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P61073 (CXCR4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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=LESTR
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
Gene names
Name:CXCR4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length352 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Acts as a receptor for extracellular ubiquitin; leading to enhanced intracellular calcium ions and reduced cellular cAMP levels. 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. Acts as a coreceptor (CD4 being the primary receptor) for HIV-1 X4 isolates and as a primary receptor for some HIV-2 isolates. Promotes Env-mediated fusion of the virus. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes. Ref.1 Ref.2 Ref.6 Ref.20 Ref.21 Ref.27 Ref.29 Ref.30 Ref.33 Ref.39 Ref.44 Ref.45 Ref.47

Subunit structure

Monomer. Can form dimers. Interacts with CD164. Interacts with HIV-1 surface protein gp120 and Tat. 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. Interacts (via the cytoplasmic C-terminal) with ITCH (via the WW domains I and II); the interaction, enhanced by CXCL12, ubiquitinates CXCR4 and leads to its degradation. Interacts with extracellular ubiquitin. Interacts with human cytomegalovirus/HHV-5 protein UL78. Interacts with DBN1; this interaction is enhanced by antigenic stimulation. Following LPS binding, may form a complex with GDF5, HSP90AA1 and HSPA8. Ref.25 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.38 Ref.40 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.50 Ref.51 Ref.53

Subcellular location

Cell membrane; Multi-pass membrane protein. Cell junction. Early endosome. Late endosome. Lysosome. Note: In unstimulated cells, diffuse pattern on plasma membrane. On agonist stimulation, colocalizes with ITCH at the plasma membrane where it becomes ubiquitinated. In the presence of antigen, distributes to the immunological synapse forming at the T-cell-APC contact area, where it localizes at the peripheral and distal supramolecular activation cluster (SMAC). Ref.35 Ref.43 Ref.46 Ref.49

Tissue specificity

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. Ref.33

Domain

The amino-terminus is critical for ligand binding. Residues in all four extracellular regions contribute to HIV-1 coreceptor activity. Ref.28

Post-translational modification

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. Ref.43 Ref.44

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. Ref.35

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.

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. Ref.31 Ref.34

Involvement in disease

WHIM syndrome (WHIM) [MIM:193670]: Immunodeficiency 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.36

Miscellaneous

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

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Caution

Was originally (Ref.1 and Ref.2) thought to be a receptor for neuropeptide Y type 3 (NPY3R) (NPY3-R).

Sequence caution

The sequence CAA12166.1 differs from that shown. Reason: Intron retention.

Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentCell junction
Cell membrane
Endosome
Lysosome
Membrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Host cell receptor for virus entry
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Proteoglycan
Sulfation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from direct assay Ref.29. Source: UniProtKB

T cell proliferation

Inferred from electronic annotation. Source: Ensembl

activation of MAPK activity

Traceable author statement PubMed 10570282. Source: ProtInc

ameboidal cell migration

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Traceable author statement PubMed 10942389. Source: ProtInc

brain development

Inferred from electronic annotation. Source: Ensembl

calcium-mediated signaling

Inferred from mutant phenotype PubMed 19064997. Source: MGI

cellular response to cytokine stimulus

Inferred from direct assay Ref.49. Source: UniProtKB

chemokine-mediated signaling pathway

Non-traceable author statement Ref.7. Source: GOC

dendritic cell chemotaxis

Traceable author statement PubMed 16621978. Source: BHF-UCL

entry into host cell

Traceable author statement. Source: Reactome

germ cell development

Inferred from electronic annotation. Source: Ensembl

germ cell migration

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Traceable author statement Ref.4. Source: ProtInc

motor neuron axon guidance

Inferred from electronic annotation. Source: Ensembl

myelin maintenance

Inferred from sequence or structural similarity. Source: BHF-UCL

neural precursor cell proliferation

Inferred from electronic annotation. Source: Ensembl

neuron migration

Inferred from electronic annotation. Source: Ensembl

neutrophil activation

Inferred from electronic annotation. Source: InterPro

patterning of blood vessels

Inferred from electronic annotation. Source: Ensembl

positive regulation of cytosolic calcium ion concentration

Traceable author statement PubMed 10228019. Source: ProtInc

positive regulation of oligodendrocyte differentiation

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

regulation of chemotaxis

Inferred from mutant phenotype PubMed 19106094. Source: UniProtKB

response to hypoxia

Inferred from expression pattern PubMed 15174142. Source: UniProtKB

response to virus

Traceable author statement PubMed 10583963. Source: ProtInc

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell leading edge

Inferred from direct assay PubMed 12421915. Source: UniProtKB

cell surface

Inferred from direct assay PubMed 10521508Ref.29PubMed 19106094. Source: UniProtKB

cytoplasm

Traceable author statement PubMed 10415069. Source: ProtInc

cytoplasmic membrane-bounded vesicle

Inferred from direct assay PubMed 19106094. Source: UniProtKB

cytoplasmic vesicle

Inferred from direct assay PubMed 10521508. Source: UniProtKB

early endosome

Inferred from direct assay Ref.49. Source: UniProtKB

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

growth cone

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

late endosome

Inferred from direct assay Ref.49. Source: UniProtKB

lysosome

Inferred from direct assay Ref.49. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.49. Source: UniProtKB

   Molecular_functionC-X-C chemokine receptor activity

Non-traceable author statement Ref.7. Source: UniProtKB

G-protein coupled receptor activity

Traceable author statement Ref.4. Source: ProtInc

actin binding

Inferred from direct assay PubMed 12421915. Source: UniProtKB

coreceptor activity

Traceable author statement PubMed 10754293. Source: ProtInc

myosin light chain binding

Inferred from direct assay PubMed 12421915. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.29PubMed 12421915Ref.38PubMed 19106094. Source: UniProtKB

ubiquitin binding

Inferred from direct assay Ref.45. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction Ref.43. Source: UniProtKB

virus receptor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P61073-1)

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.
Isoform 2 (identifier: P61073-2)

Also known as: CXCR4-LO;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 352352C-X-C chemokine receptor type 4
PRO_0000069352

Regions

Topological domain1 – 3838Extracellular
Transmembrane39 – 6325Helical; Name=1
Topological domain64 – 7714Cytoplasmic
Transmembrane78 – 9922Helical; Name=2
Topological domain100 – 11011Extracellular
Transmembrane111 – 13020Helical; Name=3
Topological domain131 – 15424Cytoplasmic
Transmembrane155 – 17420Helical; Name=4
Topological domain175 – 19521Extracellular
Transmembrane196 – 21621Helical; Name=5
Topological domain217 – 24125Cytoplasmic
Transmembrane242 – 26120Helical; Name=6
Topological domain262 – 28221Extracellular
Transmembrane283 – 30220Helical; Name=7
Topological domain303 – 35250Cytoplasmic
Region1 – 2121Important for chemokine binding, signaling and HIV-1 coreceptor activity
Region94 – 974Chemokine binding
Region113 – 1175Chemokine binding
Region135 – 14713Involved in dimerization; when bound to chemokine
Region186 – 1905Chemokine binding, important for signaling and HIV-1 coreceptor activity
Region191 – 21020Involved in dimerization
Region266 – 2683Involved in dimerization
Motif133 – 1353Important for signaling

Sites

Binding site1711Chemokine
Binding site2881Chemokine

Amino acid modifications

Modified residue71Sulfotyrosine; partial Ref.40
Modified residue121Sulfotyrosine; partial Ref.40
Modified residue211Sulfotyrosine Ref.34 Ref.40 Ref.51
Modified residue3191Phosphoserine Ref.42
Modified residue3211Phosphoserine Ref.44
Modified residue3241Phosphoserine; by PKC and GRK6 Ref.43 Ref.44
Modified residue3251Phosphoserine; by PKC and GRK6 Ref.43 Ref.44
Modified residue3301Phosphoserine; by GRK6 Ref.44
Modified residue3391Phosphoserine; by GRK6 Ref.44
Modified residue3481Phosphoserine Ref.42
Modified residue3511Phosphoserine Ref.44
Glycosylation111N-linked (GlcNAc...) Ref.31
Glycosylation181O-linked (Xyl...) (chondroitin sulfate) Ref.34
Glycosylation1761N-linked (GlcNAc...) Potential
Disulfide bond28 ↔ 274 Ref.53
Disulfide bond109 ↔ 186 Ref.53

Natural variations

Alternative sequence1 – 55MEGIS → MSIPLPLLQ in isoform 2.
VSP_001890

Experimental info

Mutagenesis2 – 98Missing: Reduced CXCL12 binding. Abolishes signaling. Ref.30 Ref.34
Mutagenesis4 – 2017Missing: Reduced CXCL12 binding. Impaired signaling. Reduced coreceptor activity for HIV-1 isolates LAI and NDK. Ref.30
Mutagenesis71Y → 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. Ref.30 Ref.34
Mutagenesis71Y → 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. Ref.30 Ref.34
Mutagenesis81T → A: No effect on sulfate incorporation; when associated with A-9 and A-13. Ref.34
Mutagenesis91S → A: No effect on sulfate incorporation; when associated with A-8 and A-13. Ref.34
Mutagenesis10 – 2011Missing: Reduced CXCL12 binding. No effect on signaling. Ref.30
Mutagenesis111N → A: Reduced molecular weight. Enhanced coreceptor activity on R5 HIV-1 isolate Envs. Slight further enhancement of coreceptor activity; when associated with A-13. Ref.31
Mutagenesis121Y → A: Greatly reduced coreceptor activity for HIV-1 isolates LAI and NDK; when associated with A-7. Ref.30 Ref.34
Mutagenesis121Y → 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. Ref.30 Ref.34
Mutagenesis131T → A: Enhanced coreceptor activity on R5 HIV-1 isolate Envs. No effect on sulfate incorporation; when associated with A-8 and A-9. Ref.31
Mutagenesis14 – 152EE → AA: Reduced CXCL12 binding. Reduced coreceptor activity for HIV-1 isolate NDK.
Mutagenesis181S → 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. Ref.34
Mutagenesis211Y → A: Reduced CXCL12 binding. Reduced coreceptor activity for HIV-1 isolates LAI and NDk. Ref.30 Ref.34
Mutagenesis211Y → 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. Ref.30 Ref.34
Mutagenesis971D → N: Reduced CXCL12 binding. Abolishes signaling. Markedly reduced coreceptor activity for HIV-1 isolate LAI. Ref.30
Mutagenesis1191N → D: No reduction of agonist-induced G-protein activation. Ref.39
Mutagenesis1191N → K: Loss of agonist-induced G-protein activation. Ref.39
Mutagenesis1191N → S: Constitutive G-protein activation, with further activation induced by agonist. Ref.39
Mutagenesis1251L → W: Increased thermostability.
Mutagenesis1331D → N: No reduction of agonist-induced G-protein activation. Ref.39
Mutagenesis1341R → A: Loss of agonist-induced G-protein activation. Ref.39
Mutagenesis1351Y → A: No reduction of agonist-induced G-protein activation. Ref.39
Mutagenesis1711D → N: Reduced coreceptor activity for HIV-1 isolate NDK. Ref.30
Mutagenesis1761N → A: Enhanced coreceptor activity on R5 HIV-1 isolate Envs; when associated with A-11. Ref.31
Mutagenesis1831R → A: Reduced coreceptor activity for several HIV-1 isolates. Ref.27
Mutagenesis1871D → A: Reduced CXCL12 binding. Abolishes signaling. Ref.30
Mutagenesis1881R → A: Reduced coreceptor activity for several HIV-1 isolates. Ref.27
Mutagenesis1931D → A, S or N: Greatly reduced coreceptor activity for HIV-1 isolate NDK. Reduced coreceptor activity for several other HIV-1 isolates. Ref.27 Ref.30
Mutagenesis1931D → R: Abolishes coreceptor activity for HIV-1 isolate NDK. Reduced coreceptor activity for several other HIV-1 isolates. Ref.27 Ref.30
Mutagenesis2401T → P: Retains ligand-binding affinity but abolishes signaling.
Mutagenesis2621D → A: Markedly reduced coreceptor activity for HIV-1 isolate LAI. Ref.30
Mutagenesis2681E → A: Markedly reduced coreceptor activity for HIV-1 isolate NDK. Less effect for HIV-1 isolate LAI. Ref.30
Mutagenesis2881E → Q: Reduced CXCL12 binding. Impaired signaling. Reduced coreceptor activity for HIV-1 isolate LAI. Enhanced coreceptor activity for HIV-1 isolate NDK. Ref.30
Mutagenesis3241S → A: Moderate degradation. About 60% reduction in binding ITCH and no ubiquitination nor protein degradation; when associated with A-325. Ref.43
Mutagenesis3241S → D: Enhanced binding to ITCH. Enhanced binding to ITCH and greatly increased protein degradation; when associated with D-324. Ref.43
Mutagenesis3241S → D: Enhanced binding to ITCH. Enhanced binding to ITCH and greatly increased protein degradation; when associated with D-325.
Mutagenesis3251S → A: Moderate degradation. About 60% reduction in binding ITCH and no ubiquitination nor protein degradation; when associated with A-324. Ref.43
Mutagenesis3301S → A: No effect on binding to ITCH. Ref.43
Sequence conflict242 – 2443VIL → IIP in AAK29630. Ref.12
Sequence conflict2781N → S in BAG35177. Ref.13

Secondary structure

............................................ 352
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 26, 2004. Version 1.
Checksum: 8C8476A186786B83

FASTA35239,746
        10         20         30         40         50         60 
MEGISIYTSD NYTEEMGSGD YDSMKEPCFR EENANFNKIF LPTIYSIIFL TGIVGNGLVI 

        70         80         90        100        110        120 
LVMGYQKKLR SMTDKYRLHL SVADLLFVIT LPFWAVDAVA NWYFGNFLCK AVHVIYTVNL 

       130        140        150        160        170        180 
YSSVLILAFI SLDRYLAIVH ATNSQRPRKL LAEKVVYVGV WIPALLLTIP DFIFANVSEA 

       190        200        210        220        230        240 
DDRYICDRFY PNDLWVVVFQ FQHIMVGLIL PGIVILSCYC IIISKLSHSK GHQKRKALKT 

       250        260        270        280        290        300 
TVILILAFFA CWLPYYIGIS IDSFILLEII KQGCEFENTV HKWISITEAL AFFHCCLNPI 

       310        320        330        340        350 
LYAFLGAKFK TSAQHALTSV SRGSSLKILS KGKRGGHSSV STESESSSFH SS 

« Hide

Isoform 2 (CXCR4-LO) [UniParc] [UniParc].

Checksum: 83F9E099F41FAB9B
Show »

FASTA35640,221

References

« Hide 'large scale' references
[1]"Molecular cloning, characterization, and localization of the human homolog to the reported bovine NPY Y3 receptor: lack of NPY binding and activation."
Herzog H., Hort Y.J., Shine J., Selbie L.A.
DNA Cell Biol. 12:465-471(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PRELIMINARY FUNCTION.
Tissue: Lung.
[2]"A proposed bovine neuropeptide Y (NPY) receptor cDNA clone, or its human homologue, confers neither NPY binding sites nor NPY responsiveness on transfected cells."
Jazin E.E., Yoo H., Blomqvist A.G., Yee F., Weng G., Walker M.W., Salon J., Larhammar D., Wahlestedt C.R.
Regul. Pept. 47:247-258(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PRELIMINARY FUNCTION.
Tissue: Fetal brain.
[3]"Molecular cloning of the cDNA and chromosomal localization of the gene for a putative seven-transmembrane segment (7-TMS) receptor isolated from human spleen."
Federsppiel B., Melhado I.G., Duncan A.M.V., Delaney A.D., Schappert K., Clark-Lewis I., Jirik F.R.
Genomics 16:707-712(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Fetal spleen.
[4]"Cloning of a human seven-transmembrane domain receptor, LESTR, that is highly expressed in leukocytes."
Loetscher M., Geiser T., O'Reilly T., Zwahlen R., Baggiolini M., Moser B.
J. Biol. Chem. 269:232-237(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Monocyte.
[5]"Molecular cloning of cDNAs encoding a LD78 receptor and putative leukocyte chemotactic peptide receptors."
Nomura H., Nielsen B.W., Matsushima K.
Int. Immunol. 5:1239-1249(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[6]"HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor."
Feng Y., Broder C.C., Kennedy P.E., Berger E.A.
Science 272:872-877(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION OF ITS HIV-1 CORECEPTOR FUNCTION.
[7]"Genomic organization and functional characterization of the chemokine receptor CXCR4, a major entry co-receptor for human immunodeficiency virus type 1."
Wegner S.A., Ehrenberg P.K., Chang G., Dayhoff D.E., Sleeker A.L., Michael N.L.
J. Biol. Chem. 273:4754-4760(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Peripheral blood leukocyte.
[8]"Genomic organization and promoter characterization of human CXCR4 gene."
Caruz A., Samsom M., Alonso J.M., Alcami J., Baleux F., Virelizier J.-L., Parmentier M., Arenzana-Seisdedos F.
FEBS Lett. 426:271-278(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[9]"Partial resistance to infection by R5X4 primary HIV type 1 isolates in an exposed-uninfected individual homozygous for CCR5 32-base pair deletion."
Xiao L., Weiss S.H., Qari S.H., Rudolph D., Zhao C., Denny T.N., Hodge T., Lal R.B.
AIDS Res. Hum. Retroviruses 15:1201-1208(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[10]"Genomic organization and expression of the CXCR4 gene in mouse and man: absence of a splice variant corresponding to mouse CXCR4-B in human tissues."
Frodl R., Gierschik P., Moepps B.
J. Recept. Signal Transduct. 18:321-344(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Peripheral blood lymphocyte.
[11]"CXCR4-Lo: molecular cloning and functional expression of a novel human CXCR4 splice variant."
Gupta S.K., Pillarisetti K.
J. Immunol. 163:2368-2372(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Neutrophil.
[12]Fan Z., Li T., Li J., Luo B.
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[13]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Adrenal gland.
[14]"cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
Warren C.N., Aronstam R.S., Sharma S.V.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Lung.
[15]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[16]SeattleSNPs variation discovery resource
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[17]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[18]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[19]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Colon.
[20]"The lymphocyte chemoattractant SDF-1 is a ligand for LESTR/fusin and blocks HIV-1 entry."
Bleul C.C., Farzan M., Choe H., Parolin C., Clark-Lewis I., Sodroski J., Springer T.A.
Nature 382:829-833(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[21]"The CXC chemokine SDF-1 is the ligand for LESTR/fusin and prevents infection by T-cell-line-adapted HIV-1."
Oberlin E., Amara A., Bachelerie F., Bessia C., Virelizier J.-L., Arenzana-Seisdedos F., Schwartz O., Heard J.-M., Clark-Lewis I., Legler D.F., Loetscher M., Baggiolini M., Moser B.
Nature 382:833-835(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[22]Erratum
Oberlin E., Amara A., Bachelerie F., Bessia C., Virelizier J.-L., Arenzana-Seisdedos F., Schwartz O., Heard J.-M., Clark-Lewis I., Legler D.F., Loetscher M., Baggiolini M., Moser B.
Nature 384:288-288(1996)
[23]"Evidence for cell-surface association between fusin and the CD4-gp120 complex in human cell lines."
Lapham C.K., Ouyang J., Chandrasekhar B., Nguyen N.Y., Dimitrov D.S., Golding H.
Science 274:602-605(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION AS HIV-1 CORECEPTOR.
[24]"CD4-independent infection by HIV-2 is mediated by fusin/CXCR4."
Endres M.J., Clapham P.R., Marsh M., Ahuja M., Turner J.D., McKnight A., Thomas J.F., Stoebenau-Haggarty B., Choe S., Vance P.J., Wells T.N.C., Power C.A., Sutterwala S.S., Doms R.W., Landau N.R., Hoxie J.A.
Cell 87:745-756(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION AS HIV-2 PRIMARY RECEPTOR IN SOME ISOLATES.
[25]"AMD3100, a small molecule inhibitor of HIV-1 entry via the CXCR4 co-receptor."
Donzella G.A., Schols D., Lin S.W., Este J.A., Nagashima K.A., Maddon P.J., Allaway G.P., Sakmar T.P., Henson G., De Clercq E., Moore J.P.
Nat. Med. 4:72-77(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: ANTAGONIST, INTERACTION WITH CXCL12, CHARACTERIZATION AS HIV-1 CORECEPTOR.
[26]"Tyrosine sulfation of the amino terminus of CCR5 facilitates HIV-1 entry."
Farzan M., Mirzabekov T., Kolchinsky P., Wyatt R., Cayabyab M., Gerard N.P., Gerard C., Sodroski J., Choe H.
Cell 96:667-676(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SULFATION.
[27]"Effect of mutations in the second extracellular loop of CXCR4 on its utilization by human and feline immunodeficiency viruses."
Brelot A., Heveker N., Adema K., Hosie M.J., Willett B., Alizon M.
J. Virol. 73:2576-2586(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ARG-183; ARG-188 AND ASP-193.
[28]"Identification of CXCR4 domains that support coreceptor and chemokine receptor functions."
Doranz B.J., Orsini M.J., Turner J.D., Hoffman T.L., Berson J.F., Hoxie J.A., Peiper S.C., Brass L.F., Doms R.W.
J. Virol. 73:2752-2761(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAINS, INTERACTION WITH HIV-1 SURFACE PROTEIN GP120.
[29]"beta-arrestin differentially regulates the chemokine receptor CXCR4-mediated signaling and receptor internalization, and this implicates multiple interaction sites between beta-arrestin and CXCR4."
Cheng Z.J., Zhao J., Sun Y., Hu W., Wu Y.L., Cen B., Wu G.-X., Pei G.
J. Biol. Chem. 275:2479-2485(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARRB2, FUNCTION.
[30]"Identification of residues of CXCR4 critical for human immunodeficiency virus coreceptor and chemokine receptor activities."
Brelot A., Heveker N., Montes M., Alizon M.
J. Biol. Chem. 275:23736-23744(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CXCL12, MUTAGENESIS OF 2-GLU--SER-9; 4-ILE--ASP-20; TYR-7; 10-ASP--ASP-20; TYR-12; 14-GLU-GLU-15; TYR-21; ASP-97; ASP-171; ASP-187; ASP-193; ASP-262; GLU-268 AND GLU-288.
[31]"N-linked glycosylation of CXCR4 masks coreceptor function for CCR5-dependent human immunodeficiency virus type 1 isolates."
Chabot D.J., Chen H., Dimitrov D.S., Broder C.C.
J. Virol. 74:4404-4413(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-11, INTERACTION WITH HIV-1 ENV, SUBUNIT, MUTAGENESIS OF ASN-11; THR-13 AND ASN-176.
[32]"Selective CXCR4 antagonism by Tat: implications for in vivo expansion of coreceptor use by HIV-1."
Xiao H., Neuveut C., Tiffany H.L., Benkirane M., Rich E.A., Murphy P.M., Jeang K.-T.
Proc. Natl. Acad. Sci. U.S.A. 97:11466-11471(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 TAT.
[33]"A CD14-independent LPS receptor cluster."
Triantafilou K., Triantafilou M., Dedrick R.L.
Nat. Immunol. 2:338-345(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION AS LPS RECEPTOR, INTERACTION WITH GDF5; HSP90AA1 AND HSPA8, TISSUE SPECIFICITY.
[34]"The role of post-translational modifications of the CXCR4 amino terminus in stromal-derived factor 1 alpha association and HIV-1 entry."
Farzan M., Babcock G.J., Vasilieva N., Wright P.L., Kiprilov E., Mirzabekov T., Choe H.
J. Biol. Chem. 277:29484-29489(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT SER-18, IDENTIFICATION OF PROTEOGLYCAN, INTERACTION WITH CXCL12, SULFATION AT TYR-21, MUTAGENESIS OF TYR-7; THR-8; SER-9; TYR-12; SER-18 AND TYR-21.
[35]"The E3 ubiquitin ligase AIP4 mediates ubiquitination and sorting of the G protein-coupled receptor CXCR4."
Marchese A., Raiborg C., Santini F., Keen J.H., Stenmark H., Benovic J.L.
Dev. Cell 5:709-722(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION BY ITCH, SUBCELLULAR LOCATION.
[36]"Mutations in the chemokine receptor gene CXCR4 are associated with WHIM syndrome, a combined immunodeficiency disease."
Hernandez P.A., Gorlin R.J., Lukens J.N., Taniuchi S., Bohinjec J., Francois F., Klotman M.E., Diaz G.A.
Nat. Genet. 34:70-74(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE.
[37]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[38]"Endolyn (CD164) modulates the CXCL12-mediated migration of umbilical cord blood CD133+ cells."
Forde S., Tye B.J., Newey S.E., Roubelakis M., Smythe J., McGuckin C.P., Pettengell R., Watt S.M.
Blood 109:1825-1833(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CD164.
[39]"Direct assessment of CXCR4 mutant conformations reveals complex link between receptor structure and G(alpha)(i) activation."
Berchiche Y.A., Chow K.Y., Lagane B., Leduc M., Percherancier Y., Fujii N., Tamamura H., Bachelerie F., Heveker N.
J. Biol. Chem. 282:5111-5115(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASN-119; ASP-133; ARG-134 AND TYR-135.
[40]"Sequential tyrosine sulfation of CXCR4 by tyrosylprotein sulfotransferases."
Seibert C., Veldkamp C.T., Peterson F.C., Chait B.T., Volkman B.F., Sakmar T.P.
Biochemistry 47:11251-11262(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SULFATION AT TYR-7; TYR-12 AND TYR-21, INTERACTION WITH CXCL12.
[41]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[42]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319 AND SER-348, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[43]"The E3 ubiquitin ligase atrophin interacting protein 4 binds directly to the chemokine receptor CXCR4 via a novel WW domain-mediated interaction."
Bhandari D., Robia S.L., Marchese A.
Mol. Biol. Cell 20:1324-1339(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ITCH, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-324 AND SER-325, MUTAGENESIS OF SER-324; SER-325 AND SER-330.
[44]"Site-specific phosphorylation of CXCR4 is dynamically regulated by multiple kinases and results in differential modulation of CXCR4 signaling."
Busillo J.M., Armando S., Sengupta R., Meucci O., Bouvier M., Benovic J.L.
J. Biol. Chem. 285:7805-7817(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-321; SER-324; SER-325; SER-330; SER-339 AND SER-351, INTERACTION WITH ARRB2 AND ARRC, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.
[45]"CXC chemokine receptor 4 is a cell surface receptor for extracellular ubiquitin."
Saini V., Marchese A., Majetschak M.
J. Biol. Chem. 285:15566-15576(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH UBIQUITIN.
[46]"F-actin-binding protein drebrin regulates CXCR4 recruitment to the immune synapse."
Perez-Martinez M., Gordon-Alonso M., Cabrero J.R., Barrero-Villar M., Rey M., Mittelbrunn M., Lamana A., Morlino G., Calabia C., Yamazaki H., Shirao T., Vazquez J., Gonzalez-Amaro R., Veiga E., Sanchez-Madrid F.
J. Cell Sci. 123:1160-1170(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DBN1, SUBCELLULAR LOCATION.
[47]"Arrestin-2 interacts with the endosomal sorting complex required for transport machinery to modulate endosomal sorting of CXCR4."
Malik R., Marchese A.
Mol. Biol. Cell 21:2529-2541(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH UBIQUITIN.
[48]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[49]"Down-modulation of the G-protein-coupled estrogen receptor, GPER, from the cell surface occurs via a trans-Golgi-proteasome pathway."
Cheng S.B., Quinn J.A., Graeber C.T., Filardo E.J.
J. Biol. Chem. 286:22441-22455(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[50]"Human cytomegalovirus-encoded UL33 and UL78 heteromerize with host CCR5 and CXCR4 impairing their HIV coreceptor activity."
Tadagaki K., Tudor D., Gbahou F., Tschische P., Waldhoer M., Bomsel M., Jockers R., Kamal M.
Blood 119:4908-4918(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HHV-5 PROTEIN UL78.
[51]"Recognition of a CXCR4 sulfotyrosine by the chemokine stromal cell-derived factor-1alpha (SDF-1alpha/CXCL12)."
Veldkamp C.T., Seibert C., Peterson F.C., Sakmar T.P., Volkman B.F.
J. Mol. Biol. 359:1400-1409(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-38, SULFATION AT TYR-21, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CXCL12.
[52]"Structural basis of CXCR4 sulfotyrosine recognition by the chemokine SDF-1/CXCL12."
Veldkamp C.T., Seibert C., Peterson F.C., De la Cruz N.B., Haugner J.C. III, Basnet H., Sakmar T.P., Volkman B.F.
Sci. Signal. 1:RA4-RA4(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-38 OF SULFATED MUTANT ALA-28 IN COMPLEX WITH CXCL12.
[53]"Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists."
Wu B., Chien E.Y., Mol C.D., Fenalti G., Liu W., Katritch V., Abagyan R., Brooun A., Wells P., Bi F.C., Hamel D.J., Kuhn P., Handel T.M., Cherezov V., Stevens R.C.
Science 330:1066-1071(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-325 OF MUTANTS LEU-125 AND THR-240 IN COMPLEX WITH ANTAGONISTS CVX15 AND IT1T, HOMODIMERIZATION, DISULFIDE BONDS.
+Additional computationally mapped references.

Web resources

CXCR4base

CXCR4 mutation db

Wikipedia

CXC chemokine receptors entry

Wikipedia

CXCR4 entry

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS33295.1. [P61073-2]
CCDS46420.1.
PIRA45747.
RefSeqNP_001008540.1. NM_001008540.1. [P61073-2]
NP_003458.1. NM_003467.2. [P61073-1]
UniGeneHs.593413.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2K03NMR-B/D1-38[»]
2K04NMR-B/D1-38[»]
2K05NMR-B/D1-38[»]
3ODUX-ray2.50A/B2-319[»]
3OE0X-ray2.90A2-319[»]
3OE6X-ray3.20A2-325[»]
3OE8X-ray3.10A/B/C2-319[»]
3OE9X-ray3.10A/B2-319[»]
ProteinModelPortalP61073.
SMRP61073. Positions 1-318.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113607. 23 interactions.
DIPDIP-34773N.
DIP-46290N.
IntActP61073. 14 interactions.
MINTMINT-6630550.
STRING9606.ENSP00000386884.

Chemistry

BindingDBP61073.
ChEMBLCHEMBL2107.
DrugBankDB00452. Framycetin.
GuidetoPHARMACOLOGY71.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP61073.

Polymorphism databases

DMDM46577576.

Proteomic databases

MaxQBP61073.
PaxDbP61073.
PRIDEP61073.

Protocols and materials databases

DNASU7852.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000241393; ENSP00000241393; ENSG00000121966. [P61073-1]
ENST00000409817; ENSP00000386884; ENSG00000121966. [P61073-2]
GeneID7852.
KEGGhsa:7852.
UCSCuc002tuy.3. human. [P61073-2]
uc002tuz.3. human.

Organism-specific databases

CTD7852.
GeneCardsGC02M136871.
HGNCHGNC:2561. CXCR4.
HPACAB011447.
MIM162643. gene.
193670. phenotype.
neXtProtNX_P61073.
Orphanet51636. WHIM syndrome.
PharmGKBPA27058.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG328039.
HOVERGENHBG106917.
KOK04189.
OMASHSKGYQ.
OrthoDBEOG73Z2TB.
PhylomeDBP61073.
TreeFamTF330966.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
SignaLinkP61073.

Gene expression databases

ArrayExpressP61073.
BgeeP61073.
CleanExHS_CXCR4.
GenevestigatorP61073.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR001277. Chemokine_CXCR4.
IPR022726. Chemokine_CXCR4_N_dom.
IPR000355. Chemokine_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERPTHR24227. PTHR24227. 1 hit.
PTHR24227:SF7. PTHR24227:SF7. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
PF12109. CXCR4_N. 1 hit.
[Graphical view]
PRINTSPR00657. CCCHEMOKINER.
PR00645. CXCCHMKINER4.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCXCR4. human.
EvolutionaryTraceP61073.
GeneWikiCXCR4.
GenomeRNAi7852.
NextBio30286.
PMAP-CutDBP61073.
PROP61073.
SOURCESearch...

Entry information

Entry nameCXCR4_HUMAN
AccessionPrimary (citable) accession number: P61073
Secondary accession number(s): B2R5N0 expand/collapse secondary AC list , O60835, P30991, P56438, Q53S69, Q9BXA0, Q9UKN2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: July 9, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries