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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Receptor for a number of inflammatory CC-chemokines including CCL3/MIP-1-alpha, CCL4/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.5 Publications
(Microbial infection) Acts as a coreceptor (CD4 being the primary receptor) of human immunodeficiency virus-1/HIV-1.5 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>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 binding Source: GO_Central
  • chemokine receptor activity Source: ProtInc
  • coreceptor activity Source: ProtInc
  • phosphatidylinositol phospholipase C activity Source: ProtInc
  • virus receptor activity Source: UniProtKB-KW

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionG-protein coupled receptor, Host cell receptor for virus entry, Receptor, Transducer
Biological processHost-virus interaction

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-173107 Binding and entry of HIV virion
R-HSA-380108 Chemokine receptors bind chemokines
R-HSA-418594 G alpha (i) signalling events
R-HSA-6783783 Interleukin-10 signaling

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P51681

SIGNOR Signaling Network Open Resource

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SIGNORi
P51681

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CCR5
Synonyms:CMKBR5
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000160791.13

Human Gene Nomenclature Database

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HGNCi
HGNC:1606 CCR5

Online Mendelian Inheritance in Man (OMIM)

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MIMi
601373 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P51681

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 30ExtracellularSequence analysisAdd BLAST30
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>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

Keywords - Cellular componenti

Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi3Y → D: No sulfation and greatly decreased binding of 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 of 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 of 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
Mutagenesisi20C → A: Decreases to 40% surface expression. No effect on conformational integrity. Disrupts binding of CCL4. Decreases cell HIV infection. 1 Publication1
Mutagenesisi101C → A: Decreases to 40% surface expression. Disrupts conformational integrity. Disrupts binding of CCL4. Decreases HIV cell infection. 1 Publication1
Mutagenesisi178C → A: Decreases to 40% surface expression. Disrupts conformational integrity. Disrupts binding of CCL4. Decreases HIV cell infection. 1 Publication1
Mutagenesisi269C → A: Decreases to 40% surface expression. No effect on conformational integrity. Disrupts binding of CCL4. Decreases cell HIV infection. 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

DisGeNET

More...
DisGeNETi
1234

MalaCards human disease database

More...
MalaCardsi
CCR5
MIMi609423 phenotype
610379 phenotype
612522 phenotype

Open Targets

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OpenTargetsi
ENSG00000160791

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
319269 Susceptibility/resistance to HIV infection

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA26170

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL274

Drug and drug target database

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DrugBanki
DB05501 AMD-070
DB05062 INCB9471
DB04835 Maraviroc

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
62

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
CCR5

Domain mapping of disease mutations (DMDM)

More...
DMDMi
1705896

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000692571 – 352C-C chemokine receptor type 5Add BLAST352

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei3Sulfotyrosine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi6O-linked (GalNAc...) serine1 Publication1
Glycosylationi7O-linked (GalNAc...) serine1 Publication1
Modified residuei10Sulfotyrosine1 Publication1
Modified residuei14Sulfotyrosine1 Publication1
Modified residuei15SulfotyrosineSequence analysis1
Glycosylationi16O-linked (GalNAc...) threonineSequence analysis1
Glycosylationi17O-linked (GalNAc...) serineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi20 ↔ 269Combined sources
Disulfide bondi101 ↔ 178PROSITE-ProRule annotationCombined sources
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P51681

PeptideAtlas

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PeptideAtlasi
P51681

PRoteomics IDEntifications database

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PRIDEi
P51681

ProteomicsDB human proteome resource

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ProteomicsDBi
56367

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P51681

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P51681

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P51681

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000160791 Expressed in 154 organ(s), highest expression level in visceral pleura

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P51681 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P51681 HS

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with PRAF2 (PubMed:15757671). 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 (PubMed:11733580, PubMed:8663314, PubMed:8699119, PubMed:10383387). Interacts with GRK2 (PubMed:10085131). Interacts with ARRB1 and ARRB2 (PubMed:11448957, PubMed:16144840). Interacts with CNIH4 (PubMed:24405750).9 Publications
(Microbial infection) Interacts with HIV-1 surface protein gp120.2 Publications
(Microbial infection) May interact with human cytomegalovirus/HHV-5 protein UL78.1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
107639, 17 interactors

Database of interacting proteins

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DIPi
DIP-5866N

Protein interaction database and analysis system

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IntActi
P51681, 14 interactors

Molecular INTeraction database

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MINTi
P51681

STRING: functional protein association networks

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STRINGi
9606.ENSP00000292303

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P51681

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1352
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P51681

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P51681

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P51681

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG3656 Eukaryota
ENOG410XRW9 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000154569

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG106917

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P51681

KEGG Orthology (KO)

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KOi
K04180

Identification of Orthologs from Complete Genome Data

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OMAi
FGNTMCQ

Database of Orthologous Groups

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OrthoDBi
EOG091G0B7A

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P51681

TreeFam database of animal gene trees

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TreeFami
TF330966

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR002240 Chemokine_CCR5
IPR000355 Chemokine_rcpt
IPR000276 GPCR_Rhodpsn
IPR017452 GPCR_Rhodpsn_7TM

Pfam protein domain database

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Pfami
View protein in Pfam
PF00001 7tm_1, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00657 CCCHEMOKINER
PR01110 CHEMOKINER5
PR00237 GPCRRHODOPSN

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00237 G_PROTEIN_RECEP_F1_1, 1 hit
PS50262 G_PROTEIN_RECEP_F1_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i88ECE1F38E6D45A7
GO

<p>This subsection of the ‘Sequence’ section provides information on polymorphic variants. If the variant is associated with a disease state, the description of the latter can be found in the <a href="http://www.uniprot.org/manual/involvement_in_disease">'Involvement in disease'</a> subsection.<p><a href='/help/polymorphism' target='_top'>More...</a></p>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.3 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
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>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 → L1 Publication1
Natural variantiVAR_02406720C → S1 PublicationCorresponds to variant dbSNP:rs145061115Ensembl.1
Natural variantiVAR_01183929A → S1 PublicationCorresponds to variant dbSNP:rs1800939Ensembl.1
Natural variantiVAR_00348231R → H in INCCR5-72A. Corresponds to variant dbSNP:rs56340326Ensembl.1
Natural variantiVAR_00348334P → L in TZCCR5-179. 1
Natural variantiVAR_02406842I → F1 Publication1
Natural variantiVAR_01184055L → Q2 PublicationsCorresponds to variant dbSNP:rs1799863Ensembl.1
Natural variantiVAR_01184160R → S Associated with susceptibility to HIV-1; reduced surface expression and function of CCR5 protein. 2 PublicationsCorresponds to variant dbSNP:rs1800940EnsemblClinVar.1
Natural variantiVAR_00348462K → R in UGCCR5-145B. 1
Natural variantiVAR_00348568Y → H in ZWCCR5-7. Corresponds to variant dbSNP:rs758090461Ensembl.1
Natural variantiVAR_02406973A → V1 PublicationCorresponds to variant dbSNP:rs56198941Ensembl.1
Natural variantiVAR_00348695D → N in MWCCR5-107. Corresponds to variant dbSNP:rs149975182Ensembl.1
Natural variantiVAR_00348797G → E in INCCR5-467. 1
Natural variantiVAR_080410106G → R Rare polymorphism; protects against HIV-1 infection; CD4+ T-cells from R-106 carriers are less susceptible to infection by HIV-1 R5; results in reduced CCR5 surface expression. 1 PublicationCorresponds to variant dbSNP:rs183662584Ensembl.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 Rare polymorphism; protects against HIV-1 infection; CD4+ T-cells from R-178 carriers are less susceptible to infection by HIV-1 R5; results in reduced CCR5 surface expression. 2 PublicationsCorresponds to variant dbSNP:rs199824195Ensembl.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 → L1 PublicationCorresponds to variant dbSNP:rs1017863136Ensembl.1
Natural variantiVAR_011842223R → Q2 PublicationsCorresponds to variant dbSNP:rs1800452EnsemblClinVar.1
Natural variantiVAR_024071228Missing 1 Publication1
Natural variantiVAR_003495239T → S in INCCR5-71A. 1
Natural variantiVAR_003496246L → P in UGCCR5-145A. Corresponds to variant dbSNP:rs143181119Ensembl.1
Natural variantiVAR_003497288T → M in INCCR5-72A. Corresponds to variant dbSNP:rs534088482Ensembl.1
Natural variantiVAR_011843301G → V1 PublicationCorresponds to variant dbSNP:rs1800943Ensembl.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 dbSNP:rs1800944EnsemblClinVar.1
Natural variantiVAR_003504339Y → F in TZCCR5-181A and MWCCR5-107. 2 PublicationsCorresponds to variant dbSNP:rs1800945Ensembl.1
Natural variantiVAR_003505345E → G in UGCCR5-145C. 1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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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

The Consensus CDS (CCDS) project

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CCDSi
CCDS2739.1

Protein sequence database of the Protein Information Resource

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PIRi
A43113

NCBI Reference Sequences

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RefSeqi
NP_000570.1, NM_000579.3
NP_001093638.1, NM_001100168.1

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.450802

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000292303; ENSP00000292303; ENSG00000160791
ENST00000445772; ENSP00000404881; ENSG00000160791

Database of genes from NCBI RefSeq genomes

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GeneIDi
1234

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:1234

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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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[»]
5UIWX-ray2.20A2-352[»]
5YD3X-ray1.35B/D/F/H11-19[»]
5YD4X-ray1.35B/D/F/H11-19[»]
5YD5X-ray1.96B/D11-19[»]
5YY4X-ray1.59B11-19[»]
6FGPNMR-A1-27[»]
ProteinModelPortaliP51681
SMRiP51681
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107639, 17 interactors
DIPiDIP-5866N
IntActiP51681, 14 interactors
MINTiP51681
STRINGi9606.ENSP00000292303

Chemistry databases

BindingDBiP51681
ChEMBLiCHEMBL274
DrugBankiDB05501 AMD-070
DB05062 INCB9471
DB04835 Maraviroc
GuidetoPHARMACOLOGYi62

Protein family/group databases

Information system for G protein-coupled receptors (GPCRs)

More...
GPCRDBi
Search...

PTM databases

iPTMnetiP51681
PhosphoSitePlusiP51681
SwissPalmiP51681

Polymorphism and mutation databases

BioMutaiCCR5
DMDMi1705896

Proteomic databases

PaxDbiP51681
PeptideAtlasiP51681
PRIDEiP51681
ProteomicsDBi56367

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1234
DisGeNETi1234
EuPathDBiHostDB:ENSG00000160791.13

GeneCards: human genes, protein and diseases

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GeneCardsi
CCR5
HGNCiHGNC:1606 CCR5
MalaCardsiCCR5
MIMi601373 gene
609423 phenotype
610379 phenotype
612522 phenotype
neXtProtiNX_P51681
OpenTargetsiENSG00000160791
Orphaneti319269 Susceptibility/resistance to HIV infection
PharmGKBiPA26170

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG3656 Eukaryota
ENOG410XRW9 LUCA
GeneTreeiENSGT00940000154569
HOVERGENiHBG106917
InParanoidiP51681
KOiK04180
OMAiFGNTMCQ
OrthoDBiEOG091G0B7A
PhylomeDBiP51681
TreeFamiTF330966

Enzyme and pathway databases

ReactomeiR-HSA-173107 Binding and entry of HIV virion
R-HSA-380108 Chemokine receptors bind chemokines
R-HSA-418594 G alpha (i) signalling events
R-HSA-6783783 Interleukin-10 signaling
SignaLinkiP51681
SIGNORiP51681

Miscellaneous databases

EvolutionaryTraceiP51681

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
CCR5

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
1234

Protein Ontology

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PROi
PR:P51681

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000160791 Expressed in 154 organ(s), highest expression level in visceral pleura
ExpressionAtlasiP51681 baseline and differential
GenevisibleiP51681 HS

Family and domain databases

InterProiView protein in InterPro
IPR002240 Chemokine_CCR5
IPR000355 Chemokine_rcpt
IPR000276 GPCR_Rhodpsn
IPR017452 GPCR_Rhodpsn_7TM
PfamiView protein in Pfam
PF00001 7tm_1, 1 hit
PRINTSiPR00657 CCCHEMOKINER
PR01110 CHEMOKINER5
PR00237 GPCRRHODOPSN
PROSITEiView protein in PROSITE
PS00237 G_PROTEIN_RECEP_F1_1, 1 hit
PS50262 G_PROTEIN_RECEP_F1_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCCR5_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>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
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: December 5, 2018
This is version 190 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  4. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  5. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  6. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  8. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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