ID SKIL_MOUSE Reviewed; 675 AA. AC Q60665; Q60702; Q78E90; Q80VK5; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 21-JUN-2005, sequence version 2. DT 28-JUN-2023, entry version 171. DE RecName: Full=Ski-like protein; DE AltName: Full=Ski-related oncogene; DE AltName: Full=Ski-related protein; GN Name=Skil; Synonyms=Skir, Sno; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RC STRAIN=BALB/cJ; TISSUE=Brain, and Heart; RX PubMed=8834472; RX DOI=10.1002/(sici)1097-0177(199602)205:2<114::aid-aja3>3.0.co;2-l; RA Pelzer T.H., Lyons G.E., Kim S., Moreadith R.W.; RT "Cloning and characterization of the murine homolog of the sno proto- RT oncogene reveals a novel splice variant."; RL Dev. Dyn. 205:114-125(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC STRAIN=C3H/HeJ; TISSUE=Skeletal muscle; 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 2). RC STRAIN=FVB/N; TISSUE=Mammary tumor; 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 [4] RP INTERACTION WITH CPNE4. RX PubMed=12522145; DOI=10.1074/jbc.m212632200; RA Tomsig J.L., Snyder S.L., Creutz C.E.; RT "Identification of targets for calcium signaling through the copine family RT of proteins. Characterization of a coiled-coil copine-binding motif."; RL J. Biol. Chem. 278:10048-10054(2003). RN [5] RP UBIQUITINATION. RX PubMed=23610558; DOI=10.1371/journal.pbio.1001538; RA Kelly C.E., Thymiakou E., Dixon J.E., Tanaka S., Godwin J., Episkopou V.; RT "Rnf165/Ark2C enhances BMP-Smad signaling to mediate motor axon RT extension."; RL PLoS Biol. 11:E1001538-E1001538(2013). CC -!- FUNCTION: May have regulatory role in cell division or differentiation CC in response to extracellular signals. {ECO:0000250}. CC -!- SUBUNIT: Interacts with CPNE4 (via VWFA domain) (PubMed:12522145). CC Interacts with SMAD2, SMAD3 and RNF111. Interacts with WWP1 (By CC similarity). {ECO:0000250|UniProtKB:P12757, CC ECO:0000269|PubMed:12522145}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q60665-1; Sequence=Displayed; CC Name=2; CC IsoId=Q60665-2; Sequence=VSP_014265; CC -!- PTM: Ubiquitinated by RNF111 and ARK2C, promoting proteasomal CC degradation, leading to enhance the BMP-Smad signaling. CC {ECO:0000269|PubMed:23610558}. 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; U10530; AAB50266.1; -; mRNA. DR EMBL; U10532; AAB50267.1; -; mRNA. DR EMBL; U14655; AAB65849.1; -; mRNA. DR EMBL; BC049934; AAH49934.1; -; mRNA. DR CCDS; CCDS38408.1; -. [Q60665-1] DR CCDS; CCDS50886.1; -. [Q60665-2] DR RefSeq; NP_001034179.1; NM_001039090.2. [Q60665-2] DR RefSeq; NP_035516.2; NM_011386.3. [Q60665-1] DR RefSeq; XP_006535490.1; XM_006535427.3. DR AlphaFoldDB; Q60665; -. DR SMR; Q60665; -. DR BioGRID; 203269; 12. DR STRING; 10090.ENSMUSP00000113256; -. DR GlyGen; Q60665; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q60665; -. DR PhosphoSitePlus; Q60665; -. DR EPD; Q60665; -. DR MaxQB; Q60665; -. DR PaxDb; Q60665; -. DR ProteomicsDB; 257020; -. [Q60665-1] DR ProteomicsDB; 257021; -. [Q60665-2] DR Antibodypedia; 1923; 591 antibodies from 37 providers. DR DNASU; 20482; -. DR Ensembl; ENSMUST00000029194; ENSMUSP00000029194; ENSMUSG00000027660. [Q60665-1] DR Ensembl; ENSMUST00000118204; ENSMUSP00000112413; ENSMUSG00000027660. [Q60665-1] DR Ensembl; ENSMUST00000118470; ENSMUSP00000113256; ENSMUSG00000027660. [Q60665-2] DR GeneID; 20482; -. DR KEGG; mmu:20482; -. DR UCSC; uc008ovv.2; mouse. [Q60665-1] DR AGR; MGI:106203; -. DR CTD; 6498; -. DR MGI; MGI:106203; Skil. DR VEuPathDB; HostDB:ENSMUSG00000027660; -. DR eggNOG; ENOG502QT5P; Eukaryota. DR GeneTree; ENSGT00940000158435; -. DR HOGENOM; CLU_025786_0_0_1; -. DR InParanoid; Q60665; -. DR OMA; HAHRMEE; -. DR OrthoDB; 5400889at2759; -. DR PhylomeDB; Q60665; -. DR TreeFam; TF324133; -. DR Reactome; R-MMU-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity. DR BioGRID-ORCS; 20482; 1 hit in 81 CRISPR screens. DR ChiTaRS; Skil; mouse. DR PRO; PR:Q60665; -. DR Proteomes; UP000000589; Chromosome 3. DR RNAct; Q60665; protein. DR Bgee; ENSMUSG00000027660; Expressed in caudate-putamen and 264 other tissues. DR ExpressionAtlas; Q60665; baseline and differential. DR Genevisible; Q60665; MM. DR GO; GO:0001669; C:acrosomal vesicle; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0016605; C:PML body; ISO:MGI. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. 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; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI. DR GO; GO:0046332; F:SMAD binding; ISO:MGI. DR GO; GO:0001825; P:blastocyst formation; IMP:MGI. DR GO; GO:0030154; P:cell differentiation; IDA:MGI. DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IMP:MGI. DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI. DR GO; GO:0070306; P:lens fiber cell differentiation; IDA:MGI. DR GO; GO:0002260; P:lymphocyte homeostasis; IMP:MGI. DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IBA:GO_Central. DR GO; GO:0045596; P:negative regulation of cell differentiation; IDA:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IMP:MGI. DR GO; GO:0050772; P:positive regulation of axonogenesis; ISO:MGI. DR GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; IMP:MGI. DR GO; GO:1902231; P:positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI. DR GO; GO:0051726; P:regulation of cell cycle; IMP:MGI. DR GO; GO:0034097; P:response to cytokine; IEA:Ensembl. DR GO; GO:0070848; P:response to growth factor; ISO:MGI. DR GO; GO:0007519; P:skeletal muscle tissue development; ISO:MGI. DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl. DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IGI:MGI. 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. PE 1: Evidence at protein level; KW Alternative splicing; Coiled coil; Isopeptide bond; Phosphoprotein; KW Reference proteome; Ubl conjugation. FT CHAIN 1..675 FT /note="Ski-like protein" FT /id="PRO_0000129388" FT REGION 1..28 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 415..461 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 475..518 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 526..669 FT /evidence="ECO:0000255" FT COMPBIAS 1..16 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 426..443 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 475..496 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 498..518 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 449 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P12757" FT CROSSLNK 47 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P12757" FT CROSSLNK 67 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P12757" FT CROSSLNK 486 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P12757" FT CROSSLNK 518 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P12757" FT VAR_SEQ 428..474 FT /note="SKSTSKQSEKPHESSQHQKTVSYPDVSLEEQEKMDLKTSRELYSCLD -> N FT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:8834472, ECO:0000303|PubMed:9207045" FT /id="VSP_014265" FT CONFLICT 63..66 FT /note="GEHA -> RAR (in Ref. 2; AAB65849)" FT /evidence="ECO:0000305" FT CONFLICT 130 FT /note="P -> T (in Ref. 2; AAB65849)" FT /evidence="ECO:0000305" FT CONFLICT 150 FT /note="S -> T (in Ref. 2; AAB65849)" FT /evidence="ECO:0000305" FT CONFLICT 205 FT /note="L -> S (in Ref. 2; AAB65849)" FT /evidence="ECO:0000305" FT CONFLICT 229 FT /note="A -> T (in Ref. 2; AAB65849)" FT /evidence="ECO:0000305" FT CONFLICT 302..303 FT /note="MH -> ID (in Ref. 1; AAB50266/AAB50267)" FT /evidence="ECO:0000305" FT CONFLICT 542 FT /note="R -> G (in Ref. 1; AAB50266/AAB50267)" FT /evidence="ECO:0000305" FT CONFLICT 618 FT /note="A -> P (in Ref. 1; AAB50266/AAB50267)" FT /evidence="ECO:0000305" FT CONFLICT 622 FT /note="A -> G (in Ref. 2; AAB65849)" FT /evidence="ECO:0000305" FT CONFLICT 638..639 FT /note="RQ -> QR (in Ref. 2; AAB65849)" FT /evidence="ECO:0000305" SQ SEQUENCE 675 AA; 76359 MW; CE17BBC167693869 CRC64; MENLQSKFSL VQGSNKKLNG MEDDGSPPVK KMMTDIHANG KTLTKVKKEH LDDYGDASVE PDGEHAKRNR VSLPETLNLN PSLKHTLAQF HLSSQSSLGG PAAFSARYSQ ESMSPTVFLP LPSPQVLPGP LLIPSDSSTE LTQTLLEGES ISCFQVGGEK RLCLPQVLNS VLREFSLQQI NTVCDELYIY CSRCTSDQLH ILKVLGILPF NAPSCGLITL TDAQRLCNAL LRPRTFPQNG SILPAKSSLA QLKETGSAFE VEHECLGKCQ GLFAPQFYVQ PDAPCIQCLE CCGMFAPQTF VMHSHRSPDK RTCHWGFESA KWHCYLHVNQ KYLGTPEEKK LKIILEEMKE KFSMRNGKRI QSKTDTPSGM ELPSWYPVIK QEGDHVPQTH SFLHPSYYLY MCDKVVAPNV SLTSAASQSK EATKAETSKS TSKQSEKPHE SSQHQKTVSY PDVSLEEQEK MDLKTSRELY SCLDSSISNN STSRKKSESA VCSLVRGTSK RDSEDSSPLL VRDGEDDKGK IMEDVMRTYV RQQEKLNSIL QRKQQLQMEV EMLSSSKAMK ELTEEQQNLQ KELESLQSEH AQRMEEFYIE QRDLEKKLEQ VMQQKCTCDS TLEKDREAEY AAQLAELRQR LDHAEADRQE LQDELRQERE ARQKLEMMIK ELKLQIGKSS KPSKD //