Q99650 (OSMR_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 104.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Oncostatin-M-specific receptor subunit beta Alternative name(s): Interleukin-31 receptor subunit beta Short name=IL-31 receptor subunit beta Short name=IL-31R subunit beta Short name=IL-31R-beta Short name=IL-31RB | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Reference proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 979 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 | 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/IFN-gamma and bacterial lipopolysaccharides (LPS). 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 | Amyloidosis, primary localized cutaneous, 1 (PLCA1) [MIM:105250]: A 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 that may be exacerbated by chronic scratching and rubbing. Primary localized cutaneous amyloidosis is often divided into macular and lichen subtypes although many affected individuals often show both variants coexisting. Lichen amyloidosis characteristically presents as a pruritic eruption of grouped hyperkeratotic papules with a predilection for the shins, calves, ankles and dorsa of feet and thighs. Papules may coalesce to form hyperkeratotic plaques that can resemble lichen planus, lichen simplex or nodular prurigo. Macular amyloidosis is characterized by small pigmented macules that may merge to produce macular hyperpigmentation, sometimes with a reticulate or rippled pattern. In macular and lichen amyloidosis, amyloid is deposited in the papillary dermis in association with grouped colloid bodies, thought to represent degenerate basal keratinocytes. The amyloid deposits probably reflect a combination of degenerate keratin filaments, serum amyloid P component, and deposition of immunoglobulins. |
| Sequence similarities | Belongs to the type I cytokine receptor family. Type 2 subfamily. Contains 4 fibronectin type-III domains. |
| Sequence caution | The sequence AAH63468.1 differs from that shown. Reason: Erroneous termination at position 216. Translated as Glu. The sequence AAH63468.1 differs from that shown. Reason: Frameshift at positions 232 and 288. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Membrane |
| Coding sequence diversity | Alternative splicing Polymorphism |
| Disease | Amyloidosis Disease mutation |
| Domain | Repeat Signal Transmembrane Transmembrane helix |
| Molecular function | Receptor |
| PTM | Disulfide bond Glycoprotein Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | cell proliferation Traceable author statement Ref.1. Source: ProtInc positive regulation of acute inflammatory responseInferred by curator Ref.1. Source: BHF-UCL positive regulation of cell proliferationInferred from genetic interaction Ref.1. Source: BHF-UCL |
| Cellular_component | oncostatin-M receptor complex Inferred from direct assay Ref.1. Source: BHF-UCL |
| Molecular_function | oncostatin-M receptor activity Traceable author statement Ref.1. Source: ProtInc |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 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. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 27 | 27 | Potential | ||||||||
| Chain | 28 – 979 | 952 | Oncostatin-M-specific receptor subunit beta | PRO_0000259759 | |||||||
Regions | |||||||||||
| Topological domain | 28 – 740 | 713 | Extracellular Potential | ||||||||
| Transmembrane | 741 – 761 | 21 | Helical; Potential | ||||||||
| Topological domain | 762 – 979 | 218 | Cytoplasmic Potential | ||||||||
| Domain | 332 – 424 | 93 | Fibronectin type-III 1 | ||||||||
| Domain | 430 – 524 | 95 | Fibronectin type-III 2 | ||||||||
| Domain | 526 – 619 | 94 | Fibronectin type-III 3 | ||||||||
| Domain | 625 – 732 | 108 | Fibronectin type-III 4 | ||||||||
| Motif | 415 – 419 | 5 | WSXWS motif | ||||||||
| Motif | 770 – 778 | 9 | Box 1 motif | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 826 | 1 | Phosphoserine Ref.4 | ||||||||
| Modified residue | 889 | 1 | Phosphoserine Ref.4 | ||||||||
| Glycosylation | 163 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 326 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 380 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 446 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 580 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 245 ↔ 255 | By similarity | |||||||||
Natural variations | |||||||||||
| Alternative sequence | 331 – 342 | 12 | VYLMN…SVNFE → GETRVVTAHRGH in isoform 2. | VSP_021527 | |||||||
| Alternative sequence | 343 – 979 | 637 | Missing in isoform 2. | VSP_021528 | |||||||
| Natural variant | 187 | 1 | H → Q. Corresponds to variant rs34675408 [ dbSNP | Ensembl ]. | VAR_043512 | |||||||
| Natural variant | 210 | 1 | G → W. Ref.2 Corresponds to variant rs17855841 [ dbSNP | Ensembl ]. | VAR_028972 | |||||||
| Natural variant | 527 | 1 | E → K. Corresponds to variant rs10941412 [ dbSNP | Ensembl ]. | VAR_028973 | |||||||
| Natural variant | 553 | 1 | D → N. Corresponds to variant rs2278329 [ dbSNP | Ensembl ]. | VAR_028974 | |||||||
| Natural variant | 618 | 1 | G → A in PLCA1. Ref.6 | VAR_043513 | |||||||
| Natural variant | 647 | 1 | D → V in PLCA1. Ref.7 | VAR_065810 | |||||||
| Natural variant | 691 | 1 | I → T in PLCA1. Ref.6 | VAR_043514 | |||||||
| Natural variant | 694 | 1 | P → L in PLCA1. Ref.7 | VAR_065811 | |||||||
| Natural variant | 697 | 1 | K → T in PLCA1. Ref.7 | VAR_065812 | |||||||
| Natural variant | 936 | 1 | P → S. Corresponds to variant rs3749737 [ dbSNP | Ensembl ]. | VAR_028975 | |||||||
| Natural variant | 959 | 1 | P → R. Corresponds to variant rs34080825 [ dbSNP | Ensembl ]. | VAR_043515 | |||||||
Sequences
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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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), 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. Gross J.A.Nat. Immunol. 5:752-760(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, OLIGOMERIZATION, INDUCTION. |
| [4] | "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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-826 AND SER-889, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [5] | "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma. |
| [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] [Europe PMC] [Abstract] Cited for: VARIANTS PLCA1 ALA-618 AND THR-691. |
| [7] | "Novel IL31RA gene mutation and ancestral OSMR mutant allele in familial primary cutaneous amyloidosis." Lin M.W., Lee D.D., Liu T.T., Lin Y.F., Chen S.Y., Huang C.C., Weng H.Y., Liu Y.F., Tanaka A., Arita K., Lai-Cheong J., Palisson F., Chang Y.T., Wong C.K., Matsuura I., McGrath J.A., Tsai S.F. Eur. J. Hum. Genet. 18:26-32(2010) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PLCA1 VAL-647; LEU-694 AND THR-697. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U60805 mRNA. Translation: AAC50946.1. BC010943 mRNA. Translation: AAH10943.1. BC063468 mRNA. Translation: AAH63468.1. Sequence problems. BC125209 mRNA. Translation: AAI25210.1. BC125210 mRNA. Translation: AAI25211.1. |
| IPI | IPI00022674. IPI00807681. |
| RefSeq | NP_001161827.1. NM_001168355.1. NP_003990.1. NM_003999.2. |
| UniGene | Hs.120658. Hs.658389. |
3D structure databases | |
| ProteinModelPortal | Q99650. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q99650. 1 interaction. |
| STRING | 9606.ENSP00000274276. |
PTM databases | |
| PhosphoSite | Q99650. |
Polymorphism databases | |
| DMDM | 74724833. |
Proteomic databases | |
| PaxDb | Q99650. |
| PRIDE | Q99650. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000274276; ENSP00000274276; ENSG00000145623. ENST00000502536; ENSP00000422023; ENSG00000145623. |
| GeneID | 9180. |
| KEGG | hsa:9180. |
| UCSC | uc003jlm.2. human. uc003jln.2. human. |
Organism-specific databases | |
| CTD | 9180. |
| GeneCards | GC05P038845. |
| HGNC | HGNC:8507. OSMR. |
| HPA | HPA017278. |
| MIM | 105250. phenotype. 601743. gene. |
| neXtProt | NX_Q99650. |
| Orphanet | 49804. Lichen amyloidosis. |
| PharmGKB | PA32837. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | NOG43445. |
| HOGENOM | HOG000115294. |
| HOVERGEN | HBG082088. |
| InParanoid | Q99650. |
| KO | K05057. |
| OMA | EPKDFSC. |
| OrthoDB | EOG4FBHS4. |
| PhylomeDB | Q99650. |
Gene expression databases | |
| ArrayExpress | Q99650. |
| Bgee | Q99650. |
| CleanEx | HS_OSMR. |
| Genevestigator | Q99650. |
| GermOnline | ENSG00000145623. Homo sapiens. |
Family and domain databases | |
| Gene3D | 2.60.40.10. 5 hits. |
| InterPro | IPR003961. Fibronectin_type3. IPR003529. Hematopoietin_rcpt_Gp130_CS. IPR013783. Ig-like_fold. [Graphical view] |
| Pfam | PF00041. fn3. 1 hit. [Graphical view] |
| SMART | SM00060. FN3. 4 hits. [Graphical view] |
| SUPFAM | SSF49265. FN_III-like. 5 hits. |
| PROSITE | PS50853. FN3. 4 hits. PS01353. HEMATOPO_REC_L_F2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChiTaRS | OSMR. human. |
| GenomeRNAi | 9180. |
| NextBio | 34417. |
| SOURCE | Search... |
Entry information
| Entry name | OSMR_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q99650 Secondary accession number(s): Q6P4E8, Q96QJ6 | ||||||||
| Entry 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. | ||||||||
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 |

Clusters with
