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P13725 (ONCM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Oncostatin-M

Short name=OSM
Gene names
Name:OSM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length252 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Growth regulator. Inhibits the proliferation of a number of tumor cell lines. Stimulates proliferation of AIDS-KS cells. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells. Uses both type I OSM receptor (heterodimers composed of LIPR and IL6ST) and type II OSM receptor (heterodimers composed of OSMR and IL6ST). Involved in the maturation of fetal hepatocytes, thereby promoting liver development and regeneration By similarity. Ref.8 Ref.12

Subcellular location

Secreted.

Post-translational modification

Propeptide processing is not important for receptor binding activity but may be important growth-inhibitory activity.

Sequence similarities

Belongs to the LIF/OSM family.

Ontologies

Keywords
   Biological processGrowth regulation
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionCytokine
Mitogen
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbehavioral response to pain

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Traceable author statement Ref.12. Source: ProtInc

immune response

Inferred from electronic annotation. Source: InterPro

multicellular organismal development

Traceable author statement Ref.11. Source: ProtInc

negative regulation of cell proliferation

Traceable author statement Ref.11. Source: ProtInc

negative regulation of hormone secretion

Inferred from direct assay PubMed 7867561. Source: MGI

negative regulation of meiosis

Inferred from electronic annotation. Source: Ensembl

peripheral nervous system development

Inferred from electronic annotation. Source: Ensembl

positive regulation of MAPK cascade

Inferred from direct assay PubMed 7508917. Source: MGI

positive regulation of acute inflammatory response

Inferred by curator Ref.13. Source: BHF-UCL

positive regulation of apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell division

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of cell proliferation

Inferred from direct assay Ref.13. Source: BHF-UCL

positive regulation of peptidyl-serine phosphorylation

Inferred from direct assay PubMed 7508917. Source: MGI

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.13. Source: BHF-UCL

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 7508917. Source: MGI

regulation of growth

Inferred from electronic annotation. Source: UniProtKB-KW

response to heat

Inferred from electronic annotation. Source: Ensembl

tyrosine phosphorylation of Stat1 protein

Inferred from electronic annotation. Source: Ensembl

tyrosine phosphorylation of Stat3 protein

Inferred from electronic annotation. Source: Ensembl

tyrosine phosphorylation of Stat5 protein

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular space

Traceable author statement Ref.1. Source: ProtInc

oncostatin-M receptor complex

Inferred from direct assay Ref.13. Source: BHF-UCL

   Molecular_functioncytokine activity

Inferred from direct assay Ref.13. Source: BHF-UCL

growth factor activity

Inferred from direct assay Ref.13. Source: BHF-UCL

oncostatin-M receptor binding

Inferred from physical interaction Ref.13. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Ref.7 Ref.8
Chain26 – 220195Oncostatin-M
PRO_0000017720
Propeptide221 – 25232
PRO_0000017721

Amino acid modifications

Glycosylation1001N-linked (GlcNAc...) Potential
Glycosylation2171N-linked (GlcNAc...) Potential
Disulfide bond31 ↔ 152 Ref.10
Disulfide bond74 ↔ 192 Ref.10

Natural variations

Natural variant91T → M.
Corresponds to variant rs5763919 [ dbSNP | Ensembl ].
VAR_049782

Experimental info

Mutagenesis741C → S: Inactive.
Mutagenesis1921C → S: Inactive.
Mutagenesis2011F → G: Inactive.
Mutagenesis2091F → G: Inactive.
Mutagenesis2201R → G: Inhibits propeptide cleavage. Ref.9
Mutagenesis2211R → G: Inhibits propeptide cleavage. Ref.9

Secondary structure

...................... 252
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13725 [UniParc].

Last modified August 1, 1990. Version 2.
Checksum: A5BE281175D101B9

FASTA25228,484
        10         20         30         40         50         60 
MGVLLTQRTL LSLVLALLFP SMASMAAIGS CSKEYRVLLG QLQKQTDLMQ DTSRLLDPYI 

        70         80         90        100        110        120 
RIQGLDVPKL REHCRERPGA FPSEETLRGL GRRGFLQTLN ATLGCVLHRL ADLEQRLPKA 

       130        140        150        160        170        180 
QDLERSGLNI EDLEKLQMAR PNILGLRNNI YCMAQLLDNS DTAEPTKAGR GASQPPTPTP 

       190        200        210        220        230        240 
ASDAFQRKLE GCRFLHGYHR FMHSVGRVFS KWGESPNRSR RHSPHQALRK GVRRTRPSRK 

       250 
GKRLMTRGQL PR 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning, sequence analysis, and functional expression of a novel growth regulator, oncostatin M."
Malik N., Kallestad J.C., Gunderson N.L., Austin S.D., Neubauer M.G., Ochs V., Marquardt H., Zarling J.M., Shoyab M., Wei C.M., Linsley P.S., Rose T.M.
Mol. Cell. Biol. 9:2847-2853(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[7]"Oncostatin M: a growth regulator produced by differentiated histiocytic lymphoma cells."
Zarling J.M., Shoyab M., Marquardt H., Hanson M.B., Lioubin M.N., Todaro G.J.
Proc. Natl. Acad. Sci. U.S.A. 83:9739-9743(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 26-51.
[8]"Identification of a major growth factor for AIDS-Kaposi's sarcoma cells as oncostatin M."
Nair B.C., DeVico A.L., Nakamura S., Copeland T.D., Chen Y., Patel A., O'Neil T., Oroszlan S., Gallo R.C., Sarngadharan M.G.
Science 255:1430-1432(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 26-45, FUNCTION.
Tissue: T-cell.
[9]"Cleavage of a hydrophilic C-terminal domain increases growth-inhibitory activity of oncostatin M."
Linsley P.S., Kallestad J., Ochs V., Neubauer M.
Mol. Cell. Biol. 10:1882-1890(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING, MUTAGENESIS OF ARG-220 AND ARG-221.
[10]"Disulfide bond assignment and identification of regions required for functional activity of oncostatin M."
Kallestad J.C., Shoyab M., Linsley P.S.
J. Biol. Chem. 266:8940-8945(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
[11]"Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6."
Rose T.M., Bruce A.G.
Proc. Natl. Acad. Sci. U.S.A. 88:8641-8645(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: INHIBITION OF M1 MYELOID LEUKEMIC CELLS.
[12]"Oncostatin M as a potent mitogen for AIDS-Kaposi's sarcoma-derived cells."
Miles S.A., Martinez-Maza O., Rezai A., Magpantay L., Kishimoto T., Nakamura S., Radka S.F., Linsley P.S.
Science 255:1432-1434(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Dual oncostatin M (OSM) receptors. Cloning and characterization of an alternative signaling subunit conferring OSM-specific receptor activation."
Mosley B., De Imus C., Friend D., Boiani N., Thoma B., Park L.S., Cosman D.
J. Biol. Chem. 271:32635-32643(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH OSMR AND IL6ST.
[14]"Crystal structure and functional dissection of the cytostatic cytokine oncostatin M."
Deller M.C., Hudson K.R., Ikemizu S., Bravo J., Jones E.Y., Heath J.K.
Structure 8:863-874(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 26-212.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M27288, M27286, M27287 Genomic DNA. Translation: AAA36388.1.
CR456534 mRNA. Translation: CAG30420.1.
CR541703 mRNA. Translation: CAG46504.1.
AC004264 Genomic DNA. Translation: AAC05173.1.
CH471095 Genomic DNA. Translation: EAW59864.1.
BC011589 mRNA. Translation: AAH11589.1.
PIRA32489.
RefSeqNP_065391.1. NM_020530.4.
UniGeneHs.248156.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EVSX-ray2.20A26-212[»]
ProteinModelPortalP13725.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111049. 3 interactions.
DIPDIP-5785N.
IntActP13725. 1 interaction.
MINTMINT-1352068.
STRING9606.ENSP00000215781.

PTM databases

PhosphoSiteP13725.

Polymorphism databases

DMDM129168.

Proteomic databases

PaxDbP13725.
PRIDEP13725.

Protocols and materials databases

DNASU5008.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000215781; ENSP00000215781; ENSG00000099985.
GeneID5008.
KEGGhsa:5008.
UCSCuc003ahb.3. human.

Organism-specific databases

CTD5008.
GeneCardsGC22M030658.
HGNCHGNC:8506. OSM.
HPAHPA029814.
MIM165095. gene.
neXtProtNX_P13725.
PharmGKBPA32836.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG39662.
HOGENOMHOG000074128.
HOVERGENHBG007867.
InParanoidP13725.
KOK05418.
OMAGYHRFMH.
OrthoDBEOG7NGQC9.
PhylomeDBP13725.
TreeFamTF338204.

Enzyme and pathway databases

SignaLinkP13725.

Gene expression databases

ArrayExpressP13725.
BgeeP13725.
CleanExHS_OSM.
GenevestigatorP13725.

Family and domain databases

Gene3D1.20.1250.10. 1 hit.
InterProIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR001581. Leukemia_IF/oncostatin.
IPR019827. Leukemia_IF/oncostatin_CS.
[Graphical view]
PfamPF01291. LIF_OSM. 1 hit.
[Graphical view]
SMARTSM00080. LIF_OSM. 1 hit.
[Graphical view]
SUPFAMSSF47266. SSF47266. 1 hit.
PROSITEPS00590. LIF_OSM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP13725.
GeneWikiOncostatin_M.
GenomeRNAi5008.
NextBio19284.
PMAP-CutDBP13725.
PROP13725.
SOURCESearch...

Entry information

Entry nameONCM_HUMAN
AccessionPrimary (citable) accession number: P13725
Secondary accession number(s): Q6FHP8, Q9UCP6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: August 1, 1990
Last modified: April 16, 2014
This is version 149 of the entry and version 2 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM