SKIV2_HUMAN
ID SKIV2_HUMAN Reviewed; 1246 AA.
AC Q15477; O15005; Q12902; Q15476; Q5ST66;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Helicase SKI2W;
DE Short=Ski2;
DE EC=3.6.4.-;
DE AltName: Full=Helicase-like protein;
DE Short=HLP;
GN Name=SKIV2L; Synonyms=DDX13, SKI2W, SKIV2, W;
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].
RC TISSUE=Liver;
RX PubMed=7759100; DOI=10.1016/0888-7543(95)80008-a;
RA Lee S.-G., Lee I., Park S.H., Kang C., Song K.;
RT "Identification and characterization of a human cDNA homologous to yeast
RT SKI2.";
RL Genomics 25:660-666(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANTS ARG-151 AND LEU-214.
RX PubMed=7610041; DOI=10.1093/nar/23.12.2120;
RA Dangel A.W., Shen L., Mendoza A.R., Wu L.-C., Yu C.Y.;
RT "Human helicase gene SKI2W in the HLA class III region exhibits striking
RT structural similarities to the yeast antiviral gene SKI2 and to the human
RT gene KIAA0052: emergence of a new gene family.";
RL Nucleic Acids Res. 23:2120-2126(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-214.
RX PubMed=8812450; DOI=10.1006/geno.1996.0459;
RA Albertella M.R., Jones H., Thomson W., Olavesen M.G., Campbell R.D.;
RT "Localization of eight additional genes in the human major
RT histocompatibility complex, including the gene encoding the casein kinase
RT II beta subunit (CSNK2B).";
RL Genomics 36:240-251(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-151; LEU-214; MET-917
RP AND VAL-1071.
RA Rowen L., Dankers C., Baskin D., Faust J., Loretz C., Ahearn M.E.,
RA Banta A., Swartzell S., Smith T.M., Spies T., Hood L.;
RT "Sequence determination of 300 kilobases of the human class III MHC
RT locus.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP IDENTIFICATION IN THE SKI COMPLEX.
RX PubMed=16024656; DOI=10.1101/gad.1292105;
RA Zhu B., Mandal S.S., Pham A.D., Zheng Y., Erdjument-Bromage H., Batra S.K.,
RA Tempst P., Reinberg D.;
RT "The human PAF complex coordinates transcription with events downstream of
RT RNA synthesis.";
RL Genes Dev. 19:1668-1673(2005).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND IDENTIFICATION BY
RP 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 [12]
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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, 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 [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245 AND SER-256, AND
RP 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [19]
RP INTERACTION WITH ISOFORM 2 OF HBS1L.
RX PubMed=28204585; DOI=10.1093/nar/gkw862;
RA Kalisiak K., Kulinski T.M., Tomecki R., Cysewski D., Pietras Z.,
RA Chlebowski A., Kowalska K., Dziembowski A.;
RT "A short splicing isoform of HBS1L links the cytoplasmic exosome and SKI
RT complexes in humans.";
RL Nucleic Acids Res. 45:2068-2080(2017).
RN [20]
RP VARIANTS [LARGE SCALE ANALYSIS] VAL-183 AND ILE-765.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [21]
RP VARIANT THES2 GLY-341.
RX PubMed=22444670; DOI=10.1016/j.ajhg.2012.02.009;
RA Fabre A., Charroux B., Martinez-Vinson C., Roquelaure B., Odul E.,
RA Sayar E., Smith H., Colomb V., Andre N., Hugot J.P., Goulet O., Lacoste C.,
RA Sarles J., Royet J., Levy N., Badens C.;
RT "SKIV2L mutations cause syndromic diarrhea, or trichohepatoenteric
RT syndrome.";
RL Am. J. Hum. Genet. 90:689-692(2012).
CC -!- FUNCTION: Helicase; has ATPase activity. Component of the SKI complex
CC which is thought to be involved in exosome-mediated RNA decay and
CC associates with transcriptionally active genes in a manner dependent on
CC PAF1 complex (PAF1C).
CC -!- SUBUNIT: Component of the SKI complex which consists of WDR61, SKIV2L
CC and TTC37. Interacts with HBS1L isoform 2 (PubMed:28204585).
CC {ECO:0000269|PubMed:16024656, ECO:0000269|PubMed:28204585}.
CC -!- INTERACTION:
CC Q15477; P54284: CACNB3; NbExp=3; IntAct=EBI-373226, EBI-1184651;
CC Q15477; P54646: PRKAA2; NbExp=3; IntAct=EBI-373226, EBI-1383852;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm {ECO:0000305}.
CC -!- DISEASE: Trichohepatoenteric syndrome 2 (THES2) [MIM:614602]: A
CC syndrome characterized by intrauterine growth retardation, severe
CC diarrhea in infancy requiring total parenteral nutrition, facial
CC dysmorphism, immunodeficiency, and hair abnormalities, mostly
CC trichorrhexis nodosa. Hepatic involvement contributes to the poor
CC prognosis of affected patients. {ECO:0000269|PubMed:22444670}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB52523.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U09877; AAB52523.1; ALT_INIT; mRNA.
DR EMBL; X98378; CAA67024.1; -; Genomic_DNA.
DR EMBL; Z48796; CAA88733.1; -; mRNA.
DR EMBL; AF019413; AAB67978.1; -; Genomic_DNA.
DR EMBL; AL662849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL645922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS4731.1; -.
DR PIR; S56752; S56752.
DR RefSeq; NP_008860.4; NM_006929.4.
DR PDB; 7QDR; EM; 3.70 A; A=1-1246.
DR PDB; 7QDS; EM; 3.80 A; A=1-1246.
DR PDB; 7QDY; EM; 3.10 A; A=1-1246.
DR PDB; 7QDZ; EM; 3.60 A; A=1-1246.
DR PDB; 7QE0; EM; 6.50 A; A=1-1246.
DR PDBsum; 7QDR; -.
DR PDBsum; 7QDS; -.
DR PDBsum; 7QDY; -.
DR PDBsum; 7QDZ; -.
DR PDBsum; 7QE0; -.
DR AlphaFoldDB; Q15477; -.
DR SMR; Q15477; -.
DR BioGRID; 112390; 100.
DR CORUM; Q15477; -.
DR IntAct; Q15477; 26.
DR MINT; Q15477; -.
DR STRING; 9606.ENSP00000364543; -.
DR MoonDB; Q15477; Predicted.
DR GlyGen; Q15477; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q15477; -.
DR PhosphoSitePlus; Q15477; -.
DR BioMuta; SKIV2L; -.
DR DMDM; 313104288; -.
DR EPD; Q15477; -.
DR jPOST; Q15477; -.
DR MassIVE; Q15477; -.
DR MaxQB; Q15477; -.
DR PaxDb; Q15477; -.
DR PeptideAtlas; Q15477; -.
DR PRIDE; Q15477; -.
DR ProteomicsDB; 60607; -.
DR Antibodypedia; 28089; 93 antibodies from 24 providers.
DR DNASU; 6499; -.
DR Ensembl; ENST00000375394.7; ENSP00000364543.2; ENSG00000204351.12.
DR Ensembl; ENST00000383336.6; ENSP00000372827.4; ENSG00000206353.11.
DR Ensembl; ENST00000412823.4; ENSP00000400626.2; ENSG00000232616.9.
DR Ensembl; ENST00000421789.4; ENSP00000399530.2; ENSG00000228896.9.
DR Ensembl; ENST00000429465.4; ENSP00000412310.2; ENSG00000223493.9.
DR Ensembl; ENST00000448219.4; ENSP00000394400.2; ENSG00000225737.9.
DR GeneID; 6499; -.
DR KEGG; hsa:6499; -.
DR MANE-Select; ENST00000375394.7; ENSP00000364543.2; NM_006929.5; NP_008860.4.
DR UCSC; uc003nyn.2; human.
DR CTD; 6499; -.
DR DisGeNET; 6499; -.
DR GeneCards; SKIV2L; -.
DR GeneReviews; SKIV2L; -.
DR HGNC; HGNC:10898; SKIV2L.
DR HPA; ENSG00000204351; Low tissue specificity.
DR MalaCards; SKIV2L; -.
DR MIM; 600478; gene.
DR MIM; 614602; phenotype.
DR neXtProt; NX_Q15477; -.
DR OpenTargets; ENSG00000204351; -.
DR Orphanet; 84064; Syndromic diarrhea.
DR PharmGKB; PA35798; -.
DR VEuPathDB; HostDB:ENSG00000204351; -.
DR eggNOG; KOG0947; Eukaryota.
DR GeneTree; ENSGT00940000158255; -.
DR HOGENOM; CLU_002902_1_0_1; -.
DR InParanoid; Q15477; -.
DR OMA; DRNIWVH; -.
DR OrthoDB; 176060at2759; -.
DR PhylomeDB; Q15477; -.
DR TreeFam; TF314438; -.
DR PathwayCommons; Q15477; -.
DR Reactome; R-HSA-390471; Association of TriC/CCT with target proteins during biosynthesis.
DR Reactome; R-HSA-429958; mRNA decay by 3' to 5' exoribonuclease.
DR SignaLink; Q15477; -.
DR BioGRID-ORCS; 6499; 50 hits in 1079 CRISPR screens.
DR ChiTaRS; SKIV2L; human.
DR GeneWiki; SKIV2L; -.
DR GenomeRNAi; 6499; -.
DR Pharos; Q15477; Tbio.
DR PRO; PR:Q15477; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q15477; protein.
DR Bgee; ENSG00000204351; Expressed in right lobe of liver and 95 other tissues.
DR ExpressionAtlas; Q15477; baseline and differential.
DR Genevisible; Q15477; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0055087; C:Ski complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0070478; P:nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay; IBA:GO_Central.
DR GO; GO:0006401; P:RNA catabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR025696; rRNA_proc-arch_dom.
DR InterPro; IPR016438; Ski2-like.
DR InterPro; IPR012961; Ski2_C.
DR InterPro; IPR040801; Ski2_N.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF08148; DSHCT; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF13234; rRNA_proc-arch; 1.
DR Pfam; PF17911; Ski2_N; 1.
DR PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01142; DSHCT; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Disease variant; Helicase; Hydrolase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW RNA-binding.
FT CHAIN 1..1246
FT /note="Helicase SKI2W"
FT /id="PRO_0000102091"
FT DOMAIN 319..475
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 585..755
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 220..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 423..426
FT /note="DEVH box"
FT BINDING 332..339
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VARIANT 151
FT /note="Q -> R (in dbSNP:rs438999)"
FT /evidence="ECO:0000269|PubMed:7610041, ECO:0000269|Ref.4"
FT /id="VAR_060379"
FT VARIANT 183
FT /note="L -> V (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035944"
FT VARIANT 214
FT /note="M -> L (in dbSNP:rs437179)"
FT /evidence="ECO:0000269|PubMed:7610041,
FT ECO:0000269|PubMed:8812450, ECO:0000269|Ref.4"
FT /id="VAR_060380"
FT VARIANT 324
FT /note="R -> W (in dbSNP:rs36038685)"
FT /id="VAR_055888"
FT VARIANT 341
FT /note="V -> G (in THES2; dbSNP:rs281875237)"
FT /evidence="ECO:0000269|PubMed:22444670"
FT /id="VAR_067721"
FT VARIANT 765
FT /note="M -> I (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs557829269)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035945"
FT VARIANT 887
FT /note="D -> N (in dbSNP:rs3911893)"
FT /id="VAR_055889"
FT VARIANT 917
FT /note="V -> M (in dbSNP:rs106287)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_055890"
FT VARIANT 1071
FT /note="A -> V (in dbSNP:rs449643)"
FT /evidence="ECO:0000269|Ref.4"
FT /id="VAR_055891"
FT VARIANT 1153
FT /note="G -> R (in dbSNP:rs2734329)"
FT /id="VAR_060381"
FT VARIANT 1238
FT /note="V -> G (in dbSNP:rs2746400)"
FT /id="VAR_060382"
FT CONFLICT 366
FT /note="S -> T (in Ref. 1; AAB52523)"
FT /evidence="ECO:0000305"
FT CONFLICT 623
FT /note="H -> Q (in Ref. 2; CAA88733)"
FT /evidence="ECO:0000305"
FT CONFLICT 1052
FT /note="L -> F (in Ref. 2; CAA88733)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1246 AA; 137755 MW; 9F00097BA83A4AEC CRC64;
MMETERLVLP PPDPLDLPLR AVELGCTGHW ELLNLPGAPE SSLPHGLPPC APDLQQEAEQ
LFLSSPAWLP LHGVEHSARK WQRKTDPWSL LAVLGAPVPS DLQAQRHPTT GQILGYKEVL
LENTNLSATT SLSLRRPPGP ASQSLWGNPT QYPFWPGGMD EPTITDLNTR EEAEEEIDFE
KDLLTIPPGF KKGMDFAPKD CPTPAPGLLS LSCMLEPLDL GGGDEDENEA VGQPGGPRGD
TVSASPCSAP LARASSLEDL VLKEASTAVS TPEAPEPPSQ EQWAIPVDAT SPVGDFYRLI
PQPAFQWAFE PDVFQKQAIL HLERHDSVFV AAHTSAGKTV VAEYAIALAQ KHMTRTIYTS
PIKALSNQKF RDFRNTFGDV GLLTGDVQLH PEASCLIMTT EILRSMLYSG SDVIRDLEWV
IFDEVHYIND VERGVVWEEV LIMLPDHVSI ILLSATVPNA LEFADWIGRL KRRQIYVIST
VTRPVPLEHY LFTGNSSKTQ GELFLLLDSR GAFHTKGYYA AVEAKKERMS KHAQTFGAKQ
PTHQGGPAQD RGVYLSLLAS LRTRAQLPVV VFTFSRGRCD EQASGLTSLD LTTSSEKSEI
HLFLQRCLAR LRGSDRQLPQ VLHMSELLNR GLGVHHSGIL PILKEIVEML FSRGLVKVLF
ATETFAMGVN MPARTVVFDS MRKHDGSTFR DLLPGEYVQM AGRAGRRGLD PTGTVILLCK
GRVPEMADLH RMMMGKPSQL QSQFRLTYTM ILNLLRVDAL RVEDMMKRSF SEFPSRKDSK
AHEQALAELT KRLGALEEPD MTGQLVDLPE YYSWGEELTE TQHMIQRRIM ESVNGLKSLS
AGRVVVVKNQ EHHNALGVIL QVSSNSTSRV FTTLVLCDKP LSQDPQDRGP ATAEVPYPDD
LVGFKLFLPE GPCDHTVVKL QPGDMAAITT KVLRVNGEKI LEDFSKRQQP KFKKDPPLAA
VTTAVQELLR LAQAHPAGPP TLDPVNDLQL KDMSVVEGGL RARKLEELIQ GAQCVHSPRF
PAQYLKLRER MQIQKEMERL RFLLSDQSLL LLPEYHQRVE VLRTLGYVDE AGTVKLAGRV
ACAMSSHELL LTELMFDNAL STLRPEEIAA LLSGLVCQSP GDAGDQLPNT LKQGIERVRA
VAKRIGEVQV ACGLNQTVEE FVGELNFGLV EVVYEWARGM PFSELAGLSG TPEGLVVRCI
QRLAEMCRSL RGAARLVGEP VLGAKMETAA TLLRRDIVFA ASLYTQ
