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Protein

C-C chemokine receptor type 5

Gene

CCR5

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

Functioni

Receptor for a number of inflammatory CC-chemokines including MIP-1-alpha, MIP-1-beta and RANTES and subsequently transduces a signal by increasing the intracellular calcium ion level. May play a role in the control of granulocytic lineage proliferation or differentiation. Acts as a coreceptor (CD4 being the primary receptor) for HIV-1 R5 isolates.6 Publications
(Microbial infection) Acts as a receptor for human immunodeficiency virus-1/HIV-1.2 Publications

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • C-C chemokine binding Source: UniProtKB
  • C-C chemokine receptor activity Source: UniProtKB
  • chemokine (C-C motif) ligand 5 binding Source: UniProtKB
  • chemokine receptor activity Source: ProtInc
  • coreceptor activity Source: ProtInc
  • phosphatidylinositol phospholipase C activity Source: ProtInc
  • virus receptor activity Source: UniProtKB-KW

GO - Biological processi

  • calcium ion transport Source: UniProtKB
  • calcium-mediated signaling Source: UniProtKB
  • cell-cell signaling Source: UniProtKB
  • cell surface receptor signaling pathway Source: ProtInc
  • cellular defense response Source: ProtInc
  • cellular response to lipopolysaccharide Source: UniProtKB
  • chemotaxis Source: ProtInc
  • dendritic cell chemotaxis Source: BHF-UCL
  • entry into host cell Source: Reactome
  • fusion of virus membrane with host plasma membrane Source: Reactome
  • G-protein coupled receptor signaling pathway Source: UniProtKB
  • immune response Source: ProtInc
  • inflammatory response Source: ProtInc
  • MAPK cascade Source: UniProtKB
  • positive regulation of cytosolic calcium ion concentration Source: ProtInc
  • release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: UniProtKB
  • response to cholesterol Source: UniProtKB
  • signaling Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Host cell receptor for virus entry, Receptor, Transducer

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

BioCyciZFISH:ENSG00000160683-MONOMER.
ZFISH:ENSG00000160791-MONOMER.
ReactomeiR-HSA-173107. Binding and entry of HIV virion.
R-HSA-380108. Chemokine receptors bind chemokines.
R-HSA-418594. G alpha (i) signalling events.
SignaLinkiP51681.
SIGNORiP51681.

Names & Taxonomyi

Protein namesi
Recommended name:
C-C chemokine receptor type 5
Short name:
C-C CKR-5
Short name:
CC-CKR-5
Short name:
CCR-5
Short name:
CCR5
Alternative name(s):
CHEMR13
HIV-1 fusion coreceptor
CD_antigen: CD195
Gene namesi
Name:CCR5
Synonyms:CMKBR5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:1606. CCR5.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 30ExtracellularSequence analysisAdd BLAST30
Transmembranei31 – 58Helical; Name=1Sequence analysisAdd BLAST28
Topological domaini59 – 68CytoplasmicSequence analysis10
Transmembranei69 – 89Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini90 – 102ExtracellularSequence analysisAdd BLAST13
Transmembranei103 – 124Helical; Name=3Sequence analysisAdd BLAST22
Topological domaini125 – 141CytoplasmicSequence analysisAdd BLAST17
Transmembranei142 – 166Helical; Name=4Sequence analysisAdd BLAST25
Topological domaini167 – 198ExtracellularSequence analysisAdd BLAST32
Transmembranei199 – 218Helical; Name=5Sequence analysisAdd BLAST20
Topological domaini219 – 235CytoplasmicSequence analysisAdd BLAST17
Transmembranei236 – 260Helical; Name=6Sequence analysisAdd BLAST25
Topological domaini261 – 277ExtracellularSequence analysisAdd BLAST17
Transmembranei278 – 301Helical; Name=7Sequence analysisAdd BLAST24
Topological domaini302 – 352CytoplasmicSequence analysisAdd BLAST51

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • cytoplasm Source: ProtInc
  • endosome Source: UniProtKB
  • external side of plasma membrane Source: UniProtKB
  • integral component of plasma membrane Source: ProtInc
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Diabetes mellitus, insulin-dependent, 22 (IDDM22)1 Publication
Disease susceptibility is associated with variations affecting the gene represented in this entry.
Disease descriptionA multifactorial disorder of glucose homeostasis that is characterized by susceptibility to ketoacidosis in the absence of insulin therapy. Clinical features are polydipsia, polyphagia and polyuria which result from hyperglycemia-induced osmotic diuresis and secondary thirst. These derangements result in long-term complications that affect the eyes, kidneys, nerves, and blood vessels.
See also OMIM:612522

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi3Y → D: No sulfation and greatly decreased binding CCL4 and CCL5; when associated with D-10; D-14 and D-15. Restored most CCL4 binding; when associated with D-10 and D-15. 2 Publications1
Mutagenesisi3Y → F: No sulfation and greatly decreases binding of CCL4 and CCL5; when associated with F-10; F-14 and F-15. 2 Publications1
Mutagenesisi6S → A: No change in glycosylation status and greatly decreased CCL4 binding. Loss of molecular mass of about 2 kDa as compared to wild type. Dramatically reduced binding of CCL4; when associated with A-7; A-16; A-17. Similar molecular mass loss. Dramatically reduced binding of CCL4; when associated with A-7 only. 1 Publication1
Mutagenesisi7S → A: No change in glycosylation status and binds CCL4 as efficiently as wild type. Loss of molecular mass of about 2 kDa as compared to wild type. Dramatically reduced binding of CCL4; when associated with A-6; A-16; A-17. Similar molecular mass loss. Dramatically reduced binding of CCL4; when associated with A-6 only. 1 Publication1
Mutagenesisi10Y → F: No sulfation and greatly decreases binding of CCL4 and CCL5; when associated with F-3; F-14 and F-15. Small loss of sulfation; when associated with F-14 and F-15. 2 Publications1
Mutagenesisi14Y → D: No sulfation and greatly decreased binding CCL4 and CCL5; when associated with D-3; D-10 and D-14. No restoration of CCL4 binding; when associated with D-10 and D-15. 2 Publications1
Mutagenesisi14Y → F: No sulfation and greatly decreases binding of CCL4 and CCL5; when associated with F-3; F-10; and F-15. Small loss of sulfation; when associated with F-10 and F-15. 2 Publications1
Mutagenesisi15Y → D: No sulfation and greatly decreased binding CCL4 and CCL5; when associated with D-3; D-10 and D-14. Restored most CCL4 binding; when associated with D-3 and D-10. 2 Publications1
Mutagenesisi15Y → F: No sulfation and greatly decreases binding of CCL4 and CCL5; when associated with F-3; F-10 and F-14. Small loss of sulfation; when associated with F-10 and F-14. 2 Publications1
Mutagenesisi16T → A: Similar decrease in molecular mass when treated with O-glycosidase as for wild type; when associated with A-17. 1 Publication1
Mutagenesisi17S → A: Similar decrease in molecular mass when treated with O-glycosidase as for wild type; when associated with A-16. 1 Publication1
Mutagenesisi321C → A: Small reduction in palmitoylation. Cell surface expression reduced by 50%. Greatly reduced palmitoylation. Cell surface expression greatly reduced; when associated with A-323 or A-324. No palmitoylation. Cell surface expression greatly reduced. HIV entry reduced by 50%; when associated with A-323 and A-324. 1 Publication1
Mutagenesisi323C → A: Small reduction in palmitoylation. Cell surface expression reduced by 50%. Greatly reduced palmitoylation. Cell surface expression greatly reduced; when associated with A-321 or A-324. No palmitoylation. Cell surface expression greatly reduced. HIV entry reduced by 50%; when associated with A-321 and A-324. 1 Publication1
Mutagenesisi324C → A: Small reduction in palmitoylation. Cell surface expression reduced by 50%. Greatly reduced palmitoylation. Cell surface expression greatly reduced; when associated with A-321 or A-323. No palmitoylation. Cell surface expression greatly reduced. HIV entry reduced by 50%; when associated with A-321 and A-323. 1 Publication1
Mutagenesisi336S → A: APO-RANTES-stimulated phosphorylation reduced by 15%; APO-RANTES-stimulated phosphorylation reduced by 30-50%; when associated with A-337 or A-342 or A-349; APO-RANTES-stimulated phosphorylation reduced by 80%; when associated with A-337 and A-342 or A-349; No APO-RANTES-stimulated phosphorylation; when associated with A-337; A-342 and A349; abolishes interaction with ARRB2; when associated with S-337; S-342 and S-349. 2 Publications1
Mutagenesisi337S → A: APO-RANTES-stimulated phosphorylation reduced by 18%; APO-RANTES-stimulated phosphorylation reduced by 30-50% on APO-RANTES stimulation; when associated with A-336 or A-342 or A-349; APO-RANTES-stimulated phosphorylation reduced by 80%; when associated with A-336 and A-342 or A-349; No APO-RANTES-stimulated phosphorylation; when associated with A-336; A-342 and A349; abolishes interaction with ARRB2; when associated with S-336; S-342 and S-349. 2 Publications1
Mutagenesisi342S → A: APO-RANTES-stimulated phosphorylation reduced by 42%. Phosphorylation reduced by 50% on APO-RANTES stimulation; when associated with A-336 or A-337 or A-349; APO-RANTES-stimulated phosphorylation reduced by 80% when associated with A-336 and A-337 or A-349; No APO-RANTES-stimulated phosphorylation; when associated with A-336; A-337 and A349; abolishes interaction with ARRB2; when associated with S-336; S-337 and S-349. 2 Publications1
Mutagenesisi349S → A: APO-RANTES-stimulated phosphorylation reduced by 43%; APO-RANTES-stimulated phosphorylation reduced by 30-50%; when associated with A-336 or A-337 or A-342; APO-RANTES-stimulated phosphorylation reduced by 80%; when associated with A-336 and A-337 or A-342; No APO-RANTES-stimulated phosphorylation stimulation; when associated with A-336; A-337 and A347; abolishes interaction with ARRB2; when associated with S-336; S-337 and S-342. 2 Publications1

Keywords - Diseasei

Diabetes mellitus

Organism-specific databases

DisGeNETi1234.
MalaCardsiCCR5.
MIMi609423. phenotype.
610379. phenotype.
612522. phenotype.
OpenTargetsiENSG00000160791.
Orphaneti319269. Susceptibility/resistance to HIV infection.
PharmGKBiPA26170.

Chemistry databases

ChEMBLiCHEMBL274.
DrugBankiDB04835. Maraviroc.
GuidetoPHARMACOLOGYi62.

Polymorphism and mutation databases

BioMutaiCCR5.
DMDMi1705896.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000692571 – 352C-C chemokine receptor type 5Add BLAST352

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3Sulfotyrosine1 Publication1
Glycosylationi6O-linked (GalNAc...)1 Publication1
Glycosylationi7O-linked (GalNAc...)1 Publication1
Modified residuei10Sulfotyrosine1 Publication1
Modified residuei14Sulfotyrosine1 Publication1
Modified residuei15SulfotyrosineSequence analysis1
Glycosylationi16O-linked (GalNAc...)Sequence analysis1
Glycosylationi17O-linked (GalNAc...)Sequence analysis1
Disulfide bondi101 ↔ 178PROSITE-ProRule annotation
Lipidationi321S-palmitoyl cysteine1 Publication1
Lipidationi323S-palmitoyl cysteine1 Publication1
Lipidationi324S-palmitoyl cysteine1 Publication1
Modified residuei336Phosphoserine; by BARK11 Publication1
Modified residuei337Phosphoserine; by BARK11 Publication1
Modified residuei342Phosphoserine; by BARK11 Publication1
Modified residuei349Phosphoserine; by BARK11 Publication1

Post-translational modificationi

Sulfated on at least 2 of the N-terminal tyrosines. Sulfation contributes to the efficiency of HIV-1 entry and is required for efficient binding of the chemokines, CCL3 and CCL4.3 Publications
O-glycosylated, but not N-glycosylated. Ser-6 appears to be the major site. Also sialylated glycans present which contribute to chemokine binding. Thr-16 and Ser-17 may also be glycosylated and, if so, with small moieties such as a T-antigen.2 Publications
Palmitoylation in the C-terminal is important for cell surface expression, and to a lesser extent, for HIV entry.1 Publication
Phosphorylation on serine residues in the C-terminal is stimulated by binding CC chemokines especially by APO-RANTES.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein, Sulfation

Proteomic databases

PaxDbiP51681.
PeptideAtlasiP51681.
PRIDEiP51681.

PTM databases

iPTMnetiP51681.
PhosphoSitePlusiP51681.
SwissPalmiP51681.

Expressioni

Tissue specificityi

Highly expressed in spleen, thymus, in the myeloid cell line THP-1, in the promyeloblastic cell line KG-1a and on CD4+ and CD8+ T-cells. Medium levels in peripheral blood leukocytes and in small intestine. Low levels in ovary and lung.2 Publications

Inductioni

(Microbial infection) May be down-regulated by human cytomegalovirus/HHV-5 protein UL78.1 Publication

Gene expression databases

BgeeiENSG00000160791.
ExpressionAtlasiP51681. baseline and differential.
GenevisibleiP51681. HS.

Interactioni

Subunit structurei

Interacts with PRAF2. Efficient ligand binding to CCL3/MIP-1alpha and CCL4/MIP-1beta requires sulfation, O-glycosylation and sialic acid modifications. Glycosylation on Ser-6 is required for efficient binding of CCL4. Interacts with GRK2. Interacts with ARRB1 and ARRB2. Interacts with CNIH4 (PubMed:24405750). ARRB2.8 Publications
(Microbial infection) Interacts with HIV-1 surface protein gp120 (PubMed:9632396, PubMed:21763489).2 Publications
(Microbial infection) May interact with human cytomegalovirus/HHV-5 protein UL78.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CCL4P132362EBI-489374,EBI-6625160
CCL5P135014EBI-489374,EBI-2848366
CD4P017302EBI-489374,EBI-353826

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • C-C chemokine binding Source: UniProtKB
  • chemokine (C-C motif) ligand 5 binding Source: UniProtKB

Protein-protein interaction databases

BioGridi107639. 17 interactors.
DIPiDIP-5866N.
IntActiP51681. 11 interactors.
MINTiMINT-103024.
STRINGi9606.ENSP00000292303.

Chemistry databases

BindingDBiP51681.

Structurei

Secondary structure

1352
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 13Combined sources4
Helixi14 – 17Combined sources4
Turni20 – 22Combined sources3
Helixi26 – 57Combined sources32
Helixi64 – 91Combined sources28
Helixi98 – 131Combined sources34
Helixi133 – 139Combined sources7
Helixi142 – 165Combined sources24
Beta strandi167 – 172Combined sources6
Beta strandi175 – 180Combined sources6
Helixi187 – 202Combined sources16
Helixi204 – 223Combined sources20
Helixi229 – 232Combined sources4
Helixi234 – 259Combined sources26
Helixi261 – 264Combined sources4
Helixi269 – 288Combined sources20
Helixi289 – 291Combined sources3
Helixi293 – 300Combined sources8
Helixi302 – 312Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ND8model-A1-352[»]
1NE0model-A1-352[»]
1OPNmodel-A1-352[»]
1OPTmodel-A1-352[»]
1OPWmodel-A1-352[»]
2L87NMR-A1-27[»]
2MZXNMR-A186-195[»]
2RLLNMR-A7-15[»]
2RRSNMR-A157-174[»]
4MBSX-ray2.71A/B2-352[»]
ProteinModelPortaliP51681.
SMRiP51681.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51681.

Family & Domainsi

Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3656. Eukaryota.
ENOG410XRW9. LUCA.
GeneTreeiENSGT00760000118785.
HOVERGENiHBG106917.
InParanoidiP51681.
KOiK04180.
OMAiGNTMCQL.
OrthoDBiEOG091G0B7A.
PhylomeDBiP51681.
TreeFamiTF330966.

Family and domain databases

InterProiIPR002240. Chemokine_CCR5.
IPR000355. Chemokine_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00657. CCCHEMOKINER.
PR01110. CHEMOKINER5.
PR00237. GPCRRHODOPSN.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P51681-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDYQVSSPIY DINYYTSEPC QKINVKQIAA RLLPPLYSLV FIFGFVGNML
60 70 80 90 100
VILILINCKR LKSMTDIYLL NLAISDLFFL LTVPFWAHYA AAQWDFGNTM
110 120 130 140 150
CQLLTGLYFI GFFSGIFFII LLTIDRYLAV VHAVFALKAR TVTFGVVTSV
160 170 180 190 200
ITWVVAVFAS LPGIIFTRSQ KEGLHYTCSS HFPYSQYQFW KNFQTLKIVI
210 220 230 240 250
LGLVLPLLVM VICYSGILKT LLRCRNEKKR HRAVRLIFTI MIVYFLFWAP
260 270 280 290 300
YNIVLLLNTF QEFFGLNNCS SSNRLDQAMQ VTETLGMTHC CINPIIYAFV
310 320 330 340 350
GEKFRNYLLV FFQKHIAKRF CKCCSIFQQE APERASSVYT RSTGEQEISV

GL
Length:352
Mass (Da):40,524
Last modified:October 1, 1996 - v1
Checksum:i88ECE1F38E6D45A7
GO

Polymorphismi

Variations in CCR5 are associated with resistance or susceptibility to immunodeficiency virus type 1 (resistance or susceptibility to HIV-1) [MIMi:609423]. Variations in CCR5 gene also influence the rate of progression to AIDS after infection.2 Publications
Ser-60 variant, a naturally occurring mutation in a conserved residue in the first intracellular domain of CCR5, results in reduced amounts of the protein in the membrane and consequently may be associated with reduced susceptibility to infection by microbes that depend on these molecules as their receptors.1 Publication
Variations in CCR5 are associated with susceptibility to West Nile virus (WNV) infection [MIMi:610379].1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00348110Y → D in INCCR5-71A; results in absent sulfation and greatly decreased binding CCL4 and CCL5 when associated with D-3, D-10 and D-15; restored most CCL4 binding when associated with D-3 and D-15. 1 Publication1
Natural variantiVAR_02406612I → L.1 Publication1
Natural variantiVAR_02406720C → S.1 PublicationCorresponds to variant rs145061115dbSNPEnsembl.1
Natural variantiVAR_01183929A → S.1 PublicationCorresponds to variant rs1800939dbSNPEnsembl.1
Natural variantiVAR_00348231R → H in INCCR5-72A. Corresponds to variant rs56340326dbSNPEnsembl.1
Natural variantiVAR_00348334P → L in TZCCR5-179. 1
Natural variantiVAR_02406842I → F.1 Publication1
Natural variantiVAR_01184055L → Q.2 PublicationsCorresponds to variant rs1799863dbSNPEnsembl.1
Natural variantiVAR_01184160R → S Associated with susceptibility to HIV-1; reduced surface expression and function of CCR5 protein. 2 PublicationsCorresponds to variant rs1800940dbSNPEnsembl.1
Natural variantiVAR_00348462K → R in UGCCR5-145B. 1
Natural variantiVAR_00348568Y → H in ZWCCR5-7. Corresponds to variant rs758090461dbSNPEnsembl.1
Natural variantiVAR_02406973A → V.1 PublicationCorresponds to variant rs56198941dbSNPEnsembl.1
Natural variantiVAR_00348695D → N in MWCCR5-107. Corresponds to variant rs149975182dbSNPEnsembl.1
Natural variantiVAR_00348797G → E in INCCR5-467. 1
Natural variantiVAR_003488122L → P in ZWCCR5-7. 1
Natural variantiVAR_003489158F → S in UGCCR5-145A. 1
Natural variantiVAR_003490176Y → C in KECCR5-116. 1
Natural variantiVAR_003491177T → A in INCCR5-45C. 1
Natural variantiVAR_012481178C → R Found in a HIV-resistant individiual. 1 PublicationCorresponds to variant rs199824195dbSNPEnsembl.1
Natural variantiVAR_003492185S → N in UGCCR5-145A. 1
Natural variantiVAR_003493210M → V in ZWCCR5-7. 1
Natural variantiVAR_003494214Y → C in KECCR5-3B. 1
Natural variantiVAR_024070215S → L.1 Publication1
Natural variantiVAR_011842223R → Q.2 PublicationsCorresponds to variant rs1800452dbSNPEnsembl.1
Natural variantiVAR_024071228Missing .1 Publication1
Natural variantiVAR_003495239T → S in INCCR5-71A. 1
Natural variantiVAR_003496246L → P in UGCCR5-145A. Corresponds to variant rs143181119dbSNPEnsembl.1
Natural variantiVAR_003497288T → M in INCCR5-72A. Corresponds to variant rs534088482dbSNPEnsembl.1
Natural variantiVAR_011843301G → V.1 PublicationCorresponds to variant rs1800943dbSNPEnsembl.1
Natural variantiVAR_003498302E → G in TZCCR5-179. 1
Natural variantiVAR_003499303K → E in THCCR5-5. 1
Natural variantiVAR_003500306N → S in MWCCR5-1567. 1
Natural variantiVAR_003501322K → R in THCCR5-5. 1
Natural variantiVAR_003502333E → G in THCCR5-2. 1
Natural variantiVAR_003503335A → V in MWCCR5-1567, MWCCR5-1568, ZWCCR5-14 and ZWCCR5-112. 2 PublicationsCorresponds to variant rs1800944dbSNPEnsembl.1
Natural variantiVAR_003504339Y → F in TZCCR5-181A and MWCCR5-107. 2 PublicationsCorresponds to variant rs1800945dbSNPEnsembl.1
Natural variantiVAR_003505345E → G in UGCCR5-145C. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91492 Genomic DNA. Translation: CAA62796.1.
U54994 mRNA. Translation: AAC50598.1.
U57840 mRNA. Translation: AAB17071.1.
U83326 Genomic DNA. Translation: AAC51797.1.
AF011500 mRNA. Translation: AAB65700.1.
AF011501 mRNA. Translation: AAB65701.1.
AF011502 mRNA. Translation: AAB65702.1.
AF011503 mRNA. Translation: AAB65703.1.
AF011505 mRNA. Translation: AAB65705.1.
AF011506 mRNA. Translation: AAB65706.1.
AF011507 mRNA. Translation: AAB65707.1.
AF011508 mRNA. Translation: AAB65708.1.
AF011509 mRNA. Translation: AAB65709.1.
AF011510 mRNA. Translation: AAB65710.1.
AF011511 mRNA. Translation: AAB65711.1.
AF011512 mRNA. Translation: AAB65712.1.
AF011513 mRNA. Translation: AAB65713.1.
AF011514 mRNA. Translation: AAB65714.1.
AF011515 mRNA. Translation: AAB65715.1.
AF011516 mRNA. Translation: AAB65716.1.
AF011517 mRNA. Translation: AAB65717.1.
AF011518 mRNA. Translation: AAB65718.1.
AF011519 mRNA. Translation: AAB65719.1.
AF011520 mRNA. Translation: AAB65720.1.
AF011521 mRNA. Translation: AAB65721.1.
AF011522 mRNA. Translation: AAB65722.1.
AF011523 mRNA. Translation: AAB65723.1.
AF011524 mRNA. Translation: AAB65724.1.
AF011525 mRNA. Translation: AAB65725.1.
AF011526 mRNA. Translation: AAB65726.1.
AF011527 mRNA. Translation: AAB65727.1.
AF011528 mRNA. Translation: AAB65728.1.
AF011529 mRNA. Translation: AAB65729.1.
AF011530 mRNA. Translation: AAB65730.1.
AF011531 mRNA. Translation: AAB65731.1.
AF011532 mRNA. Translation: AAB65732.1.
AF011533 mRNA. Translation: AAB65733.1.
AF011534 mRNA. Translation: AAB65734.1.
AF011535 mRNA. Translation: AAB65735.1.
AF011536 mRNA. Translation: AAB65736.1.
AF011537 mRNA. Translation: AAB65737.1.
AF031237 Genomic DNA. Translation: AAB94735.1.
AF052539 Genomic DNA. Translation: AAD18131.1.
AY221093 Genomic DNA. Translation: AAO65971.1.
U95626 Genomic DNA. Translation: AAB57793.1.
BC038398 mRNA. Translation: AAH38398.1.
CCDSiCCDS2739.1.
PIRiA43113.
RefSeqiNP_000570.1. NM_000579.3.
NP_001093638.1. NM_001100168.1.
UniGeneiHs.450802.

Genome annotation databases

EnsembliENST00000292303; ENSP00000292303; ENSG00000160791.
ENST00000445772; ENSP00000404881; ENSG00000160791.
GeneIDi1234.
KEGGihsa:1234.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

CC chemokine receptors entry

Wikipedia

CCR5 receptor entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91492 Genomic DNA. Translation: CAA62796.1.
U54994 mRNA. Translation: AAC50598.1.
U57840 mRNA. Translation: AAB17071.1.
U83326 Genomic DNA. Translation: AAC51797.1.
AF011500 mRNA. Translation: AAB65700.1.
AF011501 mRNA. Translation: AAB65701.1.
AF011502 mRNA. Translation: AAB65702.1.
AF011503 mRNA. Translation: AAB65703.1.
AF011505 mRNA. Translation: AAB65705.1.
AF011506 mRNA. Translation: AAB65706.1.
AF011507 mRNA. Translation: AAB65707.1.
AF011508 mRNA. Translation: AAB65708.1.
AF011509 mRNA. Translation: AAB65709.1.
AF011510 mRNA. Translation: AAB65710.1.
AF011511 mRNA. Translation: AAB65711.1.
AF011512 mRNA. Translation: AAB65712.1.
AF011513 mRNA. Translation: AAB65713.1.
AF011514 mRNA. Translation: AAB65714.1.
AF011515 mRNA. Translation: AAB65715.1.
AF011516 mRNA. Translation: AAB65716.1.
AF011517 mRNA. Translation: AAB65717.1.
AF011518 mRNA. Translation: AAB65718.1.
AF011519 mRNA. Translation: AAB65719.1.
AF011520 mRNA. Translation: AAB65720.1.
AF011521 mRNA. Translation: AAB65721.1.
AF011522 mRNA. Translation: AAB65722.1.
AF011523 mRNA. Translation: AAB65723.1.
AF011524 mRNA. Translation: AAB65724.1.
AF011525 mRNA. Translation: AAB65725.1.
AF011526 mRNA. Translation: AAB65726.1.
AF011527 mRNA. Translation: AAB65727.1.
AF011528 mRNA. Translation: AAB65728.1.
AF011529 mRNA. Translation: AAB65729.1.
AF011530 mRNA. Translation: AAB65730.1.
AF011531 mRNA. Translation: AAB65731.1.
AF011532 mRNA. Translation: AAB65732.1.
AF011533 mRNA. Translation: AAB65733.1.
AF011534 mRNA. Translation: AAB65734.1.
AF011535 mRNA. Translation: AAB65735.1.
AF011536 mRNA. Translation: AAB65736.1.
AF011537 mRNA. Translation: AAB65737.1.
AF031237 Genomic DNA. Translation: AAB94735.1.
AF052539 Genomic DNA. Translation: AAD18131.1.
AY221093 Genomic DNA. Translation: AAO65971.1.
U95626 Genomic DNA. Translation: AAB57793.1.
BC038398 mRNA. Translation: AAH38398.1.
CCDSiCCDS2739.1.
PIRiA43113.
RefSeqiNP_000570.1. NM_000579.3.
NP_001093638.1. NM_001100168.1.
UniGeneiHs.450802.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ND8model-A1-352[»]
1NE0model-A1-352[»]
1OPNmodel-A1-352[»]
1OPTmodel-A1-352[»]
1OPWmodel-A1-352[»]
2L87NMR-A1-27[»]
2MZXNMR-A186-195[»]
2RLLNMR-A7-15[»]
2RRSNMR-A157-174[»]
4MBSX-ray2.71A/B2-352[»]
ProteinModelPortaliP51681.
SMRiP51681.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107639. 17 interactors.
DIPiDIP-5866N.
IntActiP51681. 11 interactors.
MINTiMINT-103024.
STRINGi9606.ENSP00000292303.

Chemistry databases

BindingDBiP51681.
ChEMBLiCHEMBL274.
DrugBankiDB04835. Maraviroc.
GuidetoPHARMACOLOGYi62.

Protein family/group databases

GPCRDBiSearch...

PTM databases

iPTMnetiP51681.
PhosphoSitePlusiP51681.
SwissPalmiP51681.

Polymorphism and mutation databases

BioMutaiCCR5.
DMDMi1705896.

Proteomic databases

PaxDbiP51681.
PeptideAtlasiP51681.
PRIDEiP51681.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000292303; ENSP00000292303; ENSG00000160791.
ENST00000445772; ENSP00000404881; ENSG00000160791.
GeneIDi1234.
KEGGihsa:1234.

Organism-specific databases

CTDi1234.
DisGeNETi1234.
GeneCardsiCCR5.
HGNCiHGNC:1606. CCR5.
MalaCardsiCCR5.
MIMi601373. gene.
609423. phenotype.
610379. phenotype.
612522. phenotype.
neXtProtiNX_P51681.
OpenTargetsiENSG00000160791.
Orphaneti319269. Susceptibility/resistance to HIV infection.
PharmGKBiPA26170.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3656. Eukaryota.
ENOG410XRW9. LUCA.
GeneTreeiENSGT00760000118785.
HOVERGENiHBG106917.
InParanoidiP51681.
KOiK04180.
OMAiGNTMCQL.
OrthoDBiEOG091G0B7A.
PhylomeDBiP51681.
TreeFamiTF330966.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000160683-MONOMER.
ZFISH:ENSG00000160791-MONOMER.
ReactomeiR-HSA-173107. Binding and entry of HIV virion.
R-HSA-380108. Chemokine receptors bind chemokines.
R-HSA-418594. G alpha (i) signalling events.
SignaLinkiP51681.
SIGNORiP51681.

Miscellaneous databases

EvolutionaryTraceiP51681.
GeneWikiiCCR5.
GenomeRNAii1234.
PROiP51681.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000160791.
ExpressionAtlasiP51681. baseline and differential.
GenevisibleiP51681. HS.

Family and domain databases

InterProiIPR002240. Chemokine_CCR5.
IPR000355. Chemokine_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00657. CCCHEMOKINER.
PR01110. CHEMOKINER5.
PR00237. GPCRRHODOPSN.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCCR5_HUMAN
AccessioniPrimary (citable) accession number: P51681
Secondary accession number(s): O14692
, O14693, O14695, O14696, O14697, O14698, O14699, O14700, O14701, O14702, O14703, O14704, O14705, O14706, O14707, O14708, O15538, Q9UPA4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 2, 2016
This is version 171 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. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  3. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  8. SIMILARITY comments
    Index of protein domains and families

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 one 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.