FANCJ_HUMAN
ID FANCJ_HUMAN Reviewed; 1249 AA.
AC Q9BX63; A0A024QZ45; Q3MJE2; Q8NCI5;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 2.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Fanconi anemia group J protein {ECO:0000305};
DE Short=Protein FACJ;
DE EC=3.6.4.13 {ECO:0000269|PubMed:20639400};
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|HGNC:HGNC:20473}; Synonyms=BACH1, FANCJ;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 708-747;
RP 765-790; 815-831; 1079-1085; 1169-1174 AND 1215-1225, FUNCTION, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH BRCA1, MUTAGENESIS OF
RP LYS-52, VARIANTS BC ALA-47 AND ILE-299, VARIANTS ILE-193 AND PRO-919, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11301010; DOI=10.1016/s0092-8674(01)00304-x;
RA Cantor S.B., Bell D.W., Ganesan S., Kass E.M., Drapkin R., Grossman S.,
RA Wahrer D.C.R., Sgroi D.C., Lane W.S., Haber D.A., Livingston D.M.;
RT "BACH1, a novel helicase-like protein, interacts directly with BRCA1 and
RT contributes to its DNA repair function.";
RL Cell 105:149-160(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PRO-919.
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 558-1249 (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP PHOSPHORYLATION AT SER-990, AND MUTAGENESIS OF SER-986; SER-988; THR-989;
RP SER-990; PRO-991; THR-992; PHE-993; THR-997; SER-1001; SER-1003; SER-1004;
RP SER-1007; TYR-1011 AND THR-1013.
RX PubMed=14576433; DOI=10.1126/science.1088753;
RA Yu X., Chini C.C.S., He M., Mer G., Chen J.;
RT "The BRCT domain is a phospho-protein binding domain.";
RL Science 302:639-642(2003).
RN [7]
RP FUNCTION, MUTAGENESIS OF LYS-52, AND CHARACTERIZATION OF VARIANTS BC ALA-47
RP AND ILE-299.
RX PubMed=14983014; DOI=10.1073/pnas.0308717101;
RA Cantor S.B., Drapkin R., Zhang F., Lin Y., Han J., Pamidi S.,
RA Livingston D.M.;
RT "The BRCA1-associated protein BACH1 is a DNA helicase targeted by
RT clinically relevant inactivating mutations.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:2357-2362(2004).
RN [8]
RP FUNCTION, VARIANT PRO-919, AND DISEASE.
RX PubMed=16153896; DOI=10.1016/j.ccr.2005.08.004;
RA Litman R., Peng M., Jin Z., Zhang F., Zhang J., Powell S., Andreassen P.R.,
RA Cantor S.B.;
RT "BACH1 is critical for homologous recombination and appears to be the
RT Fanconi anemia gene product FANCJ.";
RL Cancer Cell 8:255-265(2005).
RN [9]
RP FUNCTION, MUTAGENESIS OF LYS-52, AND DISEASE.
RX PubMed=16116421; DOI=10.1038/ng1627;
RA Bridge W.L., Vandenberg C.J., Franklin R.J., Hiom K.;
RT "The BRIP1 helicase functions independently of BRCA1 in the Fanconi anemia
RT pathway for DNA crosslink repair.";
RL Nat. Genet. 37:953-957(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-927; SER-930 AND SER-990, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-930 AND SER-1032, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1237, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP ACETYLATION AT LYS-1249.
RX PubMed=22792074; DOI=10.1371/journal.pgen.1002786;
RA Xie J., Peng M., Guillemette S., Quan S., Maniatis S., Wu Y., Venkatesh A.,
RA Shaffer S.A., Brosh R.M. Jr., Cantor S.B.;
RT "FANCJ/BACH1 acetylation at lysine 1249 regulates the DNA damage
RT response.";
RL PLoS Genet. 8:E1002786-E1002786(2012).
RN [14]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CIAO1; CIAO2B AND MMS19.
RX PubMed=23585563; DOI=10.1074/jbc.m112.416602;
RA Seki M., Takeda Y., Iwai K., Tanaka K.;
RT "IOP1 protein is an external component of the human cytosolic iron-sulfur
RT cluster assembly (CIA) machinery and functions in the MMS19 protein-
RT dependent CIA pathway.";
RL J. Biol. Chem. 288:16680-16689(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505; SER-956; SER-1004 AND
RP SER-1032, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 985-998 IN COMPLEX WITH BRCA1, AND
RP SUBUNIT.
RX PubMed=15125843; DOI=10.1016/s1097-2765(04)00238-2;
RA Shiozaki E.N., Gu L., Yan N., Shi Y.;
RT "Structure of the BRCT repeats of BRCA1 bound to a BACH1 phosphopeptide:
RT implications for signaling.";
RL Mol. Cell 14:405-412(2004).
RN [17]
RP VARIANTS CYS-173 AND PRO-919.
RX PubMed=11920628; DOI=10.1002/ijc.10214;
RA Luo L., Lei H., Du Q., von Wachenfeldt A., Kockum I., Luthman H.,
RA Vorechovsky I., Lindblom A.;
RT "No mutations in the BACH1 gene in BRCA1 and BRCA2 negative breast-cancer
RT families linked to 17q22.";
RL Int. J. Cancer 98:638-639(2002).
RN [18]
RP VARIANTS PRO-919 AND LEU-1034.
RX PubMed=12565990; DOI=10.1016/s0959-8049(02)00498-7;
RA Karppinen S.-M., Vuosku J., Heikkinen K., Allinen M., Winqvist R.;
RT "No evidence of involvement of germline BACH1 mutations in Finnish breast
RT and ovarian cancer families.";
RL Eur. J. Cancer 39:366-371(2003).
RN [19]
RP VARIANTS CYS-173; ILE-193; PRO-195; TRP-419; VAL-531; LEU-540; TYR-832;
RP PRO-919 AND GLY-935.
RX PubMed=12872252; DOI=10.1002/humu.10238;
RA Rutter J.L., Smith A.M., Davila M.R., Sigurdson A.J., Giusti R.M.,
RA Pineda M.A., Doody M.M., Tucker M.A., Greene M.H., Zhang J.,
RA Struewing J.P.;
RT "Mutational analysis of the BRCA1-interacting genes ZNF350/ZBRK1 and
RT BRIP1/BACH1 among BRCA1 and BRCA2-negative probands from breast-ovarian
RT cancer families and among early-onset breast cancer cases and reference
RT individuals.";
RL Hum. Mutat. 22:121-128(2003).
RN [20]
RP VARIANT FANCJ PRO-349.
RX PubMed=16116424; DOI=10.1038/ng1624;
RA Levran O., Attwooll C., Henry R.T., Milton K.L., Neveling K., Rio P.,
RA Batish S.D., Kalb R., Velleuer E., Barral S., Ott J., Petrini J.,
RA Schindler D., Hanenberg H., Auerbach A.D.;
RT "The BRCA1-interacting helicase BRIP1 is deficient in Fanconi anemia.";
RL Nat. Genet. 37:931-933(2005).
RN [21]
RP VARIANTS FANCJ HIS-255; CYS-647 AND CYS-707, AND VARIANT TRP-264.
RX PubMed=16116423; DOI=10.1038/ng1625;
RA Levitus M., Waisfisz Q., Godthelp B.C., Vries Y., Hussain S., Wiegant W.W.,
RA Elghalbzouri-Maghrani E., Steltenpool J., Rooimans M.A., Pals G.,
RA Arwert F., Mathew C.G., Zdzienicka M.Z., Hiom K., De Winter J.P.,
RA Joenje H.;
RT "The DNA helicase BRIP1 is defective in Fanconi anemia complementation
RT group J.";
RL Nat. Genet. 37:934-935(2005).
RN [22]
RP VARIANT [LARGE SCALE ANALYSIS] PRO-919.
RX PubMed=18987736; DOI=10.1038/nature07485;
RA Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
RA Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
RA Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
RA Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
RA Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
RA Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
RA Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S.,
RA Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A.,
RA DiPersio J.F., Wilson R.K.;
RT "DNA sequencing of a cytogenetically normal acute myeloid leukaemia
RT genome.";
RL Nature 456:66-72(2008).
RN [23]
RP VARIANT FANCJ PRO-349, COFACTOR, CHARACTERIZATION OF VARIANT FANCJ PRO-349,
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=20639400; DOI=10.1182/blood-2009-11-256016;
RA Wu Y., Sommers J.A., Suhasini A.N., Leonard T., Deakyne J.S., Mazin A.V.,
RA Shin-Ya K., Kitao H., Brosh R.M. Jr.;
RT "Fanconi anemia group J mutation abolishes its DNA repair function by
RT uncoupling DNA translocation from helicase activity or disruption of
RT protein-DNA complexes.";
RL Blood 116:3780-3791(2010).
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. {ECO:0000269|PubMed:11301010,
CC ECO:0000269|PubMed:14983014, ECO:0000269|PubMed:16116421,
CC ECO:0000269|PubMed:16153896}.
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:0000269|PubMed:20639400};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000269|PubMed:20639400};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:20639400};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:20639400};
CC -!- SUBUNIT: Binds directly to the BRCT domains of BRCA1 (PubMed:15125843).
CC Interacts with the CIA complex components CIAO1, CIAO2B and MMS19
CC (PubMed:23585563). {ECO:0000269|PubMed:15125843,
CC ECO:0000269|PubMed:23585563}.
CC -!- INTERACTION:
CC Q9BX63; P54132: BLM; NbExp=16; IntAct=EBI-3509650, EBI-621372;
CC Q9BX63; P38398: BRCA1; NbExp=24; IntAct=EBI-3509650, EBI-349905;
CC Q9BX63; Q9BPX1: HSD17B14; NbExp=3; IntAct=EBI-3509650, EBI-742664;
CC Q9BX63; P40692: MLH1; NbExp=14; IntAct=EBI-3509650, EBI-744248;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11301010,
CC ECO:0000269|PubMed:23585563}. Cytoplasm {ECO:0000269|PubMed:23585563}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BX63-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BX63-2; Sequence=VSP_012540, VSP_012541;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC testis. {ECO:0000269|PubMed:11301010}.
CC -!- DOMAIN: 4Fe-4S iron-sulfur-binding is required for helicase activity.
CC {ECO:0000269|PubMed:20639400}.
CC -!- PTM: Phosphorylated. Phosphorylation is necessary for interaction with
CC BRCA1, and is cell-cycle regulated. {ECO:0000269|PubMed:14576433}.
CC -!- PTM: Acetylation at Lys-1249 facilitates DNA end processing required
CC for repair and checkpoint signaling. {ECO:0000269|PubMed:22792074}.
CC -!- DISEASE: Breast cancer (BC) [MIM:114480]: A common malignancy
CC originating from breast epithelial tissue. Breast neoplasms can be
CC distinguished by their histologic pattern. Invasive ductal carcinoma is
CC by far the most common type. Breast cancer is etiologically and
CC genetically heterogeneous. Important genetic factors have been
CC indicated by familial occurrence and bilateral involvement. Mutations
CC at more than one locus can be involved in different families or even in
CC the same case. {ECO:0000269|PubMed:11301010,
CC ECO:0000269|PubMed:14983014}. Note=Disease susceptibility is associated
CC with variants affecting the gene represented in this entry.
CC -!- DISEASE: Fanconi anemia complementation group J (FANCJ) [MIM:609054]: A
CC disorder affecting all bone marrow elements and resulting in anemia,
CC leukopenia and thrombopenia. It is associated with cardiac, renal and
CC limb malformations, dermal pigmentary changes, and a predisposition to
CC the development of malignancies. At the cellular level it is associated
CC with hypersensitivity to DNA-damaging agents, chromosomal instability
CC (increased chromosome breakage) and defective DNA repair.
CC {ECO:0000269|PubMed:16116423, ECO:0000269|PubMed:16116424,
CC ECO:0000269|PubMed:20639400}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC11156.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Fanconi Anemia Mutation Database;
CC URL="https://www2.rockefeller.edu/fanconi/genes/jumpj";
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DR EMBL; AF360549; AAK38111.1; -; mRNA.
DR EMBL; AC002994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC005969; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC060798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471179; EAW51430.1; -; Genomic_DNA.
DR EMBL; CH471179; EAW51432.1; -; Genomic_DNA.
DR EMBL; CH471179; EAW51431.1; -; Genomic_DNA.
DR EMBL; CH471179; EAW51433.1; -; Genomic_DNA.
DR EMBL; BC101472; AAI01473.1; -; mRNA.
DR EMBL; BC101474; AAI01475.1; -; mRNA.
DR EMBL; AK074713; BAC11156.1; ALT_INIT; mRNA.
DR CCDS; CCDS11631.1; -. [Q9BX63-1]
DR RefSeq; NP_114432.2; NM_032043.2. [Q9BX63-1]
DR PDB; 1T15; X-ray; 1.85 A; B=988-995.
DR PDB; 1T29; X-ray; 2.30 A; B=985-998.
DR PDB; 3AL3; X-ray; 2.15 A; B=1129-1138.
DR PDBsum; 1T15; -.
DR PDBsum; 1T29; -.
DR PDBsum; 3AL3; -.
DR AlphaFoldDB; Q9BX63; -.
DR SMR; Q9BX63; -.
DR BioGRID; 123841; 73.
DR ComplexPortal; CPX-4426; BRCA1-B complex.
DR CORUM; Q9BX63; -.
DR DIP; DIP-41787N; -.
DR ELM; Q9BX63; -.
DR IntAct; Q9BX63; 25.
DR MINT; Q9BX63; -.
DR STRING; 9606.ENSP00000259008; -.
DR BindingDB; Q9BX63; -.
DR iPTMnet; Q9BX63; -.
DR PhosphoSitePlus; Q9BX63; -.
DR BioMuta; BRIP1; -.
DR DMDM; 57012613; -.
DR CPTAC; CPTAC-3220; -.
DR CPTAC; CPTAC-3221; -.
DR CPTAC; CPTAC-3222; -.
DR CPTAC; CPTAC-3281; -.
DR CPTAC; CPTAC-918; -.
DR EPD; Q9BX63; -.
DR jPOST; Q9BX63; -.
DR MassIVE; Q9BX63; -.
DR MaxQB; Q9BX63; -.
DR PaxDb; Q9BX63; -.
DR PeptideAtlas; Q9BX63; -.
DR PRIDE; Q9BX63; -.
DR ProteomicsDB; 79352; -. [Q9BX63-1]
DR ProteomicsDB; 79353; -. [Q9BX63-2]
DR Antibodypedia; 18594; 319 antibodies from 36 providers.
DR CPTC; Q9BX63; 5 antibodies.
DR DNASU; 83990; -.
DR Ensembl; ENST00000259008.7; ENSP00000259008.2; ENSG00000136492.10. [Q9BX63-1]
DR Ensembl; ENST00000577598.5; ENSP00000464654.1; ENSG00000136492.10. [Q9BX63-2]
DR Ensembl; ENST00000682453.1; ENSP00000506943.1; ENSG00000136492.10. [Q9BX63-1]
DR Ensembl; ENST00000683039.1; ENSP00000508303.1; ENSG00000136492.10. [Q9BX63-1]
DR GeneID; 83990; -.
DR KEGG; hsa:83990; -.
DR MANE-Select; ENST00000259008.7; ENSP00000259008.2; NM_032043.3; NP_114432.2.
DR UCSC; uc002izk.3; human. [Q9BX63-1]
DR CTD; 83990; -.
DR DisGeNET; 83990; -.
DR GeneCards; BRIP1; -.
DR GeneReviews; BRIP1; -.
DR HGNC; HGNC:20473; BRIP1.
DR HPA; ENSG00000136492; Tissue enhanced (bone marrow, lymphoid tissue, testis).
DR MalaCards; BRIP1; -.
DR MIM; 114480; phenotype.
DR MIM; 605882; gene.
DR MIM; 609054; phenotype.
DR neXtProt; NX_Q9BX63; -.
DR OpenTargets; ENSG00000136492; -.
DR Orphanet; 84; Fanconi anemia.
DR Orphanet; 145; Hereditary breast and ovarian cancer syndrome.
DR PharmGKB; PA134906421; -.
DR VEuPathDB; HostDB:ENSG00000136492; -.
DR eggNOG; KOG1132; Eukaryota.
DR GeneTree; ENSGT00950000182970; -.
DR InParanoid; Q9BX63; -.
DR OMA; CHSKNFT; -.
DR OrthoDB; 186062at2759; -.
DR PhylomeDB; Q9BX63; -.
DR TreeFam; TF329449; -.
DR BRENDA; 3.6.4.12; 2681.
DR PathwayCommons; Q9BX63; -.
DR Reactome; R-HSA-2564830; Cytosolic iron-sulfur cluster assembly.
DR Reactome; R-HSA-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-HSA-5693554; Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
DR Reactome; R-HSA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR Reactome; R-HSA-5693579; Homologous DNA Pairing and Strand Exchange.
DR Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-HSA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-HSA-69473; G2/M DNA damage checkpoint.
DR Reactome; R-HSA-9701192; Defective HDR through Homologous Recombination (HRR) due to BRCA1 loss-of-function.
DR Reactome; R-HSA-9704331; Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA1 binding function.
DR Reactome; R-HSA-9704646; Defective HDR through Homologous Recombination Repair (HRR) due to PALB2 loss of BRCA2/RAD51/RAD51C binding function.
DR Reactome; R-HSA-9709570; Impaired BRCA2 binding to RAD51.
DR Reactome; R-HSA-9709603; Impaired BRCA2 binding to PALB2.
DR SignaLink; Q9BX63; -.
DR SIGNOR; Q9BX63; -.
DR BioGRID-ORCS; 83990; 98 hits in 1082 CRISPR screens.
DR ChiTaRS; BRIP1; human.
DR EvolutionaryTrace; Q9BX63; -.
DR GeneWiki; BRIP1; -.
DR GenomeRNAi; 83990; -.
DR Pharos; Q9BX63; Tbio.
DR PRO; PR:Q9BX63; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9BX63; protein.
DR Bgee; ENSG00000136492; Expressed in ventricular zone and 125 other tissues.
DR ExpressionAtlas; Q9BX63; baseline and differential.
DR Genevisible; Q9BX63; HS.
DR GO; GO:0070532; C:BRCA1-B complex; IPI:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA: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; IDA:HGNC.
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; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
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; IEA:Ensembl.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; NAS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IC:ComplexPortal.
DR GO; GO:0006302; P:double-strand break repair; NAS:UniProtKB.
DR GO; GO:1990918; P:double-strand break repair involved in meiotic recombination; IBA:GO_Central.
DR GO; GO:0035825; P:homologous recombination; IC:ComplexPortal.
DR GO; GO:0010705; P:meiotic DNA double-strand break processing involved in reciprocal meiotic recombination; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
DR GO; GO:0072520; P:seminiferous tubule development; IEA:Ensembl.
DR GO; GO:0007286; P:spermatid development; IEA:Ensembl.
DR GO; GO:0007284; P:spermatogonial cell division; IEA:Ensembl.
DR Gene3D; 3.40.50.300; -; 3.
DR IDEAL; IID00181; -.
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 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Acetylation; Alternative splicing; ATP-binding;
KW Cytoplasm; Direct protein sequencing; Disease variant; DNA damage;
KW DNA repair; Fanconi anemia; Helicase; Hydrolase; Iron; Iron-sulfur;
KW Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1249
FT /note="Fanconi anemia group J protein"
FT /id="PRO_0000055173"
FT DOMAIN 11..442
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT REGION 102..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..1063
FT /note="Interaction with BRCA1"
FT /evidence="ECO:0000269|PubMed:11301010"
FT REGION 1018..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1108..1127
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 1022..1036
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1126
FT /note="Basic and acidic 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 283
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 298
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 310
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT BINDING 350
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 927
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 930
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 956
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 990
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:14576433,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 1004
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1032
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1237
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1249
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:22792074"
FT VAR_SEQ 969..994
FT /note="NDPVFLEEAGKAEKIVISRSTSPTFN -> SMKSSSHLPLIEKSFIIFSEMI
FT FIWV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012540"
FT VAR_SEQ 995..1249
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_012541"
FT VARIANT 47
FT /note="P -> A (in BC; early onset; loss of ATPase and
FT helicase activities; dbSNP:rs28903098)"
FT /evidence="ECO:0000269|PubMed:11301010,
FT ECO:0000269|PubMed:14983014"
FT /id="VAR_020896"
FT VARIANT 173
FT /note="R -> C (in dbSNP:rs4988345)"
FT /evidence="ECO:0000269|PubMed:11920628,
FT ECO:0000269|PubMed:12872252"
FT /id="VAR_020897"
FT VARIANT 193
FT /note="V -> I (in dbSNP:rs4988346)"
FT /evidence="ECO:0000269|PubMed:11301010,
FT ECO:0000269|PubMed:12872252"
FT /id="VAR_020898"
FT VARIANT 195
FT /note="L -> P (in dbSNP:rs4988347)"
FT /evidence="ECO:0000269|PubMed:12872252"
FT /id="VAR_020899"
FT VARIANT 255
FT /note="Q -> H (in FANCJ)"
FT /evidence="ECO:0000269|PubMed:16116423"
FT /id="VAR_023700"
FT VARIANT 264
FT /note="R -> W (in dbSNP:rs28997569)"
FT /evidence="ECO:0000269|PubMed:16116423"
FT /id="VAR_023701"
FT VARIANT 299
FT /note="M -> I (in BC; early onset; reduces helicase
FT efficiency on longer substrates; dbSNP:rs137852985)"
FT /evidence="ECO:0000269|PubMed:11301010,
FT ECO:0000269|PubMed:14983014"
FT /id="VAR_020900"
FT VARIANT 349
FT /note="A -> P (in FANCJ; destabilizes iron-sulfur-binding
FT and abolishes helicase activity; dbSNP:rs149364097)"
FT /evidence="ECO:0000269|PubMed:16116424,
FT ECO:0000269|PubMed:20639400"
FT /id="VAR_023702"
FT VARIANT 419
FT /note="R -> W (in dbSNP:rs150624408)"
FT /evidence="ECO:0000269|PubMed:12872252"
FT /id="VAR_020901"
FT VARIANT 531
FT /note="F -> V (in dbSNP:rs4988350)"
FT /evidence="ECO:0000269|PubMed:12872252"
FT /id="VAR_020902"
FT VARIANT 540
FT /note="Q -> L (in dbSNP:rs4988349)"
FT /evidence="ECO:0000269|PubMed:12872252"
FT /id="VAR_020903"
FT VARIANT 633
FT /note="I -> M (in dbSNP:rs28997572)"
FT /id="VAR_052192"
FT VARIANT 647
FT /note="W -> C (in FANCJ; associated with C-707;
FT dbSNP:rs786202760)"
FT /evidence="ECO:0000269|PubMed:16116423"
FT /id="VAR_023703"
FT VARIANT 707
FT /note="R -> C (in FANCJ; associated with C-647;
FT dbSNP:rs764803896)"
FT /evidence="ECO:0000269|PubMed:16116423"
FT /id="VAR_023704"
FT VARIANT 832
FT /note="C -> Y (in dbSNP:rs4988355)"
FT /evidence="ECO:0000269|PubMed:12872252"
FT /id="VAR_020904"
FT VARIANT 919
FT /note="S -> P (in dbSNP:rs4986764)"
FT /evidence="ECO:0000269|PubMed:11301010,
FT ECO:0000269|PubMed:11920628, ECO:0000269|PubMed:12565990,
FT ECO:0000269|PubMed:12872252, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:16153896, ECO:0000269|PubMed:18987736"
FT /id="VAR_020905"
FT VARIANT 935
FT /note="V -> G (in dbSNP:rs4988356)"
FT /evidence="ECO:0000269|PubMed:12872252"
FT /id="VAR_020906"
FT VARIANT 1034
FT /note="P -> L (in a patient with ovarian cancer; unknown
FT pathological significance; dbSNP:rs1199923024)"
FT /evidence="ECO:0000269|PubMed:12565990"
FT /id="VAR_020907"
FT VARIANT 1148
FT /note="D -> E (in dbSNP:rs28997573)"
FT /id="VAR_052193"
FT MUTAGEN 52
FT /note="K->R: Disrupts BRCA1-mediated double-strand break
FT repair. Loss of ATPase and DNA helicase activities."
FT /evidence="ECO:0000269|PubMed:11301010,
FT ECO:0000269|PubMed:14983014, ECO:0000269|PubMed:16116421"
FT MUTAGEN 986
FT /note="S->A: Does not affect the interaction with BRCA1."
FT /evidence="ECO:0000269|PubMed:14576433"
FT MUTAGEN 988
FT /note="S->A: Does not affect the interaction with BRCA1."
FT /evidence="ECO:0000269|PubMed:14576433"
FT MUTAGEN 989
FT /note="T->A: Does not affect the interaction with BRCA1."
FT /evidence="ECO:0000269|PubMed:14576433"
FT MUTAGEN 990
FT /note="S->A: Disrupts the interaction with BRCA1."
FT /evidence="ECO:0000269|PubMed:14576433"
FT MUTAGEN 991
FT /note="P->A: Abolishes phosphorylation of S-990. Impairs
FT the interaction with BRCA1."
FT /evidence="ECO:0000269|PubMed:14576433"
FT MUTAGEN 992
FT /note="T->A: Does not affect the interaction with BRCA1."
FT /evidence="ECO:0000269|PubMed:14576433"
FT MUTAGEN 993
FT /note="F->A: Abolishes phosphorylation of S-990. Impairs
FT the interaction with BRCA1."
FT /evidence="ECO:0000269|PubMed:14576433"
FT MUTAGEN 997
FT /note="T->A: Does not affect the interaction with BRCA1."
FT /evidence="ECO:0000269|PubMed:14576433"
FT MUTAGEN 1001
FT /note="S->A: Does not affect the interaction with BRCA1."
FT /evidence="ECO:0000269|PubMed:14576433"
FT MUTAGEN 1003
FT /note="S->A: Does not affect the interaction with BRCA1."
FT /evidence="ECO:0000269|PubMed:14576433"
FT MUTAGEN 1004
FT /note="S->A: Does not affect the interaction with BRCA1."
FT /evidence="ECO:0000269|PubMed:14576433"
FT MUTAGEN 1007
FT /note="S->A: Does not affect the interaction with BRCA1."
FT /evidence="ECO:0000269|PubMed:14576433"
FT MUTAGEN 1011
FT /note="Y->A: Does not affect the interaction with BRCA1."
FT /evidence="ECO:0000269|PubMed:14576433"
FT MUTAGEN 1013
FT /note="T->A: Does not affect the interaction with BRCA1."
FT /evidence="ECO:0000269|PubMed:14576433"
FT CONFLICT 641
FT /note="I -> V (in Ref. 5; BAC11156)"
FT /evidence="ECO:0000305"
FT CONFLICT 767
FT /note="E -> I (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1249 AA; 140867 MW; 8ED691F03A442BE1 CRC64;
MSSMWSEYTI GGVKIYFPYK AYPSQLAMMN SILRGLNSKQ HCLLESPTGS GKSLALLCSA
LAWQQSLSGK PADEGVSEKA EVQLSCCCAC HSKDFTNNDM NQGTSRHFNY PSTPPSERNG
TSSTCQDSPE KTTLAAKLSA KKQASIYRDE NDDFQVEKKR IRPLETTQQI RKRHCFGTEV
HNLDAKVDSG KTVKLNSPLE KINSFSPQKP PGHCSRCCCS TKQGNSQESS NTIKKDHTGK
SKIPKIYFGT RTHKQIAQIT RELRRTAYSG VPMTILSSRD HTCVHPEVVG NFNRNEKCME
LLDGKNGKSC YFYHGVHKIS DQHTLQTFQG MCKAWDIEEL VSLGKKLKAC PYYTARELIQ
DADIIFCPYN YLLDAQIRES MDLNLKEQVV ILDEAHNIED CARESASYSV TEVQLRFARD
ELDSMVNNNI RKKDHEPLRA VCCSLINWLE ANAEYLVERD YESACKIWSG NEMLLTLHKM
GITTATFPIL QGHFSAVLQK EEKISPIYGK EEAREVPVIS ASTQIMLKGL FMVLDYLFRQ
NSRFADDYKI AIQQTYSWTN QIDISDKNGL LVLPKNKKRS RQKTAVHVLN FWCLNPAVAF
SDINGKVQTI VLTSGTLSPM KSFSSELGVT FTIQLEANHI IKNSQVWVGT IGSGPKGRNL
CATFQNTETF EFQDEVGALL LSVCQTVSQG ILCFLPSYKL LEKLKERWLS TGLWHNLELV
KTVIVEPQGG EKTNFDELLQ VYYDAIKYKG EKDGALLVAV CRGKVSEGLD FSDDNARAVI
TIGIPFPNVK DLQVELKRQY NDHHSKLRGL LPGRQWYEIQ AYRALNQALG RCIRHRNDWG
ALILVDDRFR NNPSRYISGL SKWVRQQIQH HSTFESALES LAEFSKKHQK VLNVSIKDRT
NIQDNESTLE VTSLKYSTSP YLLEAASHLS PENFVEDEAK ICVQELQCPK IITKNSPLPS
SIISRKEKND PVFLEEAGKA EKIVISRSTS PTFNKQTKRV SWSSFNSLGQ YFTGKIPKAT
PELGSSENSA SSPPRFKTEK MESKTVLPFT DKCESSNLTV NTSFGSCPQS ETIISSLKID
ATLTRKNHSE HPLCSEEALD PDIELSLVSE EDKQSTSNRD FETEAEDESI YFTPELYDPE
DTDEEKNDLA ETDRGNRLAN NSDCILAKDL FEIRTIKEVD SAREVKAEDC IDTKLNGILH
IEESKIDDID GNVKTTWINE LELGKTHEIE IKNFKPSPSK NKGMFPGFK
