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P26951

- IL3RA_HUMAN

UniProt

P26951 - IL3RA_HUMAN

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Protein

Interleukin-3 receptor subunit alpha

Gene

IL3RA

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

Functioni

This is a receptor for interleukin-3.

GO - Molecular functioni

  1. interleukin-3 receptor activity Source: ProtInc

GO - Biological processi

  1. cellular response to interleukin-3 Source: GOC
  2. interleukin-3-mediated signaling pathway Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Enzyme and pathway databases

ReactomeiREACT_1695. GPVI-mediated activation cascade.
REACT_19290. G beta:gamma signalling through PI3Kgamma.
REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
REACT_23891. Interleukin receptor SHC signaling.
SignaLinkiP26951.

Names & Taxonomyi

Protein namesi
Recommended name:
Interleukin-3 receptor subunit alpha
Short name:
IL-3 receptor subunit alpha
Short name:
IL-3R subunit alpha
Short name:
IL-3R-alpha
Short name:
IL-3RA
Alternative name(s):
CD_antigen: CD123
Gene namesi
Name:IL3RA
Synonyms:IL3R
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:6012. IL3RA.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 305287ExtracellularSequence AnalysisAdd
BLAST
Transmembranei306 – 32520HelicalSequence AnalysisAdd
BLAST
Topological domaini326 – 37853CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29831.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 378360Interleukin-3 receptor subunit alphaPRO_0000010883Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi46 – 461N-linked (GlcNAc...)Sequence Analysis
Glycosylationi64 – 641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi80 – 801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi109 – 1091N-linked (GlcNAc...)Sequence Analysis
Glycosylationi212 – 2121N-linked (GlcNAc...)Sequence Analysis
Glycosylationi218 – 2181N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiP26951.
PRIDEiP26951.

PTM databases

PhosphoSiteiP26951.

Expressioni

Gene expression databases

BgeeiP26951.
CleanExiHS_IL3RA.
ExpressionAtlasiP26951. baseline and differential.
GenevestigatoriP26951.

Organism-specific databases

HPAiCAB018374.
HPA003539.

Interactioni

Subunit structurei

Heterodimer of an alpha and a beta subunit. The beta subunit is common to the IL3, IL5 and GM-CSF receptors.

Protein-protein interaction databases

BioGridi109778. 11 interactions.
DIPiDIP-3293N.
IntActiP26951. 12 interactions.
MINTiMINT-7241956.
STRINGi9606.ENSP00000327890.

Structurei

Secondary structure

1
378
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi26 – 338Combined sources
Turni34 – 374Combined sources
Beta strandi38 – 458Combined sources
Beta strandi50 – 545Combined sources
Turni55 – 573Combined sources
Beta strandi58 – 614Combined sources
Turni64 – 663Combined sources
Beta strandi67 – 693Combined sources
Beta strandi75 – 773Combined sources
Beta strandi79 – 857Combined sources
Turni86 – 894Combined sources
Beta strandi90 – 978Combined sources
Beta strandi106 – 11510Combined sources
Turni116 – 1183Combined sources
Beta strandi119 – 1268Combined sources
Beta strandi135 – 1428Combined sources
Turni143 – 1453Combined sources
Beta strandi147 – 1504Combined sources
Beta strandi153 – 1564Combined sources
Beta strandi162 – 1687Combined sources
Helixi170 – 1734Combined sources
Turni174 – 1763Combined sources
Beta strandi178 – 18710Combined sources
Beta strandi189 – 1913Combined sources
Beta strandi196 – 2016Combined sources
Helixi202 – 2054Combined sources
Beta strandi212 – 2143Combined sources
Beta strandi223 – 2275Combined sources
Beta strandi236 – 2427Combined sources
Beta strandi250 – 2567Combined sources
Beta strandi258 – 2614Combined sources
Beta strandi270 – 2767Combined sources
Turni277 – 2793Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4JZJX-ray2.80C/D20-307[»]
ProteinModelPortaliP26951.
SMRiP26951. Positions 25-291.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi282 – 2865WSXWS motif
Motifi334 – 3429Box 1 motif

Domaini

The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding.
The box 1 motif is required for JAK interaction and/or activation.

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG44788.
GeneTreeiENSGT00520000055993.
HOGENOMiHOG000201004.
HOVERGENiHBG107484.
InParanoidiP26951.
KOiK04737.
OMAiKNLRMEP.
OrthoDBiEOG7TJ3J7.
PhylomeDBiP26951.
TreeFamiTF331549.

Family and domain databases

Gene3Di2.60.40.10. 2 hits.
InterProiIPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR015321. IL-6_rcpt_alpha-bd.
IPR003532. Short_hematopoietin_rcpt_2_CS.
[Graphical view]
PfamiPF09240. IL6Ra-bind. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 2 hits.
PROSITEiPS01356. HEMATOPO_REC_S_F2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P26951-1) [UniParc]FASTAAdd to Basket

Also known as: SP1

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
MVLLWLTLLL IALPCLLQTK EDPNPPITNL RMKAKAQQLT WDLNRNVTDI
60 70 80 90 100
ECVKDADYSM PAVNNSYCQF GAISLCEVTN YTVRVANPPF STWILFPENS
110 120 130 140 150
GKPWAGAENL TCWIHDVDFL SCSWAVGPGA PADVQYDLYL NVANRRQQYE
160 170 180 190 200
CLHYKTDAQG TRIGCRFDDI SRLSSGSQSS HILVRGRSAA FGIPCTDKFV
210 220 230 240 250
VFSQIEILTP PNMTAKCNKT HSFMHWKMRS HFNRKFRYEL QIQKRMQPVI
260 270 280 290 300
TEQVRDRTSF QLLNPGTYTV QIRARERVYE FLSAWSTPQR FECDQEEGAN
310 320 330 340 350
TRAWRTSLLI ALGTLLALVC VFVICRRYLV MQRLFPRIPH MKDPIGDSFQ
360 370
NDKLVVWEAG KAGLEECLVT EVQVVQKT
Length:378
Mass (Da):43,330
Last modified:October 1, 1993 - v1
Checksum:i716CE1803F2E5FC0
GO
Isoform 2 (identifier: P26951-2) [UniParc]FASTAAdd to Basket

Also known as: SP2

The sequence of this isoform differs from the canonical sequence as follows:
     22-100: DPNPPITNLR...STWILFPENS → G

Show »
Length:300
Mass (Da):34,466
Checksum:iD90ED8C49F3BD8CC
GO

Sequence cautioni

The sequence BAA08393.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121A → T.2 Publications
Corresponds to variant rs6647004 [ dbSNP | Ensembl ].
VAR_021113
Natural varianti77 – 771E → G.1 Publication
Corresponds to variant rs17886756 [ dbSNP | Ensembl ].
VAR_021114
Natural varianti123 – 1231S → T.1 Publication
Corresponds to variant rs17883572 [ dbSNP | Ensembl ].
VAR_021115
Natural varianti323 – 3231V → L.1 Publication
Corresponds to variant rs17883366 [ dbSNP | Ensembl ].
VAR_021116

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei22 – 10079DPNPP…FPENS → G in isoform 2. 1 PublicationVSP_040622Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74782 mRNA. Translation: AAA59148.1.
D49410 Genomic DNA. Translation: BAA08393.1. Sequence problems.
FJ550347 mRNA. Translation: ACM24116.1.
AK290568 mRNA. Translation: BAF83257.1.
AY789109 Genomic DNA. Translation: AAV40832.1.
BX296563, AL683870, BX119906 Genomic DNA. Translation: CAI39694.1.
BX296563, BX119906 Genomic DNA. Translation: CAI39695.1.
BX901885 Genomic DNA. No translation available.
BC035407 mRNA. Translation: AAH35407.1.
CCDSiCCDS14113.1. [P26951-1]
CCDS59158.1. [P26951-2]
PIRiA40266.
RefSeqiNP_001254642.1. NM_001267713.1. [P26951-2]
NP_002174.1. NM_002183.3. [P26951-1]
XP_005274488.1. XM_005274431.2. [P26951-1]
XP_005274837.1. XM_005274780.2. [P26951-1]
UniGeneiHs.632790.

Genome annotation databases

EnsembliENST00000331035; ENSP00000327890; ENSG00000185291. [P26951-1]
ENST00000381469; ENSP00000370878; ENSG00000185291. [P26951-2]
GeneIDi3563.
KEGGihsa:3563.
UCSCiuc004cps.3. human. [P26951-1]

Polymorphism databases

DMDMi417184.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M74782 mRNA. Translation: AAA59148.1 .
D49410 Genomic DNA. Translation: BAA08393.1 . Sequence problems.
FJ550347 mRNA. Translation: ACM24116.1 .
AK290568 mRNA. Translation: BAF83257.1 .
AY789109 Genomic DNA. Translation: AAV40832.1 .
BX296563 , AL683870 , BX119906 Genomic DNA. Translation: CAI39694.1 .
BX296563 , BX119906 Genomic DNA. Translation: CAI39695.1 .
BX901885 Genomic DNA. No translation available.
BC035407 mRNA. Translation: AAH35407.1 .
CCDSi CCDS14113.1. [P26951-1 ]
CCDS59158.1. [P26951-2 ]
PIRi A40266.
RefSeqi NP_001254642.1. NM_001267713.1. [P26951-2 ]
NP_002174.1. NM_002183.3. [P26951-1 ]
XP_005274488.1. XM_005274431.2. [P26951-1 ]
XP_005274837.1. XM_005274780.2. [P26951-1 ]
UniGenei Hs.632790.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4JZJ X-ray 2.80 C/D 20-307 [» ]
ProteinModelPortali P26951.
SMRi P26951. Positions 25-291.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109778. 11 interactions.
DIPi DIP-3293N.
IntActi P26951. 12 interactions.
MINTi MINT-7241956.
STRINGi 9606.ENSP00000327890.

Chemistry

DrugBanki DB00020. Sargramostim.
GuidetoPHARMACOLOGYi 1705.

PTM databases

PhosphoSitei P26951.

Polymorphism databases

DMDMi 417184.

Proteomic databases

PaxDbi P26951.
PRIDEi P26951.

Protocols and materials databases

DNASUi 3563.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000331035 ; ENSP00000327890 ; ENSG00000185291 . [P26951-1 ]
ENST00000381469 ; ENSP00000370878 ; ENSG00000185291 . [P26951-2 ]
GeneIDi 3563.
KEGGi hsa:3563.
UCSCi uc004cps.3. human. [P26951-1 ]

Organism-specific databases

CTDi 3563.
GeneCardsi GC0XP001455.
HGNCi HGNC:6012. IL3RA.
HPAi CAB018374.
HPA003539.
MIMi 308385. gene.
430000. gene.
neXtProti NX_P26951.
PharmGKBi PA29831.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG44788.
GeneTreei ENSGT00520000055993.
HOGENOMi HOG000201004.
HOVERGENi HBG107484.
InParanoidi P26951.
KOi K04737.
OMAi KNLRMEP.
OrthoDBi EOG7TJ3J7.
PhylomeDBi P26951.
TreeFami TF331549.

Enzyme and pathway databases

Reactomei REACT_1695. GPVI-mediated activation cascade.
REACT_19290. G beta:gamma signalling through PI3Kgamma.
REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
REACT_23891. Interleukin receptor SHC signaling.
SignaLinki P26951.

Miscellaneous databases

GeneWikii IL3RA.
GenomeRNAii 3563.
NextBioi 13916.
PROi P26951.
SOURCEi Search...

Gene expression databases

Bgeei P26951.
CleanExi HS_IL3RA.
ExpressionAtlasi P26951. baseline and differential.
Genevestigatori P26951.

Family and domain databases

Gene3Di 2.60.40.10. 2 hits.
InterProi IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR015321. IL-6_rcpt_alpha-bd.
IPR003532. Short_hematopoietin_rcpt_2_CS.
[Graphical view ]
Pfami PF09240. IL6Ra-bind. 1 hit.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 2 hits.
PROSITEi PS01356. HEMATOPO_REC_S_F2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Expression cloning of the human IL-3 receptor cDNA reveals a shared beta subunit for the human IL-3 and GM-CSF receptors."
    Kitamura T., Sato N., Arai K., Miyajima A.
    Cell 66:1165-1174(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Structure of the gene encoding the alpha subunit of the human interleukin 3 receptor."
    Kosugi H., Nakagawa Y., Hotta T., Saito H., Miyajima A., Arai K., Yokota T.
    Biochem. Biophys. Res. Commun. 208:360-367(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "A new isoform of IL-3 receptor alpha with novel differentiation activity and high affinity binding mode."
    Chen J., Olsen J., Ford S., Mirza S., Walker A., Murphy J.M., Young I.G.
    J. Biol. Chem. 284:5763-5773(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING.
  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 1).
    Tissue: Lung.
  5. SeattleSNPs variation discovery resource
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-12; GLY-77; THR-123 AND LEU-323.
  6. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT THR-12.
  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.

Entry informationi

Entry nameiIL3RA_HUMAN
AccessioniPrimary (citable) accession number: P26951
Secondary accession number(s): A8K3F3
, B9VI81, Q5HYQ7, Q5HYQ8, Q9UEH7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: November 26, 2014
This is version 140 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

Miscellaneous

The gene coding for this protein is located in the pseudoautosomal region 1 (PAR1) of X and Y chromosomes.

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 X
    Human chromosome X: 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

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