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A0A2R9AJD0 · A0A2R9AJD0_PANPA

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. It is unclear whether it also mediates the formation of other types of polyubiquitin chains. 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 appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle. Required for FANCD2 targeting to sites of DNA damage. 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.

Catalytic activity

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.
    EC:2.3.2.27 (UniProtKB | ENZYME | Rhea)

GO annotations

AspectTerm
Cellular ComponentBRCA1-A complex
Cellular ComponentBRCA1-BARD1 complex
Cellular Componentchromosome
Cellular Componentcytoplasm
Cellular Componentplasma membrane
Molecular FunctionDNA binding
Molecular Functionubiquitin-protein transferase activity
Molecular Functionzinc ion binding
Biological Processchordate embryonic development
Biological Processdosage compensation by inactivation of X chromosome
Biological Processdouble-strand break repair via homologous recombination
Biological Processfatty acid biosynthetic process
Biological Processnegative regulation of fatty acid biosynthetic process
Biological Processpositive regulation of transcription by RNA polymerase II
Biological Processprotein autoubiquitination
Biological Processprotein K6-linked ubiquitination

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Breast cancer type 1 susceptibility protein homolog
  • EC number

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Pan

Accessions

  • Primary accession
    A0A2R9AJD0

Proteomes

Subcellular Location

Chromosome
Cytoplasm
Nucleus
Note: Localizes at sites of DNA damage at double-strand breaks (DSBs); recruitment to DNA damage sites is mediated by the BRCA1-A complex.

Keywords

PTM/Processing

Keywords

Expression

Gene expression databases

Interaction

Subunit

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. Interacts with EXD2. Interacts (via C-terminus) with DHX9; this interaction is direct and links BRCA1 to the RNA polymerase II holoenzyme.

Family & Domains

Features

Showing features for domain, compositional bias, region, coiled coil.

Type
IDPosition(s)Description
Domain24-65RING-type
Compositional bias230-248Polar residues
Region230-267Disordered
Region306-338Disordered
Compositional bias324-338Basic and acidic residues
Region650-739Disordered
Compositional bias665-698Basic and acidic residues
Compositional bias701-721Polar residues
Compositional bias723-739Basic and acidic residues
Compositional bias896-911Basic and acidic residues
Region896-915Disordered
Compositional bias1174-1189Polar residues
Region1174-1209Disordered
Region1315-1388Disordered
Compositional bias1331-1346Basic and acidic residues
Compositional bias1347-1388Polar residues
Coiled coil1390-1417
Compositional bias1433-1461Polar residues
Region1433-1498Disordered
Compositional bias1471-1485Polar residues
Region1558-1635Disordered
Compositional bias1606-1621Polar residues
Domain1635-1729BRCT
Domain1738-1837BRCT

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,845
  • Mass (Da)
    205,923
  • Last updated
    2018-06-20 v1
  • MD5 Checksum
    DEA729BACCBDA5116F4C0CA070436FA7
MDLSALRVEEVQNVINAMQKILECPICLELIKEPVSTKCDHIFCKFCMLKLLNQKKGPSQCPLCKNDITKRSLQESTRFSQLVEELLKIICAFQLDTGLEYANSYNFAKKENNSPEHLKDEVSIIQSMGYRNRAKRLLQSEPENPSLQETSLSVQLSNLGTVRTLRTKQRIQPQKKSVYIELGSDSSEDTVNKATYCSVGDQELLQITPQGTRNEISLDSAKKAACEFSETDVTNTEHHQPSNNDLNTTEKRATERHPEKYQGSSVSNLHVEPCGTNTHASSLQHENSSLLLTKDRMNVEKAEFCNKSKQPGLARSQHNRWAGSKETCNDRRTPSTEKKVDLNADPLCERKEWNKQKLPCSENPRDTEDVPWITLNSSIQKVNEWFSRSDELLGSDDSHDGGSESNAKVADVLDVLNEVDEYSGSSEKIDLLASDPHEALICKSERVHSKSVESNTEDKIFGKTYRRKASLPNLSHVTENLIIGAFVTEPQIIQERPLTNKLKRKRRATSGLHPEDFIKKADLAVQKTPEMINQGTNQMEQNGQVMNITNSGHENKTKGDSIQNEKNPNPIESLEKESAFKTKAEPISSSISNMELELNIHNSKAPKKNRLRRKSSTRHIHALELVVSRNLSPPNCTELQIDSCSSSEEIKKKKYNQMPVRHSRNLQLMEDKEPATGVKKSNKPNEQTSKRHDSDTFPELKLTNAPGSFTNCSNTSELKEFVNPSLPREEKEEKLETVKVSNNAEDPKDLMLSGERVLQTERSVESSSISLVPGTDYGTQESISLLEVSTLGKAKTEPNKCVSQCAAFENPKGLIHGCSKDTRNDTEGFKYPLGHEVNHSRETSIEMEESELDAQYLQNTFKVSKRQSFALFSNPGNPEEECATFSAHCRSLKKQSPKVTFEREQKEQNQGKNESNIKPVQTVNITAGFPVVCQKDKPVDYAKCSIKGGSRFCLSSQFRGNETGLITPNKHGLLQNPYHIPPLFPIKSFVKTKCKKNLLEENFEEHSMSPEREMGNENIPSTVSTISRNNIRENLFKEASSSNINEVGSSINEVGSSDENIQAELGRNRGPKLNAMLRLGVLQPEVYKQSLPGSNCKHPEIKKQEYEEVVQTVNTDFSPCLISDNLEQPMGSSHASQVCSETPDDLLDDGEIKEDTSFAENDIKESSAVFSKSVQRGELSRSPSPFTHTHLAQGYRRGAKKLESSEENLSSEDEELPCFQHLLFGKVSNIPSQSTRHSTVATECLSKNTEENLLSLKNSLNDCSNQVILAKASQEHHLSEETKCSASLFSSQCSELEDLTANTNTQDPFLIGSSKQMRHQSEIQGVGLSDKELVSDDEERGTGLEENNQEEQSMDSNLGEAASGCESETSVSEDCSGLSSQSDILTTQQRDTMQDNLIKLQQEMAELEAVLEQHGSQPSNSYPSIISDSSALEDLQNPEQSTSEKAVLTSQKSSEYPISQNPEGLSADKFEVSADSSTSKNKEPGVERSSPSKCPSLDDRWYMHSCSGSLQNRNYPSQEELIKVVDVEEQQLEESGPHDLTETSYLPRQDLEGTPYLESGISLFSDDPESDPSEDKAPESAHVGNIPSSTSALKVPQLKVAESAQSPAAAHTTNTAGYNAMEESVSREKPELTASTERVNKRMSMVVSGLTPEEFMLVYKFARKHHITLTNLITEETTHVVMKTDAEFVCERTLKYFLGIAGGKWVVSYFWVTQSIKERKMLNEIFLLSIPLSLSLPLFFQIFRGLEICCYGPFTNMPTDQLEWMVQLCGASVVKELSSFTLGTGVHPIVVVQPDAWTEDNGFHAIGQMCEAPVVTREWVLDSVALYQCQELDTYLIPQIPHSHY

Computationally mapped potential isoform sequences

There are 6 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A2R9AFG1A0A2R9AFG1_PANPA1849
A0A2R9ADZ2A0A2R9ADZ2_PANPA145
A0A2R9AFP9A0A2R9AFP9_PANPA96
A0A2R9AFJ2A0A2R9AFJ2_PANPA693
A0A2R9AEP6A0A2R9AEP6_PANPA59
A0A2R9AJH1A0A2R9AJH1_PANPA671

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias230-248Polar residues
Compositional bias324-338Basic and acidic residues
Compositional bias665-698Basic and acidic residues
Compositional bias701-721Polar residues
Compositional bias723-739Basic and acidic residues
Compositional bias896-911Basic and acidic residues
Compositional bias1174-1189Polar residues
Compositional bias1331-1346Basic and acidic residues
Compositional bias1347-1388Polar residues
Compositional bias1433-1461Polar residues
Compositional bias1471-1485Polar residues
Compositional bias1606-1621Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJFE02044625
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AJFE02044626
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AJFE02044627
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AJFE02044628
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AJFE02044629
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AJFE02044630
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AJFE02044631
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AJFE02044632
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AJFE02044633
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AJFE02044634
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

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