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P53347

- ONCM_MOUSE

UniProt

P53347 - ONCM_MOUSE

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Protein

Oncostatin-M

Gene

Osm

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  1. cytokine activity Source: MGI

GO - Biological processi

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

Keywords - Molecular functioni

Cytokine

Keywords - Biological processi

Growth regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Oncostatin-M
Short name:
OSM
Gene namesi
Name:Osm
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:104749. Osm.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: UniProtKB-KW
  2. oncostatin-M receptor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 205181Oncostatin-MPRO_0000017722Add
BLAST
Propeptidei206 – 26358By similarityPRO_0000408764Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 139By similarity
Glycosylationi30 – 301N-linked (GlcNAc...)Sequence Analysis
Glycosylationi44 – 441N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi71 ↔ 177By similarity
Glycosylationi145 – 1451N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

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

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiP53347.

PTM databases

PhosphoSiteiP53347.

Expressioni

Gene expression databases

BgeeiP53347.
CleanExiMM_OSM.
GenevestigatoriP53347.

Interactioni

Protein-protein interaction databases

DIPiDIP-5786N.

Structurei

3D structure databases

ProteinModelPortaliP53347.
SMRiP53347. Positions 28-197.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the LIF/OSM family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG39662.
GeneTreeiENSGT00390000004850.
HOGENOMiHOG000074128.
HOVERGENiHBG007867.
InParanoidiP53347.
KOiK05418.
OMAiGYHRFMH.
OrthoDBiEOG7NGQC9.
PhylomeDBiP53347.
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.

P53347-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQTRLLRTLL SLTLSLLILS MALANRGCSN SSSQLLSQLQ NQANLTGNTE
60 70 80 90 100
SLLEPYIRLQ NLNTPDLRAA CTQHSVAFPS EDTLRQLSKP HFLSTVYTTL
110 120 130 140 150
DRVLYQLDAL RQKFLKTPAF PKLDSARHNI LGIRNNVFCM ARLLNHSLEI
160 170 180 190 200
PEPTQTDSGA SRSTTTPDVF NTKIGSCGFL WGYHRFMGSV GRVFREWDDG
210 220 230 240 250
STRSRRQSPL RARRKGTRRI RVRHKGTRRI RVRRKGTRRI WVRRKGSRKI
260
RPSRSTQSPT TRA
Length:263
Mass (Da):30,114
Last modified:October 1, 1996 - v1
Checksum:i18326DB214797BCC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti217 – 2171T → S in BAE33358. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D31942 mRNA. Translation: BAA06712.1.
AK155637 mRNA. Translation: BAE33358.1.
AL807825 Genomic DNA. Translation: CAI25749.1.
BC099866 mRNA. Translation: AAH99866.1.
CCDSiCCDS24382.1.
PIRiS64719.
RefSeqiNP_001013383.1. NM_001013365.2.
UniGeneiMm.131422.

Genome annotation databases

EnsembliENSMUST00000075221; ENSMUSP00000074708; ENSMUSG00000058755.
GeneIDi18413.
KEGGimmu:18413.
UCSCiuc007hus.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D31942 mRNA. Translation: BAA06712.1 .
AK155637 mRNA. Translation: BAE33358.1 .
AL807825 Genomic DNA. Translation: CAI25749.1 .
BC099866 mRNA. Translation: AAH99866.1 .
CCDSi CCDS24382.1.
PIRi S64719.
RefSeqi NP_001013383.1. NM_001013365.2.
UniGenei Mm.131422.

3D structure databases

ProteinModelPortali P53347.
SMRi P53347. Positions 28-197.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-5786N.

PTM databases

PhosphoSitei P53347.

Proteomic databases

PRIDEi P53347.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000075221 ; ENSMUSP00000074708 ; ENSMUSG00000058755 .
GeneIDi 18413.
KEGGi mmu:18413.
UCSCi uc007hus.2. mouse.

Organism-specific databases

CTDi 5008.
MGIi MGI:104749. Osm.

Phylogenomic databases

eggNOGi NOG39662.
GeneTreei ENSGT00390000004850.
HOGENOMi HOG000074128.
HOVERGENi HBG007867.
InParanoidi P53347.
KOi K05418.
OMAi GYHRFMH.
OrthoDBi EOG7NGQC9.
PhylomeDBi P53347.
TreeFami TF338204.

Miscellaneous databases

NextBioi 294040.
PROi P53347.
SOURCEi Search...

Gene expression databases

Bgeei P53347.
CleanExi MM_OSM.
Genevestigatori P53347.

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

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiONCM_MOUSE
AccessioniPrimary (citable) accession number: P53347
Secondary accession number(s): Q3U1Y5, Q5SPX6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 29, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3