BRIP1
entrez
83990
canonical
uniprot
Q9BX63
canonical
ensembl
ENSG00000136492
resolver
ensp
ENSP00000259008
resolver
ensp
ENSP00000463272
resolver
ensp
ENSP00000507646
resolver
ensp
ENSP00000508184
resolver
ensp
ENSP00000524998
resolver
ensp
ENSP00000593557
resolver
ensp
ENSP00000736675
resolver
ensp
ENSP00000736676
resolver
enst
ENST00000584322
resolver
enst
ENST00000683235
resolver
enst
ENST00000683381
resolver
genesymbol
BRIP1
resolver
genesymbol_syn
BACH1
resolver
genesymbol_syn
FANCJ
resolver
hgnc
HGNC:20473
resolver
uniprot
A0A024QZ45
resolver
uniprot
A0A804HJU1
resolver
uniprot
A0A804HL36
resolver
uniprot
J3QKX0
resolver
uniprot
Q3MJE2
resolver
uniprot
Q8NCI5
resolver
uniprot_entry
A0A804HJU1_HUMAN
resolver
uniprot_entry
A0A804HL36_HUMAN
resolver
uniprot_entry
FANCJ_HUMAN
resolver
uniprot_entry
J3QKX0_HUMAN
resolver
uniprot_sec
A0A024QZ45
resolver
uniprot_sec
Q3MJE2
resolver
uniprot_sec
Q8NCI5
resolver
activity_regulation
ACTIVITY REGULATION: Helicase activity on forked substrates is stimulated by replication protein A complex heterotrimer (RPA1, RPA2, RPA3) (PubMed:17596542). Helicase activity on G-quadruplex DNA is stimulated 3-fold by RPA, and inhibited by MSH2/MSH6 (PubMed:18426915). Unwinding of G-quadruplex DNA is inhibited by ATP-gamma-S and telomestatin (TMS); TMA does not inhibit unwinding of forked-duplex DNA (PubMed:18426915). Helicase activity on dsDNA and G-quadruplex DNA is inhibited by porphyrin derivatives meso-tetra (N-methyl-4-pyridyl) porphine tetra tosylate (T4) and N-methyl mesoporphyrin IX (NMM) (PubMed:18426915). {ECO:0000269|PubMed:17596542, ECO:0000269|PubMed:18426915}.
uniprot
proteins
amino_acid_sequence
MSSMWSEYTIGGVKIYFPYKAYPSQLAMMNSILRGLNSKQHCLLESPTGSGKSLALLCSALAWQQSLSGKPADEGVSEKAEVQLSCCCACHSKDFTNNDMNQGTSRHFNYPSTPPSERNGTSSTCQDSPEKTTLAAKLSAKKQASIYRDENDDFQVEKKRIRPLETTQQIRKRHCFGTEVHNLDAKVDSGKTVKLNSPLEKINSFSPQKPPGHCSRCCCSTKQGNSQESSNTIKKDHTGKSKIPKIYFGTRTHKQIAQITRELRRTAYSGVPMTILSSRDHTCVHPEVVGNFNRNEKCMELLDGKNGKSCYFYHGVHKISDQHTLQTFQGMCKAWDIEELVSLGKKLKACPYYTARELIQDADIIFCPYNYLLDAQIRESMDLNLKEQVVILDEAHNIEDCARESASYSVTEVQLRFARDELDSMVNNNIRKKDHEPLRAVCCSLINWLEANAEYLVERDYESACKIWSGNEMLLTLHKMGITTATFPILQGHFSAVLQKEEKISPIYGKEEAREVPVISASTQIMLKGLFMVLDYLFRQNSRFADDYKIAIQQTYSWTNQIDISDKNGLLVLPKNKKRSRQKTAVHVLNFWCLNPAVAFSDINGKVQTIVLTSGTLSPMKSFSSELGVTFTIQLEANHIIKNSQVWVGTIGSGPKGRNLCATFQNTETFEFQDEVGALLLSVCQTVSQGILCFLPSYKLLEKLKERWLSTGLWHNLELVKTVIVEPQGGEKTNFDELLQVYYDAIKYKGEKDGALLVAVCRGKVSEGLDFSDDNARAVITIGIPFPNVKDLQVELKRQYNDHHSKLRGLLPGRQWYEIQAYRALNQALGRCIRHRNDWGALILVDDRFRNNPSRYISGLSKWVRQQIQHHSTFESALESLAEFSKKHQKVLNVSIKDRTNIQDNESTLEVTSLKYSTSPYLLEAASHLSPENFVEDEAKICVQELQCPKIITKNSPLPSSIISRKEKNDPVFLEEAGKAEKIVISRSTSPTFNKQTKRVSWSSFNSLGQYFTGKIPKATPELGSSENSASSPPRFKTEKMESKTVLPFTDKCESSNLTVNTSFGSCPQSETIISSLKIDATLTRKNHSEHPLCSEEALDPDIELSLVSEEDKQSTSNRDFETEAEDESIYFTPELYDPEDTDEEKNDLAETDRGNRLANNSDCILAKDLFEIRTIKEVDSAREVKAEDCIDTKLNGILHIEESKIDDIDGNVKTTWINELELGKTHEIEIKNFKPSPSKNKGMFPGFK
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:11301010, ECO:0000269|PubMed:14983014}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry.; DISEASE: Fanconi anemia complementation group J (FANCJ) [MIM:609054]: 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:16116423, ECO:0000269|PubMed:16116424, ECO:0000269|PubMed:20639400}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
5.6.2.3
uniprot
proteins
function
FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of chromosomal stability (PubMed:11301010, PubMed:14983014, PubMed:16116421, PubMed:16153896, PubMed:17596542, PubMed:36608669). Acts late in the Fanconi anemia pathway, after FANCD2 ubiquitination (PubMed:14983014, PubMed:16153896). Involved in the repair of DNA double-strand breaks by homologous recombination in a manner that depends on its association with BRCA1 (PubMed:14983014, PubMed:16153896). Involved in the repair of abasic sites at replication forks by promoting the degradation of DNA-protein cross-links: acts by catalyzing unfolding of HMCES DNA-protein cross-link via its helicase activity, exposing the underlying DNA and enabling cleavage of the DNA-protein adduct by the SPRTN metalloprotease (PubMed:16116421, PubMed:36608669). Can unwind RNA:DNA substrates (PubMed:14983014). Unwinds G-quadruplex DNA; unwinding requires a 5'-single stranded tail (PubMed:18426915, PubMed:20639400). {ECO:0000269|PubMed:11301010, ECO:0000269|PubMed:14983014, ECO:0000269|PubMed:16116421, ECO:0000269|PubMed:16153896, ECO:0000269|PubMed:17596542, ECO:0000269|PubMed:18426915, ECO:0000269|PubMed:20639400, ECO:0000269|PubMed:36608669}.
uniprot
proteins
mass_dalton
140867
uniprot
proteins
mutagenesis
MUTAGEN 52; /note="K->R: Abolishes ATPase and dsDNA helicase activities, preventing ability to unfold DNA-protein cross-links. Does not unwind G-quadruplex DNA. Disrupts BRCA1-mediated double-strand break repair."; /evidence="ECO:0000269|PubMed:11301010, ECO:0000269|PubMed:14983014, ECO:0000269|PubMed:16116421, ECO:0000269|PubMed:18426915, ECO:0000269|PubMed:36608669"; MUTAGEN 986; /note="S->A: Does not affect the interaction with BRCA1."; /evidence="ECO:0000269|PubMed:14576433"; MUTAGEN 988; /note="S->A: Does not affect the interaction with BRCA1."; /evidence="ECO:0000269|PubMed:14576433"; MUTAGEN 989; /note="T->A: Does not affect the interaction with BRCA1."; /evidence="ECO:0000269|PubMed:14576433"; MUTAGEN 990; /note="S->A: Disrupts the interaction with BRCA1."; /evidence="ECO:0000269|PubMed:14576433"; MUTAGEN 991; /note="P->A: Abolishes phosphorylation of S-990. Impairs the interaction with BRCA1."; /evidence="ECO:0000269|PubMed:14576433"; MUTAGEN 992; /note="T->A: Does not affect the interaction with BRCA1."; /evidence="ECO:0000269|PubMed:14576433"; MUTAGEN 993; /note="F->A: Abolishes phosphorylation of S-990. Impairs the interaction with BRCA1."; /evidence="ECO:0000269|PubMed:14576433"; MUTAGEN 997; /note="T->A: Does not affect the interaction with BRCA1."; /evidence="ECO:0000269|PubMed:14576433"; MUTAGEN 1001; /note="S->A: Does not affect the interaction with BRCA1."; /evidence="ECO:0000269|PubMed:14576433"; MUTAGEN 1003; /note="S->A: Does not affect the interaction with BRCA1."; /evidence="ECO:0000269|PubMed:14576433"; MUTAGEN 1004; /note="S->A: Does not affect the interaction with BRCA1."; /evidence="ECO:0000269|PubMed:14576433"; MUTAGEN 1007; /note="S->A: Does not affect the interaction with BRCA1."; /evidence="ECO:0000269|PubMed:14576433"; MUTAGEN 1011; /note="Y->A: Does not affect the interaction with BRCA1."; /evidence="ECO:0000269|PubMed:14576433"; MUTAGEN 1013; /note="T->A: Does not affect the interaction with BRCA1."; /evidence="ECO:0000269|PubMed:14576433
uniprot
proteins
post_translational_modification
PTM: Phosphorylated. Phosphorylation is necessary for interaction with BRCA1, and is cell-cycle regulated. {ECO:0000269|PubMed:14576433}.; PTM: Acetylation at Lys-1249 facilitates DNA end processing required for repair and checkpoint signaling. {ECO:0000269|PubMed:22792074}.
uniprot
proteins
protein_family
DEAD box helicase family
uniprot
proteins
protein_family
DEAH subfamily
uniprot
proteins
pubmed
11301010
uniprot
proteins
pubmed
11920628
uniprot
proteins
pubmed
12565990
uniprot
proteins
pubmed
12872252
uniprot
proteins
pubmed
14576433
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14983014
uniprot
proteins
pubmed
15125843
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16116421
uniprot
proteins
pubmed
16116423
uniprot
proteins
pubmed
16116424
uniprot
proteins
pubmed
16153896
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
16973432
uniprot
proteins
pubmed
17596542
uniprot
proteins
pubmed
18426915
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18987736
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20639400
uniprot
proteins
pubmed
22792074
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23585563
uniprot
proteins
pubmed
36608669
uniprot
proteins
sequence_length
1249
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11301010, ECO:0000269|PubMed:17596542, ECO:0000269|PubMed:23585563}. Cytoplasm {ECO:0000269|PubMed:23585563}.
uniprot
proteins