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Protein

Interleukin-15 receptor subunit alpha

Gene

IL15RA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  • cytokine receptor activity Source: UniProtKB
  • signal transducer activity Source: ProtInc

GO - Biological processi

  • cell proliferation Source: ProtInc
  • cytokine-mediated signaling pathway Source: GOC
  • signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Enzyme and pathway databases

SignaLinkiQ13261.

Names & Taxonomyi

Protein namesi
Recommended 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:
Soluble interleukin-15 receptor subunit alpha
Short name:
sIL-15 receptor subunit alpha
Short name:
sIL-15R-alpha
Short name:
sIL-15RA
Gene namesi
Name:IL15RA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:5978. IL15RA.

Subcellular locationi

Isoform 5 :
Isoform 6 :
Isoform 7 :
Isoform 8 :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini31 – 205175ExtracellularSequence AnalysisAdd
BLAST
Transmembranei206 – 22823HelicalSequence AnalysisAdd
BLAST
Topological domaini229 – 26739CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endoplasmic reticulum, Golgi apparatus, Membrane, Nucleus, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi227 – 2271Y → F: Abrogates association with SYK and phosphorylation upon IL-15 stimulation. 1 Publication

Organism-specific databases

PharmGKBiPA29791.

Polymorphism and mutation databases

BioMutaiIL15RA.
DMDMi59799763.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence AnalysisAdd
BLAST
Chaini31 – 267237Interleukin-15 receptor subunit alphaPRO_0000011044Add
BLAST
Chaini31 – ?Soluble interleukin-15 receptor subunit alphaPRO_0000333855

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi33 ↔ 75
Disulfide bondi59 ↔ 93
Glycosylationi137 – 1371N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

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.By similarity1 Publication
Phosphorylated by activated SYK.1 Publication
N-glycosylated and O-glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ13261.
PaxDbiQ13261.
PRIDEiQ13261.

Miscellaneous databases

PMAP-CutDBQ13261.

Expressioni

Tissue specificityi

Isoform 1, isoform 3, isoform 4, isoform 5, isoform 6, isoform 7, isoform 8 and isoform 9 are 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.3 Publications

Gene expression databases

BgeeiQ13261.
CleanExiHS_IL15RA.
ExpressionAtlasiQ13261. baseline and differential.
GenevestigatoriQ13261.

Organism-specific databases

HPAiCAB026215.

Interactioni

Subunit structurei

The interleukin-15 receptor IL15R is a heterotrimer of IL15RA, IL2RB and IL2RG. IL15RA also self-associates (By similarity). Interacts with SYK.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
IL15P409335EBI-980354,EBI-980274

Protein-protein interaction databases

BioGridi109814. 7 interactions.
IntActiQ13261. 9 interactions.
STRINGi9606.ENSP00000369312.

Structurei

Secondary structure

1
267
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi42 – 443Combined sources
Beta strandi54 – 596Combined sources
Beta strandi63 – 653Combined sources
Beta strandi72 – 776Combined sources
Turni79 – 813Combined sources
Beta strandi84 – 863Combined sources
Beta strandi93 – 953Combined sources
Helixi97 – 1026Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ13261.
SMRiQ13261. Positions 31-108.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13261.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 9565SushiPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 Sushi (CCP/SCR) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal, Sushi, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG41222.
GeneTreeiENSGT00390000000121.
HOGENOMiHOG000036788.
HOVERGENiHBG052061.
InParanoidiQ13261.
KOiK05074.
OMAiGSHESSH.
OrthoDBiEOG7V767N.
PhylomeDBiQ13261.
TreeFamiTF338443.

Family and domain databases

InterProiIPR000436. Sushi_SCR_CCP_dom.
[Graphical view]
SMARTiSM00032. CCP. 1 hit.
[Graphical view]
SUPFAMiSSF57535. SSF57535. 1 hit.
PROSITEiPS50923. SUSHI. 1 hit.
[Graphical view]

Sequences (9)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 9 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q13261-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAPRRARGCR TLGLPALLLL LLLRPPATRG ITCPPPMSVE HADIWVKSYS
60 70 80 90 100
LYSRERYICN SGFKRKAGTS SLTECVLNKA TNVAHWTTPS LKCIRDPALV
110 120 130 140 150
HQRPAPPSTV TTAGVTPQPE SLSPSGKEPA ASSPSSNNTA ATTAAIVPGS
160 170 180 190 200
QLMPSKSPST GTTEISSHES SHGTPSQTTA KNWELTASAS HQPPGVYPQG
210 220 230 240 250
HSDTTVAIST STVLLCGLSA VSLLACYLKS RQTPPLASVE MEAMEALPVT
260
WGTSSRDEDL ENCSHHL
Length:267
Mass (Da):28,233
Last modified:November 1, 1996 - v1
Checksum:iA9CFC885189E96BE
GO
Isoform 2 (identifier: Q13261-3) [UniParc]FASTAAdd to basket

Also known as: delta3E1E7Il-15RA

The sequence of this isoform differs from the canonical sequence as follows:
     95-128: RDPALVHQRPAPPSTVTTAGVTPQPESLSPSGKE → K

Show »
Length:234
Mass (Da):24,870
Checksum:i9ACAD3E117A8C9AF
GO
Isoform 3 (identifier: Q13261-4) [UniParc]FASTAAdd to basket

Also known as: E1E7'Il-15RA

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

Show »
Length:252
Mass (Da):26,299
Checksum:iA58933D9E843EDC6
GO
Isoform 4 (identifier: Q13261-5) [UniParc]FASTAAdd to basket

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

Show »
Length:219
Mass (Da):22,936
Checksum:iDD564A227CB6AA3F
GO
Isoform 5 (identifier: Q13261-6) [UniParc]FASTAAdd to basket

Also known as: delta2E1E7Il-15RA

The sequence of this isoform differs from the canonical sequence as follows:
     31-95: Missing.

Show »
Length:202
Mass (Da):20,904
Checksum:iD4F5DD2EA004C6D2
GO
Isoform 6 (identifier: Q13261-7) [UniParc]FASTAAdd to basket

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

Show »
Length:187
Mass (Da):18,969
Checksum:iD7A5B6202C329FB0
GO
Isoform 7 (identifier: Q13261-8) [UniParc]FASTAAdd to basket

Also known as: delta2deltaE1E73Il-15RA

The sequence of this isoform differs from the canonical sequence as follows:
     30-127: Missing.

Show »
Length:169
Mass (Da):17,641
Checksum:i238A6ECC5B7675A1
GO
Isoform 8 (identifier: Q13261-9) [UniParc]FASTAAdd to basket

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

Show »
Length:154
Mass (Da):15,707
Checksum:i23F224FD25881D2C
GO
Isoform 9 (identifier: Q13261-10) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-36: Missing.

Note: No experimental confirmation available.

Show »
Length:231
Mass (Da):24,388
Checksum:i85A770AB71977219
GO

Sequence cautioni

The sequence AAB88175.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAI41080.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence EAW86419.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti200 – 2001G → D in AAH74726 (PubMed:9110174).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti182 – 1821N → T.3 Publications
Corresponds to variant rs2228059 [ dbSNP | Ensembl ].
VAR_020967

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3636Missing in isoform 9. 1 PublicationVSP_055406Add
BLAST
Alternative sequencei30 – 12798Missing in isoform 7 and isoform 8. CuratedVSP_012623Add
BLAST
Alternative sequencei31 – 9565Missing in isoform 5 and isoform 6. CuratedVSP_012624Add
BLAST
Alternative sequencei95 – 12834RDPAL…PSGKE → K in isoform 2 and isoform 4. 2 PublicationsVSP_012625Add
BLAST
Alternative sequencei232 – 26736QTPPL…CSHHL → ASVCSCHPRSAGHTCSVGSV C in isoform 3, isoform 4, isoform 6 and isoform 8. 1 PublicationVSP_012626Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
BC107777 mRNA. Translation: AAI07778.1.
BC121140 mRNA. Translation: AAI21141.1.
BC121141 mRNA. Translation: AAI21142.1.
AF035279 mRNA. Translation: AAB88175.1. Different initiation.
CCDSiCCDS58069.1. [Q13261-10]
CCDS7074.1. [Q13261-1]
CCDS7075.2. [Q13261-3]
RefSeqiNP_001230468.1. NM_001243539.1. [Q13261-10]
NP_001243694.1. NM_001256765.1.
NP_002180.1. NM_002189.3. [Q13261-1]
NP_751950.2. NM_172200.2. [Q13261-3]
UniGeneiHs.445124.

Genome annotation databases

EnsembliENST00000379971; ENSP00000369306; ENSG00000134470. [Q13261-9]
ENST00000379977; ENSP00000369312; ENSG00000134470. [Q13261-1]
ENST00000397250; ENSP00000380422; ENSG00000134470. [Q13261-8]
ENST00000397255; ENSP00000380426; ENSG00000134470. [Q13261-4]
ENST00000525219; ENSP00000431529; ENSG00000134470. [Q13261-10]
ENST00000528354; ENSP00000435454; ENSG00000134470. [Q13261-3]
ENST00000530685; ENSP00000435995; ENSG00000134470. [Q13261-5]
GeneIDi3601.
KEGGihsa:3601.
UCSCiuc001iiv.3. human. [Q13261-1]
uc010qau.2. human. [Q13261-3]
uc021pmp.1. human. [Q13261-8]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
BC107777 mRNA. Translation: AAI07778.1.
BC121140 mRNA. Translation: AAI21141.1.
BC121141 mRNA. Translation: AAI21142.1.
AF035279 mRNA. Translation: AAB88175.1. Different initiation.
CCDSiCCDS58069.1. [Q13261-10]
CCDS7074.1. [Q13261-1]
CCDS7075.2. [Q13261-3]
RefSeqiNP_001230468.1. NM_001243539.1. [Q13261-10]
NP_001243694.1. NM_001256765.1.
NP_002180.1. NM_002189.3. [Q13261-1]
NP_751950.2. NM_172200.2. [Q13261-3]
UniGeneiHs.445124.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ13261.
SMRiQ13261. Positions 31-108.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109814. 7 interactions.
IntActiQ13261. 9 interactions.
STRINGi9606.ENSP00000369312.

Polymorphism and mutation databases

BioMutaiIL15RA.
DMDMi59799763.

Proteomic databases

MaxQBiQ13261.
PaxDbiQ13261.
PRIDEiQ13261.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379971; ENSP00000369306; ENSG00000134470. [Q13261-9]
ENST00000379977; ENSP00000369312; ENSG00000134470. [Q13261-1]
ENST00000397250; ENSP00000380422; ENSG00000134470. [Q13261-8]
ENST00000397255; ENSP00000380426; ENSG00000134470. [Q13261-4]
ENST00000525219; ENSP00000431529; ENSG00000134470. [Q13261-10]
ENST00000528354; ENSP00000435454; ENSG00000134470. [Q13261-3]
ENST00000530685; ENSP00000435995; ENSG00000134470. [Q13261-5]
GeneIDi3601.
KEGGihsa:3601.
UCSCiuc001iiv.3. human. [Q13261-1]
uc010qau.2. human. [Q13261-3]
uc021pmp.1. human. [Q13261-8]

Organism-specific databases

CTDi3601.
GeneCardsiGC10M005991.
H-InvDBHIX0035314.
HGNCiHGNC:5978. IL15RA.
HPAiCAB026215.
MIMi601070. gene.
neXtProtiNX_Q13261.
PharmGKBiPA29791.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG41222.
GeneTreeiENSGT00390000000121.
HOGENOMiHOG000036788.
HOVERGENiHBG052061.
InParanoidiQ13261.
KOiK05074.
OMAiGSHESSH.
OrthoDBiEOG7V767N.
PhylomeDBiQ13261.
TreeFamiTF338443.

Enzyme and pathway databases

SignaLinkiQ13261.

Miscellaneous databases

EvolutionaryTraceiQ13261.
GeneWikiiInterleukin_15_receptor,_alpha_subunit.
GenomeRNAii3601.
NextBioi14071.
PMAP-CutDBQ13261.
PROiQ13261.
SOURCEiSearch...

Gene expression databases

BgeeiQ13261.
CleanExiHS_IL15RA.
ExpressionAtlasiQ13261. baseline and differential.
GenevestigatoriQ13261.

Family and domain databases

InterProiIPR000436. Sushi_SCR_CCP_dom.
[Graphical view]
SMARTiSM00032. CCP. 1 hit.
[Graphical view]
SUPFAMiSSF57535. SSF57535. 1 hit.
PROSITEiPS50923. SUSHI. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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] (ISOFORMS 1 AND 9), VARIANT THR-182.
    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. 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.

Entry informationi

Entry nameiI15RA_HUMAN
AccessioniPrimary (citable) accession number: Q13261
Secondary accession number(s): B4E2C2
, Q3B769, Q5JVA1, Q5JVA2, Q5JVA4, Q6B0J2, Q7LDR4, Q7Z609
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: November 1, 1996
Last modified: May 27, 2015
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.