Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P51681

- CCR5_HUMAN

UniProt

P51681 - CCR5_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

C-C chemokine receptor type 5

Gene

CCR5

Organism
Homo sapiens (Human)
Status
Reviewed - 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

GO - Molecular functioni

  1. actin binding Source: UniProtKB
  2. C-C chemokine binding Source: UniProtKB
  3. C-C chemokine receptor activity Source: UniProtKB
  4. chemokine (C-C motif) ligand 5 binding Source: UniProtKB
  5. chemokine receptor activity Source: ProtInc
  6. coreceptor activity Source: ProtInc
  7. phosphatidylinositol phospholipase C activity Source: ProtInc

GO - Biological processi

  1. calcium ion transport Source: UniProtKB
  2. calcium-mediated signaling Source: UniProtKB
  3. cell-cell signaling Source: UniProtKB
  4. cell surface receptor signaling pathway Source: ProtInc
  5. cellular defense response Source: ProtInc
  6. cellular response to lipopolysaccharide Source: UniProtKB
  7. chemokine-mediated signaling pathway Source: GOC
  8. chemotaxis Source: ProtInc
  9. dendritic cell chemotaxis Source: BHF-UCL
  10. entry into host cell Source: Reactome
  11. G-protein coupled receptor signaling pathway Source: UniProtKB
  12. immune response Source: ProtInc
  13. inflammatory response Source: ProtInc
  14. MAPK cascade Source: UniProtKB
  15. positive regulation of cytosolic calcium ion concentration Source: ProtInc
  16. release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: UniProtKB
  17. response to cholesterol Source: UniProtKB
  18. signaling Source: UniProtKB
  19. viral process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

ReactomeiREACT_15344. Chemokine receptors bind chemokines.
REACT_19231. G alpha (i) signalling events.
REACT_6903. Binding and entry of HIV virion.
SignaLinkiP51681.

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
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:1606. CCR5.

Subcellular locationi

Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

GO - Cellular componenti

  1. cell surface Source: UniProtKB
  2. cytoplasm Source: ProtInc
  3. endosome Source: UniProtKB
  4. external side of plasma membrane Source: UniProtKB
  5. integral component of plasma membrane Source: ProtInc
  6. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Diabetes mellitus, insulin-dependent, 22 (IDDM22) [MIM:612522]: A 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.1 Publication
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi3 – 31Y → 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 Publications
Mutagenesisi3 – 31Y → F: No sulfation and greatly decreases binding of CCL4 and CCL5; when associated with F-10; F-14 and F-15. 2 Publications
Mutagenesisi6 – 61S → 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 Publication
Mutagenesisi7 – 71S → 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 Publication
Mutagenesisi10 – 101Y → 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 Publications
Mutagenesisi14 – 141Y → 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 Publications
Mutagenesisi14 – 141Y → 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 Publications
Mutagenesisi15 – 151Y → 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 Publications
Mutagenesisi15 – 151Y → 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 Publications
Mutagenesisi16 – 161T → A: Similar decrease in molecular mass when treated with O-glycosidase as for wild type; when associated with A-17. 1 Publication
Mutagenesisi17 – 171S → A: Similar decrease in molecular mass when treated with O-glycosidase as for wild type; when associated with A-16. 1 Publication
Mutagenesisi321 – 3211C → 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 Publication
Mutagenesisi323 – 3231C → 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 Publication
Mutagenesisi324 – 3241C → 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 Publication
Mutagenesisi336 – 3361S → 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 Publications
Mutagenesisi337 – 3371S → 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 Publications
Mutagenesisi342 – 3421S → 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 Publications
Mutagenesisi349 – 3491S → 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 Publications

Keywords - Diseasei

Diabetes mellitus

Organism-specific databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 352352C-C chemokine receptor type 5PRO_0000069257Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31Sulfotyrosine1 Publication
Glycosylationi6 – 61O-linked (GalNAc...)1 Publication
Glycosylationi7 – 71O-linked (GalNAc...)1 Publication
Modified residuei10 – 101Sulfotyrosine1 Publication
Modified residuei14 – 141Sulfotyrosine1 Publication
Modified residuei15 – 151SulfotyrosineSequence Analysis
Glycosylationi16 – 161O-linked (GalNAc...)Sequence Analysis
Glycosylationi17 – 171O-linked (GalNAc...)Sequence Analysis
Disulfide bondi101 ↔ 178PROSITE-ProRule annotation
Lipidationi321 – 3211S-palmitoyl cysteine1 Publication
Lipidationi323 – 3231S-palmitoyl cysteine1 Publication
Lipidationi324 – 3241S-palmitoyl cysteine1 Publication
Modified residuei336 – 3361Phosphoserine; by BARK11 Publication
Modified residuei337 – 3371Phosphoserine; by BARK11 Publication
Modified residuei342 – 3421Phosphoserine; by BARK11 Publication
Modified residuei349 – 3491Phosphoserine; by BARK11 Publication

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.
PRIDEiP51681.

PTM databases

PhosphoSiteiP51681.

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

Gene expression databases

BgeeiP51681.
ExpressionAtlasiP51681. baseline and differential.
GenevestigatoriP51681.

Interactioni

Subunit structurei

Interacts with PRAF2. Interacts with HIV-1 surface protein gp120. 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 ADRBK1. Interacts with ARRB1 and ARRB2. Interacts with human cytomegalovirus/HHV-5 protein UL78.10 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi107639. 17 interactions.
DIPiDIP-5866N.
IntActiP51681. 11 interactions.
MINTiMINT-103024.

Structurei

Secondary structure

1
352
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 134Combined sources
Helixi14 – 174Combined sources
Turni20 – 223Combined sources
Helixi26 – 5732Combined sources
Helixi64 – 9128Combined sources
Helixi98 – 13134Combined sources
Helixi133 – 1397Combined sources
Helixi142 – 16524Combined sources
Beta strandi167 – 1726Combined sources
Beta strandi175 – 1806Combined sources
Helixi187 – 20216Combined sources
Helixi204 – 22320Combined sources
Helixi229 – 2324Combined sources
Helixi234 – 25926Combined sources
Helixi261 – 2644Combined sources
Helixi269 – 28820Combined sources
Helixi289 – 2913Combined sources
Helixi293 – 3008Combined sources
Helixi302 – 31211Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ND8model-A1-352[»]
1NE0model-A1-352[»]
1OPNmodel-A1-352[»]
1OPTmodel-A1-352[»]
1OPWmodel-A1-352[»]
2L87NMR-A1-27[»]
2RLLNMR-A7-15[»]
2RRSNMR-A157-174[»]
4MBSX-ray2.71A/B3-223[»]
ProteinModelPortaliP51681.
SMRiP51681. Positions 19-313.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51681.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3030ExtracellularSequence AnalysisAdd
BLAST
Topological domaini59 – 6810CytoplasmicSequence Analysis
Topological domaini90 – 10213ExtracellularSequence AnalysisAdd
BLAST
Topological domaini125 – 14117CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini167 – 19832ExtracellularSequence AnalysisAdd
BLAST
Topological domaini219 – 23517CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini261 – 27717ExtracellularSequence AnalysisAdd
BLAST
Topological domaini302 – 35251CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei31 – 5828Helical; Name=1Sequence AnalysisAdd
BLAST
Transmembranei69 – 8921Helical; Name=2Sequence AnalysisAdd
BLAST
Transmembranei103 – 12422Helical; Name=3Sequence AnalysisAdd
BLAST
Transmembranei142 – 16625Helical; Name=4Sequence AnalysisAdd
BLAST
Transmembranei199 – 21820Helical; Name=5Sequence AnalysisAdd
BLAST
Transmembranei236 – 26025Helical; Name=6Sequence AnalysisAdd
BLAST
Transmembranei278 – 30124Helical; Name=7Sequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG148353.
HOVERGENiHBG106917.
InParanoidiP51681.
KOiK04180.
OMAiIIFTRSQ.
OrthoDBiEOG738051.
PhylomeDBiP51681.
TreeFamiTF330966.

Family and domain databases

Gene3Di1.20.1070.10. 1 hit.
InterProiIPR002240. Chemokine_CCR5.
IPR000355. Chemokine_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERiPTHR24227. PTHR24227. 1 hit.
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.
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.
Variations in CCR5 are associated with susceptibility to West Nile virus (WNV) infection [MIMi:610379].

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti10 – 101Y → D in INCCR5-71A) (No 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.
VAR_003481
Natural varianti12 – 121I → L.1 Publication
VAR_024066
Natural varianti20 – 201C → S.1 Publication
VAR_024067
Natural varianti29 – 291A → S.1 Publication
Corresponds to variant rs1800939 [ dbSNP | Ensembl ].
VAR_011839
Natural varianti31 – 311R → H in INCCR5-72A.
Corresponds to variant rs56340326 [ dbSNP | Ensembl ].
VAR_003482
Natural varianti34 – 341P → L in TZCCR5-179.
VAR_003483
Natural varianti42 – 421I → F.1 Publication
VAR_024068
Natural varianti55 – 551L → Q.2 Publications
Corresponds to variant rs1799863 [ dbSNP | Ensembl ].
VAR_011840
Natural varianti60 – 601R → S Associated with susceptibility to HIV-1; reduced surface expression and function of CCR5 protein. 1 Publication
Corresponds to variant rs1800940 [ dbSNP | Ensembl ].
VAR_011841
Natural varianti62 – 621K → R in UGCCR5-145B.
VAR_003484
Natural varianti68 – 681Y → H in ZWCCR5-7.
VAR_003485
Natural varianti73 – 731A → V.1 Publication
Corresponds to variant rs56198941 [ dbSNP | Ensembl ].
VAR_024069
Natural varianti95 – 951D → N in MWCCR5-107.
VAR_003486
Natural varianti97 – 971G → E in INCCR5-467.
VAR_003487
Natural varianti122 – 1221L → P in ZWCCR5-7.
VAR_003488
Natural varianti158 – 1581F → S in UGCCR5-145A.
VAR_003489
Natural varianti176 – 1761Y → C in KECCR5-116.
VAR_003490
Natural varianti177 – 1771T → A in INCCR5-45C.
VAR_003491
Natural varianti178 – 1781C → R Found in a HIV-resistant individiual. 1 Publication
Corresponds to variant rs199824195 [ dbSNP | Ensembl ].
VAR_012481
Natural varianti185 – 1851S → N in UGCCR5-145A.
VAR_003492
Natural varianti210 – 2101M → V in ZWCCR5-7.
VAR_003493
Natural varianti214 – 2141Y → C in KECCR5-3B.
VAR_003494
Natural varianti215 – 2151S → L.1 Publication
VAR_024070
Natural varianti223 – 2231R → Q.2 Publications
Corresponds to variant rs1800452 [ dbSNP | Ensembl ].
VAR_011842
Natural varianti228 – 2281Missing.1 Publication
VAR_024071
Natural varianti239 – 2391T → S in INCCR5-71A.
VAR_003495
Natural varianti246 – 2461L → P in UGCCR5-145A.
VAR_003496
Natural varianti288 – 2881T → M in INCCR5-72A.
VAR_003497
Natural varianti301 – 3011G → V.1 Publication
Corresponds to variant rs1800943 [ dbSNP | Ensembl ].
VAR_011843
Natural varianti302 – 3021E → G in TZCCR5-179.
VAR_003498
Natural varianti303 – 3031K → E in THCCR5-5.
VAR_003499
Natural varianti306 – 3061N → S in MWCCR5-1567.
VAR_003500
Natural varianti322 – 3221K → R in THCCR5-5.
VAR_003501
Natural varianti333 – 3331E → G in THCCR5-2.
VAR_003502
Natural varianti335 – 3351A → V in MWCCR5-1567, MWCCR5-1568, ZWCCR5-14 and ZWCCR5-112. 2 Publications
Corresponds to variant rs1800944 [ dbSNP | Ensembl ].
VAR_003503
Natural varianti339 – 3391Y → F in TZCCR5-181A and MWCCR5-107. 2 Publications
Corresponds to variant rs1800945 [ dbSNP | Ensembl ].
VAR_003504
Natural varianti345 – 3451E → G in UGCCR5-145C.
VAR_003505

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
UCSCiuc003cpo.4. human.

Polymorphism databases

DMDMi1705896.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

CC chemokine receptors entry

Wikipedia

CCR5 receptor entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS2739.1.
PIRi A43113.
RefSeqi NP_000570.1. NM_000579.3.
NP_001093638.1. NM_001100168.1.
UniGenei Hs.450802.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ND8 model - A 1-352 [» ]
1NE0 model - A 1-352 [» ]
1OPN model - A 1-352 [» ]
1OPT model - A 1-352 [» ]
1OPW model - A 1-352 [» ]
2L87 NMR - A 1-27 [» ]
2RLL NMR - A 7-15 [» ]
2RRS NMR - A 157-174 [» ]
4MBS X-ray 2.71 A/B 3-223 [» ]
ProteinModelPortali P51681.
SMRi P51681. Positions 19-313.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107639. 17 interactions.
DIPi DIP-5866N.
IntActi P51681. 11 interactions.
MINTi MINT-103024.

Chemistry

BindingDBi P51681.
ChEMBLi CHEMBL274.
DrugBanki DB04835. Maraviroc.
GuidetoPHARMACOLOGYi 62.

Protein family/group databases

GPCRDBi Search...

PTM databases

PhosphoSitei P51681.

Polymorphism databases

DMDMi 1705896.

Proteomic databases

PaxDbi P51681.
PRIDEi P51681.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000292303 ; ENSP00000292303 ; ENSG00000160791 .
ENST00000445772 ; ENSP00000404881 ; ENSG00000160791 .
GeneIDi 1234.
KEGGi hsa:1234.
UCSCi uc003cpo.4. human.

Organism-specific databases

CTDi 1234.
GeneCardsi GC03P046386.
HGNCi HGNC:1606. CCR5.
MIMi 601373. gene.
609423. phenotype.
610379. phenotype.
612522. phenotype.
neXtProti NX_P51681.
Orphaneti 319269. Susceptibility/resistance to HIV infection.
PharmGKBi PA26170.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG148353.
HOVERGENi HBG106917.
InParanoidi P51681.
KOi K04180.
OMAi IIFTRSQ.
OrthoDBi EOG738051.
PhylomeDBi P51681.
TreeFami TF330966.

Enzyme and pathway databases

Reactomei REACT_15344. Chemokine receptors bind chemokines.
REACT_19231. G alpha (i) signalling events.
REACT_6903. Binding and entry of HIV virion.
SignaLinki P51681.

Miscellaneous databases

EvolutionaryTracei P51681.
GeneWikii CCR5.
GenomeRNAii 1234.
NextBioi 5035.
PROi P51681.
SOURCEi Search...

Gene expression databases

Bgeei P51681.
ExpressionAtlasi P51681. baseline and differential.
Genevestigatori P51681.

Family and domain databases

Gene3Di 1.20.1070.10. 1 hit.
InterProi IPR002240. Chemokine_CCR5.
IPR000355. Chemokine_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view ]
PANTHERi PTHR24227. PTHR24227. 1 hit.
Pfami PF00001. 7tm_1. 1 hit.
[Graphical view ]
PRINTSi PR00657. CCCHEMOKINER.
PR01110. CHEMOKINER5.
PR00237. GPCRRHODOPSN.
PROSITEi PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and functional expression of a new human CC-chemokine receptor gene."
    Samson M., Labbe O., Mollereau C., Vassart G., Parmentier M.
    Biochemistry 35:3362-3367(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY.
  2. "Molecular cloning and functional characterization of a novel human CC chemokine receptor (CCR5) for RANTES, MIP-1beta, and MIP-1alpha."
    Raport C.J., Gosling J., Schweichart V.L., Gray P.W., Charo I.F.
    J. Biol. Chem. 271:17161-17166(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CCL4 AND CCL5, TISSUE SPECIFICITY.
    Tissue: Macrophage.
  3. "Cloning and functional expression of CC CKR5, a human monocyte CC chemokine receptor selective for MIP-1(alpha), MIP-1(beta), and RANTES."
    Combadiere C., Ahuja S.K., Tiffany H.L., Murphy P.M.
    J. Leukoc. Biol. 60:147-152(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CCL3; CCL4 AND CCL5.
  4. "Polymorphisms in the CCR5 genes of African green monkeys and mice implicate specific amino acids in infections by simian and human immunodeficiency viruses."
    Kuhmann S.E., Platt E.J., Kozak S.L., Kabat D.
    J. Virol. 71:8642-8656(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [MRNA], POLYMORPHISM.
  6. "The human CC chemokine receptor 5 (CCR5) gene. Multiple transcripts with 5'-end heterogeneity, dual promoter usage, and evidence for polymorphisms within the regulatory regions and noncoding exons."
    Mummidi S., Ahuja S.S., McDaniel B.L., Ahuja S.K.
    J. Biol. Chem. 272:30662-30671(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. Magierowska M., Barre-Sinoussi F., Issafras H., Theodorou I., Debre P.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-178.
  8. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
    Kopatz S.A., Aronstam R.S., Sharma S.V.
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  9. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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].
  11. Cited for: FUNCTION AS A HIV-1 CORECEPTOR.
  12. Cited for: FUNCTION AS A HIV-1 CORECEPTOR.
  13. "A conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding."
    Rizzuto C.D., Wyatt R., Hernandez-Ramos N., Sun Y., Kwong P.D., Hendrickson W.A., Sodroski J.
    Science 280:1949-1953(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 SURFACE PROTEIN GP120.
  14. "Tyrosine sulfation of the amino terminus of CCR5 facilitates HIV-1 entry."
    Farzan M., Mirzabekov T., Kolchinsky P., Wyatt R., Cayabyab M., Gerard N.P., Gerard C., Sodroski J., Choe H.
    Cell 96:667-676(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SULFATION AT TYR-3, GLYCOSYLATION, MUTAGENESIS OF TYR-3; TYR-10; TYR-14 AND TYR-15.
  15. "Differential effects of CC chemokines on CC chemokine receptor 5 (CCR5) phosphorylation and identification of phosphorylation sites on the CCR5 carboxyl terminus."
    Oppermann M., Mack M., Proudfoot A.E., Olbrich H.
    J. Biol. Chem. 274:8875-8885(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-336; SER-337; SER-342 AND SER-349, MUTAGENESIS OF SER-336; SER-337; SER-342 AND SER-349, INTERACTION WITH ADRBK1.
  16. "Palmitoylation of CCR5 is critical for receptor trafficking and efficient activation of intracellular signaling pathways."
    Blanpain C., Wittamer V., Vanderwinden J.-M., Boom A., Renneboog B., Lee B., Le Poul E., El Asmar L., Govaerts C., Vassart G., Doms R.W., Parmentier M.
    J. Biol. Chem. 276:23795-23804(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION AT CYS-321; CYS-323 AND CYS-324, SUBCELLULAR LOCATION, FUNCTION, MUTAGENESIS OF CYS-321; CYS-323 AND CYS-324.
  17. "Characterization of sequence determinants within the carboxyl-terminal domain of chemokine receptor CCR5 that regulate signaling and receptor internalization."
    Kraft K., Olbrich H., Majoul I., Mack M., Proudfoot A., Oppermann M.
    J. Biol. Chem. 276:34408-34418(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARRB2, MUTAGENESIS OF SER-336; SER-337; SER-342 AND SER-349.
  18. "Sialylated O-glycans and sulfated tyrosines in the NH2-terminal domain of CC chemokine receptor 5 contribute to high affinity binding of chemokines."
    Bannert N., Craig S., Farzan M., Sogah D., Santo N.V., Choe H., Sodroski J.
    J. Exp. Med. 194:1661-1673(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SULFATION, GLYCOSYLATION AT SER-6, INTERACTION WITH CCL3; CCL4 AND CCL5, MUTAGENESIS OF TYR-3; SER-6; SER-7; TYR-10; TYR-14; TYR-15; THR-16 AND SER-17, CHARACTERIZATION OF VARIANT ASP-10.
  19. "JM4 is a four-transmembrane protein binding to the CCR5 receptor."
    Schweneker M., Bachmann A.S., Moelling K.
    FEBS Lett. 579:1751-1758(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRAF2.
  20. "G protein-coupled receptor kinases promote phosphorylation and beta-arrestin-mediated internalization of CCR5 homo- and hetero-oligomers."
    Huettenrauch F., Pollok-Kopp B., Oppermann M.
    J. Biol. Chem. 280:37503-37515(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ARRB1 AND ARRB2.
  21. "CCR5 deficiency increases risk of symptomatic West Nile virus infection."
    Glass W.G., McDermott D.H., Lim J.K., Lekhong S., Yu S.F., Frank W.A., Pape J., Cheshier R.C., Murphy P.M.
    J. Exp. Med. 203:35-40(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN WEST NILE VIRUS INFECTION SUSCEPTIBILITY.
  22. "Human cytomegalovirus-encoded UL33 and UL78 heteromerize with host CCR5 and CXCR4 impairing their HIV coreceptor activity."
    Tadagaki K., Tudor D., Gbahou F., Tschische P., Waldhoer M., Bomsel M., Jockers R., Kamal M.
    Blood 119:4908-4918(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HHV-5 PROTEIN UL78.
  23. "Structure modeling of the chemokine receptor CCR5: implications for ligand binding and selectivity."
    Paterlini M.G.
    Biophys. J. 83:3012-3031(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.
  24. "Structural and functional characterization of the human CCR5 receptor in complex with HIV gp120 envelope glycoprotein and CD4 receptor by molecular modeling studies."
    Liu S., Fan S., Sun Z.
    J. Mol. Model. 9:329-336(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: 3D-STRUCTURE MODELING.
  25. "The conformation and orientation of a 27-residue CCR5 peptide in a ternary complex with HIV-1 gp120 and a CD4-mimic peptide."
    Schnur E., Noah E., Ayzenshtat I., Sargsyan H., Inui T., Ding F.X., Arshava B., Sagi Y., Kessler N., Levy R., Scherf T., Naider F., Anglister J.
    J. Mol. Biol. 410:778-797(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-27 IN COMPLEX WITH HIV-1 GP120 AND CD4 MIMIC PEPTIDE, SULFATION AT TYR-10 AND TYR-14.
  26. Cited for: VARIANTS GLN-55; LEU-215; GLN-223; VAL-335 AND PHE-339.
  27. Cited for: VARIANTS LEU-12; SER-20; SER-29; PHE-42; GLN-55; SER-60; VAL-73; GLN-223; LYS-228 DEL; VAL-301; VAL-335 AND PHE-339, ASSOCIATION WITH SUSCEPTIBILITY TO HIV-1.
  28. "A homologous naturally occurring mutation in Duffy and CCR5 leading to reduced receptor expression."
    Tamasauskas D., Powell V., Saksela K., Yazdanbakhsh K.
    Blood 97:3651-3654(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT SER-60.
  29. Cited for: INVOLVEMENT IN IDDM22.

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: October 29, 2014
This is version 151 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

External Data

Dasty 3