ID   SKIL_HUMAN              Reviewed;         684 AA.
AC   P12757; A6NGT1; B4DT50; O00464; P12756; Q07501;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   24-JAN-2024, entry version 205.
DE   RecName: Full=Ski-like protein;
DE   AltName: Full=Ski-related oncogene;
DE   AltName: Full=Ski-related protein;
GN   Name=SKIL; Synonyms=SNO;
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] (ISOFORMS SNON AND SNOA), AND VARIANT VAL-38.
RC   TISSUE=Umbilical vein endothelial cell;
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 [MRNA] (ISOFORM SNON2), AND VARIANT VAL-38.
RC   TISSUE=Kidney;
RX   PubMed=9207045; DOI=10.1093/nar/25.14.2930;
RA   Pearson-White S.H., Crittenden R.;
RT   "Proto-oncogene Sno expression, alternative isoforms and immediate early
RT   serum response.";
RL   Nucleic Acids Res. 25:2930-2937(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SNON), AND VARIANT VAL-38.
RC   TISSUE=Placenta;
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   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 13-684 (ISOFORM SNOI), AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Myoblast;
RX   PubMed=8233802; DOI=10.1093/nar/21.19.4632;
RA   Pearson-White S.;
RT   "SnoI, a novel alternatively spliced isoform of the ski proto-oncogene
RT   homolog, sno.";
RL   Nucleic Acids Res. 21:4632-4638(1993).
RN   [7]
RP   INTERACTION WITH WWP1.
RX   PubMed=15221015; DOI=10.1038/sj.onc.1207885;
RA   Komuro A., Imamura T., Saitoh M., Yoshida Y., Yamori T., Miyazono K.,
RA   Miyazawa K.;
RT   "Negative regulation of transforming growth factor-beta (TGF-beta)
RT   signaling by WW domain-containing protein 1 (WWP1).";
RL   Oncogene 23:6914-6923(2004).
RN   [8]
RP   INTERACTION WITH RNF111, AND UBIQUITINATION.
RX   PubMed=17591695; DOI=10.1128/mcb.00664-07;
RA   Levy L., Howell M., Das D., Harkin S., Episkopou V., Hill C.S.;
RT   "Arkadia activates Smad3/Smad4-dependent transcription by triggering
RT   signal-induced SnoN degradation.";
RL   Mol. Cell. Biol. 27:6068-6083(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=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   [10]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-50 AND LYS-527, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA   Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "System-wide analysis of SUMOylation dynamics in response to replication
RT   stress reveals novel small ubiquitin-like modified target proteins and
RT   acceptor lysines relevant for genome stability.";
RL   Mol. Cell. Proteomics 14:1419-1434(2015).
RN   [11]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-489 AND LYS-527, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
CC   -!- FUNCTION: May have regulatory role in cell division or differentiation
CC       in response to extracellular signals.
CC   -!- SUBUNIT: Interacts with CPNE4 (via VWFA domain) (By similarity).
CC       Interacts with SMAD2, SMAD3 and RNF111 (PubMed:17591695). Isoform 1
CC       interacts with WWP1 (PubMed:15221015). {ECO:0000250|UniProtKB:Q60665,
CC       ECO:0000269|PubMed:15221015, ECO:0000269|PubMed:17591695}.
CC   -!- INTERACTION:
CC       P12757; P13637: ATP1A3; NbExp=3; IntAct=EBI-2902468, EBI-948169;
CC       P12757; Q05D60: DEUP1; NbExp=3; IntAct=EBI-2902468, EBI-748597;
CC       P12757; Q9Y295: DRG1; NbExp=3; IntAct=EBI-2902468, EBI-719554;
CC       P12757; O95995: GAS8; NbExp=3; IntAct=EBI-2902468, EBI-1052570;
CC       P12757; O60333-2: KIF1B; NbExp=3; IntAct=EBI-2902468, EBI-10975473;
CC       P12757; P07196: NEFL; NbExp=6; IntAct=EBI-2902468, EBI-475646;
CC       P12757; Q9H4D5: NXF3; NbExp=3; IntAct=EBI-2902468, EBI-750038;
CC       P12757; O43482: OIP5; NbExp=3; IntAct=EBI-2902468, EBI-536879;
CC       P12757; P16284: PECAM1; NbExp=3; IntAct=EBI-2902468, EBI-716404;
CC       P12757; Q13485: SMAD4; NbExp=3; IntAct=EBI-2902468, EBI-347263;
CC       P12757; Q53HV7: SMUG1; NbExp=3; IntAct=EBI-2902468, EBI-749970;
CC       P12757; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2902468, EBI-5235340;
CC       P12757; O75716: STK16; NbExp=3; IntAct=EBI-2902468, EBI-749295;
CC       P12757; Q08117: TLE5; NbExp=3; IntAct=EBI-2902468, EBI-717810;
CC       P12757; P08670: VIM; NbExp=3; IntAct=EBI-2902468, EBI-353844;
CC       P12757; Q548N1: VPS28; NbExp=3; IntAct=EBI-2902468, EBI-10243107;
CC       P12757; Q9UK41: VPS28; NbExp=4; IntAct=EBI-2902468, EBI-727424;
CC       P12757; O76024: WFS1; NbExp=3; IntAct=EBI-2902468, EBI-720609;
CC       P12757; P23025: XPA; NbExp=3; IntAct=EBI-2902468, EBI-295222;
CC       P12757; Q60974: Ncor1; Xeno; NbExp=2; IntAct=EBI-2902468, EBI-349004;
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=5;
CC       Name=SNON;
CC         IsoId=P12757-1; Sequence=Displayed;
CC       Name=SNOA;
CC         IsoId=P12757-2; Sequence=VSP_004392, VSP_004394;
CC       Name=SNON2;
CC         IsoId=P12757-3; Sequence=VSP_004395, VSP_004396;
CC       Name=SNOI;
CC         IsoId=P12757-4; Sequence=VSP_004393;
CC       Name=5;
CC         IsoId=P12757-5; Sequence=VSP_040099;
CC   -!- TISSUE SPECIFICITY: Isoform SNON and isoform SNOA are widely expressed.
CC       Highest expression is found in skeletal muscle, followed by placenta
CC       and lung. Lowest expression in heart, brain and pancreas. Isoform SNOI
CC       expression is restricted to skeletal muscle.
CC       {ECO:0000269|PubMed:8233802}.
CC   -!- PTM: Ubiquitinated by RNF111 and ARK2C, promoting proteasomal
CC       degradation, leading to enhance the BMP-Smad signaling.
CC       {ECO:0000269|PubMed:17591695}.
CC   -!- SIMILARITY: Belongs to the SKI family. {ECO:0000305}.
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DR   EMBL; X15219; CAA33289.1; -; mRNA.
DR   EMBL; X15217; CAA33287.1; -; mRNA.
DR   EMBL; U70730; AAB65850.1; -; mRNA.
DR   EMBL; AK300053; BAG61862.1; -; mRNA.
DR   EMBL; AC073288; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC059386; AAH59386.1; -; mRNA.
DR   EMBL; Z19588; CAA79636.1; -; mRNA.
DR   CCDS; CCDS33890.1; -. [P12757-1]
DR   CCDS; CCDS46953.1; -. [P12757-3]
DR   CCDS; CCDS46954.1; -. [P12757-5]
DR   PIR; S06052; TVHUSN.
DR   PIR; S06054; TVHUSA.
DR   RefSeq; NP_001138569.1; NM_001145097.2. [P12757-3]
DR   RefSeq; NP_001138570.1; NM_001145098.2. [P12757-5]
DR   RefSeq; NP_001234937.1; NM_001248008.1. [P12757-1]
DR   RefSeq; NP_005405.2; NM_005414.4. [P12757-1]
DR   RefSeq; XP_005247778.1; XM_005247721.1. [P12757-1]
DR   RefSeq; XP_006713798.1; XM_006713735.1. [P12757-1]
DR   PDB; 3EQ5; X-ray; 2.45 A; A/B/C/D/E/F/G/H/I/J/K/L=137-238.
DR   PDB; 5C4V; X-ray; 2.60 A; B/D/F=238-356.
DR   PDBsum; 3EQ5; -.
DR   PDBsum; 5C4V; -.
DR   AlphaFoldDB; P12757; -.
DR   SMR; P12757; -.
DR   BioGRID; 112389; 107.
DR   CORUM; P12757; -.
DR   DIP; DIP-42138N; -.
DR   IntAct; P12757; 95.
DR   MINT; P12757; -.
DR   STRING; 9606.ENSP00000415243; -.
DR   GlyGen; P12757; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; P12757; -.
DR   PhosphoSitePlus; P12757; -.
DR   BioMuta; SKIL; -.
DR   DMDM; 313104010; -.
DR   EPD; P12757; -.
DR   jPOST; P12757; -.
DR   MassIVE; P12757; -.
DR   MaxQB; P12757; -.
DR   PaxDb; 9606-ENSP00000415243; -.
DR   PeptideAtlas; P12757; -.
DR   ProteomicsDB; 52866; -. [P12757-1]
DR   ProteomicsDB; 52867; -. [P12757-2]
DR   ProteomicsDB; 52868; -. [P12757-3]
DR   ProteomicsDB; 52869; -. [P12757-4]
DR   ProteomicsDB; 52870; -. [P12757-5]
DR   Pumba; P12757; -.
DR   Antibodypedia; 1923; 604 antibodies from 37 providers.
DR   DNASU; 6498; -.
DR   Ensembl; ENST00000259119.9; ENSP00000259119.4; ENSG00000136603.15. [P12757-1]
DR   Ensembl; ENST00000413427.6; ENSP00000400193.2; ENSG00000136603.15. [P12757-3]
DR   Ensembl; ENST00000426052.6; ENSP00000406520.2; ENSG00000136603.15. [P12757-5]
DR   Ensembl; ENST00000458537.7; ENSP00000415243.3; ENSG00000136603.15. [P12757-1]
DR   Ensembl; ENST00000465590.2; ENSP00000516712.1; ENSG00000136603.15. [P12757-1]
DR   GeneID; 6498; -.
DR   KEGG; hsa:6498; -.
DR   MANE-Select; ENST00000259119.9; ENSP00000259119.4; NM_005414.5; NP_005405.2.
DR   UCSC; uc003fgu.4; human. [P12757-1]
DR   AGR; HGNC:10897; -.
DR   CTD; 6498; -.
DR   DisGeNET; 6498; -.
DR   GeneCards; SKIL; -.
DR   HGNC; HGNC:10897; SKIL.
DR   HPA; ENSG00000136603; Low tissue specificity.
DR   MIM; 165340; gene.
DR   neXtProt; NX_P12757; -.
DR   OpenTargets; ENSG00000136603; -.
DR   PharmGKB; PA35797; -.
DR   VEuPathDB; HostDB:ENSG00000136603; -.
DR   eggNOG; ENOG502QT5P; Eukaryota.
DR   GeneTree; ENSGT00940000158435; -.
DR   HOGENOM; CLU_025786_0_0_1; -.
DR   InParanoid; P12757; -.
DR   OMA; HAHRMEE; -.
DR   OrthoDB; 5400889at2759; -.
DR   PhylomeDB; P12757; -.
DR   TreeFam; TF324133; -.
DR   PathwayCommons; P12757; -.
DR   Reactome; R-HSA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR   SignaLink; P12757; -.
DR   SIGNOR; P12757; -.
DR   BioGRID-ORCS; 6498; 20 hits in 1157 CRISPR screens.
DR   ChiTaRS; SKIL; human.
DR   EvolutionaryTrace; P12757; -.
DR   GeneWiki; SKIL; -.
DR   GenomeRNAi; 6498; -.
DR   Pharos; P12757; Tbio.
DR   PRO; PR:P12757; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; P12757; Protein.
DR   Bgee; ENSG00000136603; Expressed in tendon of biceps brachii and 193 other cell types or tissues.
DR   ExpressionAtlas; P12757; baseline and differential.
DR   GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
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:0003682; F:chromatin binding; IEA:Ensembl.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR   GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:0046332; F:SMAD binding; IPI:UniProtKB.
DR   GO; GO:0001825; P:blastocyst formation; IEA:Ensembl.
DR   GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR   GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR   GO; GO:0070306; P:lens fiber cell differentiation; IEA:Ensembl.
DR   GO; GO:0002260; P:lymphocyte homeostasis; IEA:Ensembl.
DR   GO; GO:0030514; P:negative regulation of BMP signaling pathway; IBA:GO_Central.
DR   GO; GO:0045596; P:negative regulation of cell differentiation; IEA:Ensembl.
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:0050772; P:positive regulation of axonogenesis; IMP:UniProtKB.
DR   GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR   GO; GO:1902231; P:positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR   GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR   GO; GO:0046677; P:response to antibiotic; IEP:UniProtKB.
DR   GO; GO:0034097; P:response to cytokine; IEA:Ensembl.
DR   GO; GO:0070848; P:response to growth factor; IDA:UniProtKB.
DR   GO; GO:0007519; P:skeletal muscle tissue development; IDA:UniProtKB.
DR   GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR   CDD; cd21084; DHD_Sno; 1.
DR   Gene3D; 3.10.390.10; SAND domain-like; 1.
DR   Gene3D; 3.10.260.20; Ski; 1.
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; IPR003380; SKI/SNO/DAC.
DR   InterPro; IPR037000; Ski_DNA-bd_sf.
DR   InterPro; IPR023216; Tscrpt_reg_SKI_SnoN.
DR   PANTHER; PTHR10005; SKI ONCOGENE-RELATED; 1.
DR   PANTHER; PTHR10005:SF3; SKI-LIKE PROTEIN; 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; P12757; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Coiled coil; Isopeptide bond;
KW   Phosphoprotein; Reference proteome; Ubl conjugation.
FT   CHAIN           1..684
FT                   /note="Ski-like protein"
FT                   /id="PRO_0000129387"
FT   REGION          420..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          536..684
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        437..454
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         452
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   CROSSLNK        50
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25755297"
FT   CROSSLNK        70
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        489
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        527
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:25755297,
FT                   ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         1..20
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_040099"
FT   VAR_SEQ         367..415
FT                   /note="TDAPSGMELQSWYPVIKQEGDHVSQTHSFLHPSYYLYMCDKVVAPNVSL ->
FT                   ASFLYQFLIMVMVYFEMKILCLVCNLTCMLNIAHATTTKYRLIYLYCSF (in
FT                   isoform SNOA)"
FT                   /evidence="ECO:0000303|PubMed:2762147"
FT                   /id="VSP_004392"
FT   VAR_SEQ         400..684
FT                   /note="Missing (in isoform SNOI)"
FT                   /evidence="ECO:0000303|PubMed:8233802"
FT                   /id="VSP_004393"
FT   VAR_SEQ         416..684
FT                   /note="Missing (in isoform SNOA)"
FT                   /evidence="ECO:0000303|PubMed:2762147"
FT                   /id="VSP_004394"
FT   VAR_SEQ         431
FT                   /note="S -> N (in isoform SNON2)"
FT                   /evidence="ECO:0000303|PubMed:9207045"
FT                   /id="VSP_004395"
FT   VAR_SEQ         432..477
FT                   /note="Missing (in isoform SNON2)"
FT                   /evidence="ECO:0000303|PubMed:9207045"
FT                   /id="VSP_004396"
FT   VARIANT         38
FT                   /note="A -> V (in dbSNP:rs3772173)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:2762147, ECO:0000269|PubMed:9207045"
FT                   /id="VAR_011677"
FT   CONFLICT        13
FT                   /note="G -> R (in Ref. 6; CAA79636)"
FT                   /evidence="ECO:0000305"
FT   HELIX           137..139
FT                   /evidence="ECO:0007829|PDB:3EQ5"
FT   STRAND          145..149
FT                   /evidence="ECO:0007829|PDB:3EQ5"
FT   STRAND          152..159
FT                   /evidence="ECO:0007829|PDB:3EQ5"
FT   STRAND          162..166
FT                   /evidence="ECO:0007829|PDB:3EQ5"
FT   HELIX           167..172
FT                   /evidence="ECO:0007829|PDB:3EQ5"
FT   TURN            173..177
FT                   /evidence="ECO:0007829|PDB:3EQ5"
FT   HELIX           180..190
FT                   /evidence="ECO:0007829|PDB:3EQ5"
FT   HELIX           199..207
FT                   /evidence="ECO:0007829|PDB:3EQ5"
FT   STRAND          219..222
FT                   /evidence="ECO:0007829|PDB:3EQ5"
FT   HELIX           223..234
FT                   /evidence="ECO:0007829|PDB:3EQ5"
FT   STRAND          262..266
FT                   /evidence="ECO:0007829|PDB:5C4V"
FT   STRAND          272..276
FT                   /evidence="ECO:0007829|PDB:5C4V"
FT   HELIX           278..280
FT                   /evidence="ECO:0007829|PDB:5C4V"
FT   STRAND          289..291
FT                   /evidence="ECO:0007829|PDB:5C4V"
FT   TURN            292..294
FT                   /evidence="ECO:0007829|PDB:5C4V"
FT   HELIX           300..303
FT                   /evidence="ECO:0007829|PDB:5C4V"
FT   STRAND          313..319
FT                   /evidence="ECO:0007829|PDB:5C4V"
FT   HELIX           322..324
FT                   /evidence="ECO:0007829|PDB:5C4V"
FT   HELIX           325..328
FT                   /evidence="ECO:0007829|PDB:5C4V"
FT   STRAND          335..338
FT                   /evidence="ECO:0007829|PDB:5C4V"
FT   HELIX           341..352
FT                   /evidence="ECO:0007829|PDB:5C4V"
SQ   SEQUENCE   684 AA;  76976 MW;  6A04D4ECEC214CF1 CRC64;
     MENLQTNFSL VQGSTKKLNG MGDDGSPPAK KMITDIHANG KTINKVPTVK KEHLDDYGEA
     PVETDGEHVK RTCTSVPETL HLNPSLKHTL AQFHLSSQSS LGGPAAFSAR HSQESMSPTV
     FLPLPSPQVL PGPLLIPSDS STELTQTVLE GESISCFQVG GEKRLCLPQV LNSVLREFTL
     QQINTVCDEL YIYCSRCTSD QLHILKVLGI LPFNAPSCGL ITLTDAQRLC NALLRPRTFP
     QNGSVLPAKS SLAQLKETGS AFEVEHECLG KCQGLFAPQF YVQPDAPCIQ CLECCGMFAP
     QTFVMHSHRS PDKRTCHWGF ESAKWHCYLH VNQKYLGTPE EKKLKIILEE MKEKFSMRSG
     KRNQSKTDAP SGMELQSWYP VIKQEGDHVS QTHSFLHPSY YLYMCDKVVA PNVSLTSAVS
     QSKELTKTEA SKSISRQSEK AHSSGKLQKT VSYPDVSLEE QEKMDLKTSR ELCSRLDASI
     SNNSTSKRKS ESATCNLVRD INKVGIGLVA AASSPLLVKD VICEDDKGKI MEEVMRTYLK
     QQEKLNLILQ KKQQLQMEVK MLSSSKSMKE LTEEQQNLQK ELESLQNEHA QRMEEFYVEQ
     KDLEKKLEQI MKQKCTCDSN LEKDKEAEYA GQLAELRQRL DHAEADRQEL QDELRQEREA
     RQKLEMMIKE LKLQILKSSK TAKE
//