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UniProtKB - P61073 (CXCR4_HUMAN)

Entry version 173 (10 Apr 2019)
Sequence version 1 (26 Apr 2004)
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Protein

C-X-C chemokine receptor type 4

Gene

CXCR4

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 the C-X-C chemokine CXCL12/SDF-1 that transduces a signal by increasing intracellular calcium ion levels and enhancing MAPK1/MAPK3 activation (PubMed:10452968, PubMed:28978524, PubMed:18799424, PubMed:24912431). Involved in the AKT signaling cascade (PubMed:24912431). Plays a role in regulation of cell migration, e.g. during wound healing (PubMed:28978524). Acts as a receptor for extracellular ubiquitin; leading to enhanced intracellular calcium ions and reduced cellular cAMP levels (PubMed:20228059). Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11276205). Involved in hematopoiesis and in cardiac ventricular septum formation. Also plays an essential role in vascularization of the gastrointestinal tract, probably by regulating vascular branching and/or remodeling processes in endothelial cells. Involved in cerebellar development. In the CNS, could mediate hippocampal-neuron survival (By similarity).By similarity14 Publications
(Microbial infection) Acts as a coreceptor (CD4 being the primary receptor) for human immunodeficiency virus-1/HIV-1 X4 isolates and as a primary receptor for some HIV-2 isolates. Promotes Env-mediated fusion of the virus (PubMed:8849450, PubMed:8929542, PubMed:9427609, PubMed:10074122, PubMed:10756055).5 Publications

Miscellaneous

Plerixafor (AMD3100), an antagonist of CXCR4 activity, blocks HIV-1 entry, interaction with CXCL12 and subsequent CXCR4 signaling.

Caution

Was originally thought to be a receptor for neuropeptide Y type 3 (NPY3R) (NPY3-R) (PubMed:8329116 and PubMed:8234909). Later reports showed that it acts as a receptor for the C-X-C chemokine CXCL12/SDF-1 (PubMed:9427609, PubMed:10825158, PubMed:12034737).2 Publications3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei171Chemokine1
Binding sitei288Chemokine1 Publication1 Publication1

<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

View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

<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-376176 Signaling by ROBO receptors
R-HSA-380108 Chemokine receptors bind chemokines
R-HSA-418594 G alpha (i) signalling events

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

More...SignaLinki		P61073

SIGNOR Signaling Network Open Resource

More...SIGNORi		P61073

Protein family/group databases

Transport Classification Database

More...TCDBi		9.A.14.13.17 the g-protein-coupled receptor (gpcr) family

<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-X-C chemokine receptor type 4
Short name:
CXC-R4
Short name:
CXCR-4
Alternative name(s):
FB22
Fusin
HM89
LCR1
Leukocyte-derived seven transmembrane domain receptor
Short name:
LESTR1 Publication
Lipopolysaccharide-associated protein 3
Short name:
LAP-3
Short name:
LPS-associated protein 3
NPYRL
Stromal cell-derived factor 1 receptor
Short name:
SDF-1 receptor
CD_antigen: CD184
<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:CXCR4
<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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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 2

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000121966.6

Human Gene Nomenclature Database

More...HGNCi		HGNC:2561 CXCR4

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		162643 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P61073

<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 & Seán O’Donoghue; 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 – 38Extracellular1 PublicationAdd BLAST38
<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>Transmembranei39 – 63Helical; Name=11 PublicationAdd BLAST25
Topological domaini64 – 77Cytoplasmic1 PublicationAdd BLAST14
Transmembranei78 – 99Helical; Name=21 PublicationAdd BLAST22
Topological domaini100 – 110Extracellular1 PublicationAdd BLAST11
Transmembranei111 – 130Helical; Name=31 PublicationAdd BLAST20
Topological domaini131 – 154Cytoplasmic1 PublicationAdd BLAST24
Transmembranei155 – 174Helical; Name=41 PublicationAdd BLAST20
Topological domaini175 – 195Extracellular1 PublicationAdd BLAST21
Transmembranei196 – 216Helical; Name=51 PublicationAdd BLAST21
Topological domaini217 – 241Cytoplasmic1 PublicationAdd BLAST25
Transmembranei242 – 261Helical; Name=61 PublicationAdd BLAST20
Topological domaini262 – 282Extracellular1 PublicationAdd BLAST21
Transmembranei283 – 302Helical; Name=71 PublicationAdd BLAST20
Topological domaini303 – 352Cytoplasmic1 PublicationAdd BLAST50

Keywords - Cellular componenti

Cell junction, Cell membrane, Endosome, Lysosome, 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

WHIM syndrome (WHIMS)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionImmunodeficiency disease characterized by neutropenia, hypogammaglobulinemia and extensive human papillomavirus (HPV) infection. Despite the peripheral neutropenia, bone marrow aspirates from affected individuals contain abundant mature myeloid cells, a condition termed myelokathexis.
See also OMIM:193670
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_081113334 – 352Missing in WHIMS; also found in patients with Waldenstroem macroglobulinemia; somatic mutation. 2 PublicationsAdd BLAST19
Natural variantiVAR_081114338 – 352Missing in WHIMS; common somatic mutation in patients with Waldenstroem macroglobulinemia; results in decreased CXCL12-triggered receptor internalization; enhanced AKT and MAPK signaling activation; confers resistance to ibrutinib-triggered apoptosis. 4 PublicationsAdd BLAST15
Natural variantiVAR_081115343 – 352Missing in WHIMS. 1 Publication10
CXCR4 mutations play a role in the pathogenesis of Waldenstroem macroglobulinemia (WM) and influence disease presentation and outcome, as well as response to therapy. WM is a B-cell lymphoma characterized by accumulation of malignant lymphoplasmacytic cells in the bone marrow, lymph nodes and spleen, and hypersecretion of monoclonal immunoglobulin M (IgM). Excess IgM production results in serum hyperviscosity, tissue infiltration, and autoimmune-related pathology.2 Publications

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>Mutagenesisi2 – 9Missing : Reduced CXCL12 binding. Abolishes signaling. 1 Publication8
Mutagenesisi4 – 20Missing : Reduced CXCL12 binding. Impaired signaling. Reduced coreceptor activity for HIV-1 isolates LAI and NDK. 1 PublicationAdd BLAST17
Mutagenesisi7Y → A: Reduced coreceptor activity for HIV-1 isolates LAI and NDK. Greatly reduced coreceptor activity for HIV-1 isolates LAI and NDK; when associated with A-12. 2 Publications1
Mutagenesisi7Y → F: Sulfate incorporation greatly reduced; when associated with F-12 and F-21. Moderate reduction in sulfate incorporation; when associated with F-12 and A-18. No sulfate incorporation and binding SDF-1alpha greatly reduced; when associated with F-12; A-18 and F-21. 2 Publications1
Mutagenesisi8T → A: No effect on sulfate incorporation; when associated with A-9 and A-13. 1 Publication1
Mutagenesisi9S → A: No effect on sulfate incorporation; when associated with A-8 and A-13. 1 Publication1
Mutagenesisi10 – 20Missing : Reduced CXCL12 binding. No effect on signaling. 1 PublicationAdd BLAST11
Mutagenesisi11N → A: Reduced molecular weight. Enhanced coreceptor activity on R5 HIV-1 isolate Envs. Slight further enhancement of coreceptor activity; when associated with A-13. 1 Publication1
Mutagenesisi12Y → A: Greatly reduced coreceptor activity for HIV-1 isolates LAI and NDK; when associated with A-7. 2 Publications1
Mutagenesisi12Y → F: Sulfate incorporation greatly reduced; when associated with F-7 and F-21. Moderate reduction in sulfate incorporation; when associated with F-7 and A-18. No sulfate incorporation and binding SDF-1alpha greatly reduced; when associated with F-7; A-18 and F-21. 2 Publications1
Mutagenesisi13T → A: Enhanced coreceptor activity on R5 HIV-1 isolate Envs. No effect on sulfate incorporation; when associated with A-8 and A-9. 1 Publication1
Mutagenesisi14 – 15EE → AA: Reduced CXCL12 binding. Reduced coreceptor activity for HIV-1 isolate NDK. 1 Publication2
Mutagenesisi18S → A: Sulfate incorporation greatly reduced; when associated with F-21. Moderate reduction in sulfate incorporation; when associated with F-7 and F-12. No sulfate incorporation and binding SDF-1alpha greatly reduced; when associated with F-7; F-12; and F-21. 1 Publication1
Mutagenesisi21Y → A: Reduced CXCL12 binding. Reduced coreceptor activity for HIV-1 isolates LAI and NDk. 2 Publications1
Mutagenesisi21Y → F: Sulfate incorporation greatly reduced; when associated with F-7 and F-12. Sulfate incorporation greatly reduced; when associated with A-18. No sulfate incorporation and binding SDF-1alpha greatly reduced; when associated with F-7; F-12 and A-18. 2 Publications1
Mutagenesisi97D → N: Reduced CXCL12 binding. Abolishes signaling. Markedly reduced coreceptor activity for HIV-1 isolate LAI. 1 Publication1
Mutagenesisi119N → D: No reduction of agonist-induced G-protein activation. 1 Publication1
Mutagenesisi119N → K: Loss of agonist-induced G-protein activation. 1 Publication1
Mutagenesisi119N → S: Constitutive G-protein activation, with further activation induced by agonist. 1 Publication1
Mutagenesisi125L → W: Increased thermostability. 1
Mutagenesisi133D → N: No reduction of agonist-induced G-protein activation. 1 Publication1
Mutagenesisi134R → A: Loss of agonist-induced G-protein activation. 1 Publication1
Mutagenesisi135Y → A: No reduction of agonist-induced G-protein activation. 1 Publication1
Mutagenesisi171D → N: Reduced coreceptor activity for HIV-1 isolate NDK. 1 Publication1
Mutagenesisi176N → A: Enhanced coreceptor activity on R5 HIV-1 isolate Envs; when associated with A-11. 1 Publication1
Mutagenesisi183R → A: Reduced coreceptor activity for several HIV-1 isolates. 1 Publication1
Mutagenesisi187D → A: Reduced CXCL12 binding. Abolishes signaling. 1 Publication1
Mutagenesisi188R → A: Reduced coreceptor activity for several HIV-1 isolates. 1 Publication1
Mutagenesisi193D → A, S or N: Greatly reduced coreceptor activity for HIV-1 isolate NDK. Reduced coreceptor activity for several other HIV-1 isolates. 2 Publications1
Mutagenesisi193D → R: Abolishes coreceptor activity for HIV-1 isolate NDK. Reduced coreceptor activity for several other HIV-1 isolates. 2 Publications1
Mutagenesisi240T → P: Retains ligand-binding affinity but abolishes signaling. 1
Mutagenesisi262D → A: Markedly reduced coreceptor activity for HIV-1 isolate LAI. 1 Publication1
Mutagenesisi268E → A: Markedly reduced coreceptor activity for HIV-1 isolate NDK. Less effect for HIV-1 isolate LAI. 1 Publication1
Mutagenesisi288E → Q: Reduced CXCL12 binding. Impaired signaling. Reduced coreceptor activity for HIV-1 isolate LAI. Enhanced coreceptor activity for HIV-1 isolate NDK. 1 Publication1
Mutagenesisi310K → R: No effect on ubiquitination by RNF113A. 1 Publication1
Mutagenesisi324S → A: Moderate degradation. About 60% reduction in binding ITCH and no ubiquitination nor protein degradation; when associated with A-325. 1 Publication1
Mutagenesisi324S → D: Enhanced binding to ITCH. Enhanced binding to ITCH and greatly increased protein degradation; when associated with D-324. 1 Publication1
Mutagenesisi324S → D: Enhanced binding to ITCH. Enhanced binding to ITCH and greatly increased protein degradation; when associated with D-325. 1 Publication1
Mutagenesisi325S → A: Moderate degradation. About 60% reduction in binding ITCH and no ubiquitination nor protein degradation; when associated with A-324. 1 Publication1
Mutagenesisi330S → A: No effect on binding to ITCH. 1 Publication1
Mutagenesisi331K → R: Loss of ubiquitination by RNF113A. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...DisGeNETi		7852

MalaCards human disease database

More...MalaCardsi		CXCR4
MIMi193670 phenotype

Open Targets

More...OpenTargetsi		ENSG00000121966

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

More...Orphaneti		51636 WHIM syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA27058

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2107

Drug and drug target database

More...DrugBanki		DB05501 AMD-070
DB00452 Framycetin
DB06809 Plerixafor

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		71

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		CXCR4

Domain mapping of disease mutations (DMDM)

More...DMDMi		46577576

<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_00000693521 – 352C-X-C chemokine receptor type 4Add 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 residuei7Sulfotyrosine; partial1 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>Glycosylationi11N-linked (GlcNAc...) asparagine1 Publication1
Modified residuei12Sulfotyrosine; partial1 Publication1
Glycosylationi18O-linked (Xyl...) (chondroitin sulfate) serine1 Publication1
Modified residuei21Sulfotyrosine3 Publications1
<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 bondi28 ↔ 274PROSITE-ProRule annotationCombined sources1 Publication
Disulfide bondi109 ↔ 186PROSITE-ProRule annotationCombined sources1 Publication
Glycosylationi176N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei319PhosphoserineCombined sources1
Modified residuei321PhosphoserineCombined sources1 Publication1
Modified residuei324Phosphoserine; by PKC and GRK6Combined sources2 Publications1
Modified residuei325Phosphoserine; by PKC and GRK6Combined sources2 Publications1
Modified residuei330Phosphoserine; by GRK61 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki331Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei339Phosphoserine; by GRK61 Publication1
Modified residuei348PhosphoserineCombined sources1
Modified residuei351Phosphoserine1 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

Phosphorylated on agonist stimulation. Rapidly phosphorylated on serine and threonine residues in the C-terminal. Phosphorylation at Ser-324 and Ser-325 leads to recruitment of ITCH, ubiquitination and protein degradation.3 Publications
Ubiquitinated after ligand binding, leading to its degradation (PubMed:28978524). Ubiquitinated by ITCH at the cell membrane on agonist stimulation. The ubiquitin-dependent mechanism, endosomal sorting complex required for transport (ESCRT), then targets CXCR4 for lysosomal degradation. This process is dependent also on prior Ser-/Thr-phosphorylation in the C-terminal of CXCR4. Also binding of ARRB1 to STAM negatively regulates CXCR4 sorting to lysosomes though modulating ubiquitination of SFR5S.2 Publications
Sulfation on Tyr-21 is required for efficient binding of CXCL12/SDF-1alpha and promotes its dimerization. Tyr-7 and Tyr-12 are sulfated in a sequential manner after Tyr-21 is almost fully sulfated, with the binding affinity for CXCL12/SDF-1alpha increasing with the number of sulfotyrosines present. Sulfotyrosines Tyr-7 and Tyr-12 occupy clefts on opposing CXCL12 subunits, thus bridging the CXCL12 dimer interface and promoting CXCL12 dimerization.4 Publications
O- and N-glycosylated. Asn-11 is the principal site of N-glycosylation. There appears to be very little or no glycosylation on Asn-176. N-glycosylation masks coreceptor function in both X4 and R5 laboratory-adapted and primary HIV-1 strains through inhibiting interaction with their Env glycoproteins. The O-glycosylation chondroitin sulfate attachment does not affect interaction with CXCL12/SDF-1alpha nor its coreceptor activity.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Proteoglycan, Sulfation, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P61073

MaxQB - The MaxQuant DataBase

More...MaxQBi		P61073

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

More...PaxDbi		P61073

PeptideAtlas

More...PeptideAtlasi		P61073

PRoteomics IDEntifications database

More...PRIDEi		P61073

ProteomicsDB human proteome resource

More...ProteomicsDBi		57256
57257 [P61073-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P61073

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

More...PhosphoSitePlusi		P61073

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P61073

Miscellaneous databases

CutDB - Proteolytic event database

More...PMAP-CutDBi		P61073

<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

Expressed in numerous tissues, such as peripheral blood leukocytes, spleen, thymus, spinal cord, heart, placenta, lung, liver, skeletal muscle, kidney, pancreas, cerebellum, cerebral cortex and medulla (in microglia as well as in astrocytes), brain microvascular, coronary artery and umbilical cord endothelial cells. Isoform 1 is predominant in all tissues tested.1 Publication

<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-5.1 Publication
(Microbial infection) May be down-regulated by HIV-1 tat.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000121966 Expressed in 224 organ(s), highest expression level in oviduct epithelium

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P61073 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

Monomer. Can form homodimers (PubMed:20929726). Interacts with CD164 (PubMed:17077324). Interacts with ARRB2; the interaction is dependent on the C-terminal phosphorylation of CXCR4 and allows activation of MAPK1 and MAPK3. Interacts with ARRC; the interaction is dependent on the C-terminal phosphorylation of CXCR4 and modulates calcium mobilization (PubMed:20048153). Interacts with RNF113A; the interaction, enhanced by CXCL12, promotes CXCR4 ubiquitination and subsequent degradation (PubMed:28978524). Interacts (via the cytoplasmic C-terminal) with ITCH (via the WW domains I and II); the interaction, enhanced by CXCL12, promotes CXCR4 ubiquitination and leads to its degradation. Interacts with extracellular ubiquitin. Interacts with DBN1; this interaction is enhanced by antigenic stimulation. Following LPS binding, may form a complex with GDF5, HSP90AA1 and HSPA8.15 Publications
(Microbial infection) Interacts with HIV-1 surface protein gp120 and Tat.4 Publications
(Microbial infection) Interacts with HHV-8 protein ORF K4 (PubMed:25612609).1 Publication
(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

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		113607, 46 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P61073

Database of interacting proteins

More...DIPi		DIP-34773N
DIP-46290N

Protein interaction database and analysis system

More...IntActi		P61073, 20 interactors

Molecular INTeraction database

More...MINTi		P61073

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000386884

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P61073

<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

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2K03NMR-B/D1-38[»]
2K04NMR-B/D1-38[»]
2K05NMR-B/D1-38[»]
2N55NMR-B1-38[»]
3ODUX-ray2.50A/B2-319[»]
3OE0X-ray2.90A2-319[»]
3OE6X-ray3.20A2-325[»]
3OE8X-ray3.10A/B/C2-319[»]
3OE9X-ray3.10A/B2-319[»]
4RWSX-ray3.10A2-228[»]
A231-319[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P61073

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

More...SMRi		P61073

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P61073

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 21Important for chemokine binding, signaling and HIV-1 coreceptor activity1 PublicationAdd BLAST21
Regioni94 – 97Chemokine binding1 Publication1 Publication4
Regioni113 – 117Chemokine binding5
Regioni135 – 147Involved in dimerization; when bound to chemokineAdd BLAST13
Regioni186 – 190Chemokine binding, important for signaling and HIV-1 coreceptor activity5
Regioni191 – 210Involved in dimerizationAdd BLAST20
Regioni266 – 268Involved in dimerization3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi133 – 135Important for signaling3

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The amino-terminus is critical for ligand binding. Residues in all four extracellular regions contribute to HIV-1 coreceptor activity.1 Publication

<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

More...eggNOGi		KOG3656 Eukaryota
ENOG410XRW9 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00950000182758

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG106917

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P61073

KEGG Orthology (KO)

More...KOi		K04189

Identification of Orthologs from Complete Genome Data

More...OMAi		ANWYFGK

Database of Orthologous Groups

More...OrthoDBi		773026at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P61073

TreeFam database of animal gene trees

More...TreeFami		TF330966

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR022726 Chemokine_CXCR4_N_dom
IPR000355 Chemokine_rcpt
IPR001277 CXCR4/ACKR2
IPR000276 GPCR_Rhodpsn
IPR017452 GPCR_Rhodpsn_7TM

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00001 7tm_1, 1 hit
PF12109 CXCR4_N, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00657 CCCHEMOKINER
PR00645 CXCCHMKINER4
PR00237 GPCRRHODOPSN

PROSITE; a protein domain and family database

More...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>Sequences (2)i

<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.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P61073-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MEGISIYTSD NYTEEMGSGD YDSMKEPCFR EENANFNKIF LPTIYSIIFL 
        60         70         80         90        100
TGIVGNGLVI LVMGYQKKLR SMTDKYRLHL SVADLLFVIT LPFWAVDAVA 
       110        120        130        140        150
NWYFGNFLCK AVHVIYTVNL YSSVLILAFI SLDRYLAIVH ATNSQRPRKL 
       160        170        180        190        200
LAEKVVYVGV WIPALLLTIP DFIFANVSEA DDRYICDRFY PNDLWVVVFQ 
       210        220        230        240        250
FQHIMVGLIL PGIVILSCYC IIISKLSHSK GHQKRKALKT TVILILAFFA 
       260        270        280        290        300
CWLPYYIGIS IDSFILLEII KQGCEFENTV HKWISITEAL AFFHCCLNPI 
       310        320        330        340        350
LYAFLGAKFK TSAQHALTSV SRGSSLKILS KGKRGGHSSV STESESSSFH 

SS
Length:352
Mass (Da):39,746
Last modified:April 26, 2004 - 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:i8C8476A186786B83
GO
Isoform 2 (identifier: P61073-2) [UniParc] [UniParc]FASTAAdd to basket
Also known as: CXCR4-LO

The sequence of this isoform differs from the canonical sequence as follows:
     1-5: MEGIS → MSIPLPLLQ

Show »
Length:356
Mass (Da):40,221
Checksum:i83F9E099F41FAB9B
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence CAA12166 differs from that shown. Intron retention.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti242 – 244VIL → IIP in AAK29630 (Ref. 12) Curated3
Sequence conflicti278N → S in BAG35177 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_081112333 – 352Missing Found in patients with Waldenstroem macroglobulinemia; somatic mutation. 1 PublicationAdd BLAST20
Natural variantiVAR_081113334 – 352Missing in WHIMS; also found in patients with Waldenstroem macroglobulinemia; somatic mutation. 2 PublicationsAdd BLAST19
Natural variantiVAR_081114338 – 352Missing in WHIMS; common somatic mutation in patients with Waldenstroem macroglobulinemia; results in decreased CXCL12-triggered receptor internalization; enhanced AKT and MAPK signaling activation; confers resistance to ibrutinib-triggered apoptosis. 4 PublicationsAdd BLAST15
Natural variantiVAR_081115343 – 352Missing in WHIMS. 1 Publication10

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0018901 – 5MEGIS → MSIPLPLLQ in isoform 2. 1 Publication5

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
L01639 mRNA Translation: AAA16594.1
M99293 mRNA Translation: AAA16617.1
X71635 mRNA Translation: CAA50641.1
L06797 mRNA Translation: AAA03209.1
D10924 mRNA Translation: BAA01722.1
AF005058 Genomic DNA Translation: AAB93982.1
AF052572 Genomic DNA Translation: AAC34581.1
AJ224869 Genomic DNA Translation: CAA12166.1 Sequence problems.
AF025375 mRNA Translation: AAB81970.1
Y14739 Genomic DNA Translation: CAA75034.1
AF147204 mRNA Translation: AAF00130.1
AF348491 mRNA Translation: AAK29630.1
AK312244 mRNA Translation: BAG35177.1
AY242129 mRNA Translation: AAO92296.1
BT006660 mRNA Translation: AAP35306.1
AY728138 Genomic DNA Translation: AAU05775.1
AC068492 Genomic DNA Translation: AAY24044.1
CH471058 Genomic DNA Translation: EAX11616.1
BC020968 mRNA Translation: AAH20968.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS33295.1 [P61073-2]
CCDS46420.1

Protein sequence database of the Protein Information Resource

More...PIRi		A45747

NCBI Reference Sequences

More...RefSeqi		NP_001008540.1, NM_001008540.2 [P61073-2]
NP_001334985.1, NM_001348056.1
NP_001334988.1, NM_001348059.1
NP_001334989.1, NM_001348060.1
NP_003458.1, NM_003467.2 [P61073-1]

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.593413

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000241393; ENSP00000241393; ENSG00000121966 [P61073-1]
ENST00000409817; ENSP00000386884; ENSG00000121966 [P61073-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		7852

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:7852

UCSC genome browser

More...UCSCi		uc002tuy.3 human

Keywords - Coding sequence diversityi

Alternative splicing

<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

CXCR4base

CXCR4 mutation db

Wikipedia

CXC chemokine receptors entry

Wikipedia

CXCR4 entry

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L01639 mRNA Translation: AAA16594.1
M99293 mRNA Translation: AAA16617.1
X71635 mRNA Translation: CAA50641.1
L06797 mRNA Translation: AAA03209.1
D10924 mRNA Translation: BAA01722.1
AF005058 Genomic DNA Translation: AAB93982.1
AF052572 Genomic DNA Translation: AAC34581.1
AJ224869 Genomic DNA Translation: CAA12166.1 Sequence problems.
AF025375 mRNA Translation: AAB81970.1
Y14739 Genomic DNA Translation: CAA75034.1
AF147204 mRNA Translation: AAF00130.1
AF348491 mRNA Translation: AAK29630.1
AK312244 mRNA Translation: BAG35177.1
AY242129 mRNA Translation: AAO92296.1
BT006660 mRNA Translation: AAP35306.1
AY728138 Genomic DNA Translation: AAU05775.1
AC068492 Genomic DNA Translation: AAY24044.1
CH471058 Genomic DNA Translation: EAX11616.1
BC020968 mRNA Translation: AAH20968.1
CCDSiCCDS33295.1 [P61073-2]
CCDS46420.1
PIRiA45747
RefSeqiNP_001008540.1, NM_001008540.2 [P61073-2]
NP_001334985.1, NM_001348056.1
NP_001334988.1, NM_001348059.1
NP_001334989.1, NM_001348060.1
NP_003458.1, NM_003467.2 [P61073-1]
UniGeneiHs.593413

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2K03NMR-B/D1-38[»]
2K04NMR-B/D1-38[»]
2K05NMR-B/D1-38[»]
2N55NMR-B1-38[»]
3ODUX-ray2.50A/B2-319[»]
3OE0X-ray2.90A2-319[»]
3OE6X-ray3.20A2-325[»]
3OE8X-ray3.10A/B/C2-319[»]
3OE9X-ray3.10A/B2-319[»]
4RWSX-ray3.10A2-228[»]
A231-319[»]
ProteinModelPortaliP61073
SMRiP61073
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113607, 46 interactors
CORUMiP61073
DIPiDIP-34773N
DIP-46290N
IntActiP61073, 20 interactors
MINTiP61073
STRINGi9606.ENSP00000386884

Chemistry databases

BindingDBiP61073
ChEMBLiCHEMBL2107
DrugBankiDB05501 AMD-070
DB00452 Framycetin
DB06809 Plerixafor
GuidetoPHARMACOLOGYi71

Protein family/group databases

TCDBi9.A.14.13.17 the g-protein-coupled receptor (gpcr) family

Information system for G protein-coupled receptors (GPCRs)

More...GPCRDBi		Search...

PTM databases

iPTMnetiP61073
PhosphoSitePlusiP61073
SwissPalmiP61073

Polymorphism and mutation databases

BioMutaiCXCR4
DMDMi46577576

Proteomic databases

jPOSTiP61073
MaxQBiP61073
PaxDbiP61073
PeptideAtlasiP61073
PRIDEiP61073
ProteomicsDBi57256
57257 [P61073-2]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		7852
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000241393; ENSP00000241393; ENSG00000121966 [P61073-1]
ENST00000409817; ENSP00000386884; ENSG00000121966 [P61073-2]
GeneIDi7852
KEGGihsa:7852
UCSCiuc002tuy.3 human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7852
DisGeNETi7852
EuPathDBiHostDB:ENSG00000121966.6

GeneCards: human genes, protein and diseases

More...GeneCardsi		CXCR4
HGNCiHGNC:2561 CXCR4
MalaCardsiCXCR4
MIMi162643 gene
193670 phenotype
neXtProtiNX_P61073
OpenTargetsiENSG00000121966
Orphaneti51636 WHIM syndrome
PharmGKBiPA27058

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3656 Eukaryota
ENOG410XRW9 LUCA
GeneTreeiENSGT00950000182758
HOVERGENiHBG106917
InParanoidiP61073
KOiK04189
OMAiANWYFGK
OrthoDBi773026at2759
PhylomeDBiP61073
TreeFamiTF330966

Enzyme and pathway databases

ReactomeiR-HSA-173107 Binding and entry of HIV virion
R-HSA-376176 Signaling by ROBO receptors
R-HSA-380108 Chemokine receptors bind chemokines
R-HSA-418594 G alpha (i) signalling events
SignaLinkiP61073
SIGNORiP61073

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		CXCR4 human
EvolutionaryTraceiP61073

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		CXCR4

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

More...GenomeRNAii		7852
PMAP-CutDBiP61073

Protein Ontology

More...PROi		PR:P61073

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000121966 Expressed in 224 organ(s), highest expression level in oviduct epithelium
GenevisibleiP61073 HS

Family and domain databases

InterProiView protein in InterPro
IPR022726 Chemokine_CXCR4_N_dom
IPR000355 Chemokine_rcpt
IPR001277 CXCR4/ACKR2
IPR000276 GPCR_Rhodpsn
IPR017452 GPCR_Rhodpsn_7TM
PfamiView protein in Pfam
PF00001 7tm_1, 1 hit
PF12109 CXCR4_N, 1 hit
PRINTSiPR00657 CCCHEMOKINER
PR00645 CXCCHMKINER4
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 nameiCXCR4_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: P61073
Secondary accession number(s): B2R5N0
, O60835, P30991, P56438, Q53S69, Q9BXA0, Q9UKN2
<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: April 26, 2004
Last sequence update: April 26, 2004
Last modified: April 10, 2019
This is version 173 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. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  4. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
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