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Reviewed, UniProtKB/Swiss-Prot P13725 (ONCM_HUMAN)

Last modified June 16, 2009. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Oncostatin-M
      Short name=OSM
Gene names
Name: OSM
OrganismHomo sapiens (Human)
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). Ref.8 Ref.12

Subcellular location

Secreted.

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
Direct protein sequencing
Gene Ontology (GO)
   Biological processcell proliferation Ref.12

Traceable author statement. Source: ProtInc

immune response

Inferred from electronic annotation. Source: InterPro

negative regulation of cell proliferation Ref.11

Traceable author statement. Source: ProtInc

negative regulation of hormone secretion

Inferred from direct assay. Source: MGI

positive regulation of MAPKKK cascade

Inferred from direct assay. Source: MGI

positive regulation of acute inflammatory response Ref.13

Inferred by curator. Source: UniProtKB

positive regulation of cell proliferation Ref.13

Inferred from direct assay. Source: UniProtKB

positive regulation of peptidyl-serine phosphorylation

Inferred from direct assay. Source: MGI

positive regulation of peptidyl-tyrosine phosphorylation Ref.13

Inferred from direct assay. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay. Source: MGI

regulation of growth

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular space Ref.1

Traceable author statement. Source: ProtInc

oncostatin-M receptor complex Ref.13

Inferred from direct assay. Source: UniProtKB

   Molecular functioncytokine activity Ref.1 Ref.13

Inferred from direct assay. Source: UniProtKB

growth factor activity Ref.13

Inferred from direct assay. Source: UniProtKB

oncostatin-M receptor binding Ref.13

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Ref.8 Ref.7
Chain26 – 234209Oncostatin-M
PRO_0000017720
Propeptide235 – 25218
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: dbSNP rs5763919.
VAR_049782

Experimental info

Mutagenesis741C → S: Inactive.
Mutagenesis1921C → S: Inactive.
Mutagenesis2011F → G: Inactive.
Mutagenesis2091F → G: Inactive.

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P13725-1 [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: 2779549] [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:RESEARCH84.1-RESEARCH84.11(2004) [PubMed: 15461802] [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: 10591208] [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: 15489334] [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: 3540948] [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: 1542792] [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: 2325640] [Abstract]
Cited for: PROTEOLYTIC PROCESSING.
[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: 2026606] [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: 1717982] [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: 1542793] [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: 8999038] [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: 10997905] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 26-212.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
IPIIPI00010336.
PIRA32489.
RefSeqNP_065391.1.
UniGeneHs.248156

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1EVSX-ray2.20A26-212[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:5785N.

Proteomic databases

PRIDEP13725.

Genome annotation databases

EnsemblENSG00000099985. Homo sapiens. [Contig view]
GeneID5008.
KEGGhsa:5008.

Organism-specific databases

GeneCardsGC22M028983.
H-InvDBHIX0016363.
HGNCHGNC:8506. OSM.
MIM165095. gene.
PharmGKBPA32836.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP13725.
HOVERGENP13725.
OMAP13725. EHCRERP.

Gene expression databases

ArrayExpressP13725.
BgeeP13725.
CleanExHS_OSM.
GermOnlineENSG00000099985. Homo sapiens.

Family and domain databases

InterProIPR012351. 4_helix_cytokine_core.
IPR001581. Leukemia_IF/oncostatin.
IPR019827. Leukemia_IF/oncostatin_CS.
[Graphical view]
Gene3DG3DSA:1.20.1250.10. 4_helix_cytokine_core. 1 hit.
PfamPF01291. LIF_OSM. 1 hit.
[Graphical view]
ProDomPD023062. Oncostatin. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00080. LIF_OSM. 1 hit.
[Graphical view]
PROSITEPS00590. LIF_OSM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio19284.
PMAP-CutDBP13725.
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: June 16, 2009
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 22

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents