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P53347 (ONCM_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Oncostatin-M

Short name=OSM
Gene names
Name:Osm
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length263 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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 By similarity. Uses only 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.

Subcellular location

Secreted.

Post-translational modification

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

Sequence similarities

Belongs to the LIF/OSM family.

Ontologies

Keywords
   Biological processGrowth regulation
   Cellular componentSecreted
   DomainSignal
   Molecular functionCytokine
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbehavioral response to pain

Inferred from mutant phenotype PubMed 14985435. Source: MGI

immune response

Inferred from electronic annotation. Source: InterPro

negative regulation of hormone secretion

Inferred from electronic annotation. Source: Ensembl

negative regulation of meiosis

Inferred from direct assay PubMed 11203703. Source: MGI

peripheral nervous system development

Inferred from mutant phenotype PubMed 14985435. Source: MGI

positive regulation of MAPK cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic signaling pathway

Inferred from direct assay PubMed 15012602. Source: MGI

positive regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-serine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of peptidyl-tyrosine phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of growth

Inferred from electronic annotation. Source: UniProtKB-KW

response to heat

Inferred from mutant phenotype PubMed 14985435. Source: MGI

tyrosine phosphorylation of Stat1 protein

Inferred from direct assay PubMed 15012602. Source: MGI

tyrosine phosphorylation of Stat3 protein

Inferred from direct assay PubMed 15012602. Source: MGI

tyrosine phosphorylation of Stat5 protein

Inferred from direct assay PubMed 15012602. Source: MGI

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-KW

oncostatin-M receptor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncytokine activity

Inferred from direct assay PubMed 15012602. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 205181Oncostatin-M
PRO_0000017722
Propeptide206 – 26358 By similarity
PRO_0000408764

Amino acid modifications

Glycosylation301N-linked (GlcNAc...) Potential
Glycosylation441N-linked (GlcNAc...) Potential
Glycosylation1451N-linked (GlcNAc...) Potential
Disulfide bond28 ↔ 139 By similarity
Disulfide bond71 ↔ 177 By similarity

Experimental info

Sequence conflict2171T → S in BAE33358. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P53347 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 18326DB214797BCC

FASTA26330,114
        10         20         30         40         50         60 
MQTRLLRTLL SLTLSLLILS MALANRGCSN SSSQLLSQLQ NQANLTGNTE SLLEPYIRLQ 

        70         80         90        100        110        120 
NLNTPDLRAA CTQHSVAFPS EDTLRQLSKP HFLSTVYTTL DRVLYQLDAL RQKFLKTPAF 

       130        140        150        160        170        180 
PKLDSARHNI LGIRNNVFCM ARLLNHSLEI PEPTQTDSGA SRSTTTPDVF NTKIGSCGFL 

       190        200        210        220        230        240 
WGYHRFMGSV GRVFREWDDG STRSRRQSPL RARRKGTRRI RVRHKGTRRI RVRRKGTRRI 

       250        260 
WVRRKGSRKI RPSRSTQSPT TRA 

« Hide

References

« Hide 'large scale' references
[1]"Mouse oncostatin M: an immediate early gene induced by multiple cytokines through the JAK-STAT5 pathway."
Yoshimura A., Ichihara M., Kinjyo I., Moriyama M., Copeland N.G., Gilbert D.J., Jenkins N.A., Hara T., Miyajima A.
EMBO J. 15:1055-1063(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Dendritic cell.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"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].
[5]"Reconstitution of the functional mouse oncostatin M (OSM) receptor: molecular cloning of the OSM receptor beta subunit."
Tanaka M., Hara T., Copeland N.G., Gilbert D.J., Jenkins N.A., Miyajima A.
Blood 93:804-815(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH OSMR AND IL6ST.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D31942 mRNA. Translation: BAA06712.1.
AK155637 mRNA. Translation: BAE33358.1.
AL807825 Genomic DNA. Translation: CAI25749.1.
BC099866 mRNA. Translation: AAH99866.1.
CCDSCCDS24382.1.
PIRS64719.
RefSeqNP_001013383.1. NM_001013365.2.
UniGeneMm.131422.

3D structure databases

ProteinModelPortalP53347.
SMRP53347. Positions 28-197.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-5786N.

PTM databases

PhosphoSiteP53347.

Proteomic databases

PRIDEP53347.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000075221; ENSMUSP00000074708; ENSMUSG00000058755.
GeneID18413.
KEGGmmu:18413.
UCSCuc007hus.2. mouse.

Organism-specific databases

CTD5008.
MGIMGI:104749. Osm.

Phylogenomic databases

eggNOGNOG39662.
GeneTreeENSGT00390000004850.
HOGENOMHOG000074128.
HOVERGENHBG007867.
InParanoidQ3U1Y5.
KOK05418.
OMAGYHRFMH.
OrthoDBEOG7NGQC9.
PhylomeDBP53347.
TreeFamTF338204.

Gene expression databases

BgeeP53347.
CleanExMM_OSM.
GenevestigatorP53347.

Family and domain databases

Gene3D1.20.1250.10. 1 hit.
InterProIPR009079. 4_helix_cytokine-like_core.
IPR012351. 4_helix_cytokine_core.
IPR001581. Leukemia_IF/oncostatin.
IPR019827. Leukemia_IF/oncostatin_CS.
[Graphical view]
PfamPF01291. LIF_OSM. 1 hit.
[Graphical view]
SMARTSM00080. LIF_OSM. 1 hit.
[Graphical view]
SUPFAMSSF47266. SSF47266. 1 hit.
PROSITEPS00590. LIF_OSM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio294040.
PROP53347.
SOURCESearch...

Entry information

Entry nameONCM_MOUSE
AccessionPrimary (citable) accession number: P53347
Secondary accession number(s): Q3U1Y5, Q5SPX6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 99 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot