P61073 (CXCR4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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=LESTR
NPYRL
Stromal cell-derived factor 1 receptor
Short name=SDF-1 receptor
CD_antigen=CD184

Gene names

Name:

CXCR4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	352 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.1 Ref.2 Ref.6 Ref.20 Ref.21 Ref.27 Ref.29 Ref.30 Ref.38 Ref.43 Ref.44 Ref.45
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. Ref.25 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.37 Ref.39 Ref.42 Ref.43 Ref.44 Ref.45 Ref.47 Ref.48 Ref.50
Subcellular location	Cell membrane; Multi-pass membrane protein. Note: In unstimulated cells, diffuse pattern on plasma membrane. On agonist stimulation, colocalizes with ITCH at the plasma membrane where it becomes ubiquitinated. Ref.34 Ref.42
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.
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.42 Ref.43 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.34 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.33
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.35
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 process	Host-virus interaction
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing
Domain	Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Host cell receptor for virus entry Receptor Transducer
PTM	Disulfide bond Glycoprotein Phosphoprotein Proteoglycan Sulfation Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	T cell proliferation Inferred from electronic annotation. Source: Compara activation of MAPK activity Traceable author statement PubMed 10570282. Source: ProtInc ameboidal cell migration Inferred from electronic annotation. Source: Compara apoptotic process Traceable author statement PubMed 10942389. Source: ProtInc brain development Inferred from electronic annotation. Source: Compara calcium-mediated signaling Inferred from mutant phenotype PubMed 19064997. Source: MGI dendritic cell chemotaxis Traceable author statement PubMed 16621978. Source: BHF-UCL elevation of cytosolic calcium ion concentration Traceable author statement PubMed 10228019. Source: ProtInc entry into host cell Traceable author statement. Source: Reactome germ cell development Inferred from electronic annotation. Source: Compara germ cell migration Inferred from electronic annotation. Source: Compara inflammatory response Traceable author statement Ref.4. Source: ProtInc motor neuron axon guidance Inferred from electronic annotation. Source: Compara myelin maintenance Inferred from sequence or structural similarity. Source: BHF-UCL neural precursor cell proliferation Inferred from electronic annotation. Source: Compara neuron migration Inferred from electronic annotation. Source: Compara neutrophil activation Inferred from electronic annotation. Source: InterPro patterning of blood vessels Inferred from electronic annotation. Source: Compara positive regulation of oligodendrocyte differentiation Inferred from sequence or structural similarity. Source: BHF-UCL regulation of cell migration Inferred from electronic annotation. Source: Compara 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 reproduction Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cell leading edge Inferred from direct assay PubMed 12421915. Source: UniProtKB cell surface Inferred from direct assay PubMed 10521508Ref.29PubMed 19106094. Source: UniProtKB cytoplasmic membrane-bounded vesicle Inferred from direct assay PubMed 19106094. Source: UniProtKB external side of plasma membrane Inferred from electronic annotation. Source: Compara growth cone Inferred from electronic annotation. Source: Compara integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Traceable author statement. Source: Reactome
Molecular_function	C-X-C chemokine receptor activity Non-traceable author statement Ref.7. Source: UniProtKB 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 ubiquitin binding Inferred from direct assay Ref.44. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MYH9	P35579	5	EBI-489411,EBI-350338

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 352

352

C-X-C chemokine receptor type 4

PRO_0000069352

Regions

Topological domain

1 – 38

38

Extracellular

Transmembrane

39 – 63

25

Helical; Name=1

Topological domain

64 – 77

14

Cytoplasmic

Transmembrane

78 – 99

22

Helical; Name=2

Topological domain

100 – 110

11

Extracellular

Transmembrane

111 – 130

20

Helical; Name=3

Topological domain

131 – 154

24

Cytoplasmic

Transmembrane

155 – 174

20

Helical; Name=4

Topological domain

175 – 195

21

Extracellular

Transmembrane

196 – 216

21

Helical; Name=5

Topological domain

217 – 241

25

Cytoplasmic

Transmembrane

242 – 261

20

Helical; Name=6

Topological domain

262 – 282

21

Extracellular

Transmembrane

283 – 302

20

Helical; Name=7

Topological domain

303 – 352

50

Cytoplasmic

Region

1 – 21

21

Important for chemokine binding, signaling and HIV-1 coreceptor activity

Region

94 – 97

4

Chemokine binding

Region

113 – 117

5

Chemokine binding

Region

135 – 147

13

Involved in dimerization; when bound to chemokine

Region

186 – 190

5

Chemokine binding, important for signaling and HIV-1 coreceptor activity

Region

191 – 210

20

Involved in dimerization

Region

266 – 268

3

Involved in dimerization

Motif

133 – 135

3

Important for signaling

Sites

Binding site

171

1

Chemokine

Binding site

288

1

Chemokine

Amino acid modifications

Modified residue

7

1

Sulfotyrosine; partial Ref.39

Modified residue

12

1

Sulfotyrosine; partial Ref.39

Modified residue

21

1

Sulfotyrosine Ref.33 Ref.39 Ref.48

Modified residue

319

1

Phosphoserine Ref.41

Modified residue

321

1

Phosphoserine Ref.43

Modified residue

324

1

Phosphoserine; by PKC and GRK6 Ref.42 Ref.43

Modified residue

325

1

Phosphoserine; by PKC and GRK6 Ref.42 Ref.43

Modified residue

330

1

Phosphoserine; by GRK6 Ref.43

Modified residue

339

1

Phosphoserine; by GRK6 Ref.43

Modified residue

348

1

Phosphoserine Ref.41

Modified residue

351

1

Phosphoserine Ref.43

Glycosylation

11

1

N-linked (GlcNAc...) Ref.31

Glycosylation

18

1

O-linked (Xyl...) (chondroitin sulfate) Ref.33

Glycosylation

176

1

N-linked (GlcNAc...) Potential

Disulfide bond

28 ↔ 274

Ref.50

Disulfide bond

109 ↔ 186

Ref.50

Natural variations

Alternative sequence

1 – 5

5

MEGIS → MSIPLPLLQ in isoform 2.

VSP_001890

Experimental info

Mutagenesis

2 – 9

8

Missing: Reduced CXCL12 binding. Abolishes signaling. Ref.30 Ref.33

Mutagenesis

4 – 20

17

Missing: Reduced CXCL12 binding. Impaired signaling. Reduced coreceptor activity for HIV-1 isolates LAI and NDK. Ref.30

Mutagenesis

7

1

Y → 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.33

Mutagenesis

7

1

Y → 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.33

Mutagenesis

8

1

T → A: No effect on sulfate incorporation; when associated with A-9 and A-13. Ref.33

Mutagenesis

9

1

S → A: No effect on sulfate incorporation; when associated with A-8 and A-13. Ref.33

Mutagenesis

10 – 20

11

Missing: Reduced CXCL12 binding. No effect on signaling. Ref.30

Mutagenesis

11

1

N → 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

Mutagenesis

12

1

Y → A: Greatly reduced coreceptor activity for HIV-1 isolates LAI and NDK; when associated with A-7. Ref.30 Ref.33

Mutagenesis

12

1

Y → 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.33

Mutagenesis

13

1

T → 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

Mutagenesis

14 – 15

2

EE → AA: Reduced CXCL12 binding. Reduced coreceptor activity for HIV-1 isolate NDK.

Mutagenesis

18

1

S → 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.33

Mutagenesis

21

1

Y → A: Reduced CXCL12 binding. Reduced coreceptor activity for HIV-1 isolates LAI and NDk. Ref.30 Ref.33

Mutagenesis

21

1

Y → 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.33

Mutagenesis

97

1

D → N: Reduced CXCL12 binding. Abolishes signaling. Markedly reduced coreceptor activity for HIV-1 isolate LAI. Ref.30

Mutagenesis

119

1

N → D: No reduction of agonist-induced G-protein activation. Ref.38

Mutagenesis

119

1

N → K: Loss of agonist-induced G-protein activation. Ref.38

Mutagenesis

119

1

N → S: Constitutive G-protein activation, with further activation induced by agonist. Ref.38

Mutagenesis

125

1

L → W: Increased thermostability.

Mutagenesis

133

1

D → N: No reduction of agonist-induced G-protein activation. Ref.38

Mutagenesis

134

1

R → A: Loss of agonist-induced G-protein activation. Ref.38

Mutagenesis

135

1

Y → A: No reduction of agonist-induced G-protein activation. Ref.38

Mutagenesis

171

1

D → N: Reduced coreceptor activity for HIV-1 isolate NDK. Ref.30

Mutagenesis

176

1

N → A: Enhanced coreceptor activity on R5 HIV-1 isolate Envs; when associated with A-11. Ref.31

Mutagenesis

183

1

R → A: Reduced coreceptor activity for several HIV-1 isolates. Ref.27

Mutagenesis

187

1

D → A: Reduced CXCL12 binding. Abolishes signaling. Ref.30

Mutagenesis

188

1

R → A: Reduced coreceptor activity for several HIV-1 isolates. Ref.27

Mutagenesis

193

1

D → 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

Mutagenesis

193

1

D → R: Abolishes coreceptor activity for HIV-1 isolate NDK. Reduced coreceptor activity for several other HIV-1 isolates. Ref.27 Ref.30

Mutagenesis

240

1

T → P: Retains ligand-binding affinity but abolishes signaling.

Mutagenesis

262

1

D → A: Markedly reduced coreceptor activity for HIV-1 isolate LAI. Ref.30

Mutagenesis

268

1

E → A: Markedly reduced coreceptor activity for HIV-1 isolate NDK. Less effect for HIV-1 isolate LAI. Ref.30

Mutagenesis

288

1

E → Q: Reduced CXCL12 binding. Impaired signaling. Reduced coreceptor activity for HIV-1 isolate LAI. Enhanced coreceptor activity for HIV-1 isolate NDK. Ref.30

Mutagenesis

324

1

S → A: Moderate degradation. About 60% reduction in binding ITCH and no ubiquitination nor protein degradation; when associated with A-325. Ref.42

Mutagenesis

324

1

S → D: Enhanced binding to ITCH. Enhanced binding to ITCH and greatly increased protein degradation; when associated with D-324. Ref.42

Mutagenesis

324

1

S → D: Enhanced binding to ITCH. Enhanced binding to ITCH and greatly increased protein degradation; when associated with D-325.

Mutagenesis

325

1

S → A: Moderate degradation. About 60% reduction in binding ITCH and no ubiquitination nor protein degradation; when associated with A-324. Ref.42

Mutagenesis

330

1

S → A: No effect on binding to ITCH. Ref.42

Sequence conflict

242 – 244

3

VIL → IIP in AAK29630. Ref.12

Sequence conflict

278

1

N → S in BAG35177. Ref.13

Secondary structure

1

.

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352

Helix Strand Turn

Details...

Beta strand

9 – 11

3

Beta strand

21 – 23

3

Beta strand

32 – 35

4

Helix

37 – 62

26

Turn

63 – 66

4

Beta strand

67 – 69

3

Helix

72 – 88

17

Helix

91 – 99

9

Helix

105 – 139

35

Helix

141 – 143

3

Helix

145 – 153

9

Helix

155 – 159

5

Helix

161 – 166

6

Helix

169 – 174

6

Beta strand

175 – 179

5

Beta strand

181 – 188

8

Helix

193 – 207

15

Helix

209 – 225

17

Helix

226 – 228

3

Helix

231 – 266

36

Helix

274 – 291

18

Helix

294 – 301

8

Turn

302 – 306

5

Helix

313 – 317

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 26, 2004. Version 1. Checksum: 8C8476A186786B83	FASTA	352	39,746
	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
	Isoform 2 (CXCR4-LO) [UniParc] [UniParc]. Checksum: 83F9E099F41FAB9B	FASTA	356	40,221
	10 20 30 40 50 60 MSIPLPLLQI YTSDNYTEEM GSGDYDSMKE PCFREENANF NKIFLPTIYS IIFLTGIVGN 70 80 90 100 110 120 GLVILVMGYQ KKLRSMTDKY RLHLSVADLL FVITLPFWAV DAVANWYFGN FLCKAVHVIY 130 140 150 160 170 180 TVNLYSSVLI LAFISLDRYL AIVHATNSQR PRKLLAEKVV YVGVWIPALL LTIPDFIFAN 190 200 210 220 230 240 VSEADDRYIC DRFYPNDLWV VVFQFQHIMV GLILPGIVIL SCYCIIISKL SHSKGHQKRK 250 260 270 280 290 300 ALKTTVILIL AFFACWLPYY IGISIDSFIL LEIIKQGCEF ENTVHKWISI TEALAFFHCC 310 320 330 340 350 LNPILYAFLG AKFKTSAQHA LTSVSRGSSL KILSKGKRGG HSSVSTESES SSFHSS

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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]	"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.
[34]	"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.
[35]	"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.
[36]	"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.
[37]	"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.
[38]	"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.
[39]	"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.
[40]	"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.
[41]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[42]	"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.
[43]	"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, MASS SPECTROMETRY.
[44]	"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.
[45]	"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.
[46]	"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.
[47]	"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.
[48]	"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, MASS SPECTROMETRY, INTERACTION WITH CXCL12.
[49]	"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.
[50]	"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.

IPI

IPI00028159.
IPI00216445.

PIR

A45747.

RefSeq

NP_001008540.1. NM_001008540.1.
NP_003458.1. NM_003467.2.

UniGene

Hs.593413.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2K03	NMR	-	B/D	1-38	[»]
2K04	NMR	-	B/D	1-38	[»]
2K05	NMR	-	B/D	1-38	[»]
3ODU	X-ray	2.50	A/B	2-319	[»]
3OE0	X-ray	2.90	A	2-319	[»]
3OE6	X-ray	3.20	A	2-325	[»]
3OE8	X-ray	3.10	A/B/C	2-319	[»]
3OE9	X-ray	3.10	A/B	2-319	[»]

ProteinModelPortal

P61073.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-34773N.
DIP-46290N.

IntAct

P61073. 7 interactions.

MINT

MINT-6630550.

STRING

9606.ENSP00000386884.

Protein family/group databases

GPCRDB

Search...

PTM databases

PhosphoSite

P61073.

Polymorphism databases

DMDM

46577576.

Proteomic databases

PaxDb

P61073.

PRIDE

P61073.

Protocols and materials databases

DNASU

7852.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000241393; ENSP00000241393; ENSG00000121966.
ENST00000409817; ENSP00000386884; ENSG00000121966.

GeneID

7852.

KEGG

hsa:7852.

UCSC

uc002tuy.3. human.
uc002tuz.3. human.

Organism-specific databases

CTD

7852.

GeneCards

GC02M136871.

HGNC

HGNC:2561. CXCR4.

HPA

CAB011447.

MIM

162643. gene.
193670. phenotype.

neXtProt

NX_P61073.

Orphanet

51636. WHIM syndrome.

PharmGKB

PA27058.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG328039.

HOVERGEN

HBG106917.

KO

K04189.

OMA

EENAHFN.

Enzyme and pathway databases

Pathway_Interaction_DB

ephrinbrevpathway. Ephrin B reverse signaling.
hif1_tfpathway. HIF-1-alpha transcription factor network.
s1p_s1p3_pathway. S1P3 pathway.
syndecan_4_pathway. Syndecan-4-mediated signaling events.

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.

Gene expression databases

ArrayExpress

P61073.

Bgee

P61073.

CleanEx

HS_CXCR4.

Genevestigator

P61073.

GermOnline

ENSG00000121966. Homo sapiens.

Family and domain databases

InterPro

IPR001277. Chemokine_CXCR4.
IPR022726. Chemokine_CXCR4_N.
IPR000355. Chemokine_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]

Pfam

PF00001. 7tm_1. 1 hit.
PF12109. CXCR4_N. 1 hit.
[Graphical view]

PRINTS

PR00657. CCCHEMOKINER.
PR00645. CXCCHMKINER4.
PR00237. GPCRRHODOPSN.

PROSITE

PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P61073.

ChEMBL

CHEMBL2107.

ChiTaRS

CXCR4. human.

DrugBank

DB00452. Framycetin.

EvolutionaryTrace

P61073.

GenomeRNAi

7852.

NextBio

30286.

PMAP-CutDB

P61073.

SOURCE

Search...

Entry information

Entry name

CXCR4_HUMAN

Accession

Primary (citable) accession number: P61073
Secondary accession number(s): B2R5N0 , O60835, P30991, P56438, Q53S69, Q9BXA0, Q9UKN2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2004
Last sequence update:	April 26, 2004
Last modified:	May 1, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.