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UniProtKB - P61073 (CXCR4_HUMAN)

Protein

C-X-C chemokine receptor type 4

Gene

CXCR4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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). 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 similarity13 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
Binding sitei171Chemokine1
Binding sitei288Chemokine1 Publication1 Publication1

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • C-C chemokine binding Source: CAFA
  • coreceptor activity Source: ProtInc
  • C-X-C chemokine receptor activity Source: UniProtKB
  • C-X-C motif chemokine 12 receptor activity Source: UniProtKB
  • G-protein coupled receptor activity Source: ProtInc
  • myosin light chain binding Source: UniProtKB
  • ubiquitin binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB
  • virus receptor activity Source: UniProtKB-KW
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

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

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

Protein family/group databases

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

Names & Taxonomyi

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
Gene namesi
Name:CXCR4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

EuPathDBiHostDB:ENSG00000121966.6
HGNCiHGNC:2561 CXCR4
MIMi162643 gene
neXtProtiNX_P61073

Subcellular locationi

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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 38Extracellular1 PublicationAdd BLAST38
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

Pathology & Biotechi

Involvement in diseasei

WHIM syndrome (WHIMS)1 Publication
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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

Organism-specific databases

DisGeNETi7852
MalaCardsiCXCR4
MIMi193670 phenotype
OpenTargetsiENSG00000121966
Orphaneti51636 WHIM syndrome
PharmGKBiPA27058

Chemistry databases

ChEMBLiCHEMBL2107
DrugBankiDB05501 AMD-070
DB00452 Framycetin
DB06809 Plerixafor
GuidetoPHARMACOLOGYi71

Polymorphism and mutation databases

BioMutaiCXCR4
DMDMi46577576

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000693521 – 352C-X-C chemokine receptor type 4Add BLAST352

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei7Sulfotyrosine; partial1 Publication1
Glycosylationi11N-linked (GlcNAc...) asparagine1 Publication1
Modified residuei12Sulfotyrosine; partial1 Publication1
Glycosylationi18O-linked (Xyl...) (chondroitin sulfate) serine1 Publication1
Modified residuei21Sulfotyrosine3 Publications1
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
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

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

MaxQBiP61073
PaxDbiP61073
PeptideAtlasiP61073
PRIDEiP61073
ProteomicsDBi57256
57257 [P61073-2]

PTM databases

iPTMnetiP61073
PhosphoSitePlusiP61073
SwissPalmiP61073

Miscellaneous databases

PMAP-CutDBiP61073

Expressioni

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

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

BgeeiENSG00000121966 Expressed in 224 organ(s), highest expression level in oviduct epithelium
CleanExiHS_CXCR4
GenevisibleiP61073 HS

Interactioni

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

Binary interactionsi

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi113607, 45 interactors
CORUMiP61073
DIPiDIP-34773N
DIP-46290N
IntActiP61073, 20 interactors
MINTiP61073
STRINGi9606.ENSP00000386884

Chemistry databases

BindingDBiP61073

Structurei

Secondary structure

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

3D structure databases

ProteinModelPortaliP61073
SMRiP61073
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61073

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Motifi133 – 135Important for signaling3

Domaini

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

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3656 Eukaryota
ENOG410XRW9 LUCA
GeneTreeiENSGT00760000118785
HOVERGENiHBG106917
InParanoidiP61073
KOiK04189
OMAiVHKWISI
OrthoDBiEOG091G0HEN
PhylomeDBiP61073
TreeFamiTF330966

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

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 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
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

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti242 – 244VIL → IIP in AAK29630 (Ref. 12) Curated3
Sequence conflicti278N → S in BAG35177 (PubMed:14702039).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0018901 – 5MEGIS → MSIPLPLLQ in isoform 2. 1 Publication5

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

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Cross-referencesi

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, 45 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
GPCRDBiSearch...

PTM databases

iPTMnetiP61073
PhosphoSitePlusiP61073
SwissPalmiP61073

Polymorphism and mutation databases

BioMutaiCXCR4
DMDMi46577576

Proteomic databases

MaxQBiP61073
PaxDbiP61073
PeptideAtlasiP61073
PRIDEiP61073
ProteomicsDBi57256
57257 [P61073-2]

Protocols and materials databases

DNASUi7852
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

CTDi7852
DisGeNETi7852
EuPathDBiHostDB:ENSG00000121966.6
GeneCardsiCXCR4
HGNCiHGNC:2561 CXCR4
MalaCardsiCXCR4
MIMi162643 gene
193670 phenotype
neXtProtiNX_P61073
OpenTargetsiENSG00000121966
Orphaneti51636 WHIM syndrome
PharmGKBiPA27058
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3656 Eukaryota
ENOG410XRW9 LUCA
GeneTreeiENSGT00760000118785
HOVERGENiHBG106917
InParanoidiP61073
KOiK04189
OMAiVHKWISI
OrthoDBiEOG091G0HEN
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

ChiTaRSiCXCR4 human
EvolutionaryTraceiP61073
GeneWikiiCXCR4
GenomeRNAii7852
PMAP-CutDBiP61073
PROiPR:P61073
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000121966 Expressed in 224 organ(s), highest expression level in oviduct epithelium
CleanExiHS_CXCR4
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
ProtoNetiSearch...

Entry informationi

Entry nameiCXCR4_HUMAN
AccessioniPrimary (citable) accession number: P61073
Secondary accession number(s): B2R5N0
, O60835, P30991, P56438, Q53S69, Q9BXA0, Q9UKN2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: April 26, 2004
Last modified: October 10, 2018
This is version 168 of the entry and version 1 of the sequence. See complete history.
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

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