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Reviewed, UniProtKB/Swiss-Prot Q99650 (OSMR_HUMAN)

Last modified June 16, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Oncostatin-M specific receptor subunit beta
Gene names
Name: OSMR
Synonyms: OSMRB
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length979 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Associates with IL31RA to form the IL31 receptor. Binds IL31 to activate STAT3 and possibly STAT1 and STAT5. Capable of transducing OSM-specific signaling events. Ref.1 Ref.3

Subunit structure

Heterodimer composed of OSMR and IL6ST (type II OSM receptor). Heterodimer with IL31RA to form the IL31 receptor. Ref.1 Ref.3

Subcellular location

Membrane; Single-pass type I membrane protein Potential.

Tissue specificity

Expressed at relatively high levels in all neural cells as well as fibroblast, epithelial and a variety of tumor cell lines. Ref.1

Induction

Activated by oncostatin-M. Up-regulated by IFNG and lipopolysaccharide. Ref.1 Ref.3

Domain

The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding By similarity.

The box 1 motif is required for JAK interaction and/or activation By similarity.

Involvement in disease

Defects in OSMR are the cause of amyloidosis type 9 (AMYL9) [MIM:105250]; also known as primary cutaneous amyloidosis (PCA), primary localized cutaneous amyloidosis (PLCA), familial lichen amyloidosis or familial cutaneous lichen amyloidosis. AMYL9 is a hereditary primary amyloidosis characterized by localized cutaneous amyloid deposition. This condition usually presents with itching (especially on the lower legs) and visible changes of skin hyperpigmentation and thickening (lichenification) that may be exacerbated by chronic scratching and rubbing. The amyloid deposits probably reflect a combination of degenerate keratin filaments, serum amyloid P component, and deposition of immunoglobulins. Ref.6

Sequence similarities

Belongs to the type I cytokine receptor family. Type 2 subfamily.

Contains 4 fibronectin type-III domains.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q99650-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q99650-2)

The sequence of this isoform differs from the canonical sequence as follows:
     331-342: VYLMNPFSVNFE → GETRVVTAHRGH
     343-979: Missing.
Isoform 3 (identifier: Q99650-3)

The sequence of this isoform differs from the canonical sequence as follows:
     216-979: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 979952Oncostatin-M specific receptor subunit beta
PRO_0000259759

Regions

Topological domain28 – 740713Extracellular Potential
Transmembrane741 – 76121 Potential
Topological domain762 – 979218Cytoplasmic Potential
Domain332 – 42493Fibronectin type-III 1
Domain430 – 52495Fibronectin type-III 2
Domain526 – 61994Fibronectin type-III 3
Domain625 – 732108Fibronectin type-III 4
Motif415 – 4195WSXWS motif
Motif770 – 7789Box 1 motif

Amino acid modifications

Modified residue8261Phosphoserine Ref.5
Modified residue8371Phosphotyrosine Ref.4
Modified residue8891Phosphoserine Ref.5
Glycosylation1631N-linked (GlcNAc...) Potential
Glycosylation3261N-linked (GlcNAc...) Potential
Glycosylation3801N-linked (GlcNAc...) Potential
Glycosylation4461N-linked (GlcNAc...) Potential
Glycosylation5801N-linked (GlcNAc...) Potential
Disulfide bond245 ↔ 255 By similarity

Natural variations

Alternative sequence216 – 979764Missing in isoform 3.
VSP_021529
Alternative sequence331 – 34212VYLMN…SVNFE → GETRVVTAHRGH in isoform 2.
VSP_021527
Alternative sequence343 – 979637Missing in isoform 2.
VSP_021528
Natural variant1871H → Q: dbSNP rs34675408.
VAR_043512
Natural variant2101G → W: dbSNP rs17855841. Ref.2
VAR_028972
Natural variant5271E → K: dbSNP rs10941412.
VAR_028973
Natural variant5531D → N: dbSNP rs2278329.
VAR_028974
Natural variant6181G → A in AMYL9. Ref.6
VAR_043513
Natural variant6911I → T in AMYL9. Ref.6
VAR_043514
Natural variant9361P → S: dbSNP rs3749737.
VAR_028975
Natural variant9591P → R: dbSNP rs34080825.
VAR_043515

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 179852CA3D90D9EF

FASTA979110,509
        10         20         30         40         50         60 
MALFAVFQTT FFLTLLSLRT YQSEVLAERL PLTPVSLKVS TNSTRQSLHL QWTVHNLPYH 

        70         80         90        100        110        120 
QELKMVFQIQ ISRIETSNVI WVGNYSTTVK WNQVLHWSWE SELPLECATH FVRIKSLVDD 

       130        140        150        160        170        180 
AKFPEPNFWS NWSSWEEVSV QDSTGQDILF VFPKDKLVEE GTNVTICYVS RNIQNNVSCY 

       190        200        210        220        230        240 
LEGKQIHGEQ LDPHVTAFNL NSVPFIRNKG TNIYCEASQG NVSEGMKGIV LFVSKVLEEP 

       250        260        270        280        290        300 
KDFSCETEDF KTLHCTWDPG TDTALGWSKQ PSQSYTLFES FSGEKKLCTH KNWCNWQITQ 

       310        320        330        340        350        360 
DSQETYNFTL IAENYLRKRS VNILFNLTHR VYLMNPFSVN FENVNATNAI MTWKVHSIRN 

       370        380        390        400        410        420 
NFTYLCQIEL HGEGKMMQYN VSIKVNGEYF LSELEPATEY MARVRCADAS HFWKWSEWSG 

       430        440        450        460        470        480 
QNFTTLEAAP SEAPDVWRIV SLEPGNHTVT LFWKPLSKLH ANGKILFYNV VVENLDKPSS 

       490        500        510        520        530        540 
SELHSIPAPA NSTKLILDRC SYQICVIANN SVGASPASVI VISADPENKE VEEERIAGTE 

       550        560        570        580        590        600 
GGFSLSWKPQ PGDVIGYVVD WCDHTQDVLG DFQWKNVGPN TTSTVISTDA FRPGVRYDFR 

       610        620        630        640        650        660 
IYGLSTKRIA CLLEKKTGYS QELAPSDNPH VLVDTLTSHS FTLSWKDYST ESQPGFIQGY 

       670        680        690        700        710        720 
HVYLKSKARQ CHPRFEKAVL SDGSECCKYK IDNPEEKALI VDNLKPESFY EFFITPFTSA 

       730        740        750        760        770        780 
GEGPSATFTK VTTPDEHSSM LIHILLPMVF CVLLIMVMCY LKSQWIKETC YPDIPDPYKS 

       790        800        810        820        830        840 
SILSLIKFKE NPHLIIMNVS DCIPDAIEVV SKPEGTKIQF LGTRKSLTET ELTKPNYLYL 

       850        860        870        880        890        900 
LPTEKNHSGP GPCICFENLT YNQAASDSGS CGHVPVSPKA PSMLGLMTSP ENVLKALEKN 

       910        920        930        940        950        960 
YMNSLGEIPA GETSLNYVSQ LASPMFGDKD SLPTNPVEAP HCSEYKMQMA VSLRLALPPP 

       970 
TENSSLSSIT LLDPGEHYC 

« Hide

Isoform 2.

Checksum: 85C6A38D7B8CC73C
Show »

FASTA34239,504
Isoform 3.

Checksum: 3FA9A70B4E84A5FD
Show »

FASTA21524,929

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, INDUCTION, TISSUE SPECIFICITY.
[2]"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] (ISOFORMS 1; 2 AND 3), VARIANT TRP-210.
Tissue: Colon and Placenta.
[3]"Interleukin 31, a cytokine produced by activated T cells, induces dermatitis in mice."
Dillon S.R., Sprecher C., Hammond A., Bilsborough J., Rosenfeld-Franklin M., Presnell S.R., Haugen H.S., Maurer M., Harder B., Johnston J., Bort S., Mudri S., Kuijper J.L., Bukowski T., Shea P., Dong D.L., Dasovich M., Grant F.J. expand/collapse author list , Lockwood L., Levin S.D., LeCiel C., Waggie K., Day H., Topouzis S., Kramer J., Kuestner R., Chen Z., Foster D., Parrish-Novak J., Gross J.A.
Nat. Immunol. 5:752-760(2004) [PubMed: 15184896] [Abstract]
Cited for: FUNCTION, OLIGOMERIZATION, INDUCTION.
[4]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-837, MASS SPECTROMETRY.
[5]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-826 AND SER-889, MASS SPECTROMETRY.
[6]"Oncostatin M receptor-beta mutations underlie familial primary localized cutaneous amyloidosis."
Arita K., South A.P., Hans-Filho G., Sakuma T.H., Lai-Cheong J., Clements S., Odashiro M., Odashiro D.N., Hans-Neto G., Hans N.R., Holder M.V., Bhogal B.S., Hartshorne S.T., Akiyama M., Shimizu H., McGrath J.A.
Am. J. Hum. Genet. 82:73-80(2008) [PubMed: 18179886] [Abstract]
Cited for: VARIANTS AMYL9 ALA-618 AND THR-691.
+Additional computationally mapped references.

Cross-references

Sequence databases

U60805 mRNA. Translation: AAC50946.1.
BC010943 mRNA. Translation: AAH10943.1.
BC063468 mRNA. Translation: AAH63468.1.
BC125209 mRNA. Translation: AAI25210.1.
BC125210 mRNA. Translation: AAI25211.1.
IPIIPI00022674.
IPI00807654.
IPI00807681.
RefSeqNP_003990.1.
UniGeneHs.120658

3D structure databases

ModBaseSearch...

PTM databases

PhosphoSiteQ99650.

Proteomic databases

PRIDEQ99650.

Genome annotation databases

EnsemblENSG00000145623. Homo sapiens. [Contig view]
GeneID9180.
KEGGhsa:9180.

Organism-specific databases

GeneCardsGC05P038881.
HGNCHGNC:8507. OSMR.
HPAHPA017278.
MIM105250. phenotype.
601743. gene.
Orphanet137807. Cutaneous amyloidosis.
PharmGKBPA32837.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ99650.
OMAQ99650. SFTLSWK.

Gene expression databases

ArrayExpressQ99650.
BgeeQ99650.
CleanExHS_OSMR.
GermOnlineENSG00000145623. Homo sapiens.

Family and domain databases

InterProIPR008957. Fibronectin_typ-III-like_fold.
IPR003961. FN_III.
IPR003529. Hematopoietin_rcpt_gp130_CS.
[Graphical view]
Gene3DG3DSA:2.60.40.30. FN_III-like. 2 hits.
PfamPF00041. fn3. 2 hits.
[Graphical view]
SMARTSM00060. FN3. 4 hits.
[Graphical view]
PROSITEPS50853. FN3. 4 hits.
PS01353. HEMATOPO_REC_L_F2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio34417.
SOURCESearch...

Entry information

Entry nameOSMR_HUMAN
AccessionPrimary (citable) accession number: Q99650
Secondary accession number(s): Q6P4E8, Q96QJ6
Entry history
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: May 1, 1997
Last modified: June 16, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents