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Q9BX63

- FANCJ_HUMAN

UniProt

Q9BX63 - FANCJ_HUMAN

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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

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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ9BX63.
CleanExiHS_BACH1.
HS_BRIP1.
ExpressionAtlasiQ9BX63. baseline and differential.
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. 19 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 17-62, 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

        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 BAC11156.1 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 17-62, 244-441.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 123841. 19 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

Bgeei Q9BX63.
CleanExi HS_BACH1.
HS_BRIP1.
ExpressionAtlasi Q9BX63. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 122 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

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