Reviewed, UniProtKB/Swiss-Prot P13725 (ONCM_HUMAN)

Names and origin

Protein names

Recommended name:
    Oncostatin-M
      Short name=OSM

Gene names

Name:

OSM

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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). Ref.8 Ref.12
Subcellular location	Secreted.
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 Direct protein sequencing
Gene Ontology (GO)
Biological process	cell 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 component	extracellular space Ref.1 Traceable author statement. Source: ProtInc oncostatin-M receptor complex Ref.13 Inferred from direct assay. Source: UniProtKB
Molecular function	cytokine 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 25

25

Ref.8 Ref.7

Chain

26 – 234

209

Oncostatin-M

PRO_0000017720

Propeptide

235 – 252

18

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: dbSNP rs5763919.

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.

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)
	P13725-1 [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: 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. , 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. , 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

EMBLGenBankDDBJ

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.

UniGene

Hs.248156

3D structure databases

PDBPDBe

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

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:5785N.

Proteomic databases

PRIDE

P13725.

Genome annotation databases

Ensembl

ENSG00000099985. Homo sapiens. [Contig view]

GeneID

5008.

KEGG

hsa:5008.

Organism-specific databases

GeneCards

GC22M028983.

H-InvDB

HIX0016363.

HGNC

HGNC:8506. OSM.

MIM

165095. gene.

PharmGKB

PA32836.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P13725.

HOVERGEN

P13725.

OMA

P13725. EHCRERP.

Gene expression databases

ArrayExpress

P13725.

Bgee

P13725.

CleanEx

HS_OSM.

GermOnline

ENSG00000099985. Homo sapiens.

Family and domain databases

InterPro

IPR012351. 4_helix_cytokine_core.
IPR001581. Leukemia_IF/oncostatin.
IPR019827. Leukemia_IF/oncostatin_CS.
[Graphical view]

Gene3D

G3DSA:1.20.1250.10. 4_helix_cytokine_core. 1 hit.

Pfam

PF01291. LIF_OSM. 1 hit.
[Graphical view]

ProDom

PD023062. Oncostatin. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

SM00080. LIF_OSM. 1 hit.
[Graphical view]

PROSITE

PS00590. LIF_OSM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

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:	June 16, 2009
This is version 104 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)