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CCR5 chemokine (C-C motif) receptor 5 (gene/pseudogene) [ Homo sapiens (human) ]

Gene ID: 1234, updated on 7-Dec-2014
Official Symbol
CCR5provided by HGNC
Official Full Name
chemokine (C-C motif) receptor 5 (gene/pseudogene)provided by HGNC
Primary source
HGNC:HGNC:1606
See related
HPRD:03223; MIM:601373
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Homo sapiens
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as
CKR5; CCR-5; CD195; CKR-5; CCCKR5; CMKBR5; IDDM22; CC-CKR-5
Summary
This gene encodes a member of the beta chemokine receptor family, which is predicted to be a seven transmembrane protein similar to G protein-coupled receptors. This protein is expressed by T cells and macrophages, and is known to be an important co-receptor for macrophage-tropic virus, including HIV, to enter host cells. Defective alleles of this gene have been associated with the HIV infection resistance. The ligands of this receptor include monocyte chemoattractant protein 2 (MCP-2), macrophage inflammatory protein 1 alpha (MIP-1 alpha), macrophage inflammatory protein 1 beta (MIP-1 beta) and regulated on activation normal T expressed and secreted protein (RANTES). Expression of this gene was also detected in a promyeloblastic cell line, suggesting that this protein may play a role in granulocyte lineage proliferation and differentiation. This gene is located at the chemokine receptor gene cluster region. Two transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Jul 2008]
See CCR5 in Epigenomics, MapViewer
Location:
3p21.31
Exon count:
3
Annotation release Status Assembly Chr Location
106 current GRCh38 (GCF_000001405.26) 3 NC_000003.12 (46370142..46376206)
105 previous assembly GRCh37.p13 (GCF_000001405.25) 3 NC_000003.11 (46411633..46417697)

Chromosome 3 - NC_000003.12Genomic Context describing neighboring genes Neighboring gene ubiquinol-cytochrome c reductase core protein II pseudogene 1 Neighboring gene uncharacterized LOC102724297 Neighboring gene chemokine (C-C motif) receptor 2 Neighboring gene chemokine (C-C motif) receptor-like 2 Neighboring gene lactotransferrin

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

Associated conditions

Description Tests
Diabetes mellitus, insulin-dependent, 22
MedGen: C2675864 OMIM: 612522 GeneReviews: Not available
Compare labs
Hepatitis c virus, susceptibility to
MedGen: C1835407 OMIM: 609532 GeneReviews: Not available
Compare labs
West nile virus, susceptibility to
MedGen: C1835867 OMIM: 610379 GeneReviews: Not available
Compare labs

NHGRI GWAS Catalog

Description
Multiple common variants for celiac disease influencing immune gene expression.
NHGRI GWA Catalog

Replication interactions

Interaction Pubs
Knockdown of chemokine (C-C motif) receptor 5 (CCR5) by siRNA inhibits HIV-1 replication in CD4+/CCR5+/CXCR4+ TZM-bl HeLa cells PubMed

Protein interactions

Protein Gene Interaction Pubs
Envelope surface glycoprotein gp120 env The CCR5 chemokine receptor is required for the entry of macrophage-tropic HIV-1 into target cells; the HIV-1 gp120-CD4 complex binds CCR5, which inhibits the binding of the natural CCR5 ligands macrophage inflammatory protein (MIP)-1alpha and MIP-1beta PubMed
env HIV-1 gp120 mutations S298N, F313L, and N403S result in weakening gp120's grip on gp41 rather than altering gp120 binding to specific CCR5 sites PubMed
env Peptides from a library inhibit HIV-1 replication in vitro through blocking of HIV-1 gp120 interaction with the co-receptor CCR5 PubMed
env Analysis of the distribution of V3 loop's net charge and flexibility in HIV-1 gp120 shows its selection more positive toward CXCR4 than CCR5 PubMed
env V1, V2, and V3 domains and N-linked glycosylation sites of HIV-1 gp120 confer coreceptor tropism; loss of an N-linked glycosylation site within V3 has a major influence on the virus switching from CCR5 to CXCR4 tropism in a V3 charge-dependent manner PubMed
env The specific amino acids 298-329 in the V3 loop of HIV-1 gp120 that determine cellular tropism also regulate chemokine coreceptor (CCR5 or CXCR4) preference for cell entry by the virus PubMed
env Interaction of the trimeric gp120 with CCR5 coreceptor triggers dendritic cells (DCs) to migrate between intestinal epithelial cells to sample virions and transfer infection to target cells PubMed
env Gelsolin overexpression impairs HIV-1 gp120-induced cortical F-actin reorganization and capping and gp120-mediated CD4-CCR5 and CD4-CXCR4 redistribution in permissive lymphocytes PubMed
env HIV-1 gp120 binds and signals through CD4, which leads to T cell activation with upregulation of the CXCR5, PD-1, Fas, and FasL expression PubMed
env HIV-1 gp120-induced dephosphorylation of KV2.1 and re-localization of KV2.1 on the soma and proximal dendrites results in disruption of the clustered KV2.1 via activation of CCR5/CXCR4 co-receptors or SDF-1 alpha treatment PubMed
env The V3 loop of brain-derived HIV-1 Env gp120 proteins significantly reduces the contact with N-terminal interface (Tyr10, Asn13, and Tyr14) of CCR5 as compared to lymph-node-derived gp120 proteins PubMed
env HIV-1 gp120/41 Envelope proteins form a complex with integrin alpha4beta7 and chemokine receptor CCR5 on the CD4-negative gamma-delta T cell membrane, which leads to activation of the p38-caspase pathway and induces the death of gamma-delta cells PubMed
env The coreceptor-binding site in HIV-1 gp120 is centered around an anti-parallel beta-sheet structure 'bridging sheet domain'; mutations in and adjacent to this domain have greater impact on CXCR4-mediated fusion than on CCR5-mediated fusion PubMed
env Antibodies to specific epitopes of HIV-1 gp120 block the interaction of CCR5 with the gp120/CD4 complex, suggesting that a CD4-mediated conformational change in gp120 is required for subsequent binding to CCR5 PubMed
env The binding of HIV-1 gp120 to CCR5 and entry of macrophage-tropic HIV-1 isolates into cells is blocked by CCR5 antagonists or the chemokine RANTES, which interacts with CCR5 PubMed
env Antibodies to specific epitopes of the CCR5 or CXCR4 chemokine receptors inhibit the entry of M-tropic, T-tropic, or dual-tropic HIV-1 into target cells by blocking the interaction of the receptors with the HIV-1 gp120/CD4 complex PubMed
env Binding of HIV-1 gp120 to CCR5 causes NHERF1-mediated activation of RhoA PubMed
env Stimulation of cells with HIV-1 gp120 induces the interaction of endogenous CCR5 with NHERF1, which enhances CCR5 internalization PubMed
env HIV-1 R5-tropic Env-mediated apoptosis of bystander cells is dependent on both CCR5 expression levels and fusogenic activity of the Env glycoprotein through the mechanism of apoptosis involved caspase-3 activation and mitochondrial depolarization PubMed
env NMR studies find the strong interaction of sulfated (CCR5)Tyr14 with (gp120)Arg440 PubMed
env The C-terminal region of CCR5 second extracellular loop (ECL2) comprising Cys178-Lys191 is sufficient for inhibition of HIV-1 entry by R5 and X4 strains. Peptides derived from ECL2 form a complex with HIV-1 gp120 PubMed
env Deaminases APOBEC3F- and APOBEC3G-mediated G-to-A mutations in the V3 region of HIV-1 gp120 lead to the co-receptor switch from R5 to X4 strains PubMed
env Genistein, tyrosine kinase inhibitor, inhibits cell fusion between macrophages and HIV-1 Env expressing cells. Genistein treatment does not change CD4 or CCR5 surface expression and has no effect on gp120-CD4-CCR5 complex formation PubMed
env HIV-1 gp120-induced PI3-kinase activity and calcium mobilization are inhibited by pertussis toxin and blocking antibodies directed against CCR5 and CXCR4, suggesting that this signaling is mediated through these chemokine receptors PubMed
env Sulfation of CCR5 by tyrosylprotein sulfotranferase-2 is crucial for mediating interaction with HIV-1 gp120. The pattern and the rate of sulfation for CCR5 depend on the number of amino acids N-terminal of Tyr-3 PubMed
env HIV-1 gp120-induced Ca(2+) fluxing is CD4 dependent and coreceptor specific, and is mediated by the CCR5 and CXCR4 coreceptors PubMed
env A single sulfotyrosine residue 14 in CCR5 is recognized by HIV-1 gp120 PubMed
env N362, a potential N-linked glycosylation site immediately N-terminal to CD4-binding site residues in the C3 region of gp120, contributes to fusogenicity of R5 Envs in a strain dependent manner PubMed
env Individual gp120-CD4 bonds undergo rapid destabilization and this destabilization is significantly enhanced by the coreceptor CCR5, not by CXCR4 PubMed
env CCR5 activation by gp120 triggers the assembly of endogenous Lyn, PI3K, and Pyk2 and is associated with PI3K and Pyk2 translocation from the cytoplasm to the membrane where they colocalized with Lyn PubMed
env HIV-1 gp120 induces IL-1beta release from macrophages in a time- and concentration-dependent manner through binding to the chemokine receptor CCR5 and coupling to G(i)alpha protein PubMed
env Introduction of G312V and A204E to multiple subtype A Envs and substitution of G312 and A204 with other residues increase CCR5-dependent entry into pig-tailed macaque lymphocytes PubMed
env Soluble HIV-1 gp120 protein induces CCR5 downregulation on activated CD4+ T-cells in HIV-infected individuals PubMed
env HIV-1 gp120 hydrogen bond interactions among transmembrane residues Y108, E283, and Y251, are crucial for HIV-1-gp120/sCD4 complex binding and HIV-1 fusion. HIV-1 gp120 binding to CCR5 disrupts these interhelix hydrogen bond interactions PubMed
env Maraviroc-resistant gp120 interacts much less efficiently with CCR5 and becomes critically dependent on the V3 loop-CCR5 N terminus and on positively charged elements of the drug-modified CCR5 extracellular loops 1 (His 88) and 2 (His 181) PubMed
env HIV-1-induced cell fusion is mediated by multiple regions within both the viral gp120 protein and the CCR5 coreceptor; dual-tropic virus isolates are less tolerant to changes in CCR5 than macrophage-tropic strains that have more restricted coreceptor use PubMed
env HIV-1 gp120 from a T-cell-tropic virus causes CD4-dependent antagonism of CXCR4 response to SDF-1alpha, whereas gp120 from macrophage-tropic viruses causes CD4-dependent antagonism of CCR5 response to MIP-1alpha PubMed
env HIV-1 gp120 induced cell death is inhibited by a CCR5-mediated neuroprotective pathway that involves protein kinase Akt/PKB as an essential component and can be triggered by the CCR5 agonists MIP-1beta and RANTES PubMed
env HIV-1 gp120-induced neuronal cell death involves p38 mitogen-activated protein kinase; both HIV-1 coreceptors, CCR5 and CXCR4, can mediate HIV-1 gp120-induced neurotoxicity PubMed
env The HIV-1 envelope protein gp120 from macrophage-tropic HIV and SIV induces a signal through CCR5 on CD4+ T cells and macrophages, and this gp120-mediated signal transduction induces chemotaxis of T cells PubMed
env In addition to the V3 loop of HIV-1 gp120, some conserved amino acid residues (117-123, 207, 419-422, and 438-441) are also involved in CCR5 chemokine receptor binding PubMed
env The amino-terminal residues (amino acids 1-25) and three extracellular loops (amino acids 88-102, 168-194, 261-277) of the CCR5 coreceptor are highly involved in its binding to gp120 from macrophage-tropic HIV-1 strains and in CCR5-mediated HIV-1 entry PubMed
env An adapted primary HIV-1 isolate, ADA, is able to replicate in CD4-negative cells expressing human CCR5; the gp120 glycoprotein of the adapted virus binds CCR5 directly, without prior interaction with CD4 PubMed
env Anti-CCR5 monoclonal antibodies efficiently prevent HIV-1 infection by inducing receptor dimerization, but not by interfering with HIV-1 gp120 binding to CCR5 PubMed
env Membrane fusion inhibitors inhibit HIV-1 infection in T cells by preventing gp120 interaction with CCR5 PubMed
env HIV-1 gp120 and alcohol increase the permeability of the blood-brain barrier (BBB) model, but do not result in a significant synergistic effect. Gp120 permeability involves chemokine receptor CCR5 PubMed
env HIV-1 gp120 and gp41-mediated virus-cell fusion is more dependent on viral core maturation for viruses bearing CXCR4-tropic gp120 than for those bearing CCR5-tropic gp120 PubMed
env The V3 domain of HIV-1 gp120 induces associations between CD4 and CCR5 receptors in cholesterol-rich microenvironments PubMed
env Stimulation of human monocyte-derived macrophages with HIV-1 gp120 results in the CCR5-mediated activation of Lyn and the concomitant Lyn-dependent activation of the mitogen-activated protein (MAP) kinase ERK-1/2, which leads to production of TNF-alpha PubMed
env A peptide fragment corresponding to the loop between the fifth and sixth transmembrane regions of the CCR5 receptor (amino acids 222-240) can inhibit HIV-1 infection of MT-4 cells, suggesting this region of CCR5 is involved with HIV-1 gp120 binding PubMed
env A synthetic peptide corresponding to amino acid residues 414-434 of HIV-1 gp120 downregulates the expression and function of chemokine receptors CCR5 and CXCR4 in monocytes by activating the 7-transmembrane G-protein-coupled receptor FPRL1/LXA4R PubMed
env Chemokines such as MCP-3 and MCP-2 that can compete with high affinity for MIP-1beta binding to CCR5 can also compete for monomeric HIV-1 gp120 binding to CCR5, although with variable potencies PubMed
env The chemokine receptor CCR5 is posttranslationally modified by sulfation of its N-terminal tyrosines; sulfated tyrosines contribute to the binding of CCR5 to MIP-1 alpha, MIP-1 beta, and HIV-1 gp120/CD4 complexes and to the ability of HIV-1 to enter cells PubMed
env N-formyl-methionyl-leucylphenyl-alanine binding to formyl peptide receptor (FPR) results in significant attenuation of cell responses to CCR5 ligands and in inhibition of HIV-1 gp120-mediated fusion and infection of cells expressing CD4, CCR5, and FPR PubMed
env HIV-1 gp120 from both CCR5- and CXCR4-tropic HIV-1 strains opens calcium-activated potassium (K(Ca)), chloride, and calcium-permeant nonselective cation channels in macrophages; these signals are mediated by CCR5 and CXCR4 PubMed
env AGP inhibits the binding of the HIV-1 gp120 consensus V3 domain (V3Cs) and macrophage inflammatory protein-1beta (MIP-1beta) to CCR5 on human monocyte-derived macrophages (MDM) PubMed
env CCR5 and CXCR4 coreceptor engagement by HIV-1 gp120 in primary macrophages activates 2 members of the mitogen-activated protein kinase (MAPK) superfamily, c-Jun amino-terminal kinase and p38 MAPK PubMed
env HIV-1 gp120 interactions with CXCR4 and CCR5 lead to the cross-desensitization of CCR6 and CCR7; this gp120-induced inhibition is strictly dependent on CXCR4 or CCR5 and lipid rafts but not on CD4 or V(H)3-expressing BCR PubMed
env Engagement of the CCR5 and CXCR4 receptors by HIV-1 gp120 induces tyrosine phosphorylation of the protein tyrosine kinase Pyk2 PubMed
Envelope surface glycoprotein gp160, precursor env Interaction of the trimeric gp140 with CCR5 coreceptor triggers dendritic cells (DCs) to migrate between intestinal epithelial cells to sample virions and transfer infection to target cells PubMed
Envelope transmembrane glycoprotein gp41 env HIV-1 gp120 and gp41 form a transitional complex with the CD4 receptor and CCR5/CXCR4 coreceptors during virus-cell and cell-cell membrane fusion PubMed
env HIV-1 gp120/41 Envelope proteins form a complex with integrin alpha4beta7 and chemokine receptor CCR5 on the CD4-negative gamma-delta T cell membrane, which leads to activation of the p38-caspase pathway and induces the death of gamma-delta cells PubMed
env HIV-1 R5-tropic Env-mediated apoptosis of bystander cells is dependent on both CCR5 expression levels and fusogenic activity of the Env glycoprotein through the mechanism of apoptosis involved caspase-3 activation and mitochondrial depolarization PubMed
env Sequences in the gp41 transmembrane (TM) can modulate coreceptor specificity and that Env sequences other than that of V3 may facilitate efficient CXCR4-mediated entry PubMed
env Peptide P5 (residues 628-683), comprising the entire membrane proximal region of HIV-1 gp41 and its calcium-binding site, inhibits HIV-1 envelope mediated cell-cell fusion and infection of PBMCs by both X4- and R5-tropic HIV-1 strains PubMed
env RANTES, MIP-1beta, and anti-CD4 antibodies inhibit CCR5-dependent cell-cell fusion mediated by HIV-1 gp120 and gp41 from macrophage-tropic isolates PubMed
env Secretion of IL-10 is upregulated by HIV-1 gp41 in monocytes through activation of cAMP/adenylate cyclase and p70 (S6)-kinase; up-regulation of IL-10 is paralleled by an enhanced expression of the chemokine receptor CCR5 PubMed
env HIV-1 gp41 activates innate host immune cells through FPRL1, and the activation of FPRL1 by gp41 further induces the phosphorylation of the chemokine receptor CCR5 PubMed
Nef nef HIV-1 Nef downregulates cell-surface levels of CCR5 in CHO cells expressing human CCR5; the Nef-induced downregulation of CCR5 is as efficient as the downregulation induced by the natural beta-chemokine ligand RANTES PubMed
nef HIV-1 Nef expression from unintegrated HIV-1 DNA downregulates the surface levels of CD4, CCR5, and CXCR4 on T-lymphocytes and monocytes PubMed
nef SH3 (PxxP motif) and PACS (E4) interaction surfaces as well as the myristoylation site (G2) in HIV-1 Nef are required for Nef-mediated downregulation of CCR5 PubMed
Tat tat HIV-1 Tat upregulates CCR5 expression on monocytes/macrophages but not on lymphocytes, indicating a role for Tat in HIV-1 pathogenesis and in promoting the infection of monocytes/macrophages. PubMed
tat Results from the treatment of microglia with HIV-1 Tat suggest downregulation of CCR5 mRNA expression by HIV-1 Tat, however this was deemed to not be significant PubMed
tat HIV-1 Tat is associated with upregulation of CCR5 and MIP-1alpha expression in nodular lesions found in HIV encephalopathy and progressive multifocal leukoencephalopathy (PML), indicating a role for Tat in HIV-1 pathogenesis PubMed
Vpr vpr HIV-1 Vpr depletes regulatory CD4+ T cells and enhances HIV-1 replication in a CCR5 coreceptor-dependent manner PubMed

Go to the HIV-1, Human Interaction Database

  • Binding and entry of HIV virion, organism-specific biosystem (from REACTOME)
    Binding and entry of HIV virion, organism-specific biosystemHIV enters cells by fusion at the cell surface, that results in a productive infection. The envelope (Env) protein of HIV mediates entry. Env is composed of a surface subunit, gp120, and a transmemb...
  • Chemokine receptors bind chemokines, organism-specific biosystem (from REACTOME)
    Chemokine receptors bind chemokines, organism-specific biosystemChemokine receptors are cytokine receptors found on the surface of certain cells, which interact with a type of cytokine called a chemokine. Following interaction, these receptors trigger a flux of i...
  • Chemokine signaling pathway, organism-specific biosystem (from KEGG)
    Chemokine signaling pathway, organism-specific biosystemInflammatory immune response requires the recruitment of leukocytes to the site of inflammation upon foreign insult. Chemokines are small chemoattractant peptides that provide directional cues for th...
  • Chemokine signaling pathway, conserved biosystem (from KEGG)
    Chemokine signaling pathway, conserved biosystemInflammatory immune response requires the recruitment of leukocytes to the site of inflammation upon foreign insult. Chemokines are small chemoattractant peptides that provide directional cues for th...
  • Class A/1 (Rhodopsin-like receptors), organism-specific biosystem (from REACTOME)
    Class A/1 (Rhodopsin-like receptors), organism-specific biosystemRhodopsin-like receptors (class A/1) are the largest group of GPCRs and are the best studied group from a functional and structural point of view. They show great diversity at the sequence level and ...
  • Cytokine-cytokine receptor interaction, organism-specific biosystem (from KEGG)
    Cytokine-cytokine receptor interaction, organism-specific biosystemCytokines are soluble extracellular proteins or glycoproteins that are crucial intercellular regulators and mobilizers of cells engaged in innate as well as adaptive inflammatory host defenses, cell ...
  • Cytokine-cytokine receptor interaction, conserved biosystem (from KEGG)
    Cytokine-cytokine receptor interaction, conserved biosystemCytokines are soluble extracellular proteins or glycoproteins that are crucial intercellular regulators and mobilizers of cells engaged in innate as well as adaptive inflammatory host defenses, cell ...
  • Disease, organism-specific biosystem (from REACTOME)
    Disease, organism-specific biosystemBiological processes are captured in Reactome by identifying the molecules (DNA, RNA, protein, small molecules) involved in them and describing the details of their interactions. From this molecular ...
  • Early Phase of HIV Life Cycle, organism-specific biosystem (from REACTOME)
    Early Phase of HIV Life Cycle, organism-specific biosystemIn the early phase of HIV lifecycle, an active virion binds and enters a target cell mainly by specific interactions of the viral envelope proteins with host cell surface receptors. The virion core...
  • Endocytosis, organism-specific biosystem (from KEGG)
    Endocytosis, organism-specific biosystemEndocytosis is a mechanism for cells to remove ligands, nutrients, and plasma membrane (PM) proteins, and lipids from the cell surface, bringing them into the cell interior. Transmembrane proteins en...
  • Endocytosis, conserved biosystem (from KEGG)
    Endocytosis, conserved biosystemEndocytosis is a mechanism for cells to remove ligands, nutrients, and plasma membrane (PM) proteins, and lipids from the cell surface, bringing them into the cell interior. Transmembrane proteins en...
  • G alpha (i) signalling events, organism-specific biosystem (from REACTOME)
    G alpha (i) signalling events, organism-specific biosystemThe classical signalling mechanism for G alpha (i) is inhibition of the cAMP dependent pathway through inhibition of adenylate cyclase. Decreased production of cAMP from ATP results in decreased act...
  • GPCR downstream signaling, organism-specific biosystem (from REACTOME)
    GPCR downstream signaling, organism-specific biosystemG protein-coupled receptors (GPCRs) are classically defined as the receptor, G-protein and downstream effectors, the alpha subunit of the G-protein being the primary signaling molecule. However, it h...
  • GPCR ligand binding, organism-specific biosystem (from REACTOME)
    GPCR ligand binding, organism-specific biosystemThere are more than 800 G-protein coupled receptor (GPCRs) in the human genome, making it the largest receptor superfamily. GPCRs are also the largest class of drug targets, involved in virtually all...
  • GPCRs, Class A Rhodopsin-like, organism-specific biosystem (from WikiPathways)
    GPCRs, Class A Rhodopsin-like, organism-specific biosystemThis pathway was created using the GPCRDB (Horn et al., 1998), http://www.cmbi.kun.nl/7tm/. The groupings are based on the GPCR phylogenetic tree available from the GPCRDB and the training sets used ...
  • GPCRs, Other, organism-specific biosystem (from WikiPathways)
    GPCRs, Other, organism-specific biosystemThis pathway was created using the GPCRDB (Horn et al., 1998), http://www.cmbi.kun.nl/7tm/. The groupings are based on the GPCR phylogenetic tree available from the GPCRDB and the training sets used ...
  • HIV Infection, organism-specific biosystem (from REACTOME)
    HIV Infection, organism-specific biosystemThe global pandemic of Human Immunodeficiency Virus (HIV) infection has resulted in tens of millions of people infected by the virus and millions more affected. UNAIDS estimates around 40 million ...
  • HIV Life Cycle, organism-specific biosystem (from REACTOME)
    HIV Life Cycle, organism-specific biosystemThe life cycle of HIV-1 is divided into early and late phases, shown schematically in the figure. In the early phase, an HIV-1 virion binds to receptors and co-receptors on the human host cell surfac...
  • IL12-mediated signaling events, organism-specific biosystem (from Pathway Interaction Database)
    IL12-mediated signaling events, organism-specific biosystem
    IL12-mediated signaling events
  • Peptide GPCRs, organism-specific biosystem (from WikiPathways)
    Peptide GPCRs, organism-specific biosystem
    Peptide GPCRs
  • Peptide ligand-binding receptors, organism-specific biosystem (from REACTOME)
    Peptide ligand-binding receptors, organism-specific biosystemThese receptors, a subset of the Class A/1 (Rhodopsin-like) family, all bind peptide ligands which include the chemokines, opioids and somatostatins.
  • Signal Transduction, organism-specific biosystem (from REACTOME)
    Signal Transduction, organism-specific biosystemSignal transduction is a process in which extracellular signals elicit changes in cell state and activity. Transmembrane receptors sense changes in the cellular environment by binding ligands, such a...
  • Signaling by GPCR, organism-specific biosystem (from REACTOME)
    Signaling by GPCR, organism-specific biosystemG protein-coupled receptors (GPCRs; 7TM receptors; seven transmembrane domain receptors; heptahelical receptors; G protein-linked receptors [GPLR]) are the largest family of transmembrane receptors i...
  • TCR Signaling Pathway, organism-specific biosystem (from WikiPathways)
    TCR Signaling Pathway, organism-specific biosystemThe T-cell antigen receptor (TCR) complex is composed of a ligand-binding subunit, the ? and ? chains, and a signaling subunit, namely the CD3?, ? and ? chains and the TCR? chain. This complex partic...
  • Toxoplasmosis, organism-specific biosystem (from KEGG)
    Toxoplasmosis, organism-specific biosystemToxoplasma gondii is an obligate intracellular parasite that is prevalent worldwide. The tachyzoite form acquired by oral ingestion downmodulates proinflammatory signaling pathways via various mechan...
  • Toxoplasmosis, conserved biosystem (from KEGG)
    Toxoplasmosis, conserved biosystemToxoplasma gondii is an obligate intracellular parasite that is prevalent worldwide. The tachyzoite form acquired by oral ingestion downmodulates proinflammatory signaling pathways via various mechan...
  • Viral carcinogenesis, organism-specific biosystem (from KEGG)
    Viral carcinogenesis, organism-specific biosystemThere is a strong association between viruses and the development of human malignancies. We now know that at least six human viruses, Epstein-Barr virus (EBV), hepatitis B virus (HBV), hepatitis C vi...
  • Viral carcinogenesis, conserved biosystem (from KEGG)
    Viral carcinogenesis, conserved biosystemThere is a strong association between viruses and the development of human malignancies. We now know that at least six human viruses, Epstein-Barr virus (EBV), hepatitis B virus (HBV), hepatitis C vi...
Products Interactant Other Gene Complex Source Pubs Description

Markers

Homology

Clone Names

  • FLJ78003

Gene Ontology Provided by GOA

Function Evidence Code Pubs
C-C chemokine binding IPI
Inferred from Physical Interaction
more info
PubMed 
C-C chemokine receptor activity IDA
Inferred from Direct Assay
more info
PubMed 
C-C chemokine receptor activity NAS
Non-traceable Author Statement
more info
PubMed 
actin binding IDA
Inferred from Direct Assay
more info
PubMed 
chemokine (C-C motif) ligand 5 binding IPI
Inferred from Physical Interaction
more info
PubMed 
chemokine receptor activity TAS
Traceable Author Statement
more info
PubMed 
coreceptor activity TAS
Traceable Author Statement
more info
PubMed 
phosphatidylinositol phospholipase C activity TAS
Traceable Author Statement
more info
PubMed 
protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
Process Evidence Code Pubs
G-protein coupled receptor signaling pathway IMP
Inferred from Mutant Phenotype
more info
PubMed 
MAPK cascade IEP
Inferred from Expression Pattern
more info
PubMed 
calcium ion transport IDA
Inferred from Direct Assay
more info
PubMed 
calcium-mediated signaling IDA
Inferred from Direct Assay
more info
PubMed 
cell surface receptor signaling pathway TAS
Traceable Author Statement
more info
PubMed 
cell-cell signaling IDA
Inferred from Direct Assay
more info
PubMed 
cellular defense response TAS
Traceable Author Statement
more info
PubMed 
cellular response to lipopolysaccharide IEP
Inferred from Expression Pattern
more info
PubMed 
chemokine-mediated signaling pathway IDA
Inferred from Direct Assay
more info
PubMed 
chemokine-mediated signaling pathway IEA
Inferred from Electronic Annotation
more info
 
chemokine-mediated signaling pathway NAS
Non-traceable Author Statement
more info
PubMed 
chemokine-mediated signaling pathway TAS
Traceable Author Statement
more info
PubMed 
chemotaxis TAS
Traceable Author Statement
more info
PubMed 
dendritic cell chemotaxis TAS
Traceable Author Statement
more info
PubMed 
entry into host cell TAS
Traceable Author Statement
more info
 
immune response IEA
Inferred from Electronic Annotation
more info
 
inflammatory response IEA
Inferred from Electronic Annotation
more info
 
positive regulation of cytosolic calcium ion concentration TAS
Traceable Author Statement
more info
PubMed 
release of sequestered calcium ion into cytosol by sarcoplasmic reticulum IDA
Inferred from Direct Assay
more info
PubMed 
response to cholesterol IMP
Inferred from Mutant Phenotype
more info
PubMed 
signaling IEP
Inferred from Expression Pattern
more info
PubMed 
viral process TAS
Traceable Author Statement
more info
 
Component Evidence Code Pubs
cell surface IDA
Inferred from Direct Assay
more info
PubMed 
cytoplasm TAS
Traceable Author Statement
more info
PubMed 
endosome IDA
Inferred from Direct Assay
more info
PubMed 
external side of plasma membrane IDA
Inferred from Direct Assay
more info
PubMed 
integral component of plasma membrane TAS
Traceable Author Statement
more info
PubMed 
plasma membrane TAS
Traceable Author Statement
more info
 
Preferred Names
C-C chemokine receptor type 5
Names
C-C chemokine receptor type 5
chemr13
HIV-1 fusion coreceptor
chemokine receptor CCR5
C-C motif chemokine receptor 5 A159A

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

Genomic

  1. NG_012637.1 

    Range
    5001..11065
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_000579.3NP_000570.1  C-C chemokine receptor type 5

    See proteins identical to NP_000570.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (A) represents the longer transcript. Both variants encode the same protein.
    Source sequence(s)
    AC098613, BC038398, DA818906, U54994
    Consensus CDS
    CCDS2739.1
    UniProtKB/Swiss-Prot
    P51681
    UniProtKB/TrEMBL
    Q38L21
    Conserved Domains (1) summary
    pfam00001
    Location:59297
    7tm_1; 7 transmembrane receptor (rhodopsin family)
  2. NM_001100168.1NP_001093638.1  C-C chemokine receptor type 5

    See proteins identical to NP_001093638.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (B) differs in the 5' UTR compared to variant A. Both variants encode the same protein.
    Source sequence(s)
    AC098613, BC038398, DA818906, U54994
    Consensus CDS
    CCDS2739.1
    UniProtKB/Swiss-Prot
    P51681
    UniProtKB/TrEMBL
    Q38L21
    Conserved Domains (1) summary
    pfam00001
    Location:59297
    7tm_1; 7 transmembrane receptor (rhodopsin family)

RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 106

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCh38 Primary Assembly

Genomic

  1. NC_000003.12 

    Range
    46370142..46376206
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    GenBank, FASTA, Sequence Viewer (Graphics)

Alternate CHM1_1.1

Genomic

  1. NC_018914.2 

    Range
    46361630..46367689
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    GenBank, FASTA, Sequence Viewer (Graphics)

Alternate HuRef

Genomic

  1. AC_000135.1 

    Range
    46455276..46461340
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    GenBank, FASTA, Sequence Viewer (Graphics)