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Q9BX63

- FANCJ_HUMAN

UniProt

Q9BX63 - FANCJ_HUMAN

Protein

Fanconi anemia group J protein

Gene

BRIP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    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 BRCA1.4 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Cofactori

    Binds 1 4Fe-4S cluster.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi283 – 2831Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi298 – 2981Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi310 – 3101Iron-sulfur (4Fe-4S)By similarity
    Metal bindingi350 – 3501Iron-sulfur (4Fe-4S)By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi185 – 1928ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
    2. ATP binding Source: UniProtKB-KW
    3. ATP-dependent DNA helicase activity Source: UniProtKB
    4. DNA binding Source: UniProtKB
    5. metal ion binding Source: UniProtKB-KW
    6. protein binding Source: UniProtKB

    GO - Biological processi

    1. DNA damage checkpoint Source: UniProtKB
    2. DNA duplex unwinding Source: GOC
    3. double-strand break repair Source: UniProtKB
    4. regulation of transcription from RNA polymerase II promoter Source: MGI
    5. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    4Fe-4S, ATP-binding, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_160176. Cytosolic iron-sulfur cluster assembly.
    REACT_1763. Homologous DNA pairing and strand exchange.
    SignaLinkiQ9BX63.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fanconi anemia group J protein (EC:3.6.4.13)
    Short name:
    Protein FACJ
    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 namesi
    Name:BRIP1
    Synonyms:BACH1, FANCJ
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:20473. BRIP1.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: MGI
    2. nuclear membrane Source: HPA
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti47 – 471P → A in BC; early onset; loss of ATPase and helicase activities. 1 Publication
    Corresponds to variant rs28903098 [ dbSNP | Ensembl ].
    VAR_020896
    Natural varianti299 – 2991M → I in BC; early onset; reduces helicase efficiency on longer substrates. 1 Publication
    VAR_020900
    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.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti255 – 2551Q → H in FANCJ. 1 Publication
    VAR_023700
    Natural varianti349 – 3491A → P in FANCJ; destabilizes iron-sulfur-binding and abolishes helicase activity. 2 Publications
    VAR_023702
    Natural varianti647 – 6471W → C in FANCJ; associated with C-707. 1 Publication
    VAR_023703
    Natural varianti707 – 7071R → C in FANCJ; associated with C-647. 1 Publication
    VAR_023704

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi52 – 521K → R: Disrupts BRCA1-mediated double-strand break repair. Loss of ATPase and DNA helicase activities. 3 Publications
    Mutagenesisi986 – 9861S → A: Does not affect the interaction with BRCA1. 1 Publication
    Mutagenesisi988 – 9881S → A: Does not affect the interaction with BRCA1. 1 Publication
    Mutagenesisi989 – 9891T → A: Does not affect the interaction with BRCA1. 1 Publication
    Mutagenesisi990 – 9901S → A: Disrupts the interaction with BRCA1. 1 Publication
    Mutagenesisi991 – 9911P → A: Abolishes phosphorylation of S-990. Impairs the interaction with BRCA1. 1 Publication
    Mutagenesisi992 – 9921T → A: Does not affect the interaction with BRCA1. 1 Publication
    Mutagenesisi993 – 9931F → A: Abolishes phosphorylation of S-990. Impairs the interaction with BRCA1. 1 Publication
    Mutagenesisi997 – 9971T → A: Does not affect the interaction with BRCA1. 1 Publication
    Mutagenesisi1001 – 10011S → A: Does not affect the interaction with BRCA1. 1 Publication
    Mutagenesisi1003 – 10031S → A: Does not affect the interaction with BRCA1. 1 Publication
    Mutagenesisi1004 – 10041S → A: Does not affect the interaction with BRCA1. 1 Publication
    Mutagenesisi1007 – 10071S → A: Does not affect the interaction with BRCA1. 1 Publication
    Mutagenesisi1011 – 10111Y → A: Does not affect the interaction with BRCA1. 1 Publication
    Mutagenesisi1013 – 10131T → A: Does not affect the interaction with BRCA1. 1 Publication

    Keywords - Diseasei

    Disease mutation, Fanconi anemia

    Organism-specific databases

    MIMi114480. phenotype.
    227650. phenotype.
    609054. phenotype.
    Orphaneti84. Fanconi anemia.
    145. Hereditary breast and ovarian cancer syndrome.
    PharmGKBiPA134906421.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12491249Fanconi anemia group J proteinPRO_0000055173Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei927 – 9271Phosphoserine1 Publication
    Modified residuei930 – 9301Phosphoserine2 Publications
    Modified residuei990 – 9901Phosphoserine2 Publications
    Modified residuei1032 – 10321Phosphoserine1 Publication
    Modified residuei1237 – 12371Phosphoserine1 Publication
    Modified residuei1249 – 12491N6-acetyllysine1 Publication

    Post-translational modificationi

    Phosphorylated. Phosphorylation is necessary for interaction with BRCA1, and is cell-cycle regulated.4 Publications
    Acetylation at Lys-1249 facilitates DNA end processing required for repair and checkpoint signaling.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9BX63.
    PaxDbiQ9BX63.
    PRIDEiQ9BX63.

    PTM databases

    PhosphoSiteiQ9BX63.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed, with highest levels in testis.1 Publication

    Gene expression databases

    ArrayExpressiQ9BX63.
    BgeeiQ9BX63.
    CleanExiHS_BACH1.
    HS_BRIP1.
    GenevestigatoriQ9BX63.

    Organism-specific databases

    HPAiHPA005474.

    Interactioni

    Subunit structurei

    Binds directly to the BRCT domains of BRCA1.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BLMP5413216EBI-3509650,EBI-621372
    BRCA1P3839812EBI-3509650,EBI-349905
    MLH1P4069211EBI-3509650,EBI-744248

    Protein-protein interaction databases

    BioGridi123841. 12 interactions.
    DIPiDIP-41787N.
    IntActiQ9BX63. 5 interactions.
    MINTiMINT-275883.
    STRINGi9606.ENSP00000259008.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1T15X-ray1.85B988-995[»]
    1T29X-ray2.30B985-998[»]
    3AL3X-ray2.15B1129-1138[»]
    ProteinModelPortaliQ9BX63.
    SMRiQ9BX63. Positions 244-441.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BX63.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini11 – 442432Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni888 – 1063176Interaction with BRCA1Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi158 – 17518Nuclear localization signalSequence AnalysisAdd
    BLAST
    Motifi393 – 3964DEAH box

    Domaini

    4Fe-4S iron-sulfur-binding is required for helicase activity.1 Publication

    Sequence similaritiesi

    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG1199.
    HOGENOMiHOG000068083.
    HOVERGENiHBG081519.
    InParanoidiQ9BX63.
    KOiK15362.
    PhylomeDBiQ9BX63.
    TreeFamiTF329449.

    Family and domain databases

    Gene3Di3.40.50.300. 3 hits.
    InterProiIPR006555. 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]
    PfamiPF06733. DEAD_2. 1 hit.
    PF13307. Helicase_C_2. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00491. HELICc2. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 6 hits.
    TIGRFAMsiTIGR00604. rad3. 1 hit.
    PROSITEiPS51193. HELICASE_ATP_BIND_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BX63-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MSSMWSEYTI GGVKIYFPYK AYPSQLAMMN SILRGLNSKQ HCLLESPTGS     50
    GKSLALLCSA LAWQQSLSGK PADEGVSEKA EVQLSCCCAC HSKDFTNNDM 100
    NQGTSRHFNY PSTPPSERNG TSSTCQDSPE KTTLAAKLSA KKQASIYRDE 150
    NDDFQVEKKR IRPLETTQQI RKRHCFGTEV HNLDAKVDSG KTVKLNSPLE 200
    KINSFSPQKP PGHCSRCCCS TKQGNSQESS NTIKKDHTGK SKIPKIYFGT 250
    RTHKQIAQIT RELRRTAYSG VPMTILSSRD HTCVHPEVVG NFNRNEKCME 300
    LLDGKNGKSC YFYHGVHKIS DQHTLQTFQG MCKAWDIEEL VSLGKKLKAC 350
    PYYTARELIQ DADIIFCPYN YLLDAQIRES MDLNLKEQVV ILDEAHNIED 400
    CARESASYSV TEVQLRFARD ELDSMVNNNI RKKDHEPLRA VCCSLINWLE 450
    ANAEYLVERD YESACKIWSG NEMLLTLHKM GITTATFPIL QGHFSAVLQK 500
    EEKISPIYGK EEAREVPVIS ASTQIMLKGL FMVLDYLFRQ NSRFADDYKI 550
    AIQQTYSWTN QIDISDKNGL LVLPKNKKRS RQKTAVHVLN FWCLNPAVAF 600
    SDINGKVQTI VLTSGTLSPM KSFSSELGVT FTIQLEANHI IKNSQVWVGT 650
    IGSGPKGRNL CATFQNTETF EFQDEVGALL LSVCQTVSQG ILCFLPSYKL 700
    LEKLKERWLS TGLWHNLELV KTVIVEPQGG EKTNFDELLQ VYYDAIKYKG 750
    EKDGALLVAV CRGKVSEGLD FSDDNARAVI TIGIPFPNVK DLQVELKRQY 800
    NDHHSKLRGL LPGRQWYEIQ AYRALNQALG RCIRHRNDWG ALILVDDRFR 850
    NNPSRYISGL SKWVRQQIQH HSTFESALES LAEFSKKHQK VLNVSIKDRT 900
    NIQDNESTLE VTSLKYSTPP YLLEAASHLS PENFVEDEAK ICVQELQCPK 950
    IITKNSPLPS SIISRKEKND PVFLEEAGKA EKIVISRSTS PTFNKQTKRV 1000
    SWSSFNSLGQ YFTGKIPKAT PELGSSENSA SSPPRFKTEK MESKTVLPFT 1050
    DKCESSNLTV NTSFGSCPQS ETIISSLKID ATLTRKNHSE HPLCSEEALD 1100
    PDIELSLVSE EDKQSTSNRD FETEAEDESI YFTPELYDPE DTDEEKNDLA 1150
    ETDRGNRLAN NSDCILAKDL FEIRTIKEVD SAREVKAEDC IDTKLNGILH 1200
    IEESKIDDID GNVKTTWINE LELGKTHEIE IKNFKPSPSK NKGMFPGFK 1249
    Length:1,249
    Mass (Da):140,878
    Last modified:June 1, 2001 - v1
    Checksum:i8FA4CDF15577D58E
    GO
    Isoform 2 (identifier: Q9BX63-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         969-994: NDPVFLEEAGKAEKIVISRSTSPTFN → SMKSSSHLPLIEKSFIIFSEMIFIWV
         995-1249: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:994
    Mass (Da):112,476
    Checksum:i14BFE3010AA0145C
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti641 – 6411I → V in BAC11156. (PubMed:14702039)Curated
    Sequence conflicti767 – 7671E → I AA sequence (PubMed:11301010)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti47 – 471P → A in BC; early onset; loss of ATPase and helicase activities. 1 Publication
    Corresponds to variant rs28903098 [ dbSNP | Ensembl ].
    VAR_020896
    Natural varianti173 – 1731R → C.2 Publications
    Corresponds to variant rs4988345 [ dbSNP | Ensembl ].
    VAR_020897
    Natural varianti193 – 1931V → I.2 Publications
    Corresponds to variant rs4988346 [ dbSNP | Ensembl ].
    VAR_020898
    Natural varianti195 – 1951L → P.1 Publication
    Corresponds to variant rs4988347 [ dbSNP | Ensembl ].
    VAR_020899
    Natural varianti255 – 2551Q → H in FANCJ. 1 Publication
    VAR_023700
    Natural varianti264 – 2641R → W Rare polymorphism. 1 Publication
    Corresponds to variant rs28997569 [ dbSNP | Ensembl ].
    VAR_023701
    Natural varianti299 – 2991M → I in BC; early onset; reduces helicase efficiency on longer substrates. 1 Publication
    VAR_020900
    Natural varianti349 – 3491A → P in FANCJ; destabilizes iron-sulfur-binding and abolishes helicase activity. 2 Publications
    VAR_023702
    Natural varianti419 – 4191R → W.1 Publication
    VAR_020901
    Natural varianti531 – 5311F → V.1 Publication
    Corresponds to variant rs4988350 [ dbSNP | Ensembl ].
    VAR_020902
    Natural varianti540 – 5401Q → L.1 Publication
    Corresponds to variant rs4988349 [ dbSNP | Ensembl ].
    VAR_020903
    Natural varianti633 – 6331I → M.
    Corresponds to variant rs28997572 [ dbSNP | Ensembl ].
    VAR_052192
    Natural varianti647 – 6471W → C in FANCJ; associated with C-707. 1 Publication
    VAR_023703
    Natural varianti707 – 7071R → C in FANCJ; associated with C-647. 1 Publication
    VAR_023704
    Natural varianti832 – 8321C → Y.1 Publication
    Corresponds to variant rs4988355 [ dbSNP | Ensembl ].
    VAR_020904
    Natural varianti919 – 9191P → S Very frequent polymorphism. 7 Publications
    Corresponds to variant rs4986764 [ dbSNP | Ensembl ].
    VAR_020905
    Natural varianti935 – 9351V → G.1 Publication
    Corresponds to variant rs4988356 [ dbSNP | Ensembl ].
    VAR_020906
    Natural varianti1034 – 10341P → L in a patient with ovarian cancer; unknown pathological significance. 1 Publication
    VAR_020907
    Natural varianti1148 – 11481D → E.
    Corresponds to variant rs28997573 [ dbSNP | Ensembl ].
    VAR_052193

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei969 – 99426NDPVF…SPTFN → SMKSSSHLPLIEKSFIIFSE MIFIWV in isoform 2. 1 PublicationVSP_012540Add
    BLAST
    Alternative sequencei995 – 1249255Missing in isoform 2. 1 PublicationVSP_012541Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS11631.1. [Q9BX63-1]
    RefSeqiNP_114432.2. NM_032043.2.
    UniGeneiHs.128903.

    Genome annotation databases

    EnsembliENST00000259008; ENSP00000259008; ENSG00000136492.
    GeneIDi83990.
    KEGGihsa:83990.
    UCSCiuc002izk.2. human. [Q9BX63-1]

    Polymorphism databases

    DMDMi57012613.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Fanconi Anemia Mutation Database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS11631.1. [Q9BX63-1 ]
    RefSeqi NP_114432.2. NM_032043.2.
    UniGenei Hs.128903.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1T15 X-ray 1.85 B 988-995 [» ]
    1T29 X-ray 2.30 B 985-998 [» ]
    3AL3 X-ray 2.15 B 1129-1138 [» ]
    ProteinModelPortali Q9BX63.
    SMRi Q9BX63. Positions 244-441.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123841. 12 interactions.
    DIPi DIP-41787N.
    IntActi Q9BX63. 5 interactions.
    MINTi MINT-275883.
    STRINGi 9606.ENSP00000259008.

    PTM databases

    PhosphoSitei Q9BX63.

    Polymorphism databases

    DMDMi 57012613.

    Proteomic databases

    MaxQBi Q9BX63.
    PaxDbi Q9BX63.
    PRIDEi Q9BX63.

    Protocols and materials databases

    DNASUi 83990.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000259008 ; ENSP00000259008 ; ENSG00000136492 .
    GeneIDi 83990.
    KEGGi hsa:83990.
    UCSCi uc002izk.2. human. [Q9BX63-1 ]

    Organism-specific databases

    CTDi 83990.
    GeneCardsi GC17M059759.
    GeneReviewsi BRIP1.
    H-InvDB HIX0202529.
    HGNCi HGNC:20473. BRIP1.
    HPAi HPA005474.
    MIMi 114480. phenotype.
    227650. phenotype.
    605882. gene.
    609054. phenotype.
    neXtProti NX_Q9BX63.
    Orphaneti 84. Fanconi anemia.
    145. Hereditary breast and ovarian cancer syndrome.
    PharmGKBi PA134906421.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1199.
    HOGENOMi HOG000068083.
    HOVERGENi HBG081519.
    InParanoidi Q9BX63.
    KOi K15362.
    PhylomeDBi Q9BX63.
    TreeFami TF329449.

    Enzyme and pathway databases

    Reactomei REACT_160176. Cytosolic iron-sulfur cluster assembly.
    REACT_1763. Homologous DNA pairing and strand exchange.
    SignaLinki Q9BX63.

    Miscellaneous databases

    EvolutionaryTracei Q9BX63.
    GeneWikii BRIP1.
    GenomeRNAii 83990.
    NextBioi 73148.
    PROi Q9BX63.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BX63.
    Bgeei Q9BX63.
    CleanExi HS_BACH1.
    HS_BRIP1.
    Genevestigatori Q9BX63.

    Family and domain databases

    Gene3Di 3.40.50.300. 3 hits.
    InterProi IPR006555. 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 ]
    Pfami PF06733. DEAD_2. 1 hit.
    PF13307. Helicase_C_2. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00491. HELICc2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 6 hits.
    TIGRFAMsi TIGR00604. rad3. 1 hit.
    PROSITEi PS51193. HELICASE_ATP_BIND_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.
      , 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. 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. 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. Cited for: VARIANT FANCJ PRO-349.
    18. Cited for: VARIANTS FANCJ HIS-255; CYS-647 AND CYS-707, VARIANT TRP-264.
    19. 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.

    Entry informationi

    Entry nameiFANCJ_HUMAN
    AccessioniPrimary (citable) accession number: Q9BX63
    Secondary accession number(s): Q3MJE2, Q8NCI5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 4, 2005
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 121 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3