Q9BX63 (FANCJ_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fanconi anemia group J protein
Short name=Protein FACJ
EC=3.6.4.13

Alternative name(s):
ATP-dependent RNA helicase BRIP1
BRCA1-associated C-terminal helicase 1
BRCA1-interacting protein C-terminal helicase 1
Short name=BRCA1-interacting protein 1

Gene names

Name:	BRIP1
Synonyms:	BACH1, FANCJ

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1249 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	DNA-dependent ATPase and 5' to 3' DNA helicase required for the maintenance of chromosomal stability. Acts late in the Fanconi anemia pathway, after FANCD2 ubiquitination. Involved in the repair of DNA double-strand breaks by homologous recombination in a manner that depends on its association with BRCA1. Ref.1 Ref.6 Ref.7 Ref.8
Catalytic activity	ATP + H2O = ADP + phosphate.
Cofactor	Binds 1 4Fe-4S cluster. Ref.19
Subunit structure	Binds directly to the BRCT domains of BRCA1. Ref.12
Subcellular location	Nucleus Ref.1.
Tissue specificity	Ubiquitously expressed, with highest levels in testis. Ref.1
Domain	4Fe-4S iron-sulfur-binding is required for helicase activity (Ref.19).
Post-translational modification	Phosphorylated. Phosphorylation is necessary for interaction with BRCA1, and is cell-cycle regulated. Ref.5
Involvement in disease	Breast cancer (BC) [MIM:114480]: A common malignancy originating from breast epithelial tissue. Breast neoplasms can be distinguished by their histologic pattern. Invasive ductal carcinoma is by far the most common type. Breast cancer is etiologically and genetically heterogeneous. Important genetic factors have been indicated by familial occurrence and bilateral involvement. Mutations at more than one locus can be involved in different families or even in the same case. Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.1 Ref.6 Ref.7 Ref.8 Fanconi anemia complementation group J (FANCJ) [MIM:609054]: A disorder affecting all bone marrow elements and resulting in anemia, leukopenia and thrombopenia. It is associated with cardiac, renal and limb malformations, dermal pigmentary changes, and a predisposition to the development of malignancies. At the cellular level it is associated with hypersensitivity to DNA-damaging agents, chromosomal instability (increased chromosome breakage) and defective DNA repair. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7 Ref.8 Ref.16 Ref.17 Ref.19
Sequence similarities	Belongs to the DEAD box helicase family. DEAH subfamily. Contains 1 helicase ATP-binding domain.
Sequence caution	The sequence BAC11156.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Fanconi anemia
Ligand	4Fe-4S ATP-binding Iron Iron-sulfur Metal-binding Nucleotide-binding
Molecular function	Helicase Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage checkpoint Non-traceable author statement Ref.5. Source: UniProtKB double-strand break repair Non-traceable author statement Ref.1. Source: UniProtKB regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 14504288. Source: MGI
Cellular_component	cytoplasm Inferred from direct assay PubMed 14504288. Source: MGI nuclear membrane Inferred from direct assay. Source: HPA
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent DNA helicase activity Non-traceable author statement Ref.1. Source: UniProtKB DNA binding Non-traceable author statement PubMed 15878853. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BRCA1	P38398	3	EBI-3509650,EBI-349905

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9BX63-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9BX63-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1249	1249	Fanconi anemia group J protein		PRO_0000055173
Regions
	Domain	11 – 442	432	Helicase ATP-binding
	Nucleotide binding	185 – 192	8	ATP By similarity
	Region	888 – 1063	176	Interaction with BRCA1
	Motif	158 – 175	18	Nuclear localization signal Potential
	Motif	393 – 396	4	DEAH box
Sites
	Metal binding	283	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	298	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	310	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	350	1	Iron-sulfur (4Fe-4S) By similarity
Amino acid modifications
	Modified residue	927	1	Phosphoserine Ref.9
	Modified residue	930	1	Phosphoserine Ref.9 Ref.10
	Modified residue	990	1	Phosphoserine Ref.5 Ref.9
	Modified residue	1032	1	Phosphoserine Ref.10
	Modified residue	1237	1	Phosphoserine Ref.11
Natural variations
	Alternative sequence	969 – 994	26	NDPVF…SPTFN → SMKSSSHLPLIEKSFIIFSE MIFIWV in isoform 2.		VSP_012540
	Alternative sequence	995 – 1249	255	Missing in isoform 2.		VSP_012541
	Natural variant	47	1	P → A in BC; early onset; loss of ATPase and helicase activities. Ref.1 Ref.6 Corresponds to variant rs28903098 [ dbSNP | Ensembl ].		VAR_020896
	Natural variant	173	1	R → C. Ref.13 Ref.15 Corresponds to variant rs4988345 [ dbSNP | Ensembl ].		VAR_020897
	Natural variant	193	1	V → I. Ref.1 Ref.15 Corresponds to variant rs4988346 [ dbSNP | Ensembl ].		VAR_020898
	Natural variant	195	1	L → P. Ref.15 Corresponds to variant rs4988347 [ dbSNP | Ensembl ].		VAR_020899
	Natural variant	255	1	Q → H in FANCJ. Ref.17		VAR_023700
	Natural variant	264	1	R → W Rare polymorphism. Ref.17 Corresponds to variant rs28997569 [ dbSNP | Ensembl ].		VAR_023701
	Natural variant	299	1	M → I in BC; early onset; reduces helicase efficiency on longer substrates. Ref.1 Ref.6		VAR_020900
	Natural variant	349	1	A → P in FANCJ; destabilizes iron-sulfur-binding and abolishes helicase activity. Ref.16 Ref.19		VAR_023702
	Natural variant	419	1	R → W. Ref.15		VAR_020901
	Natural variant	531	1	F → V. Ref.15 Corresponds to variant rs4988350 [ dbSNP | Ensembl ].		VAR_020902
	Natural variant	540	1	Q → L. Ref.15 Corresponds to variant rs4988349 [ dbSNP | Ensembl ].		VAR_020903
	Natural variant	633	1	I → M. Corresponds to variant rs28997572 [ dbSNP | Ensembl ].		VAR_052192
	Natural variant	647	1	W → C in FANCJ; associated with C-707. Ref.17		VAR_023703
	Natural variant	707	1	R → C in FANCJ; associated with C-647. Ref.17		VAR_023704
	Natural variant	832	1	C → Y. Ref.15 Corresponds to variant rs4988355 [ dbSNP | Ensembl ].		VAR_020904
	Natural variant	919	1	P → S Very frequent polymorphism. Ref.1 Ref.4 Ref.7 Ref.13 Ref.14 Ref.15 Ref.18 Corresponds to variant rs4986764 [ dbSNP | Ensembl ].		VAR_020905
	Natural variant	935	1	V → G. Ref.15 Corresponds to variant rs4988356 [ dbSNP | Ensembl ].		VAR_020906
	Natural variant	1034	1	P → L in a patient with ovarian cancer; unknown pathological significance. Ref.14		VAR_020907
	Natural variant	1148	1	D → E. Corresponds to variant rs28997573 [ dbSNP | Ensembl ].		VAR_052193
Experimental info
	Mutagenesis	52	1	K → R: Disrupts BRCA1-mediated double-strand break repair. Loss of ATPase and DNA helicase activities. Ref.1 Ref.6 Ref.8
	Mutagenesis	986	1	S → A: Does not affect the interaction with BRCA1. Ref.5
	Mutagenesis	988	1	S → A: Does not affect the interaction with BRCA1. Ref.5
	Mutagenesis	989	1	T → A: Does not affect the interaction with BRCA1. Ref.5
	Mutagenesis	990	1	S → A: Disrupts the interaction with BRCA1. Ref.5
	Mutagenesis	991	1	P → A: Abolishes phosphorylation of S-990. Impairs the interaction with BRCA1. Ref.5
	Mutagenesis	992	1	T → A: Does not affect the interaction with BRCA1. Ref.5
	Mutagenesis	993	1	F → A: Abolishes phosphorylation of S-990. Impairs the interaction with BRCA1. Ref.5
	Mutagenesis	997	1	T → A: Does not affect the interaction with BRCA1. Ref.5
	Mutagenesis	1001	1	S → A: Does not affect the interaction with BRCA1. Ref.5
	Mutagenesis	1003	1	S → A: Does not affect the interaction with BRCA1. Ref.5
	Mutagenesis	1004	1	S → A: Does not affect the interaction with BRCA1. Ref.5
	Mutagenesis	1007	1	S → A: Does not affect the interaction with BRCA1. Ref.5
	Mutagenesis	1011	1	Y → A: Does not affect the interaction with BRCA1. Ref.5
	Mutagenesis	1013	1	T → A: Does not affect the interaction with BRCA1. Ref.5
	Sequence conflict	641	1	I → V in BAC11156. Ref.4
	Sequence conflict	767	1	E → I AA sequence Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 8FA4CDF15577D58E	FASTA	1,249	140,878
	10 20 30 40 50 60 MSSMWSEYTI GGVKIYFPYK AYPSQLAMMN SILRGLNSKQ HCLLESPTGS GKSLALLCSA 70 80 90 100 110 120 LAWQQSLSGK PADEGVSEKA EVQLSCCCAC HSKDFTNNDM NQGTSRHFNY PSTPPSERNG 130 140 150 160 170 180 TSSTCQDSPE KTTLAAKLSA KKQASIYRDE NDDFQVEKKR IRPLETTQQI RKRHCFGTEV 190 200 210 220 230 240 HNLDAKVDSG KTVKLNSPLE KINSFSPQKP PGHCSRCCCS TKQGNSQESS NTIKKDHTGK 250 260 270 280 290 300 SKIPKIYFGT RTHKQIAQIT RELRRTAYSG VPMTILSSRD HTCVHPEVVG NFNRNEKCME 310 320 330 340 350 360 LLDGKNGKSC YFYHGVHKIS DQHTLQTFQG MCKAWDIEEL VSLGKKLKAC PYYTARELIQ 370 380 390 400 410 420 DADIIFCPYN YLLDAQIRES MDLNLKEQVV ILDEAHNIED CARESASYSV TEVQLRFARD 430 440 450 460 470 480 ELDSMVNNNI RKKDHEPLRA VCCSLINWLE ANAEYLVERD YESACKIWSG NEMLLTLHKM 490 500 510 520 530 540 GITTATFPIL QGHFSAVLQK EEKISPIYGK EEAREVPVIS ASTQIMLKGL FMVLDYLFRQ 550 560 570 580 590 600 NSRFADDYKI AIQQTYSWTN QIDISDKNGL LVLPKNKKRS RQKTAVHVLN FWCLNPAVAF 610 620 630 640 650 660 SDINGKVQTI VLTSGTLSPM KSFSSELGVT FTIQLEANHI IKNSQVWVGT IGSGPKGRNL 670 680 690 700 710 720 CATFQNTETF EFQDEVGALL LSVCQTVSQG ILCFLPSYKL LEKLKERWLS TGLWHNLELV 730 740 750 760 770 780 KTVIVEPQGG EKTNFDELLQ VYYDAIKYKG EKDGALLVAV CRGKVSEGLD FSDDNARAVI 790 800 810 820 830 840 TIGIPFPNVK DLQVELKRQY NDHHSKLRGL LPGRQWYEIQ AYRALNQALG RCIRHRNDWG 850 860 870 880 890 900 ALILVDDRFR NNPSRYISGL SKWVRQQIQH HSTFESALES LAEFSKKHQK VLNVSIKDRT 910 920 930 940 950 960 NIQDNESTLE VTSLKYSTPP YLLEAASHLS PENFVEDEAK ICVQELQCPK IITKNSPLPS 970 980 990 1000 1010 1020 SIISRKEKND PVFLEEAGKA EKIVISRSTS PTFNKQTKRV SWSSFNSLGQ YFTGKIPKAT 1030 1040 1050 1060 1070 1080 PELGSSENSA SSPPRFKTEK MESKTVLPFT DKCESSNLTV NTSFGSCPQS ETIISSLKID 1090 1100 1110 1120 1130 1140 ATLTRKNHSE HPLCSEEALD PDIELSLVSE EDKQSTSNRD FETEAEDESI YFTPELYDPE 1150 1160 1170 1180 1190 1200 DTDEEKNDLA ETDRGNRLAN NSDCILAKDL FEIRTIKEVD SAREVKAEDC IDTKLNGILH 1210 1220 1230 1240 IEESKIDDID GNVKTTWINE LELGKTHEIE IKNFKPSPSK NKGMFPGFK
	Isoform 2 [UniParc]. Checksum: 14BFE3010AA0145C	FASTA	994	112,476
	10 20 30 40 50 60 MSSMWSEYTI GGVKIYFPYK AYPSQLAMMN SILRGLNSKQ HCLLESPTGS GKSLALLCSA 70 80 90 100 110 120 LAWQQSLSGK PADEGVSEKA EVQLSCCCAC HSKDFTNNDM NQGTSRHFNY PSTPPSERNG 130 140 150 160 170 180 TSSTCQDSPE KTTLAAKLSA KKQASIYRDE NDDFQVEKKR IRPLETTQQI RKRHCFGTEV 190 200 210 220 230 240 HNLDAKVDSG KTVKLNSPLE KINSFSPQKP PGHCSRCCCS TKQGNSQESS NTIKKDHTGK 250 260 270 280 290 300 SKIPKIYFGT RTHKQIAQIT RELRRTAYSG VPMTILSSRD HTCVHPEVVG NFNRNEKCME 310 320 330 340 350 360 LLDGKNGKSC YFYHGVHKIS DQHTLQTFQG MCKAWDIEEL VSLGKKLKAC PYYTARELIQ 370 380 390 400 410 420 DADIIFCPYN YLLDAQIRES MDLNLKEQVV ILDEAHNIED CARESASYSV TEVQLRFARD 430 440 450 460 470 480 ELDSMVNNNI RKKDHEPLRA VCCSLINWLE ANAEYLVERD YESACKIWSG NEMLLTLHKM 490 500 510 520 530 540 GITTATFPIL QGHFSAVLQK EEKISPIYGK EEAREVPVIS ASTQIMLKGL FMVLDYLFRQ 550 560 570 580 590 600 NSRFADDYKI AIQQTYSWTN QIDISDKNGL LVLPKNKKRS RQKTAVHVLN FWCLNPAVAF 610 620 630 640 650 660 SDINGKVQTI VLTSGTLSPM KSFSSELGVT FTIQLEANHI IKNSQVWVGT IGSGPKGRNL 670 680 690 700 710 720 CATFQNTETF EFQDEVGALL LSVCQTVSQG ILCFLPSYKL LEKLKERWLS TGLWHNLELV 730 740 750 760 770 780 KTVIVEPQGG EKTNFDELLQ VYYDAIKYKG EKDGALLVAV CRGKVSEGLD FSDDNARAVI 790 800 810 820 830 840 TIGIPFPNVK DLQVELKRQY NDHHSKLRGL LPGRQWYEIQ AYRALNQALG RCIRHRNDWG 850 860 870 880 890 900 ALILVDDRFR NNPSRYISGL SKWVRQQIQH HSTFESALES LAEFSKKHQK VLNVSIKDRT 910 920 930 940 950 960 NIQDNESTLE VTSLKYSTPP YLLEAASHLS PENFVEDEAK ICVQELQCPK IITKNSPLPS 970 980 990 SIISRKEKSM KSSSHLPLIE KSFIIFSEMI FIWV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function." Cantor S.B., Bell D.W., Ganesan S., Kass E.M., Drapkin R., Grossman S., Wahrer D.C.R., Sgroi D.C., Lane W.S., Haber D.A., Livingston D.M. Cell 105:149-160(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 708-747; 765-790; 815-831; 1079-1085; 1169-1174 AND 1215-1225, MASS SPECTROMETRY, 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.
[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]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-927; SER-930 AND SER-990, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"The BRCA1-interacting helicase BRIP1 is deficient in Fanconi anemia." Levran O., Attwooll C., Henry R.T., Milton K.L., Neveling K., Rio P., Batish S.D., Kalb R., Velleuer E., Barral S., Ott J., Petrini J., Schindler D., Hanenberg H., Auerbach A.D. Nat. Genet. 37:931-933(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FANCJ PRO-349.
[17]	"The DNA helicase BRIP1 is defective in Fanconi anemia complementation group J." Levitus M., Waisfisz Q., Godthelp B.C., Vries Y., Hussain S., Wiegant W.W., Elghalbzouri-Maghrani E., Steltenpool J., Rooimans M.A., Pals G., Arwert F., Mathew C.G., Zdzienicka M.Z., Hiom K., De Winter J.P., Joenje H. Nat. Genet. 37:934-935(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FANCJ HIS-255; CYS-647 AND CYS-707, VARIANT TRP-264.
[18]	"DNA sequencing of a cytogenetically normal acute myeloid leukaemia genome." Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K., Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L., Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A., Abbott S. , Locke D., Hillier L.W., Miner T., Fulton L., Magrini V., Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R., Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E., Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S., Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A., DiPersio J.F., Wilson R.K. Nature 456:66-72(2008) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-919.
[19]	"Fanconi anemia group J mutation abolishes its DNA repair function by uncoupling DNA translocation from helicase activity or disruption of protein-DNA complexes." Wu Y., Sommers J.A., Suhasini A.N., Leonard T., Deakyne J.S., Mazin A.V., Shin-Ya K., Kitao H., Brosh R.M. Jr. Blood 116:3780-3791(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FANCJ PRO-349, COFACTOR, CHARACTERIZATION OF VARIANT FANCJ PRO-349.
+	Additional computationally mapped references.

Web resources

Fanconi Anemia Mutation Database

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF360549 mRNA. Translation: AAK38111.1.
AC002994 Genomic DNA. No translation available.
AC005969 Genomic DNA. No translation available.
AC060798 Genomic DNA. No translation available.
BC101472 mRNA. Translation: AAI01473.1.
BC101474 mRNA. Translation: AAI01475.1.
AK074713 mRNA. Translation: BAC11156.1. Different initiation.

IPI

IPI00012500.
IPI00514398.

RefSeq

NP_114432.2. NM_032043.2.

UniGene

Hs.128903.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1T29	X-ray	2.30	B	985-998	[»]
3AL3	X-ray	2.15	B	1129-1138	[»]

ProteinModelPortal

Q9BX63.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-41787N.

IntAct

Q9BX63. 2 interactions.

MINT

MINT-275883.

STRING

9606.ENSP00000259008.

PTM databases

PhosphoSite

Q9BX63.

Polymorphism databases

DMDM

57012613.

Proteomic databases

PaxDb

Q9BX63.

PRIDE

Q9BX63.

Protocols and materials databases

DNASU

83990.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000259008; ENSP00000259008; ENSG00000136492.

GeneID

83990.

KEGG

hsa:83990.

UCSC

uc002izk.2. human.

Organism-specific databases

CTD

83990.

GeneCards

GC17M059759.

H-InvDB

HIX0202529.

HGNC

HGNC:20473. BRIP1.

HPA

HPA005474.

MIM

114480. phenotype.
227650. phenotype.
605882. gene.
609054. phenotype.

neXtProt

NX_Q9BX63.

Orphanet

84. Fanconi anemia.
145. Hereditary breast and ovarian cancer syndrome.

PharmGKB

PA134906421.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG1199.

HOGENOM

HOG000068083.

HOVERGEN

HBG081519.

InParanoid

Q9BX63.

KO

K15362.

OrthoDB

EOG4J6RQ8.

Gene expression databases

Bgee

Q9BX63.

CleanEx

HS_BACH1.
HS_BRIP1.

Genevestigator

Q9BX63.

GermOnline

ENSG00000136492. Homo sapiens.

Family and domain databases

InterPro

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.
[Graphical view]

Pfam

PF06733. DEAD_2. 1 hit.
PF13307. Helicase_C_2. 1 hit.
[Graphical view]

SMART

SM00487. DEXDc. 1 hit.
SM00491. HELICc2. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00604. rad3. 1 hit.

PROSITE

PS00690. DEAH_ATP_HELICASE. False negative.
PS51193. HELICASE_ATP_BIND_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9BX63.

GenomeRNAi

83990.

NextBio

73148.

SOURCE

Search...

Entry information

Entry name

FANCJ_HUMAN

Accession

Primary (citable) accession number: Q9BX63
Secondary accession number(s): Q3MJE2, Q8NCI5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 4, 2005
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.