Q13261 (I15RA_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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:

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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	267 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	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 STAT3, STAT5, STAT6, JAK2 By similarity and 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: Secreted › extracellular space Ref.9.
Tissue specificity	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. 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 component	Cytoplasmic vesicle Endoplasmic reticulum Golgi apparatus Membrane Nucleus Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal Sushi Transmembrane Transmembrane helix
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell proliferation Traceable author statement. Source: ProtInc
Cellular component	Golgi 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 to membrane Inferred from electronic annotation. Source: UniProtKB-KW nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cytokine receptor activity Traceable author statement. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
IL15	P40933	3	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 30

30

Potential

Chain

31 – 267

237

Interleukin-15 receptor subunit alpha

PRO_0000011044

Chain

31 – ?

Soluble interleukin-15 receptor subunit alpha

PRO_0000333855

Regions

Topological domain

31 – 205

175

Extracellular Potential

Transmembrane

206 – 228

23

Helical; Potential

Topological domain

229 – 267

39

Cytoplasmic Potential

Domain

31 – 95

65

Sushi

Amino acid modifications

Glycosylation

137

1

N-linked (GlcNAc...) Potential

Disulfide bond

33 ↔ 75

Ref.14 Ref.15

Disulfide bond

59 ↔ 93

Ref.14 Ref.15

Natural variations

Alternative sequence

30 – 127

98

Missing in isoform 7 and isoform 8.

VSP_012623

Alternative sequence

31 – 95

65

Missing in isoform 5 and isoform 6.

VSP_012624

Alternative sequence

95 – 128

34

RDPAL…PSGKE → K in isoform 2 and isoform 4.

VSP_012625

Alternative sequence

232 – 267

36

QTPPL…CSHHL → ASVCSCHPRSAGHTCSVGSV C in isoform 3, isoform 4, isoform 6 and isoform 8.

VSP_012626

Natural variant

182

1

N → T. Ref.1 Ref.3
Corresponds to variant rs2228059 [ dbSNP | Ensembl ].

VAR_020967

Experimental info

Mutagenesis

227

1

Y → F: Abrogates association with SYK and phosphorylation upon IL-15 stimulation. Ref.10

Sequence conflict

200

1

G → D in AAH74726. Ref.8

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

267

Helix Strand Turn

Details...

Beta strand

42 – 44

3

Beta strand

54 – 59

6

Beta strand

63 – 65

3

Beta strand

72 – 77

6

Turn

79 – 81

3

Beta strand

84 – 86

3

Beta strand

93 – 95

3

Helix

97 – 102

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: A9CFC885189E96BE	FASTA	267	28,233
	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
	Isoform 2 (delta3E1E7Il-15RA) [UniParc]. Checksum: 9ACAD3E117A8C9AF	FASTA	234	24,870
	10 20 30 40 50 60 MAPRRARGCR TLGLPALLLL LLLRPPATRG ITCPPPMSVE HADIWVKSYS LYSRERYICN 70 80 90 100 110 120 SGFKRKAGTS SLTECVLNKA TNVAHWTTPS LKCIKPAASS PSSNNTAATT AAIVPGSQLM 130 140 150 160 170 180 PSKSPSTGTT EISSHESSHG TPSQTTAKNW ELTASASHQP PGVYPQGHSD TTVAISTSTV 190 200 210 220 230 LLCGLSAVSL LACYLKSRQT PPLASVEMEA MEALPVTWGT SSRDEDLENC SHHL
	Isoform 3 (E1E7'Il-15RA) [UniParc]. Checksum: A58933D9E843EDC6	FASTA	252	26,299
	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 RASVCSCHPR 250 SAGHTCSVGS VC
	Isoform 4 (delta3E1E7'Il-15RA) [UniParc]. Checksum: DD564A227CB6AA3F	FASTA	219	22,936
	10 20 30 40 50 60 MAPRRARGCR TLGLPALLLL LLLRPPATRG ITCPPPMSVE HADIWVKSYS LYSRERYICN 70 80 90 100 110 120 SGFKRKAGTS SLTECVLNKA TNVAHWTTPS LKCIKPAASS PSSNNTAATT AAIVPGSQLM 130 140 150 160 170 180 PSKSPSTGTT EISSHESSHG TPSQTTAKNW ELTASASHQP PGVYPQGHSD TTVAISTSTV 190 200 210 LLCGLSAVSL LACYLKSRAS VCSCHPRSAG HTCSVGSVC
	Isoform 5 (delta2E1E7Il-15RA) [UniParc]. Checksum: D4F5DD2EA004C6D2	FASTA	202	20,904
	10 20 30 40 50 60 MAPRRARGCR TLGLPALLLL LLLRPPATRG DPALVHQRPA PPSTVTTAGV TPQPESLSPS 70 80 90 100 110 120 GKEPAASSPS SNNTAATTAA IVPGSQLMPS KSPSTGTTEI SSHESSHGTP SQTTAKNWEL 130 140 150 160 170 180 TASASHQPPG VYPQGHSDTT VAISTSTVLL CGLSAVSLLA CYLKSRQTPP LASVEMEAME 190 200 ALPVTWGTSS RDEDLENCSH HL
	Isoform 6 (delta2E1E7'Il-15RA) [UniParc]. Checksum: D7A5B6202C329FB0	FASTA	187	18,969
	10 20 30 40 50 60 MAPRRARGCR TLGLPALLLL LLLRPPATRG DPALVHQRPA PPSTVTTAGV TPQPESLSPS 70 80 90 100 110 120 GKEPAASSPS SNNTAATTAA IVPGSQLMPS KSPSTGTTEI SSHESSHGTP SQTTAKNWEL 130 140 150 160 170 180 TASASHQPPG VYPQGHSDTT VAISTSTVLL CGLSAVSLLA CYLKSRASVC SCHPRSAGHT CSVGSVC
	Isoform 7 (delta2deltaE1E73Il-15RA) [UniParc]. Checksum: 238A6ECC5B7675A1	FASTA	169	17,641
	10 20 30 40 50 60 MAPRRARGCR TLGLPALLLL LLLRPPATRE PAASSPSSNN TAATTAAIVP GSQLMPSKSP 70 80 90 100 110 120 STGTTEISSH ESSHGTPSQT TAKNWELTAS ASHQPPGVYP QGHSDTTVAI STSTVLLCGL 130 140 150 160 SAVSLLACYL KSRQTPPLAS VEMEAMEALP VTWGTSSRDE DLENCSHHL
	Isoform 8 (delta2delta3E1E7'Il-15RA) [UniParc]. Checksum: 23F224FD25881D2C	FASTA	154	15,707
	10 20 30 40 50 60 MAPRRARGCR TLGLPALLLL LLLRPPATRE PAASSPSSNN TAATTAAIVP GSQLMPSKSP 70 80 90 100 110 120 STGTTEISSH ESSHGTPSQT TAKNWELTAS ASHQPPGVYP QGHSDTTVAI STSTVLLCGL 130 140 150 SAVSLLACYL KSRASVCSCH PRSAGHTCSV GSVC

References

	« Hide 'large scale' referencesShow '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: 8530383] [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: 14702039] [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: 15164054] [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. , 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: 15489334] [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: 9110174] [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: 10480910] [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: 11714793] [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: 12114302] [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: 15039446] [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: 15265897] [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: 16377614] [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: 17643103] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 31-132 IN COMPLEX WITH IL15, DISULFIDE BONDS.
+	Additional computationally mapped references.

Web resources

SeattleSNPs

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.
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.

IPI

IPI00031807.
IPI00549208.
IPI00549663.
IPI00550381.
IPI00550582.
IPI00550778.
IPI00550789.
IPI00551001.

RefSeq

NP_001230468.1. NM_001243539.1.
NP_002180.1. NM_002189.3.
NP_751950.2. NM_172200.2.

UniGene

Hs.524117.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2ERS	NMR	-	A	31-96	[»]
2Z3Q	X-ray	1.85	B/D	31-132	[»]
2Z3R	X-ray	2.00	B/D/F/H/J/L/N/P	31-132	[»]

ProteinModelPortal

Q13261.

SMR

Q13261. Positions 31-108.

ModBase

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Protein-protein interaction databases

IntAct

Q13261. 7 interactions.

STRING

Q13261.

Polymorphism databases

DMDM

59799763.

Proteomic databases

PRIDE

Q13261.

Protocols and materials databases

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000379977; ENSP00000369312; ENSG00000134470.

GeneID

3601.

KEGG

hsa:3601.

UCSC

uc001iiv.1. human.

Organism-specific databases

CTD

3601.

GeneCards

GC10M005991.

HGNC

HGNC:5978. IL15RA.

HPA

CAB026215.

MIM

601070. gene.

neXtProt

NX_Q13261.

PharmGKB

PA29791.

GenAtlas

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Phylogenomic databases

eggNOG

prNOG14196.

HOGENOM

HBG125999.

HOVERGEN

HBG052061.

InParanoid

Q13261.

OMA

DLENCSH.

PhylomeDB

Q13261.

Gene expression databases

ArrayExpress

Q13261.

Bgee

Q13261.

CleanEx

HS_IL15RA.

Genevestigator

Q13261.

GermOnline

ENSG00000134470. Homo sapiens.

Family and domain databases

InterPro

IPR016060. Complement_control_module.
IPR000436. Sushi_SCR_CCP.
[Graphical view]

Gene3D

G3DSA:2.10.70.10. Complement_control_module. 1 hit.

KO

K05074.

SMART

SM00032. CCP. 1 hit.
[Graphical view]

SUPFAM

SSF57535. Complement_control_module. 1 hit.

PROSITE

PS50923. SUSHI. 1 hit.
[Graphical view]

ProtoNet

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Other

NextBio

14071.

PMAP-CutDB

Q13261.

SOURCE

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Entry information

Entry name

I15RA_HUMAN

Accession

Primary (citable) accession number: Q13261
Secondary accession number(s): B4E2C2 , Q5JVA2, Q5JVA4, Q6B0J2, Q7LDR4, Q7Z609

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2005
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 104 of the entry and version 1 of the sequence. [Complete 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.