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P25025 (CXCR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
C-X-C chemokine receptor type 2

Short name=CXC-R2
Short name=CXCR-2
Alternative name(s):
CDw128b
GRO/MGSA receptor
High affinity interleukin-8 receptor B
Short name=IL-8R B
IL-8 receptor type 2
CD_antigen=CD182
Gene names
Name:CXCR2
Synonyms:IL8RB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length360 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Receptor for interleukin-8 which is a powerful neutrophil chemotactic factor. Binding of IL-8 to the receptor causes activation of neutrophils. This response is mediated via a G-protein that activates a phosphatidylinositol-calcium second messenger system. Binds to IL-8 with high affinity. Also binds with high affinity to CXCL3, GRO/MGSA and NAP-2.

Subcellular location

Cell membrane; Multi-pass membrane protein.

Post-translational modification

Phosphorylated upon ligand binding; which is required for desensitization. Ref.9

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
   Biological processChemotaxis
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacute inflammatory response to antigenic stimulus

Inferred from electronic annotation. Source: Ensembl

cell surface receptor signaling pathway

Inferred from direct assay PubMed 10734056PubMed 10878382. Source: UniProtKB

cellular defense response

Inferred from direct assay PubMed 10725748. Source: UniProtKB

chemokine-mediated signaling pathway

Inferred from direct assay PubMed 10878382. Source: GOC

chemotaxis

Inferred from direct assay PubMed 10725748. Source: UniProtKB

dendritic cell chemotaxis

Traceable author statement PubMed 16621978. Source: BHF-UCL

inflammatory response

Traceable author statement PubMed 9725262. Source: ProtInc

interleukin-8-mediated signaling pathway

Inferred from direct assay PubMed 10820279. Source: GOC

metanephric tubule morphogenesis

Inferred from electronic annotation. Source: Ensembl

midbrain development

Inferred from electronic annotation. Source: Ensembl

negative regulation of neutrophil apoptotic process

Inferred from electronic annotation. Source: Ensembl

neutrophil activation

Inferred from direct assay PubMed 10878382. Source: UniProtKB

neutrophil chemotaxis

Inferred from direct assay PubMed 10820279. Source: UniProtKB

phospholipase C-activating G-protein coupled receptor signaling pathway

Inferred from direct assay PubMed 10438939. Source: UniProtKB

positive regulation of angiogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of cardiac muscle cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from direct assay PubMed 10438939. Source: UniProtKB

positive regulation of cytosolic calcium ion concentration

Inferred from electronic annotation. Source: Ensembl

positive regulation of neutrophil chemotaxis

Inferred from electronic annotation. Source: Ensembl

positive regulation of vascular permeability

Inferred from electronic annotation. Source: Ensembl

receptor internalization

Inferred from direct assay PubMed 10734056. Source: UniProtKB

signal transduction

Inferred from direct assay PubMed 10820279. Source: UniProtKB

   Cellular_componentcell surface

Inferred from direct assay PubMed 10878382. Source: UniProtKB

integral component of plasma membrane

Traceable author statement PubMed 10438939. Source: UniProtKB

intracellular

Inferred from direct assay PubMed 10878382. Source: UniProtKB

mast cell granule

Inferred from direct assay PubMed 9725262. Source: UniProtKB

membrane

Inferred from direct assay PubMed 10725748. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionC-X-C chemokine receptor activity

Inferred from direct assay PubMed 10878382. Source: UniProtKB

interleukin-8 binding

Inferred from physical interaction PubMed 1840701. Source: UniProtKB

interleukin-8 receptor activity

Inferred from direct assay PubMed 10820279. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 23597562. Source: IntAct

signal transducer activity

Inferred from direct assay PubMed 10438939PubMed 10820279PubMed 10878382. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

IL8P101452EBI-2835281,EBI-3917999

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 360360C-X-C chemokine receptor type 2
PRO_0000069337

Regions

Topological domain1 – 4848Extracellular Potential
Transmembrane49 – 7527Helical; Name=1; Potential
Topological domain76 – 849Cytoplasmic Potential
Transmembrane85 – 10521Helical; Name=2; Potential
Topological domain106 – 12015Extracellular Potential
Transmembrane121 – 14222Helical; Name=3; Potential
Topological domain143 – 16321Cytoplasmic Potential
Transmembrane164 – 18320Helical; Name=4; Potential
Topological domain184 – 20825Extracellular Potential
Transmembrane209 – 23123Helical; Name=5; Potential
Topological domain232 – 25120Cytoplasmic Potential
Transmembrane252 – 27322Helical; Name=6; Potential
Topological domain274 – 29421Extracellular Potential
Transmembrane295 – 31521Helical; Name=7; Potential
Topological domain316 – 36045Cytoplasmic Potential

Amino acid modifications

Modified residue3471Phosphoserine Probable
Modified residue3511Phosphoserine Probable
Modified residue3521Phosphoserine Probable
Modified residue3531Phosphoserine Probable
Glycosylation221N-linked (GlcNAc...) Potential
Disulfide bond119 ↔ 196 By similarity

Natural variations

Natural variant801R → C. Ref.7
Corresponds to variant rs1805038 [ dbSNP | Ensembl ].
VAR_014679

Sequences

Sequence LengthMass (Da)Tools
P25025 [UniParc].

Last modified February 1, 1996. Version 2.
Checksum: 564F04A8BCC0A197

FASTA36040,759
        10         20         30         40         50         60 
MEDFNMESDS FEDFWKGEDL SNYSYSSTLP PFLLDAAPCE PESLEINKYF VVIIYALVFL 

        70         80         90        100        110        120 
LSLLGNSLVM LVILYSRVGR SVTDVYLLNL ALADLLFALT LPIWAASKVN GWIFGTFLCK 

       130        140        150        160        170        180 
VVSLLKEVNF YSGILLLACI SVDRYLAIVH ATRTLTQKRY LVKFICLSIW GLSLLLALPV 

       190        200        210        220        230        240 
LLFRRTVYSS NVSPACYEDM GNNTANWRML LRILPQSFGF IVPLLIMLFC YGFTLRTLFK 

       250        260        270        280        290        300 
AHMGQKHRAM RVIFAVVLIF LLCWLPYNLV LLADTLMRTQ VIQETCERRN HIDRALDATE 

       310        320        330        340        350        360 
ILGILHSCLN PLIYAFIGQK FRHGLLKILA IHGLISKDSL PKDSRPSFVG SSSGHTSTTL 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of complementary DNA encoding a functional human interleukin-8 receptor."
Murphy P.M., Tiffany H.L.
Science 253:1280-1283(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular characterization of receptors for human interleukin-8, GRO/melanoma growth-stimulatory activity and neutrophil activating peptide-2."
Cerretti D.P., Kozlosky C.J., Vanden Bos T., Nelson N., Gearing D.P., Beckmann M.P.
Mol. Immunol. 30:359-367(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[3]"Structure, genomic organization, and expression of the human interleukin-8 receptor B gene."
Sprenger H., Lloyd A.R., Lautens L.L., Bonner T.I., Kelvin D.J.
J. Biol. Chem. 269:11065-11072(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[4]"Comparison of the genomic organization and promoter function for human interleukin-8 receptors A and B."
Ahuja S.K., Shetty A., Tiffany H.L., Murphy P.M.
J. Biol. Chem. 269:26381-26389(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Placenta.
[5]SeattleSNPs variation discovery resource
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"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].
Tissue: Brain.
[7]"Single nucleotide polymorphisms in the coding regions of human CXC-chemokine receptors CXCR1, CXCR2 and CXCR3."
Kato H., Tsuchiya N., Tokunaga K.
Genes Immun. 1:330-337(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 52-162 AND 191-301, VARIANT CYS-80.
[8]"Characterization of two high affinity human interleukin-8 receptors."
Lee J., Horuk R., Rice G.C., Bennett G.L., Camerato T., Wood W.I.
J. Biol. Chem. 267:16283-16287(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[9]"Ligand-induced desensitization of the human CXC chemokine receptor-2 is modulated by multiple serine residues in the carboxyl-terminal domain of the receptor."
Mueller S.G., White J.R., Schraw W.P., Lam V., Richmond A.
J. Biol. Chem. 272:8207-8214(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-347; SER-351; SER-352 AND SER-353.
+Additional computationally mapped references.

Web resources

Wikipedia

CXC chemokine receptors entry

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M73969 mRNA. Translation: AAA83148.1.
M94582 mRNA. Translation: AAA36108.1.
M99412 Genomic DNA. Translation: AAC14460.1.
L19593 mRNA. Translation: AAB59437.1.
U11869 Genomic DNA. Translation: AAB60656.1.
AY714242 Genomic DNA. Translation: AAT97985.1.
BC037961 mRNA. Translation: AAH37961.2.
AB032733 Genomic DNA. Translation: BAA92295.1.
AB032734 Genomic DNA. Translation: BAA92296.1.
CCDSCCDS2408.1.
PIRA53611. I37898.
RefSeqNP_001161770.1. NM_001168298.1.
NP_001548.1. NM_001557.3.
XP_005246587.1. XM_005246530.1.
XP_005246588.1. XM_005246531.1.
UniGeneHs.846.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4Q3HX-ray1.44A/B356-360[»]
ProteinModelPortalP25025.
SMRP25025. Positions 38-333.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109793. 8 interactions.
DIPDIP-3782N.
IntActP25025. 5 interactions.
MINTMINT-271138.
STRING9606.ENSP00000319635.

Chemistry

BindingDBP25025.
ChEMBLCHEMBL2434.
GuidetoPHARMACOLOGY69.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP25025.

Polymorphism databases

DMDM1352454.

Proteomic databases

PaxDbP25025.
PRIDEP25025.

Protocols and materials databases

DNASU3579.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000318507; ENSP00000319635; ENSG00000180871.
GeneID3579.
KEGGhsa:3579.
UCSCuc002vgz.2. human.

Organism-specific databases

CTD3579.
GeneCardsGC02P219012.
HGNCHGNC:6027. CXCR2.
HPACAB016268.
MIM146928. gene.
neXtProtNX_P25025.
PharmGKBPA29843.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG146068.
HOGENOMHOG000234122.
HOVERGENHBG106917.
InParanoidP25025.
KOK05050.
OMALFRRTIY.
PhylomeDBP25025.
TreeFamTF330966.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkP25025.

Gene expression databases

ArrayExpressP25025.
BgeeP25025.
CleanExHS_IL8RB.
GenevestigatorP25025.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR000057. Chemokine_CXCR2.
IPR000174. Chemokine_CXCR_1/2.
IPR000355. Chemokine_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERPTHR24227. PTHR24227. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00237. GPCRRHODOPSN.
PR00427. INTRLEUKIN8R.
PR00573. INTRLEUKN8BR.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi3579.
NextBio13990.
PROP25025.
SOURCESearch...

Entry information

Entry nameCXCR2_HUMAN
AccessionPrimary (citable) accession number: P25025
Secondary accession number(s): Q8IUZ1, Q9P2T6, Q9P2T7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 148 of the entry and version 2 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 2

Human chromosome 2: entries, gene names and cross-references to MIM

Human cell differentiation molecules

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

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries