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 27-MAR-2024, entry version 180. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 261. DR IntAct; Q6P158; 84. 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; 9606-ENSP00000405111; -. DR PeptideAtlas; Q6P158; -. DR ProteomicsDB; 66819; -. [Q6P158-1] DR ProteomicsDB; 66820; -. [Q6P158-2] DR ProteomicsDB; 66821; -. [Q6P158-3] DR Pumba; Q6P158; -. DR Antibodypedia; 29537; 77 antibodies from 17 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 AGR; HGNC:20086; -. 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; PERVYVQ; -. DR OrthoDB; 1095660at2759; -. DR PhylomeDB; Q6P158; -. DR TreeFam; TF324744; -. DR PathwayCommons; Q6P158; -. DR SignaLink; Q6P158; -. DR BioGRID-ORCS; 90957; 8 hits in 1155 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 175 other cell types or tissues. DR ExpressionAtlas; Q6P158; baseline and differential. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0004386; F:helicase activity; IBA:GO_Central. 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; cd17985; DEXHc_DHX57; 1. DR CDD; cd18791; SF2_C_RHA; 1. DR CDD; cd14317; UBA_DHX57; 1. DR Gene3D; 1.20.120.1080; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1. 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; IPR048333; HA2_WH. 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_dom. 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 PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1. DR PANTHER; PTHR18934:SF256; ATP-DEPENDENT RNA HELICASE DHX57-RELATED; 1. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF21010; HA2_C; 1. DR Pfam; PF04408; HA2_N; 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; SSF90229; CCCH zinc finger; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF46934; UBA-like; 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. DR Genevisible; Q6P158; HS. 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 //