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P12755 (SKI_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ski oncogene
Alternative name(s):
Proto-oncogene c-Ski
Gene names
Name:SKI
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length728 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May play a role in terminal differentiation of skeletal muscle cells but not in the determination of cells to the myogenic lineage. Functions as a repressor of TGF-beta signaling. Ref.5

Subunit structure

Interacts with SMAD2, SMAD3 and SMAD4. Interacts with HIPK2. Part of a complex with HIPK2 and SMAD1/2/3. Interacts with PRDM16 and SMAD3; the interaction with PRDM16 promotes the recruitment SMAD3-HDAC1 complex on the promoter of TGF-beta target genes. Ref.3 Ref.5

Subcellular location

Nucleus.

Sequence similarities

Belongs to the SKI family.

Ontologies

Keywords
   Cellular componentNucleus
   DiseaseProto-oncogene
   DomainCoiled coil
Repeat
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processBMP signaling pathway

Traceable author statement. Source: Reactome

SMAD protein signal transduction

Inferred from direct assay Ref.3. Source: UniProtKB

anterior/posterior axis specification

Inferred from sequence or structural similarity. Source: BHF-UCL

bone morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

camera-type eye development

Inferred from sequence or structural similarity. Source: BHF-UCL

camera-type eye morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

cell motility

Non-traceable author statement PubMed 14583455. Source: BHF-UCL

cell proliferation

Non-traceable author statement PubMed 14583455. Source: BHF-UCL

embryonic limb morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

face morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

gene expression

Traceable author statement. Source: Reactome

lens morphogenesis in camera-type eye

Inferred from sequence or structural similarity. Source: BHF-UCL

myelination in peripheral nervous system

Inferred from sequence or structural similarity. Source: BHF-UCL

myotube differentiation

Inferred from direct assay PubMed 19008232. Source: UniProtKB

negative regulation of BMP signaling pathway

Inferred from direct assay PubMed 14699069. Source: UniProtKB

negative regulation of Schwann cell proliferation

Inferred from genetic interaction PubMed 15312649. Source: MGI

negative regulation of activin receptor signaling pathway

Inferred from direct assay PubMed 14699069. Source: UniProtKB

negative regulation of cell proliferation

Inferred from direct assay PubMed 11430826. Source: UniProtKB

negative regulation of fibroblast proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

negative regulation of osteoblast differentiation

Inferred from direct assay PubMed 14699069. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 17469184. Source: UniProtKB

negative regulation of transforming growth factor beta receptor signaling pathway

Inferred from direct assay PubMed 17469184. Source: UniProtKB

neural tube closure

Inferred from sequence or structural similarity. Source: BHF-UCL

nose morphogenesis

Inferred from sequence or structural similarity. Source: BHF-UCL

olfactory bulb development

Inferred from sequence or structural similarity. Source: BHF-UCL

palate development

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of DNA binding

Inferred from direct assay PubMed 15107821. Source: UniProtKB

positive regulation of Wnt signaling pathway

Non-traceable author statement PubMed 14583455. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: BHF-UCL

protein homotrimerization

Inferred from direct assay PubMed 8514802. Source: UniProtKB

regulation of apoptotic process

Inferred from sequence or structural similarity. Source: BHF-UCL

retina development in camera-type eye

Inferred from sequence or structural similarity. Source: BHF-UCL

skeletal muscle fiber development

Inferred from sequence or structural similarity. Source: BHF-UCL

somatic stem cell maintenance

Inferred from sequence or structural similarity. Source: BHF-UCL

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription, DNA-templated

Inferred from sequence or structural similarity. Source: BHF-UCL

transforming growth factor beta receptor signaling pathway

Non-traceable author statement PubMed 14583455. Source: BHF-UCL

   Cellular_componentPML body

Inferred from direct assay PubMed 11430826. Source: UniProtKB

centrosome

Inferred from direct assay PubMed 21600873. Source: MGI

cytoplasm

Inferred from sequence or structural similarity. Source: BHF-UCL

nuclear body

Inferred from direct assay Ref.3. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 17054724PubMed 17510063. Source: UniProtKB

protein complex

Inferred from direct assay PubMed 23610558. Source: MGI

transcription factor complex

Inferred from sequence or structural similarity. Source: BHF-UCL

transcriptional repressor complex

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_functionSMAD binding

Inferred from physical interaction PubMed 15107821PubMed 17469184. Source: UniProtKB

chromatin binding

Inferred from electronic annotation. Source: Ensembl

histone deacetylase inhibitor activity

Inferred from sequence or structural similarity. Source: BHF-UCL

protein domain specific binding

Inferred from physical interaction PubMed 11441023. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.3. Source: UniProtKB

repressing transcription factor binding

Inferred from physical interaction PubMed 12435627. Source: UniProtKB

transcription corepressor activity

Inferred from direct assay PubMed 17469184. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction PubMed 17510063. Source: UniProtKB

zinc ion binding

Inferred from direct assay PubMed 12419246. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Fam89bQ9QUI16EBI-347281,EBI-6503100From a different organism.
NCOR1O753762EBI-347281,EBI-347233
Ncor1Q609745EBI-347281,EBI-349004From a different organism.
SIN3AQ96ST33EBI-347281,EBI-347218
SMAD3P840222EBI-347281,EBI-347161
SMAD4Q134854EBI-347281,EBI-347263

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 728728Ski oncogene
PRO_0000129382

Regions

Coiled coil536 – 710175 Potential

Amino acid modifications

Modified residue4801Phosphoserine Ref.6

Secondary structure

.................................. 728
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12755 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 9B78C4840A28C2DA

FASTA72880,005
        10         20         30         40         50         60 
MEAAAGGRGC FQPHPGLQKT LEQFHLSSMS SLGGPAAFSA RWAQEAYKKE SAKEAGAAAV 

        70         80         90        100        110        120 
PAPVPAATEP PPVLHLPAIQ PPPPVLPGPF FMPSDRSTER CETVLEGETI SCFVVGGEKR 

       130        140        150        160        170        180 
LCLPQILNSV LRDFSLQQIN AVCDELHIYC SRCTADQLEI LKVMGILPFS APSCGLITKT 

       190        200        210        220        230        240 
DAERLCNALL YGGAYPPPCK KELAASLALG LELSERSVRV YHECFGKCKG LLVPELYSSP 

       250        260        270        280        290        300 
SAACIQCLDC RLMYPPHKFV VHSHKALENR TCHWGFDSAN WRAYILLSQD YTGKEEQARL 

       310        320        330        340        350        360 
GRCLDDVKEK FDYGNKYKRR VPRVSSEPPA SIRPKTDDTS SQSPAPSEKD KPSSWLRTLA 

       370        380        390        400        410        420 
GSSNKSLGCV HPRQRLSAFR PWSPAVSASE KELSPHLPAL IRDSFYSYKS FETAVAPNVA 

       430        440        450        460        470        480 
LAPPAQQKVV SSPPCAAAVS RAPEPLATCT QPRKRKLTVD TPGAPETLAP VAAPEEDKDS 

       490        500        510        520        530        540 
EAEVEVESRE EFTSSLSSLS SPSFTSSSSA KDLGSPGARA LPSAVPDAAA PADAPSGLEA 

       550        560        570        580        590        600 
ELEHLRQALE GGLDTKEAKE KFLHEVVKMR VKQEEKLSAA LQAKRSLHQE LEFLRVAKKE 

       610        620        630        640        650        660 
KLREATEAKR NLRKEIERLR AENEKKMKEA NESRLRLKRE LEQARQARVC DKGCEAGRLR 

       670        680        690        700        710        720 
AKYSAQIEDL QVKLQHAEAD REQLRADLLR EREAREHLEK VVKELQEQLW PRARPEAAGS 


EGAAELEP 

« Hide

References

« Hide 'large scale' references
[1]"Isolation of human cDNA clones of ski and the ski-related gene, sno."
Nomura N., Sasamoto S., Ishii S., Date T., Matsui M., Ishizaki R.
Nucleic Acids Res. 17:5489-5500(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Requirement of the co-repressor homeodomain-interacting protein kinase 2 for ski-mediated inhibition of bone morphogenetic protein-induced transcriptional activation."
Harada J., Kokura K., Kanei-Ishii C., Nomura T., Khan M.M., Kim Y., Ishii S.
J. Biol. Chem. 278:38998-39005(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIPK2; SMAD2; SMAD3 AND SMAD4.
[4]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[5]"SKI and MEL1 cooperate to inhibit transforming growth factor-beta signal in gastric cancer cells."
Takahata M., Inoue Y., Tsuda H., Imoto I., Koinuma D., Hayashi M., Ichikura T., Yamori T., Nagasaki K., Yoshida M., Matsuoka M., Morishita K., Yuki K., Hanyu A., Miyazawa K., Inazawa J., Miyazono K., Imamura T.
J. Biol. Chem. 284:3334-3344(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PRDM16 AND SMAD3.
[6]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X15218 mRNA. Translation: CAA33288.1.
AL590822 Genomic DNA. No translation available.
PIRTVHUSK. S06053.
RefSeqNP_003027.1. NM_003036.3.
UniGeneHs.656507.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MR1X-ray2.85C/D219-313[»]
1SBXX-ray1.65A91-192[»]
ProteinModelPortalP12755.
SMRP12755. Positions 91-192, 218-312.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112388. 45 interactions.
DIPDIP-31514N.
IntActP12755. 11 interactions.
MINTMINT-269973.
STRING9606.ENSP00000367797.

PTM databases

PhosphoSiteP12755.

Polymorphism databases

DMDM134517.

Proteomic databases

PaxDbP12755.
PRIDEP12755.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378536; ENSP00000367797; ENSG00000157933.
GeneID6497.
KEGGhsa:6497.
UCSCuc001aja.4. human.

Organism-specific databases

CTD6497.
GeneCardsGC01P002173.
HGNCHGNC:10896. SKI.
HPACAB010449.
MIM164780. gene.
neXtProtNX_P12755.
Orphanet1606. 1p36 deletion syndrome.
2462. Shprintzen-Goldberg syndrome.
PharmGKBPA35796.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG82850.
HOGENOMHOG000039989.
HOVERGENHBG006599.
InParanoidP12755.
OMAARQIRVC.
OrthoDBEOG72RN0F.
PhylomeDBP12755.
TreeFamTF324133.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_71. Gene Expression.
SignaLinkP12755.

Gene expression databases

ArrayExpressP12755.
BgeeP12755.
CleanExHS_SKI.
GenevestigatorP12755.

Family and domain databases

Gene3D3.10.260.20. 1 hit.
3.10.390.10. 1 hit.
InterProIPR014890. c-SKI_SMAD4-bd_dom.
IPR009061. DNA-bd_dom_put.
IPR010919. SAND_dom-like.
IPR028760. Ski.
IPR003380. Transform_Ski.
IPR023216. Tscrpt_reg_SKI_SnoN.
[Graphical view]
PANTHERPTHR10005. PTHR10005. 1 hit.
PTHR10005:SF2. PTHR10005:SF2. 1 hit.
PfamPF08782. c-SKI_SMAD_bind. 1 hit.
PF02437. Ski_Sno. 1 hit.
[Graphical view]
SMARTSM01046. c-SKI_SMAD_bind. 1 hit.
[Graphical view]
SUPFAMSSF46955. SSF46955. 1 hit.
SSF63763. SSF63763. 1 hit.
ProtoNetSearch...

Other

ChiTaRSSKI. human.
EvolutionaryTraceP12755.
GeneWikiSKI_protein.
GenomeRNAi6497.
NextBio25255.
PROP12755.
SOURCESearch...

Entry information

Entry nameSKI_HUMAN
AccessionPrimary (citable) accession number: P12755
Secondary accession number(s): Q5SYT7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: April 16, 2014
This is version 140 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM