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UniProtKB - Q9BX63 (FANCJ_HUMAN)

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Protein

Fanconi anemia group J protein

Gene

BRIP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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

[4Fe-4S] cluster1 PublicationNote: Binds 1 [4Fe-4S] cluster.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi283Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi298Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi310Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi350Iron-sulfur (4Fe-4S)By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi185 – 192ATPPROSITE-ProRule annotation8

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • ATP binding Source: UniProtKB-KW
  • ATP-dependent DNA helicase activity Source: UniProtKB
  • chromatin binding Source: Ensembl
  • DNA binding Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionHelicase, Hydrolase
Biological processDNA damage, DNA repair
Ligand4Fe-4S, ATP-binding, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.6.4.12 2681
ReactomeiR-HSA-2564830 Cytosolic iron-sulfur cluster assembly
R-HSA-5685938 HDR through Single Strand Annealing (SSA)
R-HSA-5685942 HDR through Homologous Recombination (HRR)
R-HSA-5693554 Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA)
R-HSA-5693568 Resolution of D-loop Structures through Holliday Junction Intermediates
R-HSA-5693579 Homologous DNA Pairing and Strand Exchange
R-HSA-5693607 Processing of DNA double-strand break ends
R-HSA-5693616 Presynaptic phase of homologous DNA pairing and strand exchange
R-HSA-6804756 Regulation of TP53 Activity through Phosphorylation
R-HSA-69473 G2/M DNA damage checkpoint
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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

EuPathDBiHostDB:ENSG00000136492.8
HGNCiHGNC:20473 BRIP1
MIMi605882 gene
neXtProtiNX_Q9BX63

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Breast cancer (BC)2 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:114480
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02089647P → A in BC; early onset; loss of ATPase and helicase activities. 2 PublicationsCorresponds to variant dbSNP:rs28903098EnsemblClinVar.1
Natural variantiVAR_020900299M → I in BC; early onset; reduces helicase efficiency on longer substrates. 2 Publications1
Fanconi anemia complementation group J (FANCJ)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:609054
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_023700255Q → H in FANCJ. 1 Publication1
Natural variantiVAR_023702349A → P in FANCJ; destabilizes iron-sulfur-binding and abolishes helicase activity. 2 Publications1
Natural variantiVAR_023703647W → C in FANCJ; associated with C-707. 1 Publication1
Natural variantiVAR_023704707R → C in FANCJ; associated with C-647. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi52K → R: Disrupts BRCA1-mediated double-strand break repair. Loss of ATPase and DNA helicase activities. 3 Publications1
Mutagenesisi986S → A: Does not affect the interaction with BRCA1. 1 Publication1
Mutagenesisi988S → A: Does not affect the interaction with BRCA1. 1 Publication1
Mutagenesisi989T → A: Does not affect the interaction with BRCA1. 1 Publication1
Mutagenesisi990S → A: Disrupts the interaction with BRCA1. 1 Publication1
Mutagenesisi991P → A: Abolishes phosphorylation of S-990. Impairs the interaction with BRCA1. 1 Publication1
Mutagenesisi992T → A: Does not affect the interaction with BRCA1. 1 Publication1
Mutagenesisi993F → A: Abolishes phosphorylation of S-990. Impairs the interaction with BRCA1. 1 Publication1
Mutagenesisi997T → A: Does not affect the interaction with BRCA1. 1 Publication1
Mutagenesisi1001S → A: Does not affect the interaction with BRCA1. 1 Publication1
Mutagenesisi1003S → A: Does not affect the interaction with BRCA1. 1 Publication1
Mutagenesisi1004S → A: Does not affect the interaction with BRCA1. 1 Publication1
Mutagenesisi1007S → A: Does not affect the interaction with BRCA1. 1 Publication1
Mutagenesisi1011Y → A: Does not affect the interaction with BRCA1. 1 Publication1
Mutagenesisi1013T → A: Does not affect the interaction with BRCA1. 1 Publication1

Keywords - Diseasei

Disease mutation, Fanconi anemia

Organism-specific databases

DisGeNETi83990
GeneReviewsiBRIP1
MalaCardsiBRIP1
MIMi114480 phenotype
609054 phenotype
Orphaneti84 Fanconi anemia
145 Hereditary breast and ovarian cancer syndrome
PharmGKBiPA134906421

Polymorphism and mutation databases

BioMutaiBRIP1
DMDMi57012613

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000551731 – 1249Fanconi anemia group J proteinAdd BLAST1249

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei505PhosphoserineCombined sources1
Modified residuei927PhosphoserineCombined sources1
Modified residuei930PhosphoserineCombined sources1
Modified residuei956PhosphoserineCombined sources1
Modified residuei990PhosphoserineCombined sources1 Publication1
Modified residuei1004PhosphoserineCombined sources1
Modified residuei1032PhosphoserineCombined sources1
Modified residuei1237PhosphoserineCombined sources1
Modified residuei1249N6-acetyllysine1 Publication1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9BX63
MaxQBiQ9BX63
PaxDbiQ9BX63
PeptideAtlasiQ9BX63
PRIDEiQ9BX63
ProteomicsDBi79352
79353 [Q9BX63-2]

PTM databases

iPTMnetiQ9BX63
PhosphoSitePlusiQ9BX63

Expressioni

Tissue specificityi

Ubiquitously expressed, with highest levels in testis.1 Publication

Gene expression databases

BgeeiENSG00000136492
CleanExiHS_BACH1
HS_BRIP1
ExpressionAtlasiQ9BX63 baseline and differential
GenevisibleiQ9BX63 HS

Organism-specific databases

HPAiHPA005474

Interactioni

Subunit structurei

Binds directly to the BRCT domains of BRCA1.1 Publication

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi123841, 43 interactors
CORUMiQ9BX63
DIPiDIP-41787N
ELMiQ9BX63
IntActiQ9BX63, 8 interactors
MINTiQ9BX63
STRINGi9606.ENSP00000259008

Chemistry databases

BindingDBiQ9BX63

Structurei

3D structure databases

ProteinModelPortaliQ9BX63
SMRiQ9BX63
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BX63

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini11 – 442Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST432

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni888 – 1063Interaction with BRCA11 PublicationAdd BLAST176

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi158 – 175Nuclear localization signalSequence analysisAdd BLAST18
Motifi393 – 396DEAH box4

Domaini

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

Sequence similaritiesi

Belongs to the DEAD box helicase family. DEAH subfamily.Curated

Phylogenomic databases

eggNOGiKOG1132 Eukaryota
COG1199 LUCA
HOGENOMiHOG000068083
HOVERGENiHBG081519
InParanoidiQ9BX63
KOiK15362
OrthoDBiEOG091G00LK
PhylomeDBiQ9BX63
TreeFamiTF329449

Family and domain databases

InterProiView protein in InterPro
IPR006555 ATP-dep_Helicase_C
IPR010614 DEAD_2
IPR014013 Helic_SF1/SF2_ATP-bd_DinG/Rad3
IPR006554 Helicase-like_DEXD_c2
IPR014001 Helicase_ATP-bd
IPR027417 P-loop_NTPase
IPR013020 Rad3/Chl1-like
PfamiView protein in Pfam
PF06733 DEAD_2, 1 hit
PF13307 Helicase_C_2, 1 hit
SMARTiView protein in SMART
SM00487 DEXDc, 1 hit
SM00488 DEXDc2, 1 hit
SM00491 HELICc2, 1 hit
SUPFAMiSSF52540 SSF52540, 6 hits
TIGRFAMsiTIGR00604 rad3, 1 hit
PROSITEiView protein in PROSITE
PS51193 HELICASE_ATP_BIND_2, 1 hit

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

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

        10         20         30         40         50
MSSMWSEYTI GGVKIYFPYK AYPSQLAMMN SILRGLNSKQ HCLLESPTGS 
        60         70         80         90        100
GKSLALLCSA LAWQQSLSGK PADEGVSEKA EVQLSCCCAC HSKDFTNNDM 
       110        120        130        140        150
NQGTSRHFNY PSTPPSERNG TSSTCQDSPE KTTLAAKLSA KKQASIYRDE 
       160        170        180        190        200
NDDFQVEKKR IRPLETTQQI RKRHCFGTEV HNLDAKVDSG KTVKLNSPLE 
       210        220        230        240        250
KINSFSPQKP PGHCSRCCCS TKQGNSQESS NTIKKDHTGK SKIPKIYFGT 
       260        270        280        290        300
RTHKQIAQIT RELRRTAYSG VPMTILSSRD HTCVHPEVVG NFNRNEKCME 
       310        320        330        340        350
LLDGKNGKSC YFYHGVHKIS DQHTLQTFQG MCKAWDIEEL VSLGKKLKAC 
       360        370        380        390        400
PYYTARELIQ DADIIFCPYN YLLDAQIRES MDLNLKEQVV ILDEAHNIED 
       410        420        430        440        450
CARESASYSV TEVQLRFARD ELDSMVNNNI RKKDHEPLRA VCCSLINWLE 
       460        470        480        490        500
ANAEYLVERD YESACKIWSG NEMLLTLHKM GITTATFPIL QGHFSAVLQK 
       510        520        530        540        550
EEKISPIYGK EEAREVPVIS ASTQIMLKGL FMVLDYLFRQ NSRFADDYKI 
       560        570        580        590        600
AIQQTYSWTN QIDISDKNGL LVLPKNKKRS RQKTAVHVLN FWCLNPAVAF 
       610        620        630        640        650
SDINGKVQTI VLTSGTLSPM KSFSSELGVT FTIQLEANHI IKNSQVWVGT 
       660        670        680        690        700
IGSGPKGRNL CATFQNTETF EFQDEVGALL LSVCQTVSQG ILCFLPSYKL 
       710        720        730        740        750
LEKLKERWLS TGLWHNLELV KTVIVEPQGG EKTNFDELLQ VYYDAIKYKG 
       760        770        780        790        800
EKDGALLVAV CRGKVSEGLD FSDDNARAVI TIGIPFPNVK DLQVELKRQY 
       810        820        830        840        850
NDHHSKLRGL LPGRQWYEIQ AYRALNQALG RCIRHRNDWG ALILVDDRFR 
       860        870        880        890        900
NNPSRYISGL SKWVRQQIQH HSTFESALES LAEFSKKHQK VLNVSIKDRT 
       910        920        930        940        950
NIQDNESTLE VTSLKYSTPP YLLEAASHLS PENFVEDEAK ICVQELQCPK 
       960        970        980        990       1000
IITKNSPLPS SIISRKEKND PVFLEEAGKA EKIVISRSTS PTFNKQTKRV 
      1010       1020       1030       1040       1050
SWSSFNSLGQ YFTGKIPKAT PELGSSENSA SSPPRFKTEK MESKTVLPFT 
      1060       1070       1080       1090       1100
DKCESSNLTV NTSFGSCPQS ETIISSLKID ATLTRKNHSE HPLCSEEALD 
      1110       1120       1130       1140       1150
PDIELSLVSE EDKQSTSNRD FETEAEDESI YFTPELYDPE DTDEEKNDLA 
      1160       1170       1180       1190       1200
ETDRGNRLAN NSDCILAKDL FEIRTIKEVD SAREVKAEDC IDTKLNGILH 
      1210       1220       1230       1240 
IEESKIDDID GNVKTTWINE LELGKTHEIE IKNFKPSPSK NKGMFPGFK
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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti641I → V in BAC11156 (PubMed:14702039).Curated1
Sequence conflicti767E → I AA sequence (PubMed:11301010).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02089647P → A in BC; early onset; loss of ATPase and helicase activities. 2 PublicationsCorresponds to variant dbSNP:rs28903098EnsemblClinVar.1
Natural variantiVAR_020897173R → C2 PublicationsCorresponds to variant dbSNP:rs4988345EnsemblClinVar.1
Natural variantiVAR_020898193V → I2 PublicationsCorresponds to variant dbSNP:rs4988346EnsemblClinVar.1
Natural variantiVAR_020899195L → P1 PublicationCorresponds to variant dbSNP:rs4988347EnsemblClinVar.1
Natural variantiVAR_023700255Q → H in FANCJ. 1 Publication1
Natural variantiVAR_023701264R → W Rare polymorphism. 1 PublicationCorresponds to variant dbSNP:rs28997569EnsemblClinVar.1
Natural variantiVAR_020900299M → I in BC; early onset; reduces helicase efficiency on longer substrates. 2 Publications1
Natural variantiVAR_023702349A → P in FANCJ; destabilizes iron-sulfur-binding and abolishes helicase activity. 2 Publications1
Natural variantiVAR_020901419R → W1 Publication1
Natural variantiVAR_020902531F → V1 PublicationCorresponds to variant dbSNP:rs4988350EnsemblClinVar.1
Natural variantiVAR_020903540Q → L1 PublicationCorresponds to variant dbSNP:rs4988349EnsemblClinVar.1
Natural variantiVAR_052192633I → M. Corresponds to variant dbSNP:rs28997572EnsemblClinVar.1
Natural variantiVAR_023703647W → C in FANCJ; associated with C-707. 1 Publication1
Natural variantiVAR_023704707R → C in FANCJ; associated with C-647. 1 Publication1
Natural variantiVAR_020904832C → Y1 PublicationCorresponds to variant dbSNP:rs4988355Ensembl.1
Natural variantiVAR_020905919P → S Very frequent polymorphism. 7 PublicationsCorresponds to variant dbSNP:rs4986764Ensembl.1
Natural variantiVAR_020906935V → G1 PublicationCorresponds to variant dbSNP:rs4988356EnsemblClinVar.1
Natural variantiVAR_0209071034P → L in a patient with ovarian cancer; unknown pathological significance. 1 Publication1
Natural variantiVAR_0521931148D → E. Corresponds to variant dbSNP:rs28997573EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_012540969 – 994NDPVF…SPTFN → SMKSSSHLPLIEKSFIIFSE MIFIWV in isoform 2. 1 PublicationAdd BLAST26
Alternative sequenceiVSP_012541995 – 1249Missing in isoform 2. 1 PublicationAdd BLAST255

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.3 human [Q9BX63-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiFANCJ_HUMAN
AccessioniPrimary (citable) accession number: Q9BX63
Secondary accession number(s): Q3MJE2, Q8NCI5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: June 1, 2001
Last modified: July 18, 2018
This is version 160 of the entry and version 1 of the sequence. See 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

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