BRCA1
entrez
672
canonical
uniprot
P38398
canonical
ensembl
ENSG00000012048
resolver
ensp
ENSP00000312236
resolver
ensp
ENSP00000350283
resolver
ensp
ENSP00000417148
resolver
ensp
ENSP00000417241
resolver
ensp
ENSP00000417554
resolver
ensp
ENSP00000418775
resolver
ensp
ENSP00000418819
resolver
ensp
ENSP00000418960
resolver
ensp
ENSP00000418986
resolver
ensp
ENSP00000419103
resolver
ensp
ENSP00000419274
resolver
ensp
ENSP00000419481
resolver
ensp
ENSP00000419988
resolver
ensp
ENSP00000420201
resolver
ensp
ENSP00000420412
resolver
ensp
ENSP00000420781
resolver
ensp
ENSP00000478114
resolver
ensp
ENSP00000489431
resolver
ensp
ENSP00000494614
resolver
ensp
ENSP00000496570
resolver
ensp
ENSP00000498906
resolver
ensp
ENSP00000518978
resolver
ensp
ENSP00000570013
resolver
ensp
ENSP00000591973
resolver
ensp
ENSP00000591974
resolver
ensp
ENSP00000591975
resolver
ensp
ENSP00000615327
resolver
ensp
ENSP00000615328
resolver
ensp
ENSP00000680385
resolver
ensp
ENSP00000680386
resolver
ensp
ENSP00000680387
resolver
ensp
ENSP00000746524
resolver
ensp
ENSP00000746525
resolver
ensp
ENSP00000746526
resolver
ensp
ENSP00000746527
resolver
ensp
ENSP00000746528
resolver
ensp
ENSP00000746530
resolver
ensp
ENSP00000746531
resolver
enst
ENST00000461574
resolver
enst
ENST00000473961
resolver
enst
ENST00000476777
resolver
enst
ENST00000477152
resolver
enst
ENST00000478531
resolver
enst
ENST00000489037
resolver
enst
ENST00000493919
resolver
enst
ENST00000497488
resolver
enst
ENST00000634433
resolver
enst
ENST00000644379
resolver
enst
ENST00000644555
resolver
enst
ENST00000921915
resolver
enst
ENST00000945268
resolver
enst
ENST00000945269
resolver
genesymbol
BRCA1
resolver
genesymbol_syn
RNF53
resolver
hgnc
HGNC:1100
resolver
uniprot
A0A0U1RRA9
resolver
uniprot
A0A2R8Y587
resolver
uniprot
A0A2R8Y7V5
resolver
uniprot
A0A9Y1QPR4
resolver
uniprot
A0A9Y1QPT7
resolver
uniprot
A0A9Y1QPY6
resolver
uniprot
A0A9Y1QQ47
resolver
uniprot
A0A9Y1QQD3
resolver
uniprot
A0A9Y1QQF1
resolver
uniprot
A0A9Y1QQJ6
resolver
uniprot
A0A9Y1QQK3
resolver
uniprot
A0A9Y1QQK7
resolver
uniprot
A0A9Y1VR53
resolver
uniprot
A0A9Y1VVD0
resolver
uniprot
A0A9Y1VVE2
resolver
uniprot
A0ACM8QT95
resolver
uniprot
B4DES0
resolver
uniprot
C9IZW4
resolver
uniprot
E7ENB7
resolver
uniprot
E7EQW4
resolver
uniprot
E7EUM2
resolver
uniprot
E9PFZ0
resolver
uniprot
E9PH68
resolver
uniprot
H0Y850
resolver
uniprot
H0Y8D8
resolver
uniprot
O15129
resolver
uniprot
Q1RMC1
resolver
uniprot
Q3LRJ0
resolver
uniprot
Q3LRJ6
resolver
uniprot
Q6IN79
resolver
uniprot
Q7KYU9
resolver
uniprot_entry
A0A0U1RRA9_HUMAN
resolver
uniprot_entry
A0A2R8Y7V5_HUMAN
resolver
uniprot_entry
A0A9Y1QPR4_HUMAN
resolver
uniprot_entry
A0A9Y1QPT7_HUMAN
resolver
uniprot_entry
A0A9Y1QPY6_HUMAN
resolver
uniprot_entry
A0A9Y1QQ47_HUMAN
resolver
uniprot_entry
A0A9Y1QQD3_HUMAN
resolver
uniprot_entry
A0A9Y1QQF1_HUMAN
resolver
uniprot_entry
A0A9Y1QQJ6_HUMAN
resolver
uniprot_entry
A0A9Y1QQK3_HUMAN
resolver
uniprot_entry
A0A9Y1QQK7_HUMAN
resolver
uniprot_entry
A0A9Y1VR53_HUMAN
resolver
uniprot_entry
A0A9Y1VVD0_HUMAN
resolver
uniprot_entry
A0A9Y1VVE2_HUMAN
resolver
uniprot_entry
A0ACM8QT95_HUMAN
resolver
uniprot_entry
B4DES0_HUMAN
resolver
uniprot_entry
BRCA1_HUMAN
resolver
uniprot_entry
C9IZW4_HUMAN
resolver
uniprot_entry
E7ENB7_HUMAN
resolver
uniprot_entry
E7EQW4_HUMAN
resolver
uniprot_entry
E7EUM2_HUMAN
resolver
uniprot_entry
H0Y850_HUMAN
resolver
uniprot_entry
H0Y8D8_HUMAN
resolver
uniprot_sec
A0A2R8Y587
resolver
uniprot_sec
E9PFZ0
resolver
uniprot_sec
E9PH68
resolver
uniprot_sec
O15129
resolver
uniprot_sec
Q1RMC1
resolver
uniprot_sec
Q3LRJ0
resolver
uniprot_sec
Q3LRJ6
resolver
uniprot_sec
Q6IN79
resolver
uniprot_sec
Q7KYU9
resolver
activity_regulation
ACTIVITY REGULATION: The E3 ubiquitin-protein ligase activity is inhibited by phosphorylation by AURKA. Activity is increased by phosphatase treatment. {ECO:0000269|PubMed:18056443}.
uniprot
proteins
amino_acid_sequence
MDLSALRVEEVQNVINAMQKILECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCKNDITKRSLQESTRFSQLVEELLKIICAFQLDTGLEYANSYNFAKKENNSPEHLKDEVSIIQSMGYRNRAKRLLQSEPENPSLQETSLSVQLSNLGTVRTLRTKQRIQPQKTSVYIELGSDSSEDTVNKATYCSVGDQELLQITPQGTRDEISLDSAKKAACEFSETDVTNTEHHQPSNNDLNTTEKRAAERHPEKYQGSSVSNLHVEPCGTNTHASSLQHENSSLLLTKDRMNVEKAEFCNKSKQPGLARSQHNRWAGSKETCNDRRTPSTEKKVDLNADPLCERKEWNKQKLPCSENPRDTEDVPWITLNSSIQKVNEWFSRSDELLGSDDSHDGESESNAKVADVLDVLNEVDEYSGSSEKIDLLASDPHEALICKSERVHSKSVESNIEDKIFGKTYRKKASLPNLSHVTENLIIGAFVTEPQIIQERPLTNKLKRKRRPTSGLHPEDFIKKADLAVQKTPEMINQGTNQTEQNGQVMNITNSGHENKTKGDSIQNEKNPNPIESLEKESAFKTKAEPISSSISNMELELNIHNSKAPKKNRLRRKSSTRHIHALELVVSRNLSPPNCTELQIDSCSSSEEIKKKKYNQMPVRHSRNLQLMEGKEPATGAKKSNKPNEQTSKRHDSDTFPELKLTNAPGSFTKCSNTSELKEFVNPSLPREEKEEKLETVKVSNNAEDPKDLMLSGERVLQTERSVESSSISLVPGTDYGTQESISLLEVSTLGKAKTEPNKCVSQCAAFENPKGLIHGCSKDNRNDTEGFKYPLGHEVNHSRETSIEMEESELDAQYLQNTFKVSKRQSFAPFSNPGNAEEECATFSAHSGSLKKQSPKVTFECEQKEENQGKNESNIKPVQTVNITAGFPVVGQKDKPVDNAKCSIKGGSRFCLSSQFRGNETGLITPNKHGLLQNPYRIPPLFPIKSFVKTKCKKNLLEENFEEHSMSPEREMGNENIPSTVSTISRNNIRENVFKEASSSNINEVGSSTNEVGSSINEIGSSDENIQAELGRNRGPKLNAMLRLGVLQPEVYKQSLPGSNCKHPEIKKQEYEEVVQTVNTDFSPYLISDNLEQPMGSSHASQVCSETPDDLLDDGEIKEDTSFAENDIKESSAVFSKSVQKGELSRSPSPFTHTHLAQGYRRGAKKLESSEENLSSEDEELPCFQHLLFGKVNNIPSQSTRHSTVATECLSKNTEENLLSLKNSLNDCSNQVILAKASQEHHLSEETKCSASLFSSQCSELEDLTANTNTQDPFLIGSSKQMRHQSESQGVGLSDKELVSDDEERGTGLEENNQEEQSMDSNLGEAASGCESETSVSEDCSGLSSQSDILTTQQRDTMQHNLIKLQQEMAELEAVLEQHGSQPSNSYPSIISDSSALEDLRNPEQSTSEKAVLTSQKSSEYPISQNPEGLSADKFEVSADSSTSKNKEPGVERSSPSKCPSLDDRWYMHSCSGSLQNRNYPSQEELIKVVDVEEQQLEESGPHDLTETSYLPRQDLEGTPYLESGISLFSDDPESDPSEDRAPESARVGNIPSSTSALKVPQLKVAESAQSPAAAHTTDTAGYNAMEESVSREKPELTASTERVNKRMSMVVSGLTPEEFMLVYKFARKHHITLTNLITEETTHVVMKTDAEFVCERTLKYFLGIAGGKWVVSYFWVTQSIKERKMLNEHDFEVRGDVVNGRNHQGPKRARESQDRKIFRGLEICCYGPFTNMPTDQLEWMVQLCGASVVKELSSFTLGTGVHPIVVVQPDAWTEDNGFHAIGQMCEAPVVTREWVLDSVALYQCQELDTYLIPQIPHSHY
uniprot
proteins
disease_involvement
DISEASE: Breast cancer (BC) [MIM:114480]: A common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case. {ECO:0000269|PubMed:10323242, ECO:0000269|PubMed:11114888, ECO:0000269|PubMed:11301010, ECO:0000269|PubMed:12427738, ECO:0000269|PubMed:12442275, ECO:0000269|PubMed:12938098, ECO:0000269|PubMed:14722926, ECO:0000269|PubMed:15133502, ECO:0000269|PubMed:18285836, ECO:0000269|PubMed:21473589, ECO:0000269|PubMed:23867111, ECO:0000269|PubMed:28364669, ECO:0000269|PubMed:7545954, ECO:0000269|PubMed:7894491, ECO:0000269|PubMed:7894493, ECO:0000269|PubMed:7939630, ECO:0000269|PubMed:8554067, ECO:0000269|PubMed:8723683, ECO:0000269|PubMed:8776600, ECO:0000269|PubMed:8807330, ECO:0000269|PubMed:9482581, ECO:0000269|PubMed:9609997, ECO:0000269|PubMed:9760198}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Mutations in BRCA1 are thought to be responsible for 45% of inherited breast cancer. Moreover, BRCA1 carriers have a 4-fold increased risk of colon cancer, whereas male carriers face a 3-fold increased risk of prostate cancer. Cells lacking BRCA1 show defects in DNA repair by homologous recombination.; DISEASE: Breast-ovarian cancer, familial, 1 (BROVCA1) [MIM:604370]: A condition associated with familial predisposition to cancer of the breast and ovaries. Characteristic features in affected families are an early age of onset of breast cancer (often before age 50), increased chance of bilateral cancers (cancer that develop in both breasts, or both ovaries, independently), frequent occurrence of breast cancer among men, increased incidence of tumors of other specific organs, such as the prostate. {ECO:0000269|PubMed:12938098, ECO:0000269|PubMed:14722926, ECO:0000269|PubMed:17924331, ECO:0000269|PubMed:20513136, ECO:0000269|PubMed:28364669, ECO:0000269|PubMed:8968716}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Mutations in BRCA1 are thought to be responsible for more than 80% of inherited breast-ovarian cancer.; DISEASE: Ovarian cancer (OC) [MIM:167000]: The term ovarian cancer defines malignancies originating from ovarian tissue. Although many histologic types of ovarian tumors have been described, epithelial ovarian carcinoma is the most common form. Ovarian cancers are often asymptomatic and the recognized signs and symptoms, even of late-stage disease, are vague. Consequently, most patients are diagnosed with advanced disease. {ECO:0000269|PubMed:10196379, ECO:0000269|PubMed:10486320, ECO:0000269|PubMed:14746861, ECO:0000269|PubMed:28364669}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Pancreatic cancer 4 (PNCA4) [MIM:614320]: A malignant neoplasm of the pancreas. Tumors can arise from both the exocrine and endocrine portions of the pancreas, but 95% of them develop from the exocrine portion, including the ductal epithelium, acinar cells, connective tissue, and lymphatic tissue. {ECO:0000269|PubMed:18762988}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Fanconi anemia, complementation group S (FANCS) [MIM:617883]: A form of Fanconi anemia, a disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair. {ECO:0000269|PubMed:23269703, ECO:0000269|PubMed:25472942, ECO:0000269|PubMed:29133208}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: 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 (PubMed:10500182, PubMed:12887909, PubMed:12890688, PubMed:14976165, PubMed:16818604, PubMed:17525340, PubMed:19261748). It is unclear whether it also mediates the formation of other types of polyubiquitin chains (PubMed:12890688). The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability (PubMed:12890688, PubMed:14976165, PubMed:20351172). Regulates centrosomal microtubule nucleation (PubMed:18056443). Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle (PubMed:10724175, PubMed:11836499, PubMed:12183412, PubMed:19261748). Required for FANCD2 targeting to sites of DNA damage (PubMed:12887909). Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation (PubMed:16326698). 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 (PubMed:19369211). 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 (PubMed:16818604). Acts as a transcriptional activator (PubMed:20160719). {ECO:0000269|PubMed:10500182, ECO:0000269|PubMed:10724175, ECO:0000269|PubMed:11836499, ECO:0000269|PubMed:12183412, ECO:0000269|PubMed:12887909, ECO:0000269|PubMed:12890688, ECO:0000269|PubMed:14976165, ECO:0000269|PubMed:16326698, ECO:0000269|PubMed:16818604, ECO:0000269|PubMed:17525340, ECO:0000269|PubMed:18056443, ECO:0000269|PubMed:19261748, ECO:0000269|PubMed:19369211, ECO:0000269|PubMed:20160719, ECO:0000269|PubMed:20351172}.
uniprot
proteins
mass_dalton
207721
uniprot
proteins
mutagenesis
MUTAGEN 26; /note="I->A: Disrupts the interaction with E2 enzymes, thereby abolishing the E3 ubiquitin-protein ligase activity."; /evidence="ECO:0000269|PubMed:16818604, ECO:0000269|PubMed:20351172"; MUTAGEN 26; /note="I->E: No ubiquitination of RBBP8. No restoration RBBP8-mediated focus formation or G2/M checkpoint control upon DNA damage."; /evidence="ECO:0000269|PubMed:16818604, ECO:0000269|PubMed:20351172"; MUTAGEN 71; /note="R->G: No effect on interaction with BAP1."; /evidence="ECO:0000269|PubMed:9528852"; MUTAGEN 1143; /note="S->A: Reduces in vitro phosphorylation by ATR."; /evidence="ECO:0000269|PubMed:11114888"; MUTAGEN 1239; /note="S->A: No effect on in vitro phosphorylation by ATR."; /evidence="ECO:0000269|PubMed:11114888"; MUTAGEN 1280; /note="S->A: Reduces in vitro phosphorylation by ATR."; /evidence="ECO:0000269|PubMed:11114888"; MUTAGEN 1298; /note="S->A: No effect on in vitro phosphorylation by ATR."; /evidence="ECO:0000269|PubMed:11114888"; MUTAGEN 1330; /note="S->A: No effect on in vitro phosphorylation by ATR."; /evidence="ECO:0000269|PubMed:11114888"; MUTAGEN 1387; /note="S->A: Loss of IR-induced S-phase checkpoint. Reduces in vitro phosphorylation by ATR."; /evidence="ECO:0000269|PubMed:11114888, ECO:0000269|PubMed:12183412"; MUTAGEN 1394; /note="T->A: Reduces in vitro phosphorylation by ATR."; /evidence="ECO:0000269|PubMed:11114888"; MUTAGEN 1423; /note="S->A: Inhibition of the infrared-induced G2 arrest. Reduces phosphorylation by ATR."; /evidence="ECO:0000269|PubMed:11114888, ECO:0000269|PubMed:12183412"; MUTAGEN 1457; /note="S->A: Reduces in vitro phosphorylation by ATR."; /evidence="ECO:0000269|PubMed:11114888"; MUTAGEN 1466; /note="S->A: No effect on in vitro phosphorylation by ATR."; /evidence="ECO:0000269|PubMed:11114888"; MUTAGEN 1524; /note="S->A: No change in infrared S-phase delay; when associated with A-1387. No effect on in vitro phosphorylation by ATR."; /evidence="ECO:0000269|PubMed:11114888, ECO:0000269|PubMed:12183412"; MUTAGEN 1655; /note="S->A: Abolishes interaction with BRIP1."; /evidence="ECO:0000269|PubMed:15133502"; MUTAGEN 1656; /note="G->D: No effect on affinity for a BRIP1 phosphopeptide."; /evidence="ECO:0000269|PubMed:21473589"; MUTAGEN 1662; /note="F->S: Does not abolish ABRAXAS1 binding, but abolishes formation of a heterotetramer with ABRAXAS1."; /evidence="ECO:0000269|PubMed:26778126"; MUTAGEN 1663; /note="M->K: Does not abolish ABRAXAS1 binding, but abolishes formation of a heterotetramer with ABRAXAS1."; /evidence="ECO:0000269|PubMed:26778126"; MUTAGEN 1666; /note="Y->A: Does not abolish ABRAXAS1 binding, but impairs formation of a heterotetramer with ABRAXAS1."; /evidence="ECO:0000269|PubMed:26778126"; MUTAGEN 1670; /note="R->E: Impairs formation of a heterotetramer with ABRAXAS1."; /evidence="ECO:0000269|PubMed:26778126"; MUTAGEN 1671; /note="K->E: Impairs formation of a heterotetramer with ABRAXAS1."; /evidence="ECO:0000269|PubMed:26778126"; MUTAGEN 1700; /note="T->A: Strongly reduces affinity for a BRIP1 phosphopeptide."; /evidence="ECO:0000269|PubMed:21473589"; MUTAGEN 1702; /note="K->M: Abolishes interaction with BRIP1."; /evidence="ECO:0000269|PubMed:15133502"; MUTAGEN 1738; /note="G->E: Abolishes interaction with BRIP1."; /evidence="ECO:0000269|PubMed:15133502"; MUTAGEN 1755; /note="S->A: No effect on in vitro phosphorylation by ATR."; /evidence="ECO:0000269|PubMed:11114888"; MUTAGEN 1835; /note="R->P: Mildly reduces affinity for a BRIP1 phosphopeptide."; /evidence="ECO:0000269|PubMed:21473589"; MUTAGEN 1836; /note="E->K: Slightly reduces affinity for a BRIP1 phosphopeptide."; /evidence="ECO:0000269|PubMed:21473589
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination.
uniprot
proteins
post_translational_modification
PTM: Phosphorylated in response to IR, UV, and various stimuli that cause checkpoint activation, probably by ATM or ATR (PubMed:11114888, PubMed:12183412, PubMed:21144835). Phosphorylation at Ser-988 by CHEK2 regulates mitotic spindle assembly (PubMed:10724175, PubMed:20364141). Phosphorylation by AURKA regulates centrosomal microtubule nucleation (PubMed:18056443). {ECO:0000269|PubMed:10724175, ECO:0000269|PubMed:11114888, ECO:0000269|PubMed:12183412, ECO:0000269|PubMed:18056443, ECO:0000269|PubMed:20364141, ECO:0000269|PubMed:21144835}.; PTM: Autoubiquitinated, undergoes 'Lys-6'-linked polyubiquitination. 'Lys-6'-linked polyubiquitination does not promote degradation. Ubiquitinated in a FBXO44-dependent manner; leading to proteasomal degradation (PubMed:23086937). {ECO:0000269|PubMed:12890688, ECO:0000269|PubMed:20351172, ECO:0000269|PubMed:23086937}.
uniprot
proteins
pubmed
10196379
uniprot
proteins
pubmed
10323242
uniprot
proteins
pubmed
10486320
uniprot
proteins
pubmed
10500182
uniprot
proteins
pubmed
10724175
uniprot
proteins
pubmed
10783165
uniprot
proteins
pubmed
10851077
uniprot
proteins
pubmed
11114888
uniprot
proteins
pubmed
11239454
uniprot
proteins
pubmed
11301010
uniprot
proteins
pubmed
11573085
uniprot
proteins
pubmed
11573086
uniprot
proteins
pubmed
11739404
uniprot
proteins
pubmed
11751867
uniprot
proteins
pubmed
11836499
uniprot
proteins
pubmed
11877377
uniprot
proteins
pubmed
12183412
uniprot
proteins
pubmed
12215251
uniprot
proteins
pubmed
12360400
uniprot
proteins
pubmed
12419185
uniprot
proteins
pubmed
12427738
uniprot
proteins
pubmed
12442274
uniprot
proteins
pubmed
12442275
uniprot
proteins
pubmed
12887909
uniprot
proteins
pubmed
12890688
uniprot
proteins
pubmed
12938098
uniprot
proteins
pubmed
14636569
uniprot
proteins
pubmed
14722926
uniprot
proteins
pubmed
14746861
uniprot
proteins
pubmed
14976165
uniprot
proteins
pubmed
14990569
uniprot
proteins
pubmed
15026808
uniprot
proteins
pubmed
15096610
uniprot
proteins
pubmed
15133502
uniprot
proteins
pubmed
15365993
uniprot
proteins
pubmed
15456891
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15609993
uniprot
proteins
pubmed
16101277
uniprot
proteins
pubmed
16326698
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
16698035
uniprot
proteins
pubmed
16818604
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
17525340
uniprot
proteins
pubmed
17643121
uniprot
proteins
pubmed
17643122
uniprot
proteins
pubmed
17924331
uniprot
proteins
pubmed
18056443
uniprot
proteins
pubmed
18285836
uniprot
proteins
pubmed
18452305
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18762988
uniprot
proteins
pubmed
19261746
uniprot
proteins
pubmed
19261748
uniprot
proteins
pubmed
19261749
uniprot
proteins
pubmed
19369211
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20159462
uniprot
proteins
pubmed
20160719
uniprot
proteins
pubmed
20351172
uniprot
proteins
pubmed
20364141
uniprot
proteins
pubmed
20513136
uniprot
proteins
pubmed
21144835
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21473589
uniprot
proteins
pubmed
21673012
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23086937
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23269703
uniprot
proteins
pubmed
23867111
uniprot
proteins
pubmed
24316840
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25472942
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
26341884
uniprot
proteins
pubmed
26778126
uniprot
proteins
pubmed
26807646
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28319063
uniprot
proteins
pubmed
28364669
uniprot
proteins
pubmed
29133208
uniprot
proteins
pubmed
34552057
uniprot
proteins
pubmed
36400755
uniprot
proteins
pubmed
7545954
uniprot
proteins
pubmed
7894491
uniprot
proteins
pubmed
7894493
uniprot
proteins
pubmed
7939630
uniprot
proteins
pubmed
8554067
uniprot
proteins
pubmed
8723683
uniprot
proteins
pubmed
8776600
uniprot
proteins
pubmed
8807330
uniprot
proteins
pubmed
8938427
uniprot
proteins
pubmed
8968716
uniprot
proteins
pubmed
8972225
uniprot
proteins
pubmed
9010228
uniprot
proteins
pubmed
9482581
uniprot
proteins
pubmed
9528852
uniprot
proteins
pubmed
9609997
uniprot
proteins
pubmed
9662397
uniprot
proteins
pubmed
9760198
uniprot
proteins
pubmed
9811458
uniprot
proteins
sequence_length
1863
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15133502, ECO:0000269|PubMed:17525340, ECO:0000269|PubMed:20160719, ECO:0000269|PubMed:21144835, ECO:0000269|PubMed:26778126, ECO:0000269|PubMed:9528852}. Chromosome {ECO:0000269|PubMed:23269703, ECO:0000269|PubMed:25472942, ECO:0000269|PubMed:26778126}. Cytoplasm {ECO:0000269|PubMed:20160719}. Note=Localizes at sites of DNA damage at double-strand breaks (DSBs); recruitment to DNA damage sites is mediated by ABRAXAS1 and the BRCA1-A complex (PubMed:26778126). Translocated to the cytoplasm during UV-induced apoptosis (PubMed:20160719). {ECO:0000269|PubMed:20160719, ECO:0000269|PubMed:26778126}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm.; SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm {ECO:0000269|PubMed:8972225}.
uniprot
proteins