SKIL_HUMAN
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 03-AUG-2022, entry version 197.
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 RNF165, 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; 106.
DR CORUM; P12757; -.
DR DIP; DIP-42138N; -.
DR IntAct; P12757; 94.
DR MINT; P12757; -.
DR STRING; 9606.ENSP00000415243; -.
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; P12757; -.
DR PeptideAtlas; P12757; -.
DR PRIDE; 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 Antibodypedia; 1923; 551 antibodies from 37 providers.
DR DNASU; 6498; -.
DR Ensembl; ENST00000259119.9; ENSP00000259119.4; ENSG00000136603.14. [P12757-1]
DR Ensembl; ENST00000413427.6; ENSP00000400193.2; ENSG00000136603.14. [P12757-3]
DR Ensembl; ENST00000426052.6; ENSP00000406520.2; ENSG00000136603.14. [P12757-5]
DR Ensembl; ENST00000458537.7; ENSP00000415243.3; ENSG00000136603.14. [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 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; ECYGMFS; -.
DR OrthoDB; 1148296at2759; -.
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; 19 hits in 1081 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 191 other tissues.
DR ExpressionAtlas; P12757; baseline and differential.
DR Genevisible; P12757; HS.
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:0005667; C:transcription regulator complex; IBA:GO_Central.
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 Gene3D; 3.10.260.20; -; 1.
DR Gene3D; 3.10.390.10; -; 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; IPR028373; Ski-rel_Sno.
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:SF3; PTHR10005:SF3; 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; 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
