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Reviewed, UniProtKB/Swiss-Prot P12755 (SKI_HUMAN)

Last modified February 9, 2010. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Ski oncogene
Alternative name(s):
    C-ski
Gene names
Name: SKI
OrganismHomo sapiens (Human) [Complete 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.5 Ref.3

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
Gene Ontology (GO)
   Biological processBMP signaling pathway

Inferred from Experiment. Source: Reactome

SMAD protein signal transduction Ref.3

Inferred from direct assay. Source: UniProtKB

myotube differentiation

Inferred from direct assay. Source: UniProtKB

negative regulation of BMP signaling pathway

Inferred from direct assay. Source: UniProtKB

negative regulation of Schwann cell proliferation

Inferred from genetic interaction. Source: MGI

negative regulation of activin receptor signaling pathway

Inferred from direct assay. Source: UniProtKB

negative regulation of osteoblast differentiation

Inferred from direct assay. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay. Source: UniProtKB

negative regulation of transforming growth factor beta receptor signaling pathway Ref.5

Inferred from direct assay. Source: UniProtKB

positive regulation of DNA binding

Inferred from direct assay. Source: UniProtKB

protein heterotrimerization

Inferred from physical interaction. Source: UniProtKB

protein homotrimerization

Inferred from physical interaction. Source: UniProtKB

   Cellular componentPML body

Inferred from direct assay. Source: UniProtKB

   Molecular functionSMAD binding

Inferred from physical interaction. Source: UniProtKB

nucleotide binding

Inferred from electronic annotation. Source: InterPro

protein domain specific binding

Inferred from physical interaction. Source: UniProtKB

protein kinase binding Ref.3

Inferred from physical interaction. Source: UniProtKB

transcription corepressor activity

Inferred from direct assay. Source: UniProtKB

transcription repressor binding

Inferred from physical interaction. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction. Source: UniProtKB

zinc ion binding

Inferred from direct assay. Source: UniProtKB

Complete GO annotation...

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 residue4321Phosphoserine Ref.4
Modified residue4801Phosphoserine Ref.6

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P12755-1 [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: 2762147] [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: 16710414] [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: 12874272] [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: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432, MASS SPECTROMETRY.
[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: 19049980] [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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480, MASS SPECTROMETRY.
Tissue: T-cell.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X15218 mRNA. Translation: CAA33288.1.
AL590822 Genomic DNA. No translation available.
IPIIPI00220921.
PIRTVHUSK. S06053.
RefSeqNP_003027.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1MR1X-ray2.85C/D219-313[»]
1SBXX-ray1.65A91-192[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP12755. 4 interactions.
STRINGP12755.

Proteomic databases

PRIDEP12755.

Genome annotation databases

EnsemblENST00000378536; ENSP00000367797; ENSG00000157933; Homo sapiens. [Genome view]
GeneID6497.
KEGGhsa:6497.
UCSCuc001aja.2. human.

Organism-specific databases

CTD6497.
GeneCardsGC01P002173.
H-InvDBHIX0028862.
HGNCHGNC:10896. SKI.
HPACAB010449.
MIM164780. gene.
PharmGKBPA35796.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG05898.
HOGENOMHBG445660.
HOVERGENP12755.
InParanoidP12755.
OMANKYKRKA.
OrthoDBEOG9QVFX7.
PhylomeDBP12755.

Enzyme and pathway databases

Pathway_Interaction_DBbmppathway. BMP receptor signaling.
smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
ReactomeREACT_12034. Signaling by BMP.
REACT_6844. Signaling by TGF beta.

Gene expression databases

ArrayExpressP12755.
BgeeP12755.
CleanExHS_SKI.
GenevestigatorP12755.
GermOnlineENSG00000157933. Homo sapiens.

Family and domain databases

InterProIPR014890. c-SKI_SMAD_bd.
IPR009061. DNA-bd_dom_put.
IPR010919. SAND-like.
IPR003380. Transform_Ski.
[Graphical view]
Gene3DG3DSA:3.10.390.10. SAND. 1 hit.
G3DSA:3.10.260.20. Transform_Ski. 1 hit.
PfamPF08782. c-SKI_SMAD_bind. 1 hit.
PF02437. Ski_Sno. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio25255.
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: February 9, 2010
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 1

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents