P13725 (ONCM_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Oncostatin-M
Short name=OSM

Gene names

Name:

OSM

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	252 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	Growth regulation
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Cytokine Mitogen
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Inferred from electronic annotation. Source: Compara behavioral response to pain Inferred from electronic annotation. Source: Compara 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: Compara peripheral nervous system development Inferred from electronic annotation. Source: Compara 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 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: Compara tyrosine phosphorylation of Stat1 protein Inferred from electronic annotation. Source: Compara tyrosine phosphorylation of Stat3 protein Inferred from electronic annotation. Source: Compara tyrosine phosphorylation of Stat5 protein Inferred from electronic annotation. Source: Compara
Cellular_component	extracellular space Traceable author statement Ref.1. Source: ProtInc oncostatin-M receptor complex Inferred from direct assay Ref.13. Source: BHF-UCL
Molecular_function	cytokine 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 Traceable author statement PubMed 9920829. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Ref.7 Ref.8

Chain

26 – 220

195

Oncostatin-M

PRO_0000017720

Propeptide

221 – 252

32

PRO_0000017721

Amino acid modifications

Glycosylation

100

1

N-linked (GlcNAc...) Potential

Glycosylation

217

1

N-linked (GlcNAc...) Potential

Disulfide bond

31 ↔ 152

Ref.10

Disulfide bond

74 ↔ 192

Ref.10

Natural variations

Natural variant

9

1

T → M.
Corresponds to variant rs5763919 [ dbSNP | Ensembl ].

VAR_049782

Experimental info

Mutagenesis

74

1

C → S: Inactive.

Mutagenesis

192

1

C → S: Inactive.

Mutagenesis

201

1

F → G: Inactive.

Mutagenesis

209

1

F → G: Inactive.

Mutagenesis

220

1

R → G: Inhibits propeptide cleavage. Ref.9

Mutagenesis

221

1

R → G: Inhibits propeptide cleavage. Ref.9

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

252

Helix Strand Turn

Details...

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

Sequences

	Sequence		Length	Mass (Da)
	P13725 [UniParc]. Last modified August 1, 1990. Version 2. Checksum: A5BE281175D101B9	FASTA	252	28,484
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

IPI

IPI00010336.

PIR

A32489.

RefSeq

NP_065391.1. NM_020530.4.

UniGene

Hs.248156.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EVS	X-ray	2.20	A	26-212	[»]

ProteinModelPortal

P13725.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5785N.

MINT

MINT-1352068.

STRING

9606.ENSP00000215781.

PTM databases

PhosphoSite

P13725.

Polymorphism databases

DMDM

129168.

Proteomic databases

PaxDb

P13725.

PRIDE

P13725.

Protocols and materials databases

DNASU

5008.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000215781; ENSP00000215781; ENSG00000099985.

GeneID

5008.

KEGG

hsa:5008.

UCSC

uc003ahb.3. human.

Organism-specific databases

CTD

5008.

GeneCards

GC22M030658.

HGNC

HGNC:8506. OSM.

HPA

HPA029814.

MIM

165095. gene.

neXtProt

NX_P13725.

PharmGKB

PA32836.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG39662.

HOGENOM

HOG000074128.

HOVERGEN

HBG007867.

InParanoid

P13725.

KO

K05418.

OMA

GYHRFMH.

OrthoDB

EOG4H19X6.

PhylomeDB

P13725.

Gene expression databases

ArrayExpress

P13725.

Bgee

P13725.

CleanEx

HS_OSM.

Genevestigator

P13725.

GermOnline

ENSG00000099985. Homo sapiens.

Family and domain databases

Gene3D

1.20.1250.10. 1 hit.

InterPro

IPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR001581. Leukemia_IF/oncostatin.
IPR019827. Leukemia_IF/oncostatin_CS.
[Graphical view]

Pfam

PF01291. LIF_OSM. 1 hit.
[Graphical view]

SMART

SM00080. LIF_OSM. 1 hit.
[Graphical view]

SUPFAM

SSF47266. 4_helix_cytokine. 1 hit.

PROSITE

PS00590. LIF_OSM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P13725.

GenomeRNAi

5008.

NextBio

19284.

PMAP-CutDB

P13725.

SOURCE

Search...

Entry information

Entry name

ONCM_HUMAN

Accession

Primary (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 3, 2013
This is version 142 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.