DHX57_HUMAN
ID DHX57_HUMAN Reviewed; 1386 AA.
AC Q6P158; A2RRC7; Q53SI4; Q6P9G1; Q7Z6H3; Q8NG17; Q96M33;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Putative ATP-dependent RNA helicase DHX57;
DE EC=3.6.4.13;
DE AltName: Full=DEAH box protein 57;
GN Name=DHX57;
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 [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP SER-587.
RC TISSUE=Skin;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 405-1386 (ISOFORM 1), AND VARIANT SER-587.
RC TISSUE=Brain;
RA Lin S., Ying K., Wang Z., Xie Y., Mao Y.;
RT "Molecular cloning of a new member of DEAH-box RNA/DNA helicase gene
RT family.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-480, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475; SER-477 AND SER-480, 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-127 AND SER-132, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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).
CC -!- FUNCTION: Probable ATP-binding RNA helicase.
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 -!- INTERACTION:
CC Q6P158; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-1051531, EBI-3866279;
CC Q6P158; Q14781: CBX2; NbExp=3; IntAct=EBI-1051531, EBI-745934;
CC Q6P158; Q14781-2: CBX2; NbExp=3; IntAct=EBI-1051531, EBI-11974585;
CC Q6P158; Q9C0F1: CEP44; NbExp=3; IntAct=EBI-1051531, EBI-744115;
CC Q6P158; Q6A162: KRT40; NbExp=3; IntAct=EBI-1051531, EBI-10171697;
CC Q6P158; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-1051531, EBI-10172150;
CC Q6P158; P60371: KRTAP10-6; NbExp=3; IntAct=EBI-1051531, EBI-12012928;
CC Q6P158; P60409: KRTAP10-7; NbExp=6; IntAct=EBI-1051531, EBI-10172290;
CC Q6P158; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-1051531, EBI-10171774;
CC Q6P158; P60411: KRTAP10-9; NbExp=6; IntAct=EBI-1051531, EBI-10172052;
CC Q6P158; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-1051531, EBI-11953334;
CC Q6P158; Q9BYR9: KRTAP2-4; NbExp=3; IntAct=EBI-1051531, EBI-14065470;
CC Q6P158; Q9BYQ2: KRTAP9-4; NbExp=3; IntAct=EBI-1051531, EBI-10185730;
CC Q6P158; P41227: NAA10; NbExp=3; IntAct=EBI-1051531, EBI-747693;
CC Q6P158; Q9UPG8: PLAGL2; NbExp=3; IntAct=EBI-1051531, EBI-2876622;
CC Q6P158; P0DJD3-2: RBMY1A1; NbExp=3; IntAct=EBI-1051531, EBI-11994018;
CC Q6P158; Q2I0M5: RSPO4; NbExp=3; IntAct=EBI-1051531, EBI-12821217;
CC Q6P158; Q8WTR7: ZNF473; NbExp=3; IntAct=EBI-1051531, EBI-751409;
CC Q6P158; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-1051531, EBI-6427977;
CC Q6P158; Q96EG3: ZNF837; NbExp=3; IntAct=EBI-1051531, EBI-11962574;
CC Q6P158-2; Q9BYQ2: KRTAP9-4; NbExp=3; IntAct=EBI-10252144, EBI-10185730;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6P158-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P158-2; Sequence=VSP_018059, VSP_018060;
CC Name=3;
CC IsoId=Q6P158-3; Sequence=VSP_018056, VSP_018057, VSP_018058;
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM73547.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAY24256.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK057423; BAB71479.1; -; mRNA.
DR EMBL; AC018693; AAY24256.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC053623; AAH53623.1; -; mRNA.
DR EMBL; BC060778; AAH60778.2; -; mRNA.
DR EMBL; BC065278; AAH65278.1; -; mRNA.
DR EMBL; BC131534; AAI31535.1; -; mRNA.
DR EMBL; AF283512; AAM73547.1; ALT_INIT; mRNA.
DR CCDS; CCDS1800.1; -. [Q6P158-1]
DR RefSeq; NP_945314.1; NM_198963.2. [Q6P158-1]
DR RefSeq; XP_011531456.1; XM_011533154.2. [Q6P158-1]
DR RefSeq; XP_011531457.1; XM_011533155.2. [Q6P158-1]
DR AlphaFoldDB; Q6P158; -.
DR SMR; Q6P158; -.
DR BioGRID; 124783; 232.
DR IntAct; Q6P158; 81.
DR MINT; Q6P158; -.
DR STRING; 9606.ENSP00000405111; -.
DR CarbonylDB; Q6P158; -.
DR GlyGen; Q6P158; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6P158; -.
DR PhosphoSitePlus; Q6P158; -.
DR BioMuta; DHX57; -.
DR DMDM; 94710252; -.
DR EPD; Q6P158; -.
DR jPOST; Q6P158; -.
DR MassIVE; Q6P158; -.
DR MaxQB; Q6P158; -.
DR PaxDb; Q6P158; -.
DR PeptideAtlas; Q6P158; -.
DR PRIDE; Q6P158; -.
DR ProteomicsDB; 66819; -. [Q6P158-1]
DR ProteomicsDB; 66820; -. [Q6P158-2]
DR ProteomicsDB; 66821; -. [Q6P158-3]
DR Antibodypedia; 29537; 60 antibodies from 16 providers.
DR DNASU; 90957; -.
DR Ensembl; ENST00000457308.6; ENSP00000405111.2; ENSG00000163214.21. [Q6P158-1]
DR GeneID; 90957; -.
DR KEGG; hsa:90957; -.
DR MANE-Select; ENST00000457308.6; ENSP00000405111.2; NM_198963.3; NP_945314.1.
DR UCSC; uc002rrf.5; human. [Q6P158-1]
DR CTD; 90957; -.
DR DisGeNET; 90957; -.
DR GeneCards; DHX57; -.
DR HGNC; HGNC:20086; DHX57.
DR HPA; ENSG00000163214; Low tissue specificity.
DR neXtProt; NX_Q6P158; -.
DR OpenTargets; ENSG00000163214; -.
DR PharmGKB; PA134919698; -.
DR VEuPathDB; HostDB:ENSG00000163214; -.
DR eggNOG; KOG0920; Eukaryota.
DR GeneTree; ENSGT00940000156883; -.
DR HOGENOM; CLU_001832_4_1_1; -.
DR InParanoid; Q6P158; -.
DR OMA; PKCRFAH; -.
DR OrthoDB; 278674at2759; -.
DR PhylomeDB; Q6P158; -.
DR TreeFam; TF324744; -.
DR PathwayCommons; Q6P158; -.
DR SignaLink; Q6P158; -.
DR BioGRID-ORCS; 90957; 7 hits in 1078 CRISPR screens.
DR ChiTaRS; DHX57; human.
DR GeneWiki; DHX57; -.
DR GenomeRNAi; 90957; -.
DR Pharos; Q6P158; Tdark.
DR PRO; PR:Q6P158; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q6P158; protein.
DR Bgee; ENSG00000163214; Expressed in sperm and 173 other tissues.
DR ExpressionAtlas; Q6P158; baseline and differential.
DR Genevisible; Q6P158; HS.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR CDD; cd14317; UBA_DHX57; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR042615; DHX57_UBA.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006575; RWD-domain.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR041367; Znf-CCCH_4.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR Pfam; PF05773; RWD; 1.
DR Pfam; PF18044; zf-CCCH_4; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90229; SSF90229; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Coiled coil; Helicase; Hydrolase;
KW Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Zinc; Zinc-finger.
FT CHAIN 1..1386
FT /note="Putative ATP-dependent RNA helicase DHX57"
FT /id="PRO_0000233151"
FT DOMAIN 180..220
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 554..721
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 830..1010
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT ZN_FING 299..326
FT /note="C3H1-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 101..125
FT /evidence="ECO:0000255"
FT MOTIF 668..671
FT /note="DEVH box"
FT COMPBIAS 55..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 567..574
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..102
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_018056"
FT VAR_SEQ 530..535
FT /note="ASRQFQ -> VLNSHM (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_018057"
FT VAR_SEQ 536..1386
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_018058"
FT VAR_SEQ 636..658
FT /note="SSATRLLYCTTGVLLRRLEGDTA -> VCMLCLFPGNRNLWFLGIKSFGG
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018059"
FT VAR_SEQ 659..1386
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018060"
FT VARIANT 410
FT /note="S -> F (in dbSNP:rs11893062)"
FT /id="VAR_052190"
FT VARIANT 433
FT /note="S -> G (in dbSNP:rs35371077)"
FT /id="VAR_033861"
FT VARIANT 587
FT /note="N -> S (in dbSNP:rs7598922)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.4"
FT /id="VAR_052191"
FT CONFLICT 474
FT /note="A -> T (in Ref. 1; BAB71479)"
FT /evidence="ECO:0000305"
FT CONFLICT 976
FT /note="L -> V (in Ref. 4; AAM73547)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1386 AA; 155604 MW; FFF62BD4BF4C1F4D CRC64;
MSSSVRRKGK PGKGGGKGSS RGGRGGRSHA SKSHGSGGGG GGGGGGGGGN RKASSRIWDD
GDDFCIFSES RRPSRPSNSN ISKGESRPKW KPKAKVPLQT LHMTSENQEK VKALLRDLQE
QDADAGSERG LSGEEEDDEP DCCNDERYWP AGQEPSLVPD LDPLEYAGLA SVEPYVPEFT
VSPFAVQKLS RYGFNTERCQ AVLRMCDGDV GASLEHLLTQ CFSETFGERM KISEAVNQIS
LDECMEQRQE EAFALKSICG EKFIERIQNR VWTIGLELEY LTSRFRKSKP KESTKNVQEN
SLEICKFYLK GNCKFGSKCR FKHEVPPNQI VGRIERSVDD SHLNAIEDAS FLYELEIRFS
KDHKYPYQAP LVAFYSTNEN LPLACRLHIS EFLYDKALTF AETSEPVVYS LITLLEEESE
IVKLLTNTHH KYSDPPVNFL PVPSRTRINN PACHKTVIPN NSFVSNQIPE VEKASESEES
DEDDGPAPVI VENESYVNLK KKISKRYDWQ AKSVHAENGK ICKQFRMKQA SRQFQSILQE
RQSLPAWEER ETILNLLRKH QVVVISGMTG CGKTTQIPQF ILDDSLNGPP EKVANIICTQ
PRRISAISVA ERVAKERAER VGLTVGYQIR LESVKSSATR LLYCTTGVLL RRLEGDTALQ
GVSHIIVDEV HERTEESDFL LLVLKDIVSQ RPGLQVILMS ATLNAELFSD YFNSCPVITI
PGRTFPVDQF FLEDAIAVTR YVLQDGSPYM RSMKQISKEK LKARRNRTAF EEVEEDLRLS
LHLQDQDSVK DAVPDQQLDF KQLLARYKGV SKSVIKTMSI MDFEKVNLEL IEALLEWIVD
GKHSYPPGAI LVFLPGLAEI KMLYEQLQSN SLFNNRRSNR CVIHPLHSSL SSEEQQAVFV
KPPAGVTKII ISTNIAETSI TIDDVVYVID SGKMKEKRYD ASKGMESLED TFVSQANALQ
RKGRAGRVAS GVCFHLFTSH HYNHQLLKQQ LPEIQRVPLE QLCLRIKILE MFSAHNLQSV
FSRLIEPPHT DSLRASKIRL RDLGALTPDE RLTPLGYHLA SLPVDVRIGK LMLFGSIFRC
LDPALTIAAS LAFKSPFVSP WDKKEEANQK KLEFAFANSD YLALLQAYKG WQLSTKEGVR
ASYNYCRQNF LSGRVLQEMA SLKRQFTELL SDIGFAREGL RAREIEKRAQ GGDGVLDATG
EEANSNAENP KLISAMLCAA LYPNVVQVKS PEGKFQKTST GAVRMQPKSA ELKFVTKNDG
YVHIHPSSVN YQVRHFDSPY LLYHEKIKTS RVFIRDCSMV SVYPLVLFGG GQVNVQLQRG
EFVVSLDDGW IRFVAASHQV AELVKELRCE LDQLLQDKIK NPSIDLCTCP RGSRIISTIV
KLVTTQ
