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   27-MAR-2024, entry version 212.
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; Q6ZSG1: ARK2C; NbExp=2; IntAct=EBI-347281, EBI-2129206;
CC       P12755; O75376: NCOR1; NbExp=4; IntAct=EBI-347281, EBI-347233;
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 ARK2C, promoting proteasomal degradation, leading
CC       to enhance the BMP-Smad signaling. {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}.
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; 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; 172.
DR   CORUM; P12755; -.
DR   DIP; DIP-31514N; -.
DR   IntAct; P12755; 25.
DR   MINT; P12755; -.
DR   STRING; 9606.ENSP00000367797; -.
DR   GlyCosmos; P12755; 3 sites, 2 glycans.
DR   GlyGen; P12755; 3 sites, 2 O-linked glycans (3 sites).
DR   iPTMnet; P12755; -.
DR   PhosphoSitePlus; P12755; -.
DR   SwissPalm; P12755; -.
DR   BioMuta; SKI; -.
DR   DMDM; 134517; -.
DR   EPD; P12755; -.
DR   jPOST; P12755; -.
DR   MassIVE; P12755; -.
DR   MaxQB; P12755; -.
DR   PaxDb; 9606-ENSP00000367797; -.
DR   PeptideAtlas; P12755; -.
DR   ProteomicsDB; 52865; -.
DR   Pumba; P12755; -.
DR   Antibodypedia; 4180; 228 antibodies from 38 providers.
DR   DNASU; 6497; -.
DR   Ensembl; ENST00000378536.5; ENSP00000367797.4; ENSG00000157933.11.
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   AGR; HGNC:10896; -.
DR   CTD; 6497; -.
DR   DisGeNET; 6497; -.
DR   GeneCards; SKI; -.
DR   GeneReviews; SKI; -.
DR   HGNC; HGNC:10896; SKI.
DR   HPA; ENSG00000157933; Tissue enhanced (brain).
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; PPGRCKK; -.
DR   OrthoDB; 5400889at2759; -.
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; 29 hits in 1157 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 187 other cell types or tissues.
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:0060038; P:cardiac muscle cell proliferation; IEA:Ensembl.
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:0060392; P:negative regulation of SMAD protein signal transduction; IDA:UniProtKB.
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:0035019; P:somatic stem cell population maintenance; ISS:BHF-UCL.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; NAS:BHF-UCL.
DR   CDD; cd21083; DHD_Ski; 1.
DR   Gene3D; 3.10.390.10; SAND domain-like; 1.
DR   Gene3D; 3.10.260.20; Ski; 1.
DR   IDEAL; IID00131; -.
DR   InterPro; IPR014890; c-SKI_SMAD4-bd_dom.
DR   InterPro; IPR047315; DHD_Ski.
DR   InterPro; IPR009061; DNA-bd_dom_put_sf.
DR   InterPro; IPR010919; SAND-like_dom_sf.
DR   InterPro; IPR003380; SKI/SNO/DAC.
DR   InterPro; IPR037000; Ski_DNA-bd_sf.
DR   InterPro; IPR023216; Tscrpt_reg_SKI_SnoN.
DR   PANTHER; PTHR10005:SF15; SKI ONCOGENE; 1.
DR   PANTHER; PTHR10005; SKI ONCOGENE-RELATED; 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; Putative DNA-binding domain; 1.
DR   SUPFAM; SSF63763; SAND domain-like; 1.
DR   Genevisible; P12755; HS.
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
//