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Q9BX63 (FANCJ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fanconi anemia group J protein

Short name=Protein FACJ
EC=3.6.4.13
Alternative name(s):
ATP-dependent RNA helicase BRIP1
BRCA1-associated C-terminal helicase 1
BRCA1-interacting protein C-terminal helicase 1
Short name=BRCA1-interacting protein 1
Gene names
Name:BRIP1
Synonyms:BACH1, FANCJ
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1249 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1 Ref.6 Ref.7 Ref.8

Catalytic activity

ATP + H2O = ADP + phosphate.

Cofactor

Binds 1 4Fe-4S cluster. Ref.20

Subunit structure

Binds directly to the BRCT domains of BRCA1. Ref.13

Subcellular location

Nucleus Ref.1.

Tissue specificity

Ubiquitously expressed, with highest levels in testis. Ref.1

Domain

4Fe-4S iron-sulfur-binding is required for helicase activity (Ref.20).

Post-translational modification

Phosphorylated. Phosphorylation is necessary for interaction with BRCA1, and is cell-cycle regulated. Ref.5

Acetylation at Lys-1249 facilitates DNA end processing required for repair and checkpoint signaling. Ref.12

Involvement in 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.
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.1 Ref.6 Ref.7 Ref.8

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.8 Ref.17 Ref.18 Ref.20

Sequence similarities

Belongs to the DEAD box helicase family. DEAH subfamily.

Contains 1 helicase ATP-binding domain.

Sequence caution

The sequence BAC11156.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Fanconi anemia
   Ligand4Fe-4S
ATP-binding
Iron
Iron-sulfur
Metal-binding
Nucleotide-binding
   Molecular functionHelicase
Hydrolase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage checkpoint

Non-traceable author statement Ref.5. Source: UniProtKB

DNA duplex unwinding

Non-traceable author statement Ref.1. Source: GOC

double-strand break repair

Non-traceable author statement Ref.1. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 14504288. Source: MGI

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 14504288. Source: MGI

nuclear membrane

Inferred from direct assay. Source: HPA

nucleus

Non-traceable author statement Ref.1. Source: UniProtKB

   Molecular_function4 iron, 4 sulfur cluster binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent DNA helicase activity

Non-traceable author statement Ref.1. Source: UniProtKB

DNA binding

Non-traceable author statement PubMed 15878853. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BX63-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9BX63-2)

The sequence of this isoform differs from the canonical sequence as follows:
     969-994: NDPVFLEEAGKAEKIVISRSTSPTFN → SMKSSSHLPLIEKSFIIFSEMIFIWV
     995-1249: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12491249Fanconi anemia group J protein
PRO_0000055173

Regions

Domain11 – 442432Helicase ATP-binding
Nucleotide binding185 – 1928ATP By similarity
Region888 – 1063176Interaction with BRCA1
Motif158 – 17518Nuclear localization signal Potential
Motif393 – 3964DEAH box

Sites

Metal binding2831Iron-sulfur (4Fe-4S) By similarity
Metal binding2981Iron-sulfur (4Fe-4S) By similarity
Metal binding3101Iron-sulfur (4Fe-4S) By similarity
Metal binding3501Iron-sulfur (4Fe-4S) By similarity

Amino acid modifications

Modified residue9271Phosphoserine Ref.9
Modified residue9301Phosphoserine Ref.9 Ref.10
Modified residue9901Phosphoserine Ref.5 Ref.9
Modified residue10321Phosphoserine Ref.10
Modified residue12371Phosphoserine Ref.11
Modified residue12491N6-acetyllysine Ref.12

Natural variations

Alternative sequence969 – 99426NDPVF…SPTFN → SMKSSSHLPLIEKSFIIFSE MIFIWV in isoform 2.
VSP_012540
Alternative sequence995 – 1249255Missing in isoform 2.
VSP_012541
Natural variant471P → A in BC; early onset; loss of ATPase and helicase activities. Ref.1 Ref.6
Corresponds to variant rs28903098 [ dbSNP | Ensembl ].
VAR_020896
Natural variant1731R → C. Ref.14 Ref.16
Corresponds to variant rs4988345 [ dbSNP | Ensembl ].
VAR_020897
Natural variant1931V → I. Ref.1 Ref.16
Corresponds to variant rs4988346 [ dbSNP | Ensembl ].
VAR_020898
Natural variant1951L → P. Ref.16
Corresponds to variant rs4988347 [ dbSNP | Ensembl ].
VAR_020899
Natural variant2551Q → H in FANCJ. Ref.18
VAR_023700
Natural variant2641R → W Rare polymorphism. Ref.18
Corresponds to variant rs28997569 [ dbSNP | Ensembl ].
VAR_023701
Natural variant2991M → I in BC; early onset; reduces helicase efficiency on longer substrates. Ref.1 Ref.6
VAR_020900
Natural variant3491A → P in FANCJ; destabilizes iron-sulfur-binding and abolishes helicase activity. Ref.17 Ref.20
VAR_023702
Natural variant4191R → W. Ref.16
VAR_020901
Natural variant5311F → V. Ref.16
Corresponds to variant rs4988350 [ dbSNP | Ensembl ].
VAR_020902
Natural variant5401Q → L. Ref.16
Corresponds to variant rs4988349 [ dbSNP | Ensembl ].
VAR_020903
Natural variant6331I → M.
Corresponds to variant rs28997572 [ dbSNP | Ensembl ].
VAR_052192
Natural variant6471W → C in FANCJ; associated with C-707. Ref.18
VAR_023703
Natural variant7071R → C in FANCJ; associated with C-647. Ref.18
VAR_023704
Natural variant8321C → Y. Ref.16
Corresponds to variant rs4988355 [ dbSNP | Ensembl ].
VAR_020904
Natural variant9191P → S Very frequent polymorphism. Ref.1 Ref.4 Ref.7 Ref.14 Ref.15 Ref.16 Ref.19
Corresponds to variant rs4986764 [ dbSNP | Ensembl ].
VAR_020905
Natural variant9351V → G. Ref.16
Corresponds to variant rs4988356 [ dbSNP | Ensembl ].
VAR_020906
Natural variant10341P → L in a patient with ovarian cancer; unknown pathological significance. Ref.15
VAR_020907
Natural variant11481D → E.
Corresponds to variant rs28997573 [ dbSNP | Ensembl ].
VAR_052193

Experimental info

Mutagenesis521K → R: Disrupts BRCA1-mediated double-strand break repair. Loss of ATPase and DNA helicase activities. Ref.1 Ref.6 Ref.8
Mutagenesis9861S → A: Does not affect the interaction with BRCA1. Ref.5
Mutagenesis9881S → A: Does not affect the interaction with BRCA1. Ref.5
Mutagenesis9891T → A: Does not affect the interaction with BRCA1. Ref.5
Mutagenesis9901S → A: Disrupts the interaction with BRCA1. Ref.5
Mutagenesis9911P → A: Abolishes phosphorylation of S-990. Impairs the interaction with BRCA1. Ref.5
Mutagenesis9921T → A: Does not affect the interaction with BRCA1. Ref.5
Mutagenesis9931F → A: Abolishes phosphorylation of S-990. Impairs the interaction with BRCA1. Ref.5
Mutagenesis9971T → A: Does not affect the interaction with BRCA1. Ref.5
Mutagenesis10011S → A: Does not affect the interaction with BRCA1. Ref.5
Mutagenesis10031S → A: Does not affect the interaction with BRCA1. Ref.5
Mutagenesis10041S → A: Does not affect the interaction with BRCA1. Ref.5
Mutagenesis10071S → A: Does not affect the interaction with BRCA1. Ref.5
Mutagenesis10111Y → A: Does not affect the interaction with BRCA1. Ref.5
Mutagenesis10131T → A: Does not affect the interaction with BRCA1. Ref.5
Sequence conflict6411I → V in BAC11156. Ref.4
Sequence conflict7671E → I AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 8FA4CDF15577D58E

FASTA1,249140,878
        10         20         30         40         50         60 
MSSMWSEYTI GGVKIYFPYK AYPSQLAMMN SILRGLNSKQ HCLLESPTGS GKSLALLCSA 

        70         80         90        100        110        120 
LAWQQSLSGK PADEGVSEKA EVQLSCCCAC HSKDFTNNDM NQGTSRHFNY PSTPPSERNG 

       130        140        150        160        170        180 
TSSTCQDSPE KTTLAAKLSA KKQASIYRDE NDDFQVEKKR IRPLETTQQI RKRHCFGTEV 

       190        200        210        220        230        240 
HNLDAKVDSG KTVKLNSPLE KINSFSPQKP PGHCSRCCCS TKQGNSQESS NTIKKDHTGK 

       250        260        270        280        290        300 
SKIPKIYFGT RTHKQIAQIT RELRRTAYSG VPMTILSSRD HTCVHPEVVG NFNRNEKCME 

       310        320        330        340        350        360 
LLDGKNGKSC YFYHGVHKIS DQHTLQTFQG MCKAWDIEEL VSLGKKLKAC PYYTARELIQ 

       370        380        390        400        410        420 
DADIIFCPYN YLLDAQIRES MDLNLKEQVV ILDEAHNIED CARESASYSV TEVQLRFARD 

       430        440        450        460        470        480 
ELDSMVNNNI RKKDHEPLRA VCCSLINWLE ANAEYLVERD YESACKIWSG NEMLLTLHKM 

       490        500        510        520        530        540 
GITTATFPIL QGHFSAVLQK EEKISPIYGK EEAREVPVIS ASTQIMLKGL FMVLDYLFRQ 

       550        560        570        580        590        600 
NSRFADDYKI AIQQTYSWTN QIDISDKNGL LVLPKNKKRS RQKTAVHVLN FWCLNPAVAF 

       610        620        630        640        650        660 
SDINGKVQTI VLTSGTLSPM KSFSSELGVT FTIQLEANHI IKNSQVWVGT IGSGPKGRNL 

       670        680        690        700        710        720 
CATFQNTETF EFQDEVGALL LSVCQTVSQG ILCFLPSYKL LEKLKERWLS TGLWHNLELV 

       730        740        750        760        770        780 
KTVIVEPQGG EKTNFDELLQ VYYDAIKYKG EKDGALLVAV CRGKVSEGLD FSDDNARAVI 

       790        800        810        820        830        840 
TIGIPFPNVK DLQVELKRQY NDHHSKLRGL LPGRQWYEIQ AYRALNQALG RCIRHRNDWG 

       850        860        870        880        890        900 
ALILVDDRFR NNPSRYISGL SKWVRQQIQH HSTFESALES LAEFSKKHQK VLNVSIKDRT 

       910        920        930        940        950        960 
NIQDNESTLE VTSLKYSTPP YLLEAASHLS PENFVEDEAK ICVQELQCPK IITKNSPLPS 

       970        980        990       1000       1010       1020 
SIISRKEKND PVFLEEAGKA EKIVISRSTS PTFNKQTKRV SWSSFNSLGQ YFTGKIPKAT 

      1030       1040       1050       1060       1070       1080 
PELGSSENSA SSPPRFKTEK MESKTVLPFT DKCESSNLTV NTSFGSCPQS ETIISSLKID 

      1090       1100       1110       1120       1130       1140 
ATLTRKNHSE HPLCSEEALD PDIELSLVSE EDKQSTSNRD FETEAEDESI YFTPELYDPE 

      1150       1160       1170       1180       1190       1200 
DTDEEKNDLA ETDRGNRLAN NSDCILAKDL FEIRTIKEVD SAREVKAEDC IDTKLNGILH 

      1210       1220       1230       1240 
IEESKIDDID GNVKTTWINE LELGKTHEIE IKNFKPSPSK NKGMFPGFK 

« Hide

Isoform 2 [UniParc].

Checksum: 14BFE3010AA0145C
Show »

FASTA994112,476

References

« Hide 'large scale' references
[1]"BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function."
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.
Cell 105:149-160(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY.
[2]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
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. expand/collapse author list , 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.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 558-1249 (ISOFORM 2), VARIANT SER-919.
[5]"The BRCT domain is a phospho-protein binding domain."
Yu X., Chini C.C.S., He M., Mer G., Chen J.
Science 302:639-642(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-990, 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.
[6]"The BRCA1-associated protein BACH1 is a DNA helicase targeted by clinically relevant inactivating mutations."
Cantor S.B., Drapkin R., Zhang F., Lin Y., Han J., Pamidi S., Livingston D.M.
Proc. Natl. Acad. Sci. U.S.A. 101:2357-2362(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF LYS-52, CHARACTERIZATION OF VARIANTS BC ALA-47 AND ILE-299.
[7]"BACH1 is critical for homologous recombination and appears to be the Fanconi anemia gene product FANCJ."
Litman R., Peng M., Jin Z., Zhang F., Zhang J., Powell S., Andreassen P.R., Cantor S.B.
Cancer Cell 8:255-265(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, VARIANT SER-919, DISEASE.
[8]"The BRIP1 helicase functions independently of BRCA1 in the Fanconi anemia pathway for DNA crosslink repair."
Bridge W.L., Vandenberg C.J., Franklin R.J., Hiom K.
Nat. Genet. 37:953-957(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF LYS-52, DISEASE.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-927; SER-930 AND SER-990, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-930 AND SER-1032, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1237, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"FANCJ/BACH1 acetylation at lysine 1249 regulates the DNA damage response."
Xie J., Peng M., Guillemette S., Quan S., Maniatis S., Wu Y., Venkatesh A., Shaffer S.A., Brosh R.M. Jr., Cantor S.B.
PLoS Genet. 8:E1002786-E1002786(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT LYS-1249.
[13]"Structure of the BRCT repeats of BRCA1 bound to a BACH1 phosphopeptide: implications for signaling."
Shiozaki E.N., Gu L., Yan N., Shi Y.
Mol. Cell 14:405-412(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 985-998 IN COMPLEX WITH BRCA1, SUBUNIT.
[14]"No mutations in the BACH1 gene in BRCA1 and BRCA2 negative breast-cancer families linked to 17q22."
Luo L., Lei H., Du Q., von Wachenfeldt A., Kockum I., Luthman H., Vorechovsky I., Lindblom A.
Int. J. Cancer 98:638-639(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CYS-173 AND SER-919.
[15]"No evidence of involvement of germline BACH1 mutations in Finnish breast and ovarian cancer families."
Karppinen S.-M., Vuosku J., Heikkinen K., Allinen M., Winqvist R.
Eur. J. Cancer 39:366-371(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SER-919 AND LEU-1034.
[16]"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."
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.
Hum. Mutat. 22:121-128(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CYS-173; ILE-193; PRO-195; TRP-419; VAL-531; LEU-540; TYR-832; SER-919 AND GLY-935.
[17]"The BRCA1-interacting helicase BRIP1 is deficient in Fanconi anemia."
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.
Nat. Genet. 37:931-933(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FANCJ PRO-349.
[18]"The DNA helicase BRIP1 is defective in Fanconi anemia complementation group J."
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.
Nat. Genet. 37:934-935(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FANCJ HIS-255; CYS-647 AND CYS-707, VARIANT TRP-264.
[19]"DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome."
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. expand/collapse author list , 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.
Nature 456:66-72(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-919.
[20]"Fanconi anemia group J mutation abolishes its DNA repair function by uncoupling DNA translocation from helicase activity or disruption of protein-DNA complexes."
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.
Blood 116:3780-3791(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FANCJ PRO-349, COFACTOR, CHARACTERIZATION OF VARIANT FANCJ PRO-349.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF360549 mRNA. Translation: AAK38111.1.
AC002994 Genomic DNA. No translation available.
AC005969 Genomic DNA. No translation available.
AC060798 Genomic DNA. No translation available.
BC101472 mRNA. Translation: AAI01473.1.
BC101474 mRNA. Translation: AAI01475.1.
AK074713 mRNA. Translation: BAC11156.1. Different initiation.
RefSeqNP_114432.2. NM_032043.2.
UniGeneHs.128903.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1T29X-ray2.30B985-998[»]
3AL3X-ray2.15B1129-1138[»]
ProteinModelPortalQ9BX63.
SMRQ9BX63. Positions 17-57, 244-441.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123841. 12 interactions.
DIPDIP-41787N.
IntActQ9BX63. 5 interactions.
MINTMINT-275883.
STRING9606.ENSP00000259008.

PTM databases

PhosphoSiteQ9BX63.

Polymorphism databases

DMDM57012613.

Proteomic databases

PaxDbQ9BX63.
PRIDEQ9BX63.

Protocols and materials databases

DNASU83990.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000259008; ENSP00000259008; ENSG00000136492.
GeneID83990.
KEGGhsa:83990.
UCSCuc002izk.2. human. [Q9BX63-1]

Organism-specific databases

CTD83990.
GeneCardsGC17M059759.
H-InvDBHIX0202529.
HGNCHGNC:20473. BRIP1.
HPAHPA005474.
MIM114480. phenotype.
227650. phenotype.
605882. gene.
609054. phenotype.
neXtProtNX_Q9BX63.
Orphanet84. Fanconi anemia.
145. Hereditary breast and ovarian cancer syndrome.
PharmGKBPA134906421.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1199.
HOGENOMHOG000068083.
HOVERGENHBG081519.
InParanoidQ9BX63.
KOK15362.
PhylomeDBQ9BX63.
TreeFamTF329449.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
SignaLinkQ9BX63.

Gene expression databases

ArrayExpressQ9BX63.
BgeeQ9BX63.
CleanExHS_BACH1.
HS_BRIP1.
GenevestigatorQ9BX63.

Family and domain databases

Gene3D3.40.50.300. 3 hits.
InterProIPR006555. ATP-dep_Helicase_C.
IPR010614. DEAD_2.
IPR013020. DNA_helicase_DNA-repair_Rad3.
IPR014013. Helic_SF1/SF2_ATP-bd_DinG/Rad3.
IPR014001. Helicase_ATP-bd.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF06733. DEAD_2. 1 hit.
PF13307. Helicase_C_2. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00491. HELICc2. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 6 hits.
TIGRFAMsTIGR00604. rad3. 1 hit.
PROSITEPS51193. HELICASE_ATP_BIND_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9BX63.
GeneWikiBRIP1.
GenomeRNAi83990.
NextBio73148.
PROQ9BX63.
SOURCESearch...

Entry information

Entry nameFANCJ_HUMAN
AccessionPrimary (citable) accession number: Q9BX63
Secondary accession number(s): Q3MJE2, Q8NCI5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM