FANCJ_MOUSE
ID FANCJ_MOUSE Reviewed; 1174 AA.
AC Q5SXJ3; Q8BJQ8; Q8BKI6;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Fanconi anemia group J protein homolog {ECO:0000305};
DE Short=Protein FACJ;
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q9BX63};
DE AltName: Full=ATP-dependent RNA helicase BRIP1;
DE AltName: Full=BRCA1-associated C-terminal helicase 1;
DE AltName: Full=BRCA1-interacting protein C-terminal helicase 1;
DE Short=BRCA1-interacting protein 1;
GN Name=Brip1 {ECO:0000312|MGI:MGI:2442836}; Synonyms=Bach1, Fancj;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-577 AND 754-1174.
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
CC -!- FUNCTION: DNA-dependent ATPase and 5' to 3' DNA helicase required for
CC the maintenance of chromosomal stability. Acts late in the 'Fanconi
CC anemia' pathway, after FANCD2 ubiquitination. Involved in the repair of
CC DNA double-strand breaks by homologous recombination in a manner that
CC depends on its association with BRCA1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9BX63}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000250|UniProtKB:Q9BX63};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:Q9BX63};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:Q9BX63};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:Q9BX63};
CC -!- SUBUNIT: Binds directly to the BRCT domains of BRCA1. Interacts with
CC the CIA complex components CIAO1, CIAO2B and MMS19.
CC {ECO:0000250|UniProtKB:Q9BX63}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BX63}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9BX63}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
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DR EMBL; AL592065; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL592465; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645690; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC094252; AAH94252.1; -; mRNA.
DR EMBL; AK051878; BAC34798.2; -; mRNA.
DR EMBL; AK080771; BAC38016.1; -; mRNA.
DR CCDS; CCDS25197.1; -.
DR RefSeq; NP_840094.1; NM_178309.2.
DR RefSeq; XP_006533302.1; XM_006533239.2.
DR AlphaFoldDB; Q5SXJ3; -.
DR SMR; Q5SXJ3; -.
DR BioGRID; 231925; 1.
DR ComplexPortal; CPX-4721; BRCA1-B complex.
DR IntAct; Q5SXJ3; 1.
DR STRING; 10090.ENSMUSP00000043108; -.
DR iPTMnet; Q5SXJ3; -.
DR PhosphoSitePlus; Q5SXJ3; -.
DR EPD; Q5SXJ3; -.
DR jPOST; Q5SXJ3; -.
DR MaxQB; Q5SXJ3; -.
DR PaxDb; Q5SXJ3; -.
DR PeptideAtlas; Q5SXJ3; -.
DR PRIDE; Q5SXJ3; -.
DR ProteomicsDB; 277041; -.
DR Antibodypedia; 18594; 319 antibodies from 36 providers.
DR DNASU; 237911; -.
DR Ensembl; ENSMUST00000044423; ENSMUSP00000043108; ENSMUSG00000034329.
DR GeneID; 237911; -.
DR KEGG; mmu:237911; -.
DR UCSC; uc007ksf.2; mouse.
DR CTD; 83990; -.
DR MGI; MGI:2442836; Brip1.
DR VEuPathDB; HostDB:ENSMUSG00000034329; -.
DR eggNOG; KOG1132; Eukaryota.
DR GeneTree; ENSGT00950000182970; -.
DR HOGENOM; CLU_006515_1_0_1; -.
DR InParanoid; Q5SXJ3; -.
DR OMA; CHSKNFT; -.
DR OrthoDB; 186062at2759; -.
DR PhylomeDB; Q5SXJ3; -.
DR TreeFam; TF329449; -.
DR Reactome; R-MMU-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-MMU-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-MMU-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR Reactome; R-MMU-5693579; Homologous DNA Pairing and Strand Exchange.
DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-MMU-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
DR BioGRID-ORCS; 237911; 8 hits in 109 CRISPR screens.
DR ChiTaRS; Brip1; mouse.
DR PRO; PR:Q5SXJ3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SXJ3; protein.
DR Bgee; ENSMUSG00000034329; Expressed in animal zygote and 104 other tissues.
DR Genevisible; Q5SXJ3; MM.
DR GO; GO:0070532; C:BRCA1-B complex; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:1904385; P:cellular response to angiotensin; IEA:Ensembl.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0071295; P:cellular response to vitamin; IEA:Ensembl.
DR GO; GO:0051026; P:chiasma assembly; IMP:MGI.
DR GO; GO:0006281; P:DNA repair; IC:ComplexPortal.
DR GO; GO:1990918; P:double-strand break repair involved in meiotic recombination; IMP:MGI.
DR GO; GO:0007129; P:homologous chromosome pairing at meiosis; IMP:MGI.
DR GO; GO:0035825; P:homologous recombination; IC:ComplexPortal.
DR GO; GO:0008584; P:male gonad development; IMP:MGI.
DR GO; GO:0010705; P:meiotic DNA double-strand break processing involved in reciprocal meiotic recombination; IMP:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR GO; GO:0072520; P:seminiferous tubule development; IMP:MGI.
DR GO; GO:0007286; P:spermatid development; IMP:MGI.
DR GO; GO:0007283; P:spermatogenesis; IMP:MGI.
DR GO; GO:0007284; P:spermatogonial cell division; IMP:MGI.
DR Gene3D; 3.40.50.300; -; 3.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR010614; DEAD_2.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR006554; Helicase-like_DEXD_c2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013020; Rad3/Chl1-like.
DR PANTHER; PTHR11472; PTHR11472; 1.
DR Pfam; PF06733; DEAD_2; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00488; DEXDc2; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00604; rad3; 1.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Acetylation; ATP-binding; Cytoplasm; DNA damage; DNA repair;
KW Helicase; Hydrolase; Iron; Iron-sulfur; Metal-binding; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1174
FT /note="Fanconi anemia group J protein homolog"
FT /id="PRO_0000055174"
FT DOMAIN 11..445
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT REGION 101..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..1063
FT /note="Interaction with BRCA1"
FT /evidence="ECO:0000250"
FT REGION 923..1001
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1102..1155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 158..175
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 393..396
FT /note="DEAH box"
FT COMPBIAS 101..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..963
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 983..1001
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 185..192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 286
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 313
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 353
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT MOD_RES 929
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BX63"
FT MOD_RES 932
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BX63"
FT MOD_RES 994
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BX63"
FT MOD_RES 1174
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9BX63"
SQ SEQUENCE 1174 AA; 131360 MW; 54B244232C4E10B1 CRC64;
MSSVLSDYTI GGVKIHFPCR AYPAQLAMMN SIVRGLNSSQ HCLLESPTGS GKSLALLCSA
LAWQQSLSEK PVDEGLNKKP EAPPSCSCAC HSKNFTYSDT NLDTSPHFNS PSKPSSGRNG
VSTPCQDSPE KNTLAAKLSA KKQASIHRDE DDDFQVEKKR IRPLETTQQI RKRHCLEKDV
HHVDARLASE KRVKPESPIG KSFSDRKDSF QNVDGLCSRC CCSAKQGNNQ EPANTVKKDH
GGQCKRPKIY FGTRTHKQIA QITRELRKTA YSGVPMTILS SRDHSCVHPE VVGNFNRKEK
CMELLDGKHG KSCYFYHGVH KISNQQTLQH LQGMSRAWDI EELVSLGRKL KACPYYTARE
LIEDADIVFC PYNYLLDSQI RETMDIKLKG QVVILDEAHN IEDCARESAS YSVTEVQLRF
ARDELDSLIN GNIRKKSHEP LRDVCYNLIN WLETNSKHLV ERGYESSCKI WSGNEMLLNL
YRMGITTATF PVLQRHLSAV LQKEEKVTPI HGKEEAIQIP IISASTQVVL KGLFMVLDYL
FRENSRFADD YKVAIQQTYS WTNQIAIFDK TGVLAVPKNK KHSRQKIGVN ALNFWCLNPA
VAFSDINDKV RTIVLTSGTL SPLKSFSSEL GVTFSIQLEA NHVISNSQVW VGTVGSGPKG
RNLCATFQHT ETFEFQDEVG MLLLSVCQTV SQGILCFLPS YKLLEKLRER WIFTGLWHSL
ESVKTVIAEP QGGEKTDFDE LLQVYYDAIK FKGEKDGALL IAVCRGKVSE GLDFSDDNAR
AVITVGIPFP NVKDLQVELK RQYNDHHSKS RGLLPGRQWY EIQAYRALNQ ALGRCIRHKN
DWGALILVDD RFNNNPNRYI SGLSKWVRQQ IQHHSSFASA LESLTEFSRR HQKVTNRSKK
DEKCTKDNEP TLEVACLEDS TFTSVSESSH QSPENSTEEA EVCVQELQCP QVATKSPSVA
SHGVSRRKKS DPGLRGESLQ TMKTEKNEIS RSSSPTFGKQ TEPVNWPIFN SLRRHFNSKV
KNCTPVLKSS KNRAPGSSTF NKTALPLTGN CVPSNETADT SLGPCLQSEV IISPVKIEAT
PATNYSKQVF CCEKDLLPDT ELSPGTEEAK CPSSNKAAET EVDDDSECFT PELFDPVDTN
EENGELVETD RSSHSSDCFS AEELFETATG FGQK
