH PIVLVQPSAW TEDNDCPDIG QLCKGRLVMW DWVLDSISVY RCRDLDAYLV 1800 QNITCGRDGS EPQDSND
1818Fasta Sequence
>O54952|Brca1|Rattus norvegicus(Rat) MDLSAVRIQEVQNVLHAMQKILECPICLELIKEPVSTQCDHIFCKFCMLKLLNQKKGPSQCPLCKNEITKRSLQGSARFSQLVEELLKIIDAFELDTGMQCANGFSFSKKKNSSSELLNEDASIIQSVGYRNRVKKLQQIESGSATLKDSLSVQLSNLGIVRSMKKNRQTQPQNKSVYIALESDSSEERVNAPDGCSVRDQELFQIAPGGAGDEGKLNSAKKAACDFSEGIRNIEHHQCSDKDLNPTENHATERHPEKCPRISVANVHVEPCGTDARASSLQRGTRSLLFTEDRLDAEKAEFCDRSKQSGAAVSQQSRWADSKETCNGRPVPRTEGKADPNVDSLCGRKQWNHPKSLCPENSGATTDVPWITLNSSIQKVNEWFSRTGEMLTSDNASDRRPASNAEAAVVLEVSNEVDGCFSSSKKIDLVAPDPDNAVMCTSGRDFSKPVENIINDKIFGKTYQRKGSRPHLNHVTEIIGTFTTEPQIIQEQPFTNKLKRKRSTCLHPEDFIKKADLTVVQRISENLNQGTDQMEPNDQAMSITSNGQENRATGNDLQRGRNAHPIESLRKEPAFTAKAKSISNSISDLEVELNVHSSKAPKKNRLRRKSTRCVLPLEPISRNPSPPTCAELQIESCGSSEETKKNNSNQTPAGHIREPQLIEDTEPAADAKKNEPNEHIRKRSASDAFPEEKLMNKAGLLTSCSSPRKPQGPVNPSPERKGIEQLEMCQMPDNNKELGDLVLGGEPSGKPTEPSEESTSVSLVPDTDYDTQNSVSILEANTVRYARTGSVQCMTQFVASENPKELVHGSNNAGSGSECFKHPLRHELNHNQETIEMEDSELDTQYLQNTFQVSKRQSFALFSKLRSPQKDCTLVGARSVPSREPSPKVTSRGEQKERQGQEESEISHVQAVTVTVGLPVPCQEGKPGAVTMCADVSRLCPSSHYRSCENGLNTTDKSGISQNSHFRQSVSPLRSSIKTDNRKTLTEGRFEKHTERGMGNETAVQSTIHTISLNNRGDACLEASSGSVIEVHSTGENVQGQLDRNRGPKVNTVSLLDSTQPGVSKQSAPVSDKYLEIKQESKAVSADFSPCLFSDHLEKPMRSDKTFQVCSETPDDLLDDVEIQENASFGEGGITEKSAIFNGSVLRRESSRSPSPVTHASKSRSLHRGSRKLEFSEESDSTEDEDLPCFQHLLSRVSSTPELTRCSSVVTQRVPEKAKGTQAPRKSSISDCNNEVILGEASQEYQFSEDAKCSGSMFSSQHSAALGSPANALSQDPDFNPPSKQRRHQAENEEAFLSDKELISDHEDMAACLEEASDQEEDSIIPDSVASGYESEANLSEDCSQSDILTTQQRATMKDNLIKLQQEMAQLEAVLEQHGSQPSGHPPCLPADPCALEDLPDPEQNRSGTAILTSKNINENPVSQNPKRACDDKSQPQPPDGLPSGDKESGMRRPSPFKSPLTSSRCSARGHSRSLQNRNSTSQEELLQPAXLEKSCEPHNLTGRSCLPRQDLEGTPYPESGIRLVSSRDPDSESPKVSALVCTAPASTSALKISQGQVAGSCRSPAAGGADTAVVEIVSKIKPEVTSPKERAERDISMVVSGLTPKEVMIVQKFAEKYRLALTDVITEETTHVIIKTDAEFVCERTLKYFLGIAGGKWIVSYSWVIKSIQERKLLSVHEFEVKGDVVTGSNHQGPRRSRESQEKLFEGLQIYCCEPFTNMPKDELERMLQLCGASVVKELPLLTRDTGAHPIVLVQPSAWTEDNDCPDIGQLCKGRLVMWDWVLDSISVYRCRDLDAYLVQNITCGRDGSEPQDSND
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Keyword |
KW-0002--3D-structure KW-0007--Acetylation KW-0010--Activator KW-0131--Cell cycle KW-0158--Chromosome KW-0181--Complete proteome KW-0963--Cytoplasm KW-0227--DNA damage KW-0233--DNA recombination KW-0234--DNA repair KW-0238--DNA-binding KW-0275--Fatty acid biosynthesis KW-0276--Fatty acid metabolism KW-1017--Isopeptide bond KW-0436--Ligase KW-0444--Lipid biosynthesis KW-0443--Lipid metabolism KW-0479--Metal-binding KW-0539--Nucleus KW-0597--Phosphoprotein KW-1185--Reference proteome KW-0677--Repeat KW-0804--Transcription KW-0805--Transcription regulation KW-0043--Tumor suppressor KW-0832--Ubl conjugation KW-0833--Ubl conjugation pathway KW-0862--Zinc KW-0863--Zinc-finger
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Interpro |
IPR011364--BRCA1 IPR031099--BRCA1-associated IPR025994--BRCA1_serine_dom IPR001357--BRCT_dom IPR018957--Znf_C3HC4_RING-type IPR001841--Znf_RING IPR013083--Znf_RING/FYVE/PHD IPR017907--Znf_RING_CS
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PROSITE |
PS50172--BRCT PS00518--ZF_RING_1 PS50089--ZF_RING_2
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Pfam |
PF00533--BRCT PF12820--BRCT_assoc PF00097--zf-C3HC4
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Gene Ontology |
GO:0070531--C:BRCA1-A complex GO:0031436--C:BRCA1-BARD1 complex GO:0005694--C:chromosome GO:0005759--C:mitochondrial matrix GO:0005634--C:nucleus GO:0005886--C:plasma membrane GO:0003682--F:chromatin binding GO:0003677--F:DNA binding GO:0016874--F:ligase activity GO:0004842--F:ubiquitin-protein transferase activity GO:0008270--F:zinc ion binding GO:0007420--P:brain development GO:0007049--P:cell cycle GO:0043009--P:chordate embryonic development GO:0009048--P:dosage compensation by inactivation of X chromosome GO:0000724--P:double-strand break repair via homologous recombination GO:0006633--P:fatty acid biosynthetic process GO:0045717--P:negative regulation of fatty acid biosynthetic process GO:0035067--P:negative regulation of histone acetylation GO:0071158--P:positive regulation of cell cycle arrest GO:0035066--P:positive regulation of histone acetylation GO:0033160--P:positive regulation of protein import into nucleus, translocation GO:0045944--P:positive regulation of transcription from RNA polymerase II promoter GO:0045893--P:positive regulation of transcription, DNA-templated GO:0051865--P:protein autoubiquitination GO:0085020--P:protein K6-linked ubiquitination GO:0042127--P:regulation of cell proliferation GO:0032355--P:response to estradiol GO:0033993--P:response to lipid GO:0007584--P:response to nutrient GO:0010033--P:response to organic substance GO:0006351--P:transcription, DNA-templated
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