SKI_HUMAN
ID SKI_HUMAN Reviewed; 728 AA.
AC P12755; Q5SYT7;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Ski oncogene;
DE AltName: Full=Proto-oncogene c-Ski;
GN Name=SKI;
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].
RX PubMed=2762147; DOI=10.1093/nar/17.14.5489;
RA Nomura N., Sasamoto S., Ishii S., Date T., Matsui M., Ishizaki R.;
RT "Isolation of human cDNA clones of ski and the ski-related gene, sno.";
RL Nucleic Acids Res. 17:5489-5500(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP INTERACTION WITH HIPK2; SMAD2; SMAD3 AND SMAD4.
RX PubMed=12874272; DOI=10.1074/jbc.m307112200;
RA Harada J., Kokura K., Kanei-Ishii C., Nomura T., Khan M.M., Kim Y.,
RA Ishii S.;
RT "Requirement of the co-repressor homeodomain-interacting protein kinase 2
RT for ski-mediated inhibition of bone morphogenetic protein-induced
RT transcriptional activation.";
RL J. Biol. Chem. 278:38998-39005(2003).
RN [4]
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 [5]
RP FUNCTION, AND INTERACTION WITH PRDM16 AND SMAD3.
RX PubMed=19049980; DOI=10.1074/jbc.m808989200;
RA Takahata M., Inoue Y., Tsuda H., Imoto I., Koinuma D., Hayashi M.,
RA Ichikura T., Yamori T., Nagasaki K., Yoshida M., Matsuoka M., Morishita K.,
RA Yuki K., Hanyu A., Miyazawa K., Inazawa J., Miyazono K., Imamura T.;
RT "SKI and MEL1 cooperate to inhibit transforming growth factor-beta signal
RT in gastric cancer cells.";
RL J. Biol. Chem. 284:3334-3344(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-383; SER-432 AND SER-720, 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 [8]
RP VARIANTS SGS LEU-31; VAL-32; PRO-32; CYS-34; VAL-34; SER-34; GLN-35;
RP SER-35; 94-SER--SER-97 DEL AND 95-ASP--SER-97 DEL.
RX PubMed=23103230; DOI=10.1016/j.ajhg.2012.10.002;
RA Carmignac V., Thevenon J., Ades L., Callewaert B., Julia S.,
RA Thauvin-Robinet C., Gueneau L., Courcet J.B., Lopez E., Holman K.,
RA Renard M., Plauchu H., Plessis G., De Backer J., Child A., Arno G.,
RA Duplomb L., Callier P., Aral B., Vabres P., Gigot N., Arbustini E.,
RA Grasso M., Robinson P.N., Goizet C., Baumann C., Di Rocco M.,
RA Sanchez Del Pozo J., Huet F., Jondeau G., Collod-Beroud G., Beroud C.,
RA Amiel J., Cormier-Daire V., Riviere J.B., Boileau C., De Paepe A.,
RA Faivre L.;
RT "In-frame mutations in exon 1 of SKI cause dominant Shprintzen-Goldberg
RT syndrome.";
RL Am. J. Hum. Genet. 91:950-957(2012).
RN [9]
RP VARIANTS SGS ARG-21; VAL-32; ASP-34; CYS-34; SER-34; SER-35; 95-ASP--SER-97
RP DEL; GLU-116 AND ARG-117.
RX PubMed=23023332; DOI=10.1038/ng.2421;
RA Doyle A.J., Doyle J.J., Bessling S.L., Maragh S., Lindsay M.E.,
RA Schepers D., Gillis E., Mortier G., Homfray T., Sauls K., Norris R.A.,
RA Huso N.D., Leahy D., Mohr D.W., Caulfield M.J., Scott A.F., Destree A.,
RA Hennekam R.C., Arn P.H., Curry C.J., Van Laer L., McCallion A.S.,
RA Loeys B.L., Dietz H.C.;
RT "Mutations in the TGF-beta repressor SKI cause Shprintzen-Goldberg syndrome
RT with aortic aneurysm.";
RL Nat. Genet. 44:1249-1254(2012).
RN [10]
RP VARIANTS SGS SER-35 AND GLU-116.
RX PubMed=24357594; DOI=10.1002/ajmg.a.36340;
RG FORGE Canada Consortium;
RA Au P.Y., Racher H.E., Graham J.M. Jr., Kramer N., Lowry R.B.,
RA Parboosingh J.S., Innes A.M.;
RT "De novo exon 1 missense mutations of SKI and Shprintzen-Goldberg syndrome:
RT two new cases and a clinical review.";
RL Am. J. Med. Genet. A 164A:676-684(2014).
RN [11]
RP VARIANTS SGS THR-28; LEU-31; VAL-32; VAL-34; ALA-34; ASP-34; SER-34 AND
RP SER-35.
RX PubMed=24736733; DOI=10.1038/ejhg.2014.61;
RA Schepers D., Doyle A.J., Oswald G., Sparks E., Myers L., Willems P.J.,
RA Mansour S., Simpson M.A., Frysira H., Maat-Kievit A., Van Minkelen R.,
RA Hoogeboom J.M., Mortier G.R., Titheradge H., Brueton L., Starr L.,
RA Stark Z., Ockeloen C., Lourenco C.M., Blair E., Hobson E., Hurst J.,
RA Maystadt I., Destree A., Girisha K.M., Miller M., Dietz H.C., Loeys B.,
RA Van Laer L.;
RT "The SMAD-binding domain of SKI: a hotspot for de novo mutations causing
RT Shprintzen-Goldberg syndrome.";
RL Eur. J. Hum. Genet. 23:224-228(2015).
CC -!- FUNCTION: May play a role in terminal differentiation of skeletal
CC muscle cells but not in the determination of cells to the myogenic
CC lineage. Functions as a repressor of TGF-beta signaling.
CC {ECO:0000269|PubMed:19049980}.
CC -!- SUBUNIT: Interacts with SMAD2, SMAD3 and SMAD4. Interacts with HIPK2.
CC Part of a complex with HIPK2 and SMAD1/2/3. Interacts with PRDM16 and
CC SMAD3; the interaction with PRDM16 promotes the recruitment SMAD3-HDAC1
CC complex on the promoter of TGF-beta target genes.
CC {ECO:0000269|PubMed:12874272, ECO:0000269|PubMed:19049980}.
CC -!- INTERACTION:
CC P12755; O75376: NCOR1; NbExp=4; IntAct=EBI-347281, EBI-347233;
CC P12755; Q6ZSG1: RNF165; NbExp=2; IntAct=EBI-347281, EBI-2129206;
CC P12755; Q96ST3: SIN3A; NbExp=3; IntAct=EBI-347281, EBI-347218;
CC P12755; Q15796: SMAD2; NbExp=10; IntAct=EBI-347281, EBI-1040141;
CC P12755; P84022: SMAD3; NbExp=8; IntAct=EBI-347281, EBI-347161;
CC P12755; Q13485: SMAD4; NbExp=13; IntAct=EBI-347281, EBI-347263;
CC P12755; Q9QUI1: Fam89b; Xeno; NbExp=6; IntAct=EBI-347281, EBI-6503100;
CC P12755; Q60974: Ncor1; Xeno; NbExp=5; IntAct=EBI-347281, EBI-349004;
CC P12755; Q8VI24: Satb2; Xeno; NbExp=2; IntAct=EBI-347281, EBI-5737999;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- PTM: Ubiquitinated by RNF165, promoting proteasomal degradation,
CC leading to enhance the BMP-Smad signaling.
CC {ECO:0000250|UniProtKB:Q60698}.
CC -!- DISEASE: Shprintzen-Goldberg craniosynostosis syndrome (SGS)
CC [MIM:182212]: A very rare syndrome characterized by a marfanoid
CC habitus, craniosynostosis, characteristic dysmorphic facial features,
CC skeletal and cardiovascular abnormalities, intellectual disability,
CC developmental delay and learning disabilities.
CC {ECO:0000269|PubMed:23023332, ECO:0000269|PubMed:23103230,
CC ECO:0000269|PubMed:24357594, ECO:0000269|PubMed:24736733}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the SKI family. {ECO:0000305}.
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DR EMBL; X15218; CAA33288.1; -; mRNA.
DR EMBL; AL590822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS39.1; -.
DR PIR; S06053; TVHUSK.
DR RefSeq; NP_003027.1; NM_003036.3.
DR PDB; 1MR1; X-ray; 2.85 A; C/D=219-313.
DR PDB; 1SBX; X-ray; 1.65 A; A=91-192.
DR PDB; 5XOD; X-ray; 1.85 A; B=15-40.
DR PDB; 6ZVQ; X-ray; 2.03 A; B=11-45.
DR PDBsum; 1MR1; -.
DR PDBsum; 1SBX; -.
DR PDBsum; 5XOD; -.
DR PDBsum; 6ZVQ; -.
DR AlphaFoldDB; P12755; -.
DR SMR; P12755; -.
DR BioGRID; 112388; 170.
DR CORUM; P12755; -.
DR DIP; DIP-31514N; -.
DR IntAct; P12755; 25.
DR MINT; P12755; -.
DR STRING; 9606.ENSP00000367797; -.
DR GlyGen; P12755; 3 sites, 2 O-linked glycans (3 sites).
DR iPTMnet; P12755; -.
DR PhosphoSitePlus; P12755; -.
DR BioMuta; SKI; -.
DR DMDM; 134517; -.
DR EPD; P12755; -.
DR jPOST; P12755; -.
DR MassIVE; P12755; -.
DR MaxQB; P12755; -.
DR PaxDb; P12755; -.
DR PeptideAtlas; P12755; -.
DR PRIDE; P12755; -.
DR ProteomicsDB; 52865; -.
DR Antibodypedia; 4180; 204 antibodies from 38 providers.
DR DNASU; 6497; -.
DR Ensembl; ENST00000378536.5; ENSP00000367797.4; ENSG00000157933.10.
DR GeneID; 6497; -.
DR KEGG; hsa:6497; -.
DR MANE-Select; ENST00000378536.5; ENSP00000367797.4; NM_003036.4; NP_003027.1.
DR UCSC; uc001aja.5; human.
DR CTD; 6497; -.
DR DisGeNET; 6497; -.
DR GeneCards; SKI; -.
DR GeneReviews; SKI; -.
DR HGNC; HGNC:10896; SKI.
DR HPA; ENSG00000157933; Low tissue specificity.
DR MalaCards; SKI; -.
DR MIM; 164780; gene.
DR MIM; 182212; phenotype.
DR neXtProt; NX_P12755; -.
DR OpenTargets; ENSG00000157933; -.
DR Orphanet; 1606; 1p36 deletion syndrome.
DR Orphanet; 2462; Shprintzen-Goldberg syndrome.
DR PharmGKB; PA35796; -.
DR VEuPathDB; HostDB:ENSG00000157933; -.
DR eggNOG; ENOG502QTF6; Eukaryota.
DR GeneTree; ENSGT00940000160546; -.
DR HOGENOM; CLU_025786_0_0_1; -.
DR InParanoid; P12755; -.
DR OMA; NPPCATV; -.
DR OrthoDB; 633642at2759; -.
DR PhylomeDB; P12755; -.
DR TreeFam; TF324133; -.
DR PathwayCommons; P12755; -.
DR Reactome; R-HSA-201451; Signaling by BMP.
DR Reactome; R-HSA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR SignaLink; P12755; -.
DR SIGNOR; P12755; -.
DR BioGRID-ORCS; 6497; 27 hits in 1081 CRISPR screens.
DR ChiTaRS; SKI; human.
DR EvolutionaryTrace; P12755; -.
DR GeneWiki; SKI_protein; -.
DR GenomeRNAi; 6497; -.
DR Pharos; P12755; Tbio.
DR PRO; PR:P12755; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P12755; protein.
DR Bgee; ENSG00000157933; Expressed in nipple and 185 other tissues.
DR Genevisible; P12755; HS.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
DR GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; ISS:BHF-UCL.
DR GO; GO:0017053; C:transcription repressor complex; ISS:BHF-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:GO_Central.
DR GO; GO:0046811; F:histone deacetylase inhibitor activity; ISS:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0046332; F:SMAD binding; IPI:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0009948; P:anterior/posterior axis specification; ISS:BHF-UCL.
DR GO; GO:0060349; P:bone morphogenesis; ISS:BHF-UCL.
DR GO; GO:0043010; P:camera-type eye development; ISS:BHF-UCL.
DR GO; GO:0048593; P:camera-type eye morphogenesis; ISS:BHF-UCL.
DR GO; GO:0048870; P:cell motility; NAS:BHF-UCL.
DR GO; GO:0030326; P:embryonic limb morphogenesis; ISS:BHF-UCL.
DR GO; GO:0060325; P:face morphogenesis; ISS:BHF-UCL.
DR GO; GO:0002089; P:lens morphogenesis in camera-type eye; ISS:BHF-UCL.
DR GO; GO:0022011; P:myelination in peripheral nervous system; ISS:BHF-UCL.
DR GO; GO:0014902; P:myotube differentiation; IDA:UniProtKB.
DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; ISS:BHF-UCL.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IDA:UniProtKB.
DR GO; GO:0010626; P:negative regulation of Schwann cell proliferation; IGI:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0001843; P:neural tube closure; ISS:BHF-UCL.
DR GO; GO:0043585; P:nose morphogenesis; ISS:BHF-UCL.
DR GO; GO:0021772; P:olfactory bulb development; ISS:BHF-UCL.
DR GO; GO:0043388; P:positive regulation of DNA binding; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; NAS:BHF-UCL.
DR GO; GO:0060041; P:retina development in camera-type eye; ISS:BHF-UCL.
DR GO; GO:0060021; P:roof of mouth development; ISS:BHF-UCL.
DR GO; GO:0048741; P:skeletal muscle fiber development; ISS:BHF-UCL.
DR GO; GO:0060395; P:SMAD protein signal transduction; IDA:UniProtKB.
DR GO; GO:0035019; P:somatic stem cell population maintenance; ISS:BHF-UCL.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; NAS:BHF-UCL.
DR Gene3D; 3.10.260.20; -; 1.
DR Gene3D; 3.10.390.10; -; 1.
DR IDEAL; IID00131; -.
DR InterPro; IPR014890; c-SKI_SMAD4-bd_dom.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR010919; SAND-like_dom_sf.
DR InterPro; IPR028760; Ski.
DR InterPro; IPR003380; SKI/SNO/DAC.
DR InterPro; IPR037000; Ski_DNA-bd_sf.
DR InterPro; IPR023216; Tscrpt_reg_SKI_SnoN.
DR PANTHER; PTHR10005; PTHR10005; 1.
DR PANTHER; PTHR10005:SF15; PTHR10005:SF15; 1.
DR Pfam; PF08782; c-SKI_SMAD_bind; 1.
DR Pfam; PF02437; Ski_Sno; 1.
DR SMART; SM01046; c-SKI_SMAD_bind; 1.
DR SUPFAM; SSF46955; SSF46955; 1.
DR SUPFAM; SSF63763; SSF63763; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Craniosynostosis; Disease variant; Nucleus;
KW Phosphoprotein; Proto-oncogene; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..728
FT /note="Ski oncogene"
FT /id="PRO_0000129382"
FT REGION 321..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 536..710
FT /evidence="ECO:0000255"
FT COMPBIAS 332..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 21
FT /note="L -> R (in SGS; dbSNP:rs869312902)"
FT /evidence="ECO:0000269|PubMed:23023332"
FT /id="VAR_071170"
FT VARIANT 28
FT /note="S -> T (in SGS)"
FT /evidence="ECO:0000269|PubMed:24736733"
FT /id="VAR_071659"
FT VARIANT 31
FT /note="S -> L (in SGS)"
FT /evidence="ECO:0000269|PubMed:23103230,
FT ECO:0000269|PubMed:24736733"
FT /id="VAR_071171"
FT VARIANT 32
FT /note="L -> P (in SGS)"
FT /evidence="ECO:0000269|PubMed:23103230"
FT /id="VAR_071172"
FT VARIANT 32
FT /note="L -> V (in SGS; dbSNP:rs387907304)"
FT /evidence="ECO:0000269|PubMed:23023332,
FT ECO:0000269|PubMed:23103230, ECO:0000269|PubMed:24736733"
FT /id="VAR_071173"
FT VARIANT 34
FT /note="G -> A (in SGS)"
FT /evidence="ECO:0000269|PubMed:24736733"
FT /id="VAR_071660"
FT VARIANT 34
FT /note="G -> C (in SGS; dbSNP:rs387907306)"
FT /evidence="ECO:0000269|PubMed:23023332,
FT ECO:0000269|PubMed:23103230"
FT /id="VAR_071174"
FT VARIANT 34
FT /note="G -> D (in SGS; dbSNP:rs387907305)"
FT /evidence="ECO:0000269|PubMed:23023332,
FT ECO:0000269|PubMed:24736733"
FT /id="VAR_071175"
FT VARIANT 34
FT /note="G -> S (in SGS; dbSNP:rs387907306)"
FT /evidence="ECO:0000269|PubMed:23023332,
FT ECO:0000269|PubMed:23103230, ECO:0000269|PubMed:24736733"
FT /id="VAR_071176"
FT VARIANT 34
FT /note="G -> V (in SGS; dbSNP:rs387907305)"
FT /evidence="ECO:0000269|PubMed:23103230,
FT ECO:0000269|PubMed:24736733"
FT /id="VAR_071177"
FT VARIANT 35
FT /note="P -> Q (in SGS; dbSNP:rs397514589)"
FT /evidence="ECO:0000269|PubMed:23103230"
FT /id="VAR_071178"
FT VARIANT 35
FT /note="P -> S (in SGS; dbSNP:rs397514590)"
FT /evidence="ECO:0000269|PubMed:23023332,
FT ECO:0000269|PubMed:23103230, ECO:0000269|PubMed:24357594,
FT ECO:0000269|PubMed:24736733"
FT /id="VAR_071179"
FT VARIANT 94..97
FT /note="Missing (in SGS)"
FT /evidence="ECO:0000269|PubMed:23103230"
FT /id="VAR_071180"
FT VARIANT 95..97
FT /note="Missing (in SGS)"
FT /evidence="ECO:0000269|PubMed:23023332,
FT ECO:0000269|PubMed:23103230"
FT /id="VAR_071181"
FT VARIANT 116
FT /note="G -> E (in SGS; dbSNP:rs387907303)"
FT /evidence="ECO:0000269|PubMed:23023332,
FT ECO:0000269|PubMed:24357594"
FT /id="VAR_071182"
FT VARIANT 117
FT /note="G -> R (in SGS; dbSNP:rs869312901)"
FT /evidence="ECO:0000269|PubMed:23023332"
FT /id="VAR_071183"
FT HELIX 16..27
FT /evidence="ECO:0007829|PDB:5XOD"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:5XOD"
FT HELIX 35..39
FT /evidence="ECO:0007829|PDB:6ZVQ"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:1SBX"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:1SBX"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:1SBX"
FT HELIX 123..127
FT /evidence="ECO:0007829|PDB:1SBX"
FT TURN 128..133
FT /evidence="ECO:0007829|PDB:1SBX"
FT HELIX 136..145
FT /evidence="ECO:0007829|PDB:1SBX"
FT HELIX 155..163
FT /evidence="ECO:0007829|PDB:1SBX"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:1SBX"
FT HELIX 179..190
FT /evidence="ECO:0007829|PDB:1SBX"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:1MR1"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:1MR1"
FT HELIX 234..236
FT /evidence="ECO:0007829|PDB:1MR1"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:1MR1"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:1MR1"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:1MR1"
FT STRAND 269..275
FT /evidence="ECO:0007829|PDB:1MR1"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:1MR1"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:1MR1"
FT HELIX 296..310
FT /evidence="ECO:0007829|PDB:1MR1"
SQ SEQUENCE 728 AA; 80005 MW; 9B78C4840A28C2DA CRC64;
MEAAAGGRGC FQPHPGLQKT LEQFHLSSMS SLGGPAAFSA RWAQEAYKKE SAKEAGAAAV
PAPVPAATEP PPVLHLPAIQ PPPPVLPGPF FMPSDRSTER CETVLEGETI SCFVVGGEKR
LCLPQILNSV LRDFSLQQIN AVCDELHIYC SRCTADQLEI LKVMGILPFS APSCGLITKT
DAERLCNALL YGGAYPPPCK KELAASLALG LELSERSVRV YHECFGKCKG LLVPELYSSP
SAACIQCLDC RLMYPPHKFV VHSHKALENR TCHWGFDSAN WRAYILLSQD YTGKEEQARL
GRCLDDVKEK FDYGNKYKRR VPRVSSEPPA SIRPKTDDTS SQSPAPSEKD KPSSWLRTLA
GSSNKSLGCV HPRQRLSAFR PWSPAVSASE KELSPHLPAL IRDSFYSYKS FETAVAPNVA
LAPPAQQKVV SSPPCAAAVS RAPEPLATCT QPRKRKLTVD TPGAPETLAP VAAPEEDKDS
EAEVEVESRE EFTSSLSSLS SPSFTSSSSA KDLGSPGARA LPSAVPDAAA PADAPSGLEA
ELEHLRQALE GGLDTKEAKE KFLHEVVKMR VKQEEKLSAA LQAKRSLHQE LEFLRVAKKE
KLREATEAKR NLRKEIERLR AENEKKMKEA NESRLRLKRE LEQARQARVC DKGCEAGRLR
AKYSAQIEDL QVKLQHAEAD REQLRADLLR EREAREHLEK VVKELQEQLW PRARPEAAGS
EGAAELEP
