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UniProtKB/Swiss-Prot entry P13725


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ONCM_HUMAN
Primary accession number P13725
Secondary accession numbers None
Integrated into Swiss-Prot on January 1, 1990
Sequence was last modified on August 1, 1990 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 96)
Name and origin of the protein
Protein name Oncostatin-M [Precursor]
Synonym OSM
Gene name
Name: OSM
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2779549 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Molecular cloning, sequence analysis, and functional expression of a novel growth regulator, oncostatin M.";
Mol. Cell. Biol. 9:2847-2853(1989).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1186/gb-2004-5-10-r84; PubMed=15461802 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/990031; PubMed=10591208 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 26-51.
PubMed=3540948 [NCBI, ExPASy, EBI, Israel, Japan]
Zarling J.M., Shoyab M., Marquardt H., Hanson M.B., Lioubin M.N., Todaro G.J.;
"Oncostatin M: a growth regulator produced by differentiated histiocytic lymphoma cells.";
Proc. Natl. Acad. Sci. U.S.A. 83:9739-9743(1986).
[6]
DISULFIDE BONDS.
PubMed=2026606 [NCBI, ExPASy, EBI, Israel, Japan]
Kallestad J.C., Shoyab M., Linsley P.S.;
"Disulfide bond assignment and identification of regions required for functional activity of oncostatin M.";
J. Biol. Chem. 266:8940-8945(1991).
[7]
INHIBITION OF M1 MYELOID LEUKEMIC CELLS.
PubMed=1717982 [NCBI, ExPASy, EBI, Israel, Japan]
Rose T.M., Bruce A.G.;
"Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6.";
Proc. Natl. Acad. Sci. U.S.A. 88:8641-8645(1991).
[8]
PROTEOLYTIC PROCESSING.
PubMed=2325640 [NCBI, ExPASy, EBI, Israel, Japan]
Linsley P.S., Kallestad J., Ochs V., Neubauer M.;
"Cleavage of a hydrophilic C-terminal domain increases growth-inhibitory activity of oncostatin M.";
Mol. Cell. Biol. 10:1882-1890(1990).
[9]
INTERACTION WITH OSMR AND IL6ST.
DOI=10.1074/jbc.271.51.32635; PubMed=8999038 [NCBI, ExPASy, EBI, Israel, Japan]
Mosley B., De Imus C., Friend D., Boiani N., Thoma B., Park L.S., Cosman D.;
"Dual oncostatin M (OSM) receptors. Cloning and characterization of an alternative signaling subunit conferring OSM-specific receptor activation.";
J. Biol. Chem. 271:32635-32643(1996).
[10]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 26-212.
DOI=10.1016/S0969-2126(00)00176-3; PubMed=10997905 [NCBI, ExPASy, EBI, Israel, Japan]
Deller M.C., Hudson K.R., Ikemizu S., Bravo J., Jones E.Y., Heath J.K.;
"Crystal structure and functional dissection of the cytostatic cytokine oncostatin M.";
Structure 8:863-874(2000).
Comments
  • FUNCTION: Growth regulator. Inhibits the proliferation of a number of tumor cell lines. 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).
  • SUBCELLULAR LOCATION: Secreted.
  • SIMILARITY: Belongs to the LIF/OSM family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M27288; AAA36388.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M27286; AAA36388.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M27287; AAA36388.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456534; CAG30420.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC004264; AAC05173.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011589; AAH11589.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A32489; A32489.
RefSeq NP_065391.1; -.
UniGene Hs.248156
3D structure databases
PDB
1EVS; X-ray; 2.20 A; A=26-212.[ExPASy / RCSB / EBI]
PDBsum 1EVS; -.
ModBase P13725.
Protein-protein interaction databases
DIP DIP:5785N; -.
Organism-specific databases
H-InvDB HIX0016363; -.
HGNC HGNC:8506; OSM.
GenAtlas OSM.
MIM 165095; gene. [NCBI / EBI]
PharmGKB PA32836; -.
GeneCards P13725.
Gene expression databases
ArrayExpress P13725; -.
CleanEx HS_OSM; -.
GermOnline ENSG00000099985; Homo sapiens.
Ontologies
GO
GO:0005615; Cellular component: extracellular space (traceable author statement from ProtInc).
GO:0005147; Molecular function: oncostatin-M receptor binding (traceable author statement from ProtInc).
GO:0006955; Biological process: immune response (inferred from electronic annotation from InterPro).
GO:0008285; Biological process: negative regulation of cell proliferation (traceable author statement from ProtInc).
GO:0046888; Biological process: negative regulation of hormone secretion (inferred from direct assay from MGI).
GO:0043410; Biological process: positive regulation of MAPKKK cascade (inferred from direct assay from MGI).
GO:0033138; Biological process: positive regulation of peptidyl-serine phosphorylation (inferred from direct assay from MGI).
GO:0050731; Biological process: positive regulation of peptidyl-tyrosine phosphorylation (inferred from direct assay from MGI).
GO:0045944; Biological process: positive regulation of transcription from RNA polymerase II promoter (inferred from direct assay from MGI).
GO:0001558; Biological process: regulation of cell growth (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR012351; 4_helix_cytokine_core.
IPR001581; LIF_OSM.
Graphical view of domain structure.
Gene3D G3DSA:1.20.1250.10; 4_helix_cytokine_core; 1.
Pfam PF01291; LIF_OSM; 1.
Pfam graphical view of domain structure.
ProDom PD023062; Oncostatin; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00080; LIF_OSM; 1.
SMART graphical view of domain structure.
PROSITE PS00590; LIF_OSM; 1.
ProtoNet P13725.
Genome annotation databases
Ensembl ENSG00000099985; Homo sapiens. [Contig view]
GeneID 5008; -.
KEGG hsa:5008; -.
Phylogenomic databases
HOGENOM P13725; -.
HOVERGEN P13725; -.
Other
NextBio 19284; -.
SOURCE OSM; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Cleavage on pair of basic residues; Cytokine; Direct protein sequencing; Glycoprotein; Growth regulation; Secreted; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    25  25      
CHAIN   26   234  209     Oncostatin-M. PRO_0000017720
PROPEP   235   252  18      PRO_0000017721
CARBOHYD   100   100        N-linked (GlcNAc...) (Potential). 
CARBOHYD   217   217        N-linked (GlcNAc...) (Potential). 
DISULFID   31   152         
DISULFID   74   192         
MUTAGEN   74    74        C->S: Inactive. 
MUTAGEN   192   192        C->S: Inactive. 
MUTAGEN   201   201        F->G: Inactive. 
MUTAGEN   209   209        F->G: Inactive. 
HELIX   35    49  15      
HELIX   52    54  3      
HELIX   56    62  7      
HELIX   68    71  4      
TURN   78    80  3      
HELIX   84    89  6      
HELIX   92   115  24      
HELIX   120   122  3      
HELIX   123   126  4      
HELIX   130   156  27      
HELIX   184   210  27      
Sequence information
Length: 252 AA [This is the length of the unprocessed precursor] Molecular weight: 28484 Da [This is the MW of the unprocessed precursor] CRC64: A5BE281175D101B9 [This is a checksum on the sequence]
        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 

P13725 in FASTA format

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