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P13725

- ONCM_HUMAN

UniProt

P13725 - ONCM_HUMAN

Protein

Oncostatin-M

Gene

OSM

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 2 (01 Aug 1990)
      Previous versions | rss
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    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

    1. cytokine activity Source: BHF-UCL
    2. growth factor activity Source: BHF-UCL
    3. oncostatin-M receptor binding Source: BHF-UCL

    GO - Biological processi

    1. behavioral response to pain Source: Ensembl
    2. cell proliferation Source: ProtInc
    3. immune response Source: InterPro
    4. multicellular organismal development Source: ProtInc
    5. negative regulation of cell proliferation Source: ProtInc
    6. negative regulation of hormone secretion Source: MGI
    7. negative regulation of meiosis Source: Ensembl
    8. peripheral nervous system development Source: Ensembl
    9. positive regulation of acute inflammatory response Source: BHF-UCL
    10. positive regulation of apoptotic signaling pathway Source: Ensembl
    11. positive regulation of cell division Source: UniProtKB-KW
    12. positive regulation of cell proliferation Source: BHF-UCL
    13. positive regulation of MAPK cascade Source: MGI
    14. positive regulation of peptidyl-serine phosphorylation Source: MGI
    15. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
    16. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    17. regulation of growth Source: UniProtKB-KW
    18. response to heat Source: Ensembl
    19. tyrosine phosphorylation of Stat1 protein Source: Ensembl
    20. tyrosine phosphorylation of Stat3 protein Source: Ensembl
    21. tyrosine phosphorylation of Stat5 protein Source: Ensembl

    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: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:8506. OSM.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: ProtInc
    2. oncostatin-M receptor complex Source: BHF-UCL

    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.

    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

    ArrayExpressiP13725.
    BgeeiP13725.
    CleanExiHS_OSM.
    GenevestigatoriP13725.

    Organism-specific databases

    HPAiHPA029814.

    Interactioni

    Protein-protein interaction databases

    BioGridi111049. 3 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 – 4915
    Helixi52 – 543
    Helixi56 – 627
    Helixi68 – 714
    Turni78 – 803
    Helixi84 – 896
    Helixi92 – 11524
    Helixi120 – 1223
    Helixi123 – 1264
    Helixi130 – 15627
    Helixi184 – 21027

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MGVLLTQRTL LSLVLALLFP SMASMAAIGS CSKEYRVLLG QLQKQTDLMQ    50
    DTSRLLDPYI RIQGLDVPKL REHCRERPGA FPSEETLRGL GRRGFLQTLN 100
    ATLGCVLHRL ADLEQRLPKA QDLERSGLNI EDLEKLQMAR PNILGLRNNI 150
    YCMAQLLDNS DTAEPTKAGR GASQPPTPTP ASDAFQRKLE GCRFLHGYHR 200
    FMHSVGRVFS KWGESPNRSR RHSPHQALRK GVRRTRPSRK GKRLMTRGQL 250
    PR 252
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi129168.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS13873.1.
    PIRi A32489.
    RefSeqi NP_065391.1. NM_020530.4.
    UniGenei Hs.248156.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EVS X-ray 2.20 A 26-212 [» ]
    ProteinModelPortali P13725.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111049. 3 interactions.
    DIPi DIP-5785N.
    IntActi P13725. 2 interactions.
    MINTi MINT-1352068.
    STRINGi 9606.ENSP00000215781.

    PTM databases

    PhosphoSitei P13725.

    Polymorphism databases

    DMDMi 129168.

    Proteomic databases

    PaxDbi P13725.
    PRIDEi P13725.

    Protocols and materials databases

    DNASUi 5008.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000215781 ; ENSP00000215781 ; ENSG00000099985 .
    GeneIDi 5008.
    KEGGi hsa:5008.
    UCSCi uc003ahb.3. human.

    Organism-specific databases

    CTDi 5008.
    GeneCardsi GC22M030658.
    HGNCi HGNC:8506. OSM.
    HPAi HPA029814.
    MIMi 165095. gene.
    neXtProti NX_P13725.
    PharmGKBi PA32836.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG39662.
    HOGENOMi HOG000074128.
    HOVERGENi HBG007867.
    InParanoidi P13725.
    KOi K05418.
    OMAi GYHRFMH.
    OrthoDBi EOG7NGQC9.
    PhylomeDBi P13725.
    TreeFami TF338204.

    Enzyme and pathway databases

    SignaLinki P13725.

    Miscellaneous databases

    EvolutionaryTracei P13725.
    GeneWikii Oncostatin_M.
    GenomeRNAii 5008.
    NextBioi 19284.
    PMAP-CutDB P13725.
    PROi P13725.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P13725.
    Bgeei P13725.
    CleanExi HS_OSM.
    Genevestigatori P13725.

    Family and domain databases

    Gene3Di 1.20.1250.10. 1 hit.
    InterProi IPR009079. 4_helix_cytokine-like_core.
    IPR012351. 4_helix_cytokine_core.
    IPR001581. Leukemia_IF/oncostatin.
    IPR019827. Leukemia_IF/oncostatin_CS.
    [Graphical view ]
    Pfami PF01291. LIF_OSM. 1 hit.
    [Graphical view ]
    SMARTi SM00080. LIF_OSM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47266. SSF47266. 1 hit.
    PROSITEi PS00590. LIF_OSM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 151 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