SKI_MOUSE
ID SKI_MOUSE Reviewed; 725 AA.
AC Q60698; Q8VIL5;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Ski oncogene;
DE AltName: Full=Proto-oncogene c-Ski;
GN Name=Ski;
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].
RC STRAIN=129/Sv;
RA Chen Y., Berk M., Chen H., Stavnezer E., Colmenares C.;
RT "Mouse Ski proto-oncogene cDNA.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-324.
RC STRAIN=129/J;
RX PubMed=8573720; DOI=10.1002/aja.1002040307;
RA Namciu S., Lyons G.E., Micales B.K., Heyman H.-C., Colmenares C.,
RA Stavnezer E.;
RT "Enhanced expression of mouse c-ski accompanies terminal skeletal muscle
RT differentiation in vivo and in vitro.";
RL Dev. Dyn. 204:291-300(1995).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
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 play a role in terminal differentiation of skeletal
CC muscle cells but not in the determination of cells to the myogenic
CC lineage. Functions as a repressor of TGF-beta signaling.
CC -!- SUBUNIT: Interacts with SMAD2, SMAD3 and SMAD4. Interacts with HIPK2.
CC Part of a complex with HIPK2 and SMAD1/2/3. Interacts with PRDM16 and
CC SMAD3; the interaction with PRDM16 promotes the recruitment SMAD3-HDAC1
CC complex on the promoter of TGF-beta target genes (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q60698; Q8VI24: Satb2; NbExp=3; IntAct=EBI-15969860, EBI-5737999;
CC Q60698; P97471: Smad4; NbExp=3; IntAct=EBI-15969860, EBI-5259270;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- DEVELOPMENTAL STAGE: Is expressed in a uniform pattern in all embryonic
CC cells prior to skeletal muscle cell formation in the myotomes of
CC somites. Expression is first up-regulated in skeletal muscle at 12 dpc,
CC this up-regulation is evident first in body wall muscle and one day
CC later in limb muscles. At 13.5 dpc a most prominent expression is seen
CC in all skeletal muscles. At this stage expression is seen in all other
CC cells and tissues but at lower levels than in skeletal muscle.
CC -!- PTM: Ubiquitinated by RNF165, promoting proteasomal degradation,
CC 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; AF435852; AAL30825.1; -; mRNA.
DR EMBL; U14173; AAA99669.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; Q60698; -.
DR SMR; Q60698; -.
DR DIP; DIP-60020N; -.
DR IntAct; Q60698; 3.
DR STRING; 10090.ENSMUSP00000030917; -.
DR iPTMnet; Q60698; -.
DR PhosphoSitePlus; Q60698; -.
DR jPOST; Q60698; -.
DR MaxQB; Q60698; -.
DR PaxDb; Q60698; -.
DR PeptideAtlas; Q60698; -.
DR PRIDE; Q60698; -.
DR ProteomicsDB; 261374; -.
DR MGI; MGI:98310; Ski.
DR eggNOG; ENOG502QTF6; Eukaryota.
DR InParanoid; Q60698; -.
DR Reactome; R-MMU-201451; Signaling by BMP.
DR Reactome; R-MMU-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR ChiTaRS; Ski; mouse.
DR PRO; PR:Q60698; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q60698; protein.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0016604; C:nuclear body; ISS:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; ISS:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0016605; C:PML body; ISS:BHF-UCL.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IPI:MGI.
DR GO; GO:0017053; C:transcription repressor complex; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IGI:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:BHF-UCL.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0046811; F:histone deacetylase inhibitor activity; IGI:MGI.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; ISS:BHF-UCL.
DR GO; GO:0019901; F:protein kinase binding; ISS:BHF-UCL.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0046332; F:SMAD binding; ISS:BHF-UCL.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISS:BHF-UCL.
DR GO; GO:0008270; F:zinc ion binding; ISS:BHF-UCL.
DR GO; GO:0009948; P:anterior/posterior axis specification; IMP:MGI.
DR GO; GO:0060349; P:bone morphogenesis; IMP:MGI.
DR GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR GO; GO:0048593; P:camera-type eye morphogenesis; IMP:MGI.
DR GO; GO:0030326; P:embryonic limb morphogenesis; IMP:MGI.
DR GO; GO:0060325; P:face morphogenesis; IMP:MGI.
DR GO; GO:0048144; P:fibroblast proliferation; IMP:MGI.
DR GO; GO:0002089; P:lens morphogenesis in camera-type eye; IMP:MGI.
DR GO; GO:0022011; P:myelination in peripheral nervous system; IMP:MGI.
DR GO; GO:0014902; P:myotube differentiation; IDA:MGI.
DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; ISS:BHF-UCL.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; IGI:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:BHF-UCL.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:MGI.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISS:BHF-UCL.
DR GO; GO:0010626; P:negative regulation of Schwann cell proliferation; ISO: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; IGI:MGI.
DR GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR GO; GO:0043585; P:nose morphogenesis; IMP:MGI.
DR GO; GO:0021772; P:olfactory bulb development; IMP:MGI.
DR GO; GO:0043388; P:positive regulation of DNA binding; ISS:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0070208; P:protein heterotrimerization; ISS:BHF-UCL.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:MGI.
DR GO; GO:0060021; P:roof of mouth development; IMP:MGI.
DR GO; GO:0048741; P:skeletal muscle fiber development; IMP:MGI.
DR GO; GO:0060395; P:SMAD protein signal transduction; ISS:BHF-UCL.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IDA:MGI.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
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; IPR028760; Ski.
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:SF15; PTHR10005:SF15; 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 Coiled coil; Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome;
KW Repeat; Ubl conjugation.
FT CHAIN 1..725
FT /note="Ski oncogene"
FT /id="PRO_0000129383"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 534..708
FT /evidence="ECO:0000255"
FT COMPBIAS 15..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..77
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..511
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12755"
FT MOD_RES 429
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12755"
FT MOD_RES 477
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12755"
SQ SEQUENCE 725 AA; 80119 MW; 1BFD05C38519505C CRC64;
MEAAAAGRGG FQQPGLQKTL EQFHLSSMSS LGGPAVSRRA GQEAYKKESA KEAGAATVPA
PVPTAAEPPP VLHLPAIQPP PPVLPGPFFM PSDRSTERCE TVLEGETISC FVVGGEKRLC
LPQILNSVLR DFSLQQINSV CDELHIYCSR CTADQLEILK VMGILPFSAP SCGLITKTDA
ERLCNALLYG GAYPPPCKKE LAASLALGLE LSERSVRVYH ECFGKCKGLL VPELYSSPSA
ACIQCLDCRL MYPPHKFVVH SHKALENRTC HWGFDSANWR AYILLSQDYT GKEEQARLGR
CLDDVKEKFD YANKYKRRVP RVSEPPASIR PKTDDTSSQS PASSEKDKQS TWLRTLAGSS
NKSLGCTHPR QRLSAFRPWS PAVSASEKET SPHLPALIRD SFYSYKSFET AVAPNVALAP
PTQQKVVNSP PCTTVVSRAP EPLTTCIQPR KRKLTLDTAG APDMLTPVAA AEEDKDSEAE
VEVESREEFT SSLSSLSSPS FTSSSSAKDL SSPGMHAPPV VAPDAAAHVD APSGLEAELE
HLRQALEGGL DTKEAKEKFL HEVVKMRVKQ EEKLTAALQA KRTLHQELEF LRVAKKEKLR
EATEAKRNLR KEIERLRAEN EKKMKEANES RVRLKRELEQ ARQVRVCDKG CEAGRLRAKY
SAQVEDLQAK LQHAEADREQ LRADLLRERE AREHLEKVVR ELQEQLRPRP RPEHPGGESN
AELGP
