Entity Details

Primary name IL31R_HUMAN
Entity type UniProt
Source Source Link

Details

AccessionQ8NI17
EntryNameIL31R_HUMAN
FullNameInterleukin-31 receptor subunit alpha
TaxID9606
Evidenceevidence at protein level
Length732
SequenceStatuscomplete
DateCreated2007-02-06
DateModified2021-06-02

Ontological Relatives

GenesIL31RA

GO terms

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GOName
GO:0000165 MAPK cascade
GO:0002067 glandular epithelial cell differentiation
GO:0002438 acute inflammatory response to antigenic stimulus
GO:0003713 transcription coactivator activity
GO:0004896 cytokine receptor activity
GO:0005886 plasma membrane
GO:0006952 defense response
GO:0007169 transmembrane receptor protein tyrosine kinase signaling pathway
GO:0007259 receptor signaling pathway via JAK-STAT
GO:0008284 positive regulation of cell population proliferation
GO:0009897 external side of plasma membrane
GO:0016021 integral component of membrane
GO:0019221 cytokine-mediated signaling pathway
GO:0019901 protein kinase binding
GO:0019955 cytokine binding
GO:0030224 monocyte differentiation
GO:0030225 macrophage differentiation
GO:0030424 axon
GO:0042531 positive regulation of tyrosine phosphorylation of STAT protein
GO:0042592 homeostatic process
GO:0042734 presynaptic membrane
GO:0043031 negative regulation of macrophage activation
GO:0043066 negative regulation of apoptotic process
GO:0043235 receptor complex
GO:0045893 positive regulation of transcription, DNA-templated
GO:0051916 granulocyte colony-stimulating factor binding
GO:0098542 defense response to other organism

Subcellular Location

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Subcellular Location
Cell junction
Cell membrane
Cell projection

Domains

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DomainNameCategoryType
IPR003961 Fibronectin type IIIDomainDomain
IPR013783 Immunoglobulin-like foldFamilyHomologous superfamily
IPR015321 Type I cytokine receptor, cytokine-binding domainDomainDomain
IPR036116 Fibronectin type III superfamilyFamilyHomologous superfamily

Diseases

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Disease IDSourceNameDescription
613955 OMIMAmyloidosis, primary localized cutaneous, 2 (PLCA2)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. The disease is caused by variants affecting the gene represented in this entry.

Interactions

3 interactions