SKIL_MOUSE
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 03-AUG-2022, entry version 166.
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 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 AlphaFoldDB; Q60665; -.
DR SMR; Q60665; -.
DR BioGRID; 203269; 12.
DR STRING; 10090.ENSMUSP00000113256; -.
DR iPTMnet; Q60665; -.
DR PhosphoSitePlus; Q60665; -.
DR EPD; Q60665; -.
DR MaxQB; Q60665; -.
DR PaxDb; Q60665; -.
DR PRIDE; Q60665; -.
DR ProteomicsDB; 257020; -. [Q60665-1]
DR ProteomicsDB; 257021; -. [Q60665-2]
DR Antibodypedia; 1923; 551 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 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; ECYGMFS; -.
DR OrthoDB; 1148296at2759; -.
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 76 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:0005667; C:transcription regulator complex; IBA:GO_Central.
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 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; 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
