SKI_HORSE
ID SKI_HORSE Reviewed; 730 AA.
AC Q9TUG2;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Ski oncogene;
DE AltName: Full=Proto-oncogene c-Ski;
GN Name=SKI;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cerebellum;
RA Yamanouchi K., Suzuki S., Tojo H.;
RT "Equine c-ski cDNA sequence.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- PTM: Ubiquitinated by RNF165, promoting proteasomal degradation,
CC leading to enhance the BMP-Smad signaling.
CC {ECO:0000250|UniProtKB:Q60698}.
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; AB034731; BAA86292.1; -; mRNA.
DR RefSeq; NP_001075287.1; NM_001081818.1.
DR AlphaFoldDB; Q9TUG2; -.
DR SMR; Q9TUG2; -.
DR STRING; 9796.ENSECAP00000048345; -.
DR PaxDb; Q9TUG2; -.
DR GeneID; 100033833; -.
DR KEGG; ecb:100033833; -.
DR CTD; 6497; -.
DR InParanoid; Q9TUG2; -.
DR OrthoDB; 1148296at2759; -.
DR Proteomes; UP000002281; Unplaced.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISS:UniProtKB.
DR GO; GO:0046332; F:SMAD binding; ISS:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0032926; P:negative regulation of activin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0030514; P:negative regulation of BMP signaling pathway; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0043388; P:positive regulation of DNA binding; ISS:UniProtKB.
DR GO; GO:0060395; P:SMAD protein signal transduction; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Coiled coil; Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome;
KW Repeat; Ubl conjugation.
FT CHAIN 1..730
FT /note="Ski oncogene"
FT /id="PRO_0000129381"
FT REGION 321..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..730
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 539..712
FT /evidence="ECO:0000255"
FT COMPBIAS 331..356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12755"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12755"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12755"
SQ SEQUENCE 730 AA; 80394 MW; B5AE0DB12422DCA3 CRC64;
MEAAAGGRGG FQPHPGLQKT LEQFHLSSMS SLGGPAAFSA RWAQEAYKKE SAKEAGAAAV
PAPVPAAAEP PPVLHLPAIQ PPPPVLPGPF FMPSDRSTER CETVLEGETI SCFVVGGEKR
LCLPQILNSV LRDFSLQQIN SVCDELHTYC SRCTADQLEI LKVMGILPFS APSCGLITKT
DAERLCNALL YGGAYPPPCK KELAASLALG LELSERSVRV YHECFGKCKG LLVPELYSSP
SAACIQCLDC RLMYPPHKFV VHSHKALENR TCHWGFDSAN WRAYILLSQD YTGKEEQTRL
GRCLDDVKEK FDYGNKYKRR VPRVSSEPPA SIRKTDDTPS QHPTSSEKDK QSGWLRTLAS
PSSKSLGCVH PRQRLSAFRP WSPAVSTSDK ELPPHLPALI RDSFYSYKSF ETGVAPNVAL
APPAQQKVVS SPPCATVVSR APEPLATCVQ PRKRKLAVDT PGAPETPVPV AAPEDDKDSE
AEVEVESREE FTSSLSSLSS PSFTSSSSAK DLSSPGVHVP PVAPAAADAA APADTPSSGL
EAELEHLRQA LEGGLDTKEA KEKFLHEVVK MRVKQEEKLS AALQAKRSLH QELEFLRVAK
KEKLREATEA KRNLRKEIER LRAENEKKMK EANESRLRLK RELEQARQVR VCDKGCEAGR
LRAKYSAQIE DLQVKLQHAE ADREQLRADL LREREAREHL EKVVKELQEQ LWPRPRSEAT
GGESTAELEP
