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Q13261 (I15RA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interleukin-15 receptor subunit alpha

Short name=IL-15 receptor subunit alpha
Short name=IL-15R-alpha
Short name=IL-15RA
Alternative name(s):
CD_antigen=CD215

Cleaved into the following chain:

  1. Soluble interleukin-15 receptor subunit alpha
    Short name=sIL-15 receptor subunit alpha
    Short name=sIL-15R-alpha
    Short name=sIL-15RA
Gene names
Name:IL15RA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length267 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

High-affinity receptor for interleukin-15. Can signal both in cis and trans where IL15R from one subset of cells presents IL15 to neighboring IL2RG-expressing cells. Expression of different isoforms may alter or interfere with signal transduction. Isoform 5, isoform 6, isoform 7 and isoform 8 do not bind IL15. Signal transduction involves SYK. Ref.1 Ref.10

Subunit structure

The interleukin-15 receptor IL15R is a heterotrimer of IL15RA, IL2RB and IL2RG. IL15RA also self-associates By similarity. Interacts with SYK. Ref.10

Subcellular location

Membrane; Single-pass type I membrane protein. Nucleus membrane; Single-pass type I membrane protein. Note: Mainly found associated with the nuclear membrane. Ref.9

Isoform 5: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Cytoplasmic vesicle membrane; Single-pass type I membrane protein. Membrane; Single-pass type I membrane protein. Note: Isoform 5, isoform 6, isoform 7 and isoform 8 are associated with endoplasmic reticulum, Golgi and cytoplasmic vesicles, but not with the nuclear membrane. Ref.9

Isoform 6: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Cytoplasmic vesicle membrane; Single-pass type I membrane protein. Membrane; Single-pass type I membrane protein. Note: Isoform 5, isoform 6, isoform 7 and isoform 8 are associated with endoplasmic reticulum, Golgi and cytoplasmic vesicles, but not with the nuclear membrane. Ref.9

Isoform 7: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Cytoplasmic vesicle membrane; Single-pass type I membrane protein. Membrane; Single-pass type I membrane protein. Note: Isoform 5, isoform 6, isoform 7 and isoform 8 are associated with endoplasmic reticulum, Golgi and cytoplasmic vesicles, but not with the nuclear membrane. Ref.9

Isoform 8: Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus membrane; Single-pass type I membrane protein. Cytoplasmic vesicle membrane; Single-pass type I membrane protein. Membrane; Single-pass type I membrane protein. Note: Isoform 5, isoform 6, isoform 7 and isoform 8 are associated with endoplasmic reticulum, Golgi and cytoplasmic vesicles, but not with the nuclear membrane. Ref.9

Soluble interleukin-15 receptor subunit alpha: Secretedextracellular space Ref.9.

Tissue specificity

Isoform 1, isoform 3, isoform 4, isoform 5, isoform 6, isoform 7, isoform 8 and isoform 9are widely expressed. Expressed in fetal brain with higher expression in the hippocampus and cerebellum than in cortex and thalamus. Higher levels of soluble sIL-15RA form in comparison with membrane-bound forms is present in all brain structures. Ref.1 Ref.9 Ref.11

Post-translational modification

A soluble form (sIL-15RA) arises from proteolytic shedding of the membrane-anchored receptor. The cleavage involves ADAM17/TACE By similarity. It also binds IL-15 and thus interferes with IL-15 binding to the membrane receptor.

Phosphorylated by activated SYK. Ref.10

N-glycosylated and O-glycosylated. Ref.9

Sequence similarities

Contains 1 Sushi (CCP/SCR) domain.

Sequence caution

The sequence AAB88175.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence CAI41080.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence EAW86419.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentCytoplasmic vesicle
Endoplasmic reticulum
Golgi apparatus
Membrane
Nucleus
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
Sushi
Transmembrane
Transmembrane helix
   Molecular functionReceptor
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processJAK-STAT cascade

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Traceable author statement Ref.1. Source: ProtInc

cytokine-mediated signaling pathway

Traceable author statement PubMed 7641685. Source: GOC

negative regulation of neuron projection development

Inferred from electronic annotation. Source: Ensembl

positive regulation of natural killer cell differentiation

Inferred from electronic annotation. Source: Ensembl

response to nutrient levels

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasmic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular space

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

nuclear membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncytokine receptor activity

Traceable author statement PubMed 7641685. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 16284400. Source: IntAct

signal transducer activity

Traceable author statement PubMed 7641685Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

IL15P409333EBI-980354,EBI-980274

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13261-1)

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: Q13261-3)

Also known as: delta3E1E7Il-15RA;

The sequence of this isoform differs from the canonical sequence as follows:
     95-128: RDPALVHQRPAPPSTVTTAGVTPQPESLSPSGKE → K
Isoform 3 (identifier: Q13261-4)

Also known as: E1E7'Il-15RA;

The sequence of this isoform differs from the canonical sequence as follows:
     232-267: QTPPLASVEMEAMEALPVTWGTSSRDEDLENCSHHL → ASVCSCHPRSAGHTCSVGSVC
Isoform 4 (identifier: Q13261-5)

Also known as: delta3E1E7'Il-15RA;

The sequence of this isoform differs from the canonical sequence as follows:
     95-128: RDPALVHQRPAPPSTVTTAGVTPQPESLSPSGKE → K
     232-267: QTPPLASVEMEAMEALPVTWGTSSRDEDLENCSHHL → ASVCSCHPRSAGHTCSVGSVC
Isoform 5 (identifier: Q13261-6)

Also known as: delta2E1E7Il-15RA;

The sequence of this isoform differs from the canonical sequence as follows:
     31-95: Missing.
Isoform 6 (identifier: Q13261-7)

Also known as: delta2E1E7'Il-15RA;

The sequence of this isoform differs from the canonical sequence as follows:
     31-95: Missing.
     232-267: QTPPLASVEMEAMEALPVTWGTSSRDEDLENCSHHL → ASVCSCHPRSAGHTCSVGSVC
Isoform 7 (identifier: Q13261-8)

Also known as: delta2deltaE1E73Il-15RA;

The sequence of this isoform differs from the canonical sequence as follows:
     30-127: Missing.
Isoform 8 (identifier: Q13261-9)

Also known as: delta2delta3E1E7'Il-15RA;

The sequence of this isoform differs from the canonical sequence as follows:
     30-127: Missing.
     232-267: QTPPLASVEMEAMEALPVTWGTSSRDEDLENCSHHL → ASVCSCHPRSAGHTCSVGSVC

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 267237Interleukin-15 receptor subunit alpha
PRO_0000011044
Chain31 – ?Soluble interleukin-15 receptor subunit alphaPRO_0000333855

Regions

Topological domain31 – 205175Extracellular Potential
Transmembrane206 – 22823Helical; Potential
Topological domain229 – 26739Cytoplasmic Potential
Domain31 – 9565Sushi

Amino acid modifications

Glycosylation1371N-linked (GlcNAc...) Potential
Disulfide bond33 ↔ 75 Ref.14 Ref.15
Disulfide bond59 ↔ 93 Ref.14 Ref.15

Natural variations

Alternative sequence30 – 12798Missing in isoform 7 and isoform 8.
VSP_012623
Alternative sequence31 – 9565Missing in isoform 5 and isoform 6.
VSP_012624
Alternative sequence95 – 12834RDPAL…PSGKE → K in isoform 2 and isoform 4.
VSP_012625
Alternative sequence232 – 26736QTPPL…CSHHL → ASVCSCHPRSAGHTCSVGSV C in isoform 3, isoform 4, isoform 6 and isoform 8.
VSP_012626
Natural variant1821N → T. Ref.1 Ref.3
Corresponds to variant rs2228059 [ dbSNP | Ensembl ].
VAR_020967

Experimental info

Mutagenesis2271Y → F: Abrogates association with SYK and phosphorylation upon IL-15 stimulation. Ref.10
Sequence conflict2001G → D in AAH74726. Ref.8

Secondary structure

................. 267
Helix Strand Turn

Details...

Sequences

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

Last modified November 1, 1996. Version 1.
Checksum: A9CFC885189E96BE

FASTA26728,233
        10         20         30         40         50         60 
MAPRRARGCR TLGLPALLLL LLLRPPATRG ITCPPPMSVE HADIWVKSYS LYSRERYICN 

        70         80         90        100        110        120 
SGFKRKAGTS SLTECVLNKA TNVAHWTTPS LKCIRDPALV HQRPAPPSTV TTAGVTPQPE 

       130        140        150        160        170        180 
SLSPSGKEPA ASSPSSNNTA ATTAAIVPGS QLMPSKSPST GTTEISSHES SHGTPSQTTA 

       190        200        210        220        230        240 
KNWELTASAS HQPPGVYPQG HSDTTVAIST STVLLCGLSA VSLLACYLKS RQTPPLASVE 

       250        260 
MEAMEALPVT WGTSSRDEDL ENCSHHL 

« Hide

Isoform 2 (delta3E1E7Il-15RA) [UniParc].

Checksum: 9ACAD3E117A8C9AF
Show »

FASTA23424,870
Isoform 3 (E1E7'Il-15RA) [UniParc].

Checksum: A58933D9E843EDC6
Show »

FASTA25226,299
Isoform 4 (delta3E1E7'Il-15RA) [UniParc].

Checksum: DD564A227CB6AA3F
Show »

FASTA21922,936
Isoform 5 (delta2E1E7Il-15RA) [UniParc].

Checksum: D4F5DD2EA004C6D2
Show »

FASTA20220,904
Isoform 6 (delta2E1E7'Il-15RA) [UniParc].

Checksum: D7A5B6202C329FB0
Show »

FASTA18718,969
Isoform 7 (delta2deltaE1E73Il-15RA) [UniParc].

Checksum: 238A6ECC5B7675A1
Show »

FASTA16917,641
Isoform 8 (delta2delta3E1E7'Il-15RA) [UniParc].

Checksum: 23F224FD25881D2C
Show »

FASTA15415,707

References

« Hide 'large scale' references
[1]"Functional characterization of the human interleukin-15 receptor alpha chain and close linkage of IL15RA and IL2RA genes."
Anderson D.M., Kumaki S., Ahdieh M., Bertles J., Tometsko M., Loomis A., Giri J., Copeland N.G., Gilbert D.J., Jenkins N.A., Valentine V., Shapiro D.N., Morris S.W., Park L.S., Cosman D.
J. Biol. Chem. 270:29862-29869(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), FUNCTION, TISSUE SPECIFICITY, VARIANT THR-182.
Tissue: Bone marrow stroma.
[2]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]SeattleSNPs variation discovery resource
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT THR-182.
[4]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Trachea.
[5]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] (ISOFORM 1).
Tissue: Brain.
[8]"Large-scale concatenation cDNA sequencing."
Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 30-267 (ISOFORM 1).
Tissue: Brain.
[9]"Natural splicing of exon 2 of human interleukin-15 receptor alpha-chain mRNA results in a shortened form with a distinct pattern of expression."
Dubois S., Magrangeas F., Lehours P., Raher S., Bernard J., Boisteau O., Leroy S., Minvielle S., Godard A., Jacques Y.
J. Biol. Chem. 274:26978-26984(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORMS 1; 2; 3; 4; 5; 6; 7 AND 8), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, GLYCOSYLATION.
[10]"The IL-15R alpha chain signals through association with Syk in human B cells."
Bulanova E., Budagian V., Pohl T., Krause H., Durkop H., Paus R., Bulfone-Paus S.
J. Immunol. 167:6292-6302(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SYK, PHOSPHORYLATION BY SYK, MUTAGENESIS OF TYR-227.
[11]"Expression of IL-15 and IL-15 receptor isoforms in select structures of human fetal brain."
Kurowska M., Rudnicka W., Maslinska D., Maslinski W.
Ann. N. Y. Acad. Sci. 966:441-445(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[12]"Identification of an interleukin-15alpha receptor-binding site on human interleukin-15."
Bernard J., Harb C., Mortier E., Quemener A., Meloen R.H., Vermot-Desroches C., Wijdeness J., van Dijken P., Grotzinger J., Slootstra J.W., Plet A., Jacques Y.
J. Biol. Chem. 279:24313-24322(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: LIGAND-BINDING.
[13]"Natural, proteolytic release of a soluble form of human IL-15 receptor alpha-chain that behaves as a specific, high affinity IL-15 antagonist."
Mortier E., Bernard J., Plet A., Jacques Y.
J. Immunol. 173:1681-1688(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING, LIGAND-BINDING.
[14]"The structure of the interleukin-15 alpha receptor and its implications for ligand binding."
Lorenzen I., Dingley A.J., Jacques Y., Grotzinger J.
J. Biol. Chem. 281:6642-6647(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 31-96, DISULFIDE BONDS.
[15]"Crystal structure of the IL-15-IL-15Ralpha complex, a cytokine-receptor unit presented in trans."
Chirifu M., Hayashi C., Nakamura T., Toma S., Shuto T., Kai H., Yamagata Y., Davis S.J., Ikemizu S.
Nat. Immunol. 8:1001-1007(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 31-132 IN COMPLEX WITH IL15, DISULFIDE BONDS.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U31628 mRNA. Translation: AAC50312.1.
CR457064 mRNA. Translation: CAG33345.1.
CR542023 mRNA. Translation: CAG46820.1.
AY316538 Genomic DNA. Translation: AAP69528.1.
AK304211 mRNA. Translation: BAG65084.1.
AL137186 Genomic DNA. Translation: CAI41080.1. Sequence problems.
AL137186 Genomic DNA. Translation: CAI41082.1.
AL137186 Genomic DNA. Translation: CAI41083.1.
CH471072 Genomic DNA. Translation: EAW86417.1.
CH471072 Genomic DNA. Translation: EAW86418.1.
CH471072 Genomic DNA. Translation: EAW86419.1. Sequence problems.
BC074726 mRNA. Translation: AAH74726.1.
BC121140 mRNA. Translation: AAI21141.1.
BC121141 mRNA. Translation: AAI21142.1.
AF035279 mRNA. Translation: AAB88175.1. Different initiation.
CCDSCCDS7074.1. [Q13261-1]
CCDS7075.2. [Q13261-3]
RefSeqNP_001230468.1. NM_001243539.1.
NP_001243694.1. NM_001256765.1.
NP_002180.1. NM_002189.3. [Q13261-1]
NP_751950.2. NM_172200.2. [Q13261-3]
UniGeneHs.445124.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ERSNMR-A31-96[»]
2Z3QX-ray1.85B/D31-132[»]
2Z3RX-ray2.00B/D/F/H/J/L/N/P31-132[»]
4GS7X-ray2.35D30-97[»]
ProteinModelPortalQ13261.
SMRQ13261. Positions 31-108.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109814. 7 interactions.
IntActQ13261. 7 interactions.
STRING9606.ENSP00000369312.

Polymorphism databases

DMDM59799763.

Proteomic databases

PaxDbQ13261.
PRIDEQ13261.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379971; ENSP00000369306; ENSG00000134470. [Q13261-9]
ENST00000379977; ENSP00000369312; ENSG00000134470. [Q13261-1]
ENST00000397248; ENSP00000380421; ENSG00000134470.
ENST00000397250; ENSP00000380422; ENSG00000134470. [Q13261-8]
ENST00000397251; ENSP00000380423; ENSG00000134470. [Q13261-6]
ENST00000397255; ENSP00000380426; ENSG00000134470. [Q13261-4]
ENST00000525219; ENSP00000431529; ENSG00000134470.
ENST00000528354; ENSP00000435454; ENSG00000134470. [Q13261-3]
ENST00000530685; ENSP00000435995; ENSG00000134470. [Q13261-5]
GeneID3601.
KEGGhsa:3601.
UCSCuc001iiv.3. human. [Q13261-1]
uc010qau.2. human. [Q13261-3]
uc021pmp.1. human. [Q13261-8]

Organism-specific databases

CTD3601.
GeneCardsGC10M005991.
H-InvDBHIX0035314.
HGNCHGNC:5978. IL15RA.
HPACAB026215.
MIM601070. gene.
neXtProtNX_Q13261.
PharmGKBPA29791.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41222.
HOVERGENHBG052061.
InParanoidQ13261.
KOK05074.
OMAGSHESSH.
OrthoDBEOG7V767N.
PhylomeDBQ13261.
TreeFamTF338443.

Enzyme and pathway databases

SignaLinkQ13261.

Gene expression databases

ArrayExpressQ13261.
BgeeQ13261.
CleanExHS_IL15RA.
GenevestigatorQ13261.

Family and domain databases

InterProIPR000436. Sushi_SCR_CCP.
[Graphical view]
SMARTSM00032. CCP. 1 hit.
[Graphical view]
SUPFAMSSF57535. SSF57535. 1 hit.
PROSITEPS50923. SUSHI. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ13261.
GeneWikiInterleukin_15_receptor,_alpha_subunit.
GenomeRNAi3601.
NextBio14071.
PMAP-CutDBQ13261.
PROQ13261.
SOURCESearch...

Entry information

Entry nameI15RA_HUMAN
AccessionPrimary (citable) accession number: Q13261
Secondary accession number(s): B4E2C2 expand/collapse secondary AC list , Q5JVA1, Q5JVA2, Q5JVA4, Q6B0J2, Q7LDR4, Q7Z609
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries