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Fanconi anemia group J protein (Protein FACJ) (EC 3.6.4.13) (ATP-dependent RNA helicase BRIP1) (BRCA1-associated C-terminal helicase 1) (BRCA1-interacting protein C-terminal helicase 1) (BRCA1-interacting protein 1)

 FANCJ_HUMAN             Reviewed;        1249 AA.
Q9BX63; Q3MJE2; Q8NCI5;
04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
25-OCT-2017, entry version 153.
RecName: Full=Fanconi anemia group J protein;
Short=Protein FACJ;
EC=3.6.4.13;
AltName: Full=ATP-dependent RNA helicase BRIP1;
AltName: Full=BRCA1-associated C-terminal helicase 1;
AltName: Full=BRCA1-interacting protein C-terminal helicase 1;
Short=BRCA1-interacting protein 1;
Name=BRIP1; Synonyms=BACH1, FANCJ;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 708-747;
765-790; 815-831; 1079-1085; 1169-1174 AND 1215-1225, FUNCTION, TISSUE
SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH BRCA1, MUTAGENESIS
OF LYS-52, VARIANTS BC ALA-47 AND ILE-299, VARIANTS ILE-193 AND
SER-919, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=11301010; DOI=10.1016/S0092-8674(01)00304-X;
Cantor S.B., Bell D.W., Ganesan S., Kass E.M., Drapkin R.,
Grossman S., Wahrer D.C.R., Sgroi D.C., Lane W.S., Haber D.A.,
Livingston D.M.;
"BACH1, a novel helicase-like protein, interacts directly with BRCA1
and contributes to its DNA repair function.";
Cell 105:149-160(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 558-1249 (ISOFORM 2), AND
VARIANT SER-919.
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
PHOSPHORYLATION AT SER-990, AND MUTAGENESIS OF SER-986; SER-988;
THR-989; SER-990; PRO-991; THR-992; PHE-993; THR-997; SER-1001;
SER-1003; SER-1004; SER-1007; TYR-1011 AND THR-1013.
PubMed=14576433; DOI=10.1126/science.1088753;
Yu X., Chini C.C.S., He M., Mer G., Chen J.;
"The BRCT domain is a phospho-protein binding domain.";
Science 302:639-642(2003).
[6]
FUNCTION, MUTAGENESIS OF LYS-52, AND CHARACTERIZATION OF VARIANTS BC
ALA-47 AND ILE-299.
PubMed=14983014; DOI=10.1073/pnas.0308717101;
Cantor S.B., Drapkin R., Zhang F., Lin Y., Han J., Pamidi S.,
Livingston D.M.;
"The BRCA1-associated protein BACH1 is a DNA helicase targeted by
clinically relevant inactivating mutations.";
Proc. Natl. Acad. Sci. U.S.A. 101:2357-2362(2004).
[7]
FUNCTION, VARIANT SER-919, AND DISEASE.
PubMed=16153896; DOI=10.1016/j.ccr.2005.08.004;
Litman R., Peng M., Jin Z., Zhang F., Zhang J., Powell S.,
Andreassen P.R., Cantor S.B.;
"BACH1 is critical for homologous recombination and appears to be the
Fanconi anemia gene product FANCJ.";
Cancer Cell 8:255-265(2005).
[8]
FUNCTION, MUTAGENESIS OF LYS-52, AND DISEASE.
PubMed=16116421; DOI=10.1038/ng1627;
Bridge W.L., Vandenberg C.J., Franklin R.J., Hiom K.;
"The BRIP1 helicase functions independently of BRCA1 in the Fanconi
anemia pathway for DNA crosslink repair.";
Nat. Genet. 37:953-957(2005).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-927; SER-930 AND
SER-990, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-930 AND SER-1032, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1237, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
ACETYLATION AT LYS-1249.
PubMed=22792074; DOI=10.1371/journal.pgen.1002786;
Xie J., Peng M., Guillemette S., Quan S., Maniatis S., Wu Y.,
Venkatesh A., Shaffer S.A., Brosh R.M. Jr., Cantor S.B.;
"FANCJ/BACH1 acetylation at lysine 1249 regulates the DNA damage
response.";
PLoS Genet. 8:E1002786-E1002786(2012).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505; SER-956; SER-1004
AND SER-1032, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 985-998 IN COMPLEX WITH
BRCA1, AND SUBUNIT.
PubMed=15125843; DOI=10.1016/S1097-2765(04)00238-2;
Shiozaki E.N., Gu L., Yan N., Shi Y.;
"Structure of the BRCT repeats of BRCA1 bound to a BACH1
phosphopeptide: implications for signaling.";
Mol. Cell 14:405-412(2004).
[15]
VARIANTS CYS-173 AND SER-919.
PubMed=11920628; DOI=10.1002/ijc.10214;
Luo L., Lei H., Du Q., von Wachenfeldt A., Kockum I., Luthman H.,
Vorechovsky I., Lindblom A.;
"No mutations in the BACH1 gene in BRCA1 and BRCA2 negative breast-
cancer families linked to 17q22.";
Int. J. Cancer 98:638-639(2002).
[16]
VARIANTS SER-919 AND LEU-1034.
PubMed=12565990; DOI=10.1016/S0959-8049(02)00498-7;
Karppinen S.-M., Vuosku J., Heikkinen K., Allinen M., Winqvist R.;
"No evidence of involvement of germline BACH1 mutations in Finnish
breast and ovarian cancer families.";
Eur. J. Cancer 39:366-371(2003).
[17]
VARIANTS CYS-173; ILE-193; PRO-195; TRP-419; VAL-531; LEU-540;
TYR-832; SER-919 AND GLY-935.
PubMed=12872252; DOI=10.1002/humu.10238;
Rutter J.L., Smith A.M., Davila M.R., Sigurdson A.J., Giusti R.M.,
Pineda M.A., Doody M.M., Tucker M.A., Greene M.H., Zhang J.,
Struewing J.P.;
"Mutational analysis of the BRCA1-interacting genes ZNF350/ZBRK1 and
BRIP1/BACH1 among BRCA1 and BRCA2-negative probands from breast-
ovarian cancer families and among early-onset breast cancer cases and
reference individuals.";
Hum. Mutat. 22:121-128(2003).
[18]
VARIANT FANCJ PRO-349.
PubMed=16116424; DOI=10.1038/ng1624;
Levran O., Attwooll C., Henry R.T., Milton K.L., Neveling K., Rio P.,
Batish S.D., Kalb R., Velleuer E., Barral S., Ott J., Petrini J.,
Schindler D., Hanenberg H., Auerbach A.D.;
"The BRCA1-interacting helicase BRIP1 is deficient in Fanconi
anemia.";
Nat. Genet. 37:931-933(2005).
[19]
VARIANTS FANCJ HIS-255; CYS-647 AND CYS-707, AND VARIANT TRP-264.
PubMed=16116423; DOI=10.1038/ng1625;
Levitus M., Waisfisz Q., Godthelp B.C., Vries Y., Hussain S.,
Wiegant W.W., Elghalbzouri-Maghrani E., Steltenpool J., Rooimans M.A.,
Pals G., Arwert F., Mathew C.G., Zdzienicka M.Z., Hiom K.,
De Winter J.P., Joenje H.;
"The DNA helicase BRIP1 is defective in Fanconi anemia complementation
group J.";
Nat. Genet. 37:934-935(2005).
[20]
VARIANT [LARGE SCALE ANALYSIS] SER-919.
PubMed=18987736; DOI=10.1038/nature07485;
Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J.,
Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C.,
Graubert T.A., DiPersio J.F., Wilson R.K.;
"DNA sequencing of a cytogenetically normal acute myeloid leukaemia
genome.";
Nature 456:66-72(2008).
[21]
VARIANT FANCJ PRO-349, COFACTOR, AND CHARACTERIZATION OF VARIANT FANCJ
PRO-349.
PubMed=20639400; DOI=10.1182/blood-2009-11-256016;
Wu Y., Sommers J.A., Suhasini A.N., Leonard T., Deakyne J.S.,
Mazin A.V., Shin-Ya K., Kitao H., Brosh R.M. Jr.;
"Fanconi anemia group J mutation abolishes its DNA repair function by
uncoupling DNA translocation from helicase activity or disruption of
protein-DNA complexes.";
Blood 116:3780-3791(2010).
-!- FUNCTION: DNA-dependent ATPase and 5' to 3' DNA helicase required
for the maintenance of chromosomal stability. Acts late in the
Fanconi anemia pathway, after FANCD2 ubiquitination. Involved in
the repair of DNA double-strand breaks by homologous recombination
in a manner that depends on its association with BRCA1.
{ECO:0000269|PubMed:11301010, ECO:0000269|PubMed:14983014,
ECO:0000269|PubMed:16116421, ECO:0000269|PubMed:16153896}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000269|PubMed:20639400};
Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:20639400};
-!- SUBUNIT: Binds directly to the BRCT domains of BRCA1.
{ECO:0000269|PubMed:15125843}.
-!- INTERACTION:
P54132:BLM; NbExp=16; IntAct=EBI-3509650, EBI-621372;
P38398:BRCA1; NbExp=15; IntAct=EBI-3509650, EBI-349905;
P40692:MLH1; NbExp=11; IntAct=EBI-3509650, EBI-744248;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11301010}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9BX63-1; Sequence=Displayed;
Name=2;
IsoId=Q9BX63-2; Sequence=VSP_012540, VSP_012541;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
testis. {ECO:0000269|PubMed:11301010}.
-!- DOMAIN: 4Fe-4S iron-sulfur-binding is required for helicase
activity. {ECO:0000269|PubMed:20639400}.
-!- 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}.
-!- 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 variations
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 mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC11156.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Fanconi Anemia Mutation Database;
URL="http://www2.rockefeller.edu/fanconi/genes/jumpj";
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EMBL; AF360549; AAK38111.1; -; mRNA.
EMBL; AC002994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC005969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC060798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC101472; AAI01473.1; -; mRNA.
EMBL; BC101474; AAI01475.1; -; mRNA.
EMBL; AK074713; BAC11156.1; ALT_INIT; mRNA.
CCDS; CCDS11631.1; -. [Q9BX63-1]
RefSeq; NP_114432.2; NM_032043.2.
UniGene; Hs.128903; -.
PDB; 1T15; X-ray; 1.85 A; B=988-995.
PDB; 1T29; X-ray; 2.30 A; B=985-998.
PDB; 3AL3; X-ray; 2.15 A; B=1129-1138.
PDBsum; 1T15; -.
PDBsum; 1T29; -.
PDBsum; 3AL3; -.
ProteinModelPortal; Q9BX63; -.
SMR; Q9BX63; -.
BioGrid; 123841; 35.
CORUM; Q9BX63; -.
DIP; DIP-41787N; -.
ELM; Q9BX63; -.
IntAct; Q9BX63; 7.
MINT; MINT-275883; -.
STRING; 9606.ENSP00000259008; -.
BindingDB; Q9BX63; -.
iPTMnet; Q9BX63; -.
PhosphoSitePlus; Q9BX63; -.
BioMuta; BRIP1; -.
DMDM; 57012613; -.
EPD; Q9BX63; -.
MaxQB; Q9BX63; -.
PaxDb; Q9BX63; -.
PeptideAtlas; Q9BX63; -.
PRIDE; Q9BX63; -.
DNASU; 83990; -.
Ensembl; ENST00000259008; ENSP00000259008; ENSG00000136492.
GeneID; 83990; -.
KEGG; hsa:83990; -.
UCSC; uc002izk.3; human. [Q9BX63-1]
CTD; 83990; -.
DisGeNET; 83990; -.
EuPathDB; HostDB:ENSG00000136492.8; -.
GeneCards; BRIP1; -.
GeneReviews; BRIP1; -.
H-InvDB; HIX0202529; -.
HGNC; HGNC:20473; BRIP1.
HPA; HPA005474; -.
MalaCards; BRIP1; -.
MIM; 114480; phenotype.
MIM; 605882; gene.
MIM; 609054; phenotype.
neXtProt; NX_Q9BX63; -.
Orphanet; 84; Fanconi anemia.
Orphanet; 145; Hereditary breast and ovarian cancer syndrome.
PharmGKB; PA134906421; -.
eggNOG; KOG1132; Eukaryota.
eggNOG; COG1199; LUCA.
HOGENOM; HOG000068083; -.
HOVERGEN; HBG081519; -.
InParanoid; Q9BX63; -.
KO; K15362; -.
OrthoDB; EOG091G00LK; -.
PhylomeDB; Q9BX63; -.
TreeFam; TF329449; -.
BRENDA; 3.6.4.12; 2681.
Reactome; R-HSA-2564830; Cytosolic iron-sulfur cluster assembly.
Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA).
Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
Reactome; R-HSA-5693554; Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
Reactome; R-HSA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
Reactome; R-HSA-5693579; Homologous DNA Pairing and Strand Exchange.
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
SignaLink; Q9BX63; -.
EvolutionaryTrace; Q9BX63; -.
GeneWiki; BRIP1; -.
GenomeRNAi; 83990; -.
PRO; PR:Q9BX63; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000136492; -.
CleanEx; HS_BACH1; -.
CleanEx; HS_BRIP1; -.
ExpressionAtlas; Q9BX63; baseline and differential.
Genevisible; Q9BX63; HS.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0031965; C:nuclear membrane; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004003; F:ATP-dependent DNA helicase activity; NAS:UniProtKB.
GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:1904385; P:cellular response to angiotensin; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0071295; P:cellular response to vitamin; IEA:Ensembl.
GO; GO:0051026; P:chiasma assembly; IEA:Ensembl.
GO; GO:0000077; P:DNA damage checkpoint; NAS:UniProtKB.
GO; GO:0006260; P:DNA replication; TAS:Reactome.
GO; GO:0000731; P:DNA synthesis involved in DNA repair; TAS:Reactome.
GO; GO:0006302; P:double-strand break repair; NAS:UniProtKB.
GO; GO:1990918; P:double-strand break repair involved in meiotic recombination; IEA:Ensembl.
GO; GO:0010705; P:meiotic DNA double-strand break processing involved in reciprocal meiotic recombination; IEA:Ensembl.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
GO; GO:0072520; P:seminiferous tubule development; IEA:Ensembl.
GO; GO:0007286; P:spermatid development; IEA:Ensembl.
GO; GO:0007284; P:spermatogonial cell division; IEA:Ensembl.
GO; GO:0000732; P:strand displacement; TAS:Reactome.
InterPro; IPR006555; ATP-dep_Helicase_C.
InterPro; IPR010614; DEAD_2.
InterPro; IPR013020; DNA_helicase_DNA-repair_Rad3.
InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
InterPro; IPR006554; Helicase-like_DEXD_c2.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR027417; P-loop_NTPase.
Pfam; PF06733; DEAD_2; 1.
Pfam; PF13307; Helicase_C_2; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00488; DEXDc2; 1.
SMART; SM00491; HELICc2; 1.
SUPFAM; SSF52540; SSF52540; 6.
TIGRFAMs; TIGR00604; rad3; 1.
PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
1: Evidence at protein level;
3D-structure; 4Fe-4S; Acetylation; Alternative splicing; ATP-binding;
Complete proteome; Direct protein sequencing; Disease mutation;
DNA damage; DNA repair; Fanconi anemia; Helicase; Hydrolase; Iron;
Iron-sulfur; Metal-binding; Nucleotide-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 1249 Fanconi anemia group J protein.
/FTId=PRO_0000055173.
DOMAIN 11 442 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
NP_BIND 185 192 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 888 1063 Interaction with BRCA1.
{ECO:0000269|PubMed:11301010}.
MOTIF 158 175 Nuclear localization signal.
{ECO:0000255}.
MOTIF 393 396 DEAH box.
METAL 283 283 Iron-sulfur (4Fe-4S). {ECO:0000250}.
METAL 298 298 Iron-sulfur (4Fe-4S). {ECO:0000250}.
METAL 310 310 Iron-sulfur (4Fe-4S). {ECO:0000250}.
METAL 350 350 Iron-sulfur (4Fe-4S). {ECO:0000250}.
MOD_RES 505 505 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 927 927 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 930 930 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 956 956 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 990 990 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:14576433}.
MOD_RES 1004 1004 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1032 1032 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 1237 1237 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 1249 1249 N6-acetyllysine.
{ECO:0000269|PubMed:22792074}.
VAR_SEQ 969 994 NDPVFLEEAGKAEKIVISRSTSPTFN -> SMKSSSHLPLI
EKSFIIFSEMIFIWV (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_012540.
VAR_SEQ 995 1249 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_012541.
VARIANT 47 47 P -> A (in BC; early onset; loss of
ATPase and helicase activities;
dbSNP:rs28903098).
{ECO:0000269|PubMed:11301010,
ECO:0000269|PubMed:14983014}.
/FTId=VAR_020896.
VARIANT 173 173 R -> C (in dbSNP:rs4988345).
{ECO:0000269|PubMed:11920628,
ECO:0000269|PubMed:12872252}.
/FTId=VAR_020897.
VARIANT 193 193 V -> I (in dbSNP:rs4988346).
{ECO:0000269|PubMed:11301010,
ECO:0000269|PubMed:12872252}.
/FTId=VAR_020898.
VARIANT 195 195 L -> P (in dbSNP:rs4988347).
{ECO:0000269|PubMed:12872252}.
/FTId=VAR_020899.
VARIANT 255 255 Q -> H (in FANCJ).
{ECO:0000269|PubMed:16116423}.
/FTId=VAR_023700.
VARIANT 264 264 R -> W (rare polymorphism;
dbSNP:rs28997569).
{ECO:0000269|PubMed:16116423}.
/FTId=VAR_023701.
VARIANT 299 299 M -> I (in BC; early onset; reduces
helicase efficiency on longer
substrates).
{ECO:0000269|PubMed:11301010,
ECO:0000269|PubMed:14983014}.
/FTId=VAR_020900.
VARIANT 349 349 A -> P (in FANCJ; destabilizes iron-
sulfur-binding and abolishes helicase
activity). {ECO:0000269|PubMed:16116424,
ECO:0000269|PubMed:20639400}.
/FTId=VAR_023702.
VARIANT 419 419 R -> W. {ECO:0000269|PubMed:12872252}.
/FTId=VAR_020901.
VARIANT 531 531 F -> V (in dbSNP:rs4988350).
{ECO:0000269|PubMed:12872252}.
/FTId=VAR_020902.
VARIANT 540 540 Q -> L (in dbSNP:rs4988349).
{ECO:0000269|PubMed:12872252}.
/FTId=VAR_020903.
VARIANT 633 633 I -> M (in dbSNP:rs28997572).
/FTId=VAR_052192.
VARIANT 647 647 W -> C (in FANCJ; associated with C-707).
{ECO:0000269|PubMed:16116423}.
/FTId=VAR_023703.
VARIANT 707 707 R -> C (in FANCJ; associated with C-647).
{ECO:0000269|PubMed:16116423}.
/FTId=VAR_023704.
VARIANT 832 832 C -> Y (in dbSNP:rs4988355).
{ECO:0000269|PubMed:12872252}.
/FTId=VAR_020904.
VARIANT 919 919 P -> S (very frequent polymorphism;
dbSNP:rs4986764).
{ECO:0000269|PubMed:11301010,
ECO:0000269|PubMed:11920628,
ECO:0000269|PubMed:12565990,
ECO:0000269|PubMed:12872252,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:16153896,
ECO:0000269|PubMed:18987736}.
/FTId=VAR_020905.
VARIANT 935 935 V -> G (in dbSNP:rs4988356).
{ECO:0000269|PubMed:12872252}.
/FTId=VAR_020906.
VARIANT 1034 1034 P -> L (in a patient with ovarian cancer;
unknown pathological significance).
{ECO:0000269|PubMed:12565990}.
/FTId=VAR_020907.
VARIANT 1148 1148 D -> E (in dbSNP:rs28997573).
/FTId=VAR_052193.
MUTAGEN 52 52 K->R: Disrupts BRCA1-mediated double-
strand break repair. Loss of ATPase and
DNA helicase activities.
{ECO:0000269|PubMed:11301010,
ECO:0000269|PubMed:14983014,
ECO:0000269|PubMed:16116421}.
MUTAGEN 986 986 S->A: Does not affect the interaction
with BRCA1.
{ECO:0000269|PubMed:14576433}.
MUTAGEN 988 988 S->A: Does not affect the interaction
with BRCA1.
{ECO:0000269|PubMed:14576433}.
MUTAGEN 989 989 T->A: Does not affect the interaction
with BRCA1.
{ECO:0000269|PubMed:14576433}.
MUTAGEN 990 990 S->A: Disrupts the interaction with
BRCA1. {ECO:0000269|PubMed:14576433}.
MUTAGEN 991 991 P->A: Abolishes phosphorylation of S-990.
Impairs the interaction with BRCA1.
{ECO:0000269|PubMed:14576433}.
MUTAGEN 992 992 T->A: Does not affect the interaction
with BRCA1.
{ECO:0000269|PubMed:14576433}.
MUTAGEN 993 993 F->A: Abolishes phosphorylation of S-990.
Impairs the interaction with BRCA1.
{ECO:0000269|PubMed:14576433}.
MUTAGEN 997 997 T->A: Does not affect the interaction
with BRCA1.
{ECO:0000269|PubMed:14576433}.
MUTAGEN 1001 1001 S->A: Does not affect the interaction
with BRCA1.
{ECO:0000269|PubMed:14576433}.
MUTAGEN 1003 1003 S->A: Does not affect the interaction
with BRCA1.
{ECO:0000269|PubMed:14576433}.
MUTAGEN 1004 1004 S->A: Does not affect the interaction
with BRCA1.
{ECO:0000269|PubMed:14576433}.
MUTAGEN 1007 1007 S->A: Does not affect the interaction
with BRCA1.
{ECO:0000269|PubMed:14576433}.
MUTAGEN 1011 1011 Y->A: Does not affect the interaction
with BRCA1.
{ECO:0000269|PubMed:14576433}.
MUTAGEN 1013 1013 T->A: Does not affect the interaction
with BRCA1.
{ECO:0000269|PubMed:14576433}.
CONFLICT 641 641 I -> V (in Ref. 4; BAC11156).
{ECO:0000305}.
CONFLICT 767 767 E -> I (in Ref. 1; AA sequence).
{ECO:0000305}.
SEQUENCE 1249 AA; 140878 MW; 8FA4CDF15577D58E CRC64;
MSSMWSEYTI GGVKIYFPYK AYPSQLAMMN SILRGLNSKQ HCLLESPTGS GKSLALLCSA
LAWQQSLSGK PADEGVSEKA EVQLSCCCAC HSKDFTNNDM NQGTSRHFNY PSTPPSERNG
TSSTCQDSPE KTTLAAKLSA KKQASIYRDE NDDFQVEKKR IRPLETTQQI RKRHCFGTEV
HNLDAKVDSG KTVKLNSPLE KINSFSPQKP PGHCSRCCCS TKQGNSQESS NTIKKDHTGK
SKIPKIYFGT RTHKQIAQIT RELRRTAYSG VPMTILSSRD HTCVHPEVVG NFNRNEKCME
LLDGKNGKSC YFYHGVHKIS DQHTLQTFQG MCKAWDIEEL VSLGKKLKAC PYYTARELIQ
DADIIFCPYN YLLDAQIRES MDLNLKEQVV ILDEAHNIED CARESASYSV TEVQLRFARD
ELDSMVNNNI RKKDHEPLRA VCCSLINWLE ANAEYLVERD YESACKIWSG NEMLLTLHKM
GITTATFPIL QGHFSAVLQK EEKISPIYGK EEAREVPVIS ASTQIMLKGL FMVLDYLFRQ
NSRFADDYKI AIQQTYSWTN QIDISDKNGL LVLPKNKKRS RQKTAVHVLN FWCLNPAVAF
SDINGKVQTI VLTSGTLSPM KSFSSELGVT FTIQLEANHI IKNSQVWVGT IGSGPKGRNL
CATFQNTETF EFQDEVGALL LSVCQTVSQG ILCFLPSYKL LEKLKERWLS TGLWHNLELV
KTVIVEPQGG EKTNFDELLQ VYYDAIKYKG EKDGALLVAV CRGKVSEGLD FSDDNARAVI
TIGIPFPNVK DLQVELKRQY NDHHSKLRGL LPGRQWYEIQ AYRALNQALG RCIRHRNDWG
ALILVDDRFR NNPSRYISGL SKWVRQQIQH HSTFESALES LAEFSKKHQK VLNVSIKDRT
NIQDNESTLE VTSLKYSTPP YLLEAASHLS PENFVEDEAK ICVQELQCPK IITKNSPLPS
SIISRKEKND PVFLEEAGKA EKIVISRSTS PTFNKQTKRV SWSSFNSLGQ YFTGKIPKAT
PELGSSENSA SSPPRFKTEK MESKTVLPFT DKCESSNLTV NTSFGSCPQS ETIISSLKID
ATLTRKNHSE HPLCSEEALD PDIELSLVSE EDKQSTSNRD FETEAEDESI YFTPELYDPE
DTDEEKNDLA ETDRGNRLAN NSDCILAKDL FEIRTIKEVD SAREVKAEDC IDTKLNGILH
IEESKIDDID GNVKTTWINE LELGKTHEIE IKNFKPSPSK NKGMFPGFK


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