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Protein

Oncostatin-M

Gene

OSM

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  • cytokine activity Source: BHF-UCL
  • growth factor activity Source: BHF-UCL
  • oncostatin-M receptor binding Source: BHF-UCL

GO - Biological processi

  • behavioral response to pain Source: Ensembl
  • cell proliferation Source: ProtInc
  • immune response Source: InterPro
  • multicellular organismal development Source: ProtInc
  • negative regulation of cell proliferation Source: ProtInc
  • negative regulation of hormone secretion Source: MGI
  • negative regulation of meiotic nuclear division Source: Ensembl
  • oncostatin-M-mediated signaling pathway Source: BHF-UCL
  • peripheral nervous system development Source: Ensembl
  • positive regulation of acute inflammatory response Source: BHF-UCL
  • positive regulation of apoptotic signaling pathway Source: Ensembl
  • positive regulation of cell division Source: UniProtKB-KW
  • positive regulation of cell proliferation Source: BHF-UCL
  • positive regulation of MAPK cascade Source: MGI
  • positive regulation of peptidyl-serine phosphorylation Source: MGI
  • positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • positive regulation of tyrosine phosphorylation of Stat3 protein Source: CACAO
  • regulation of growth Source: UniProtKB-KW
  • response to heat Source: Ensembl
  • tyrosine phosphorylation of Stat1 protein Source: Ensembl
  • tyrosine phosphorylation of Stat3 protein Source: Ensembl
  • tyrosine phosphorylation of Stat5 protein Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Cytokine, Mitogen

Keywords - Biological processi

Growth regulation

Enzyme and pathway databases

SignaLinkiP13725.

Names & Taxonomyi

Protein namesi
Recommended name:
Oncostatin-M
Short name:
OSM
Gene namesi
Name:OSM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:8506. OSM.

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: ProtInc
  • intracellular Source: GOC
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi74 – 741C → S: Inactive.
Mutagenesisi192 – 1921C → S: Inactive.
Mutagenesisi201 – 2011F → G: Inactive.
Mutagenesisi209 – 2091F → G: Inactive.
Mutagenesisi220 – 2201R → G: Inhibits propeptide cleavage. 1 Publication
Mutagenesisi221 – 2211R → G: Inhibits propeptide cleavage. 1 Publication

Organism-specific databases

PharmGKBiPA32836.

Polymorphism and mutation databases

BioMutaiOSM.
DMDMi129168.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 25252 PublicationsAdd
BLAST
Chaini26 – 220195Oncostatin-MPRO_0000017720Add
BLAST
Propeptidei221 – 25232PRO_0000017721Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi31 ↔ 1521 Publication
Disulfide bondi74 ↔ 1921 Publication
Glycosylationi100 – 1001N-linked (GlcNAc...)Sequence Analysis
Glycosylationi217 – 2171N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Propeptide processing is not important for receptor binding activity but may be important growth-inhibitory activity.1 Publication

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP13725.
PRIDEiP13725.

PTM databases

PhosphoSiteiP13725.

Miscellaneous databases

PMAP-CutDBP13725.

Expressioni

Gene expression databases

BgeeiP13725.
CleanExiHS_OSM.
ExpressionAtlasiP13725. baseline and differential.
GenevisibleiP13725. HS.

Organism-specific databases

HPAiHPA029814.

Interactioni

Protein-protein interaction databases

BioGridi111049. 9 interactions.
DIPiDIP-5785N.
IntActiP13725. 2 interactions.
MINTiMINT-1352068.
STRINGi9606.ENSP00000215781.

Structurei

Secondary structure

1
252
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi35 – 4915Combined sources
Helixi52 – 543Combined sources
Helixi56 – 627Combined sources
Helixi68 – 714Combined sources
Turni78 – 803Combined sources
Helixi84 – 896Combined sources
Helixi92 – 11524Combined sources
Helixi120 – 1223Combined sources
Helixi123 – 1264Combined sources
Helixi130 – 15627Combined sources
Helixi184 – 21027Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EVSX-ray2.20A26-212[»]
ProteinModelPortaliP13725.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13725.

Family & Domainsi

Sequence similaritiesi

Belongs to the LIF/OSM family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG39662.
GeneTreeiENSGT00390000004850.
HOGENOMiHOG000074128.
HOVERGENiHBG007867.
InParanoidiP13725.
KOiK05418.
OMAiGYHRFMH.
OrthoDBiEOG7NGQC9.
PhylomeDBiP13725.
TreeFamiTF338204.

Family and domain databases

Gene3Di1.20.1250.10. 1 hit.
InterProiIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR001581. Leukemia_IF/oncostatin.
IPR019827. Leukemia_IF/oncostatin_CS.
[Graphical view]
PfamiPF01291. LIF_OSM. 1 hit.
[Graphical view]
SMARTiSM00080. LIF_OSM. 1 hit.
[Graphical view]
SUPFAMiSSF47266. SSF47266. 1 hit.
PROSITEiPS00590. LIF_OSM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P13725-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGVLLTQRTL LSLVLALLFP SMASMAAIGS CSKEYRVLLG QLQKQTDLMQ
60 70 80 90 100
DTSRLLDPYI RIQGLDVPKL REHCRERPGA FPSEETLRGL GRRGFLQTLN
110 120 130 140 150
ATLGCVLHRL ADLEQRLPKA QDLERSGLNI EDLEKLQMAR PNILGLRNNI
160 170 180 190 200
YCMAQLLDNS DTAEPTKAGR GASQPPTPTP ASDAFQRKLE GCRFLHGYHR
210 220 230 240 250
FMHSVGRVFS KWGESPNRSR RHSPHQALRK GVRRTRPSRK GKRLMTRGQL

PR
Length:252
Mass (Da):28,484
Last modified:August 1, 1990 - v2
Checksum:iA5BE281175D101B9
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91T → M.
Corresponds to variant rs5763919 [ dbSNP | Ensembl ].
VAR_049782

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13873.1.
PIRiA32489.
RefSeqiNP_065391.1. NM_020530.4.
UniGeneiHs.248156.

Genome annotation databases

EnsembliENST00000215781; ENSP00000215781; ENSG00000099985.
GeneIDi5008.
KEGGihsa:5008.
UCSCiuc003ahb.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13873.1.
PIRiA32489.
RefSeqiNP_065391.1. NM_020530.4.
UniGeneiHs.248156.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EVSX-ray2.20A26-212[»]
ProteinModelPortaliP13725.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111049. 9 interactions.
DIPiDIP-5785N.
IntActiP13725. 2 interactions.
MINTiMINT-1352068.
STRINGi9606.ENSP00000215781.

PTM databases

PhosphoSiteiP13725.

Polymorphism and mutation databases

BioMutaiOSM.
DMDMi129168.

Proteomic databases

PaxDbiP13725.
PRIDEiP13725.

Protocols and materials databases

DNASUi5008.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000215781; ENSP00000215781; ENSG00000099985.
GeneIDi5008.
KEGGihsa:5008.
UCSCiuc003ahb.3. human.

Organism-specific databases

CTDi5008.
GeneCardsiGC22M030658.
HGNCiHGNC:8506. OSM.
HPAiHPA029814.
MIMi165095. gene.
neXtProtiNX_P13725.
PharmGKBiPA32836.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG39662.
GeneTreeiENSGT00390000004850.
HOGENOMiHOG000074128.
HOVERGENiHBG007867.
InParanoidiP13725.
KOiK05418.
OMAiGYHRFMH.
OrthoDBiEOG7NGQC9.
PhylomeDBiP13725.
TreeFamiTF338204.

Enzyme and pathway databases

SignaLinkiP13725.

Miscellaneous databases

EvolutionaryTraceiP13725.
GeneWikiiOncostatin_M.
GenomeRNAii5008.
NextBioi19284.
PMAP-CutDBP13725.
PROiP13725.
SOURCEiSearch...

Gene expression databases

BgeeiP13725.
CleanExiHS_OSM.
ExpressionAtlasiP13725. baseline and differential.
GenevisibleiP13725. HS.

Family and domain databases

Gene3Di1.20.1250.10. 1 hit.
InterProiIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR001581. Leukemia_IF/oncostatin.
IPR019827. Leukemia_IF/oncostatin_CS.
[Graphical view]
PfamiPF01291. LIF_OSM. 1 hit.
[Graphical view]
SMARTiSM00080. LIF_OSM. 1 hit.
[Graphical view]
SUPFAMiSSF47266. SSF47266. 1 hit.
PROSITEiPS00590. LIF_OSM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. 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.

Entry informationi

Entry nameiONCM_HUMAN
AccessioniPrimary (citable) accession number: P13725
Secondary accession number(s): Q6FHP8, Q9UCP6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: August 1, 1990
Last modified: June 24, 2015
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.