SKIL_PONAB
ID SKIL_PONAB Reviewed; 684 AA.
AC Q5R431;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Ski-like protein;
DE AltName: Full=Ski-related protein;
GN Name=SKIL;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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). Interacts with SMAD2,
CC SMAD3 and RNF111. Interacts with WWP1. {ECO:0000250|UniProtKB:P12757,
CC ECO:0000250|UniProtKB:Q60665}.
CC -!- PTM: Ubiquitinated by RNF111 and RNF165, promoting proteasomal
CC degradation, leading to enhance the BMP-Smad signaling.
CC {ECO:0000250|UniProtKB:P12757, ECO:0000250|UniProtKB:Q60665}.
CC -!- SIMILARITY: Belongs to the SKI family. {ECO:0000305}.
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DR EMBL; CR861429; CAH93485.1; -; mRNA.
DR RefSeq; NP_001127043.1; NM_001133571.1.
DR AlphaFoldDB; Q5R431; -.
DR SMR; Q5R431; -.
DR STRING; 9601.ENSPPYP00000015973; -.
DR Ensembl; ENSPPYT00000048788; ENSPPYP00000044898; ENSPPYG00000031188.
DR GeneID; 100174070; -.
DR KEGG; pon:100174070; -.
DR CTD; 6498; -.
DR eggNOG; ENOG502QT5P; Eukaryota.
DR GeneTree; ENSGT00940000158435; -.
DR InParanoid; Q5R431; -.
DR OrthoDB; 1148296at2759; -.
DR Proteomes; UP000001595; Chromosome 3.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0046332; F:SMAD binding; IEA:InterPro.
DR GO; GO:0001825; P:blastocyst formation; IEA:Ensembl.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR GO; GO:0070306; P:lens fiber cell differentiation; IEA:Ensembl.
DR GO; GO:0002260; P:lymphocyte homeostasis; IEA:Ensembl.
DR GO; GO:0045596; P:negative regulation of cell differentiation; IEA:Ensembl.
DR GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:1902043; P:positive regulation of extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR GO; GO:1902231; P:positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage; IEA:Ensembl.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
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 2: Evidence at transcript level;
KW Coiled coil; Isopeptide bond; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..684
FT /note="Ski-like protein"
FT /id="PRO_0000129389"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 536..684
FT /evidence="ECO:0000255"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P12757"
FT CROSSLNK 50
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P12757"
FT CROSSLNK 70
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P12757"
FT CROSSLNK 489
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P12757"
FT CROSSLNK 527
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P12757"
SQ SEQUENCE 684 AA; 77089 MW; 7E671186F649305B CRC64;
MENLQTNFSL VQGSTKKLNG MEDDGSPPAK KMVTDIHANG KTINKVPTVK KEHLDDYGEA
PVETDGEHIK RTCTSVPETL HLNPSLKHTL AQFHLSSQSS LGGPAAFSAR HSQESMSPTV
FLPLPSPQVL PGPLLIPSDS STELTQTVLE GESISCFQVG GEKRLCLPQV LNSVLREFTL
QQINTVCDEL YIYCSRCTSE QLHILKVLGI LPFNAPSCGL ITLTDAQRLC NALLRPRTFP
QNGSVLPAKN SLAQLKETGS AFEVEHECLG KCQGLFAPQF YVQPDAPCIQ CLECCGMFAP
QTFVMHSHRS PDKRTCHWGF ESAKWHCYLH VNQKYLGTPE EKKLKIILEE MKEKFSMRSG
KRNQSKTDAP SGMELQSWYP VIKQEGDHVS QTHSFLHPSY YLYMCDKVVA PNVSLTSAVS
QSKELTKTEA SKSISRQSEK AHSSGKLQKT VSYPDVSLEE QEKMDLKTSR ELCSRLDASI
SNNSTSKRKS ESATCNLVRD INKVGIGLVA AASSPLLVKD VICEDDKGKI MEEVMRTYLK
QQEKLNLILQ KKQQLQMEVK MLSSSKSMKE LTEEQQNLQK ELESLQNEHA QRMEEFYVEQ
KDLEKKLEQI MKQKCTCDSN LEKDKEAEYA GQLAELRQRL DHAEADRQEL QDELRQEREA
RQKLEMMIKE LKLQILKSSK TAKE
