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   12-SEP-2018, entry version 145.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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>3.3.CO;2-N;
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
RT   early 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
RT   project: 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
RT   family of proteins. Characterization of a coiled-coil copine-binding
RT   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.,
RA   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
CC       differentiation in response to extracellular signals.
CC       {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 RNF165, 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}.
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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. [Q60665-1]
DR   UniGene; Mm.15406; -.
DR   UniGene; Mm.491655; -.
DR   ProteinModelPortal; Q60665; -.
DR   SMR; Q60665; -.
DR   BioGrid; 203269; 8.
DR   STRING; 10090.ENSMUSP00000029194; -.
DR   iPTMnet; Q60665; -.
DR   PhosphoSitePlus; Q60665; -.
DR   PaxDb; Q60665; -.
DR   PRIDE; Q60665; -.
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   CTD; 6498; -.
DR   MGI; MGI:106203; Skil.
DR   eggNOG; ENOG410IFDK; Eukaryota.
DR   eggNOG; ENOG410Y8AU; LUCA.
DR   GeneTree; ENSGT00530000063040; -.
DR   HOGENOM; HOG000039989; -.
DR   HOVERGEN; HBG006599; -.
DR   InParanoid; Q60665; -.
DR   KO; K18499; -.
DR   OMA; MEEFYIE; -.
DR   OrthoDB; EOG091G0O02; -.
DR   PhylomeDB; Q60665; -.
DR   TreeFam; TF324133; -.
DR   Reactome; R-MMU-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR   ChiTaRS; Skil; mouse.
DR   PRO; PR:Q60665; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   Bgee; ENSMUSG00000027660; Expressed in 307 organ(s), highest expression level in pineal body.
DR   CleanEx; MM_SKIL; -.
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: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 proximal promoter sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0046332; F:SMAD binding; ISO:MGI.
DR   GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR   GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II proximal promoter sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0001825; P:blastocyst formation; IMP:MGI.
DR   GO; GO:0007050; P:cell cycle arrest; 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:0048666; P:neuron development; IBA:GO_Central.
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:0070208; P:protein heterotrimerization; ISO:MGI.
DR   GO; GO:0070207; P:protein homotrimerization; ISO: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   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   Alternative splicing; Coiled coil; Complete proteome; Isopeptide bond;
KW   Phosphoprotein; Reference proteome; Ubl conjugation.
FT   CHAIN         1    675       Ski-like protein.
FT                                /FTId=PRO_0000129388.
FT   COILED      526    669       {ECO:0000255}.
FT   MOD_RES     449    449       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P12757}.
FT   CROSSLNK     47     47       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P12757}.
FT   CROSSLNK     67     67       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P12757}.
FT   CROSSLNK    486    486       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P12757}.
FT   CROSSLNK    518    518       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P12757}.
FT   VAR_SEQ     428    474       SKSTSKQSEKPHESSQHQKTVSYPDVSLEEQEKMDLKTSRE
FT                                LYSCLD -> N (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:8834472,
FT                                ECO:0000303|PubMed:9207045}.
FT                                /FTId=VSP_014265.
FT   CONFLICT     63     66       GEHA -> RAR (in Ref. 2; AAB65849).
FT                                {ECO:0000305}.
FT   CONFLICT    130    130       P -> T (in Ref. 2; AAB65849).
FT                                {ECO:0000305}.
FT   CONFLICT    150    150       S -> T (in Ref. 2; AAB65849).
FT                                {ECO:0000305}.
FT   CONFLICT    205    205       L -> S (in Ref. 2; AAB65849).
FT                                {ECO:0000305}.
FT   CONFLICT    229    229       A -> T (in Ref. 2; AAB65849).
FT                                {ECO:0000305}.
FT   CONFLICT    302    303       MH -> ID (in Ref. 1; AAB50266/AAB50267).
FT                                {ECO:0000305}.
FT   CONFLICT    542    542       R -> G (in Ref. 1; AAB50266/AAB50267).
FT                                {ECO:0000305}.
FT   CONFLICT    618    618       A -> P (in Ref. 1; AAB50266/AAB50267).
FT                                {ECO:0000305}.
FT   CONFLICT    622    622       A -> G (in Ref. 2; AAB65849).
FT                                {ECO:0000305}.
FT   CONFLICT    638    639       RQ -> QR (in Ref. 2; AAB65849).
FT                                {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
//