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P49682 (CXCR3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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 3

Short name=CXC-R3
Short name=CXCR-3
Alternative name(s):
CKR-L2
G protein-coupled receptor 9
Interferon-inducible protein 10 receptor
Short name=IP-10 receptor
CD_antigen=CD183
Gene names
Name:CXCR3
Synonyms:GPR9
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length368 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Isoform 1:Receptor for the C-X-C chemokine CXCL9, CXCL10 and CXCL11 and mediates the proliferation, survival and angiogenic activity of human mesangial cells (HMC) through a heterotrimeric G-protein signaling pathway (Ref.2). Binds to CCL21. Probably promotes cell chemotaxis response. Ref.2 Ref.3 Ref.10 Ref.14

Isoform 2:Receptor for the C-X-C chemokine CXCL4 and also mediates the inhibitory activities of CXCL9, CXCL10 and CXCL11 on the proliferation, survival and angiogenic activity of human microvascular endothelial cells (HMVEC) through a cAMP-mediated signaling pathway (Ref.2). Does not promote cell chemotaxis respons. Interaction with CXCL4 or CXCL10 leads to activation of the p38MAPK pathway and contributes to inhibition of angiogenesis. Overexpression in renal cancer cells down-regulates expression of the anti-apoptotic protein HMOX1 and promotes apoptosis. Ref.2 Ref.3 Ref.10 Ref.14

Isoform 3:Mediates the activity of CXCL11. Ref.2 Ref.3 Ref.10 Ref.14

Subunit structure

Homomer. Forms heteromers with ACKR4. Ref.15

Subcellular location

Isoform 1: Cell membrane; Multi-pass membrane protein Ref.2.

Isoform 2: Cell membrane; Multi-pass membrane protein Ref.2.

Tissue specificity

Isoform 1 and isoform 2 are mainly expressed in heart, kidney, liver and skeletal muscle. Isoform 1 is also expressed in placenta. Isoform 2 is expressed in endothelial cells. Expressed in T-cells (at protein level). Ref.2 Ref.15

Post-translational modification

Sulfation on Tyr-27 and Tyr-29 is essential for CXCL10 binding and subsequent signal transduction induction.

N-glycosylated.

Sequence similarities

Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
   Biological processAngiogenesis
Apoptosis
Chemotaxis
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransmembrane
Transmembrane helix
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMDisulfide bond
Glycoprotein
Sulfation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from mutant phenotype Ref.2. Source: UniProtKB

T cell chemotaxis

Inferred from electronic annotation. Source: Ensembl

angiogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

calcium-mediated signaling

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Traceable author statement PubMed 10942362. Source: ProtInc

cell surface receptor signaling pathway

Inferred from direct assay PubMed 11554781. Source: BHF-UCL

cellular component movement

Traceable author statement PubMed 10741397. Source: ProtInc

chemokine (C-C motif) ligand 11 production

Inferred from direct assay Ref.2. Source: UniProtKB

chemotaxis

Traceable author statement PubMed 10903763. Source: ProtInc

inflammatory response

Inferred from electronic annotation. Source: InterPro

negative regulation of angiogenesis

Inferred from direct assay Ref.2. Source: UniProtKB

negative regulation of endothelial cell proliferation

Inferred from direct assay Ref.2. Source: UniProtKB

negative regulation of execution phase of apoptosis

Inferred from direct assay Ref.2. Source: UniProtKB

positive regulation of angiogenesis

Inferred from direct assay Ref.2. Source: UniProtKB

positive regulation of cAMP metabolic process

Inferred from direct assay Ref.2. Source: UniProtKB

positive regulation of cAMP-mediated signaling

Inferred from direct assay Ref.2. Source: UniProtKB

positive regulation of cell proliferation

Inferred from direct assay Ref.2. Source: UniProtKB

positive regulation of chemotaxis

Inferred from direct assay Ref.2. Source: UniProtKB

positive regulation of cytosolic calcium ion concentration

Traceable author statement PubMed 10903743. Source: ProtInc

positive regulation of execution phase of apoptosis

Inferred from direct assay Ref.2. Source: UniProtKB

positive regulation of release of sequestered calcium ion into cytosol

Inferred from mutant phenotype Ref.2. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.2. Source: UniProtKB

regulation of leukocyte migration

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Traceable author statement PubMed 10903743. Source: ProtInc

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

plasma membrane

Inferred from direct assay Ref.2. Source: UniProtKB

   Molecular_functionC-X-C chemokine binding

Inferred from direct assay Ref.2. Source: UniProtKB

C-X-C chemokine receptor activity

Inferred from electronic annotation. Source: Ensembl

chemokine binding

Inferred from physical interaction PubMed 11554781. Source: BHF-UCL

chemokine receptor activity

Traceable author statement Ref.1. Source: ProtInc

receptor activity

Inferred from direct assay Ref.2. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P49682-1)

Also known as: CXCR3-A;

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: P49682-2)

Also known as: CXCR3-B;

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MVLE → MELRKYGPGRLAGTVIGGAAQSKSQTKSDSITKEFLPGLYTAPSSPFPPSQ
Isoform 3 (identifier: P49682-3)

Also known as: CXCR3-alt;

The sequence of this isoform differs from the canonical sequence as follows:
     210-368: VGRTALRVLQ...ETSEASYSGL → GSSSGSGCGC...AGIRAPLSPI
Note: Due to exon skipping.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 368368C-X-C chemokine receptor type 3
PRO_0000069346

Regions

Topological domain1 – 5353Extracellular Potential
Transmembrane54 – 8027Helical; Name=1; Potential
Topological domain81 – 899Cytoplasmic Potential
Transmembrane90 – 11021Helical; Name=2; Potential
Topological domain111 – 12515Extracellular Potential
Transmembrane126 – 14722Helical; Name=3; Potential
Topological domain148 – 16922Cytoplasmic Potential
Transmembrane170 – 18920Helical; Name=4; Potential
Topological domain190 – 21223Extracellular Potential
Transmembrane213 – 23321Helical; Name=5; Potential
Topological domain234 – 25522Cytoplasmic Potential
Transmembrane256 – 27722Helical; Name=6; Potential
Topological domain278 – 29821Extracellular Potential
Transmembrane299 – 32123Helical; Name=7; Potential
Topological domain322 – 36847Cytoplasmic Potential

Amino acid modifications

Modified residue271Sulfotyrosine Ref.12 Ref.13
Modified residue291Sulfotyrosine Ref.13
Glycosylation221N-linked (GlcNAc...) Potential
Glycosylation321N-linked (GlcNAc...) Potential
Disulfide bond124 ↔ 203 By similarity

Natural variations

Alternative sequence1 – 44MVLE → MELRKYGPGRLAGTVIGGAA QSKSQTKSDSITKEFLPGLY TAPSSPFPPSQ in isoform 2.
VSP_015684
Alternative sequence210 – 368159VGRTA…SYSGL → GSSSGSGCGCCSCAWAAPTR EGSRGSHRLPAGIHPGLRPQ RPPTRACEAGIRAPLSPI in isoform 3.
VSP_015685
Natural variant2921R → Q. Ref.9
Corresponds to variant rs139226823 [ dbSNP | Ensembl ].
VAR_016240
Natural variant3631A → T. Ref.9
VAR_016241

Experimental info

Mutagenesis1 – 1616Missing: Reduces binding to CXCL10 and CXCL11, and reduces CXCL10- and CXCL11-induced chemotaxis and activation. Does not affect CXCL9-induced chemotaxis and activation. Ref.12
Mutagenesis41E → K: Does not affect binding to CXCL9, CXCL10 and CXCL11 or activation. Ref.12
Mutagenesis211E → K: Reduces slightly CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Ref.12
Mutagenesis27 – 293YDY → ADA: Abolishes binding to CXCL10 and CXCL11 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Ref.12 Ref.13
Mutagenesis271Y → F: Reduces sulfation and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Abolishes binding to CXCL10. Abolishes sulfation, binding to CXCL11, ligand-induced receptor internalization and CXCL9-, CXCL10- and CXCL11-induced chemotaxis; when associated with F-29. Ref.12 Ref.13
Mutagenesis291Y → F: Reduces sulfation, binding to CXCL10 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Abolishes sulfation, binding to CXCL10 and CXCL11 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis; when associated with F-27. Ref.12 Ref.13
Mutagenesis1121D → A: Abolishes binding to CXCL10 and CXCL11. Reduces CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Ref.12
Mutagenesis1121D → K: Abolishes binding to CXCL10 and CXCL11 and CXCL10- and CXCL11-induced chemotaxis. Reduces CXCL9-induced chemotaxis. Ref.12
Mutagenesis1971R → A: Abolishes binding to CXCL10 and CXCL11 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Reduces ligand-induced receptor internalization. Ref.12
Mutagenesis2121R → A: Abolishes CXCL10-induced chemotaxis. Reduces CXCL9- and CXCL11-induced chemotaxis. Does not affect binding to CXCL10 and CXCL11. Ref.12
Mutagenesis2161R → A: Reduces CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Does not affect binding to CXCL10 and CXCL11 or receptor internalization. Ref.12
Mutagenesis2781D → A: Abolishes binding to CXCL10 and CXCL11 and CXCL11-induced chemotaxis. Reduces CXCL9 and CXCL10-induced chemotaxis. Ref.12
Mutagenesis2781D → K: Abolishes binding to CXCL10 and CXCL11 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Ref.12
Mutagenesis2821D → A: Reduces binding to CXCL10 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Abolishes binding to CXCL11. Ref.12
Mutagenesis2821D → K: Reduces binding to CXCL10 and CXCL11 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Ref.12
Mutagenesis2931E → A: Reduces binding to CXCL10 and CXCL9- and CXCL11-induced chemotaxis. Abolishes binding to CXCL11 and CXCL10-induced chemotaxis. Ref.12
Mutagenesis2931E → K: Abolishes binding to CXCL10 and CXCL11 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Ref.12
Sequence conflict751A → R in CAB02143. Ref.4
Sequence conflict1571T → I in BAG36429. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (CXCR3-A) [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: F08A3B44B2BBAD04

FASTA36840,660
        10         20         30         40         50         60 
MVLEVSDHQV LNDAEVAALL ENFSSSYDYG ENESDSCCTS PPCPQDFSLN FDRAFLPALY 

        70         80         90        100        110        120 
SLLFLLGLLG NGAVAAVLLS RRTALSSTDT FLLHLAVADT LLVLTLPLWA VDAAVQWVFG 

       130        140        150        160        170        180 
SGLCKVAGAL FNINFYAGAL LLACISFDRY LNIVHATQLY RRGPPARVTL TCLAVWGLCL 

       190        200        210        220        230        240 
LFALPDFIFL SAHHDERLNA THCQYNFPQV GRTALRVLQL VAGFLLPLLV MAYCYAHILA 

       250        260        270        280        290        300 
VLLVSRGQRR LRAMRLVVVV VVAFALCWTP YHLVVLVDIL MDLGALARNC GRESRVDVAK 

       310        320        330        340        350        360 
SVTSGLGYMH CCLNPLLYAF VGVKFRERMW MLLLRLGCPN QRGLQRQPSS SRRDSSWSET 


SEASYSGL 

« Hide

Isoform 2 (CXCR3-B) [UniParc].

Checksum: 325C8A65982A43C4
Show »

FASTA41545,523
Isoform 3 (CXCR3-alt) [UniParc].

Checksum: 8E5C6052A5A3E518
Show »

FASTA26728,715

References

« Hide 'large scale' references
[1]"Chemokine receptor specific for IP10 and mig: structure, function, and expression in activated T-lymphocytes."
Loetscher M., Gerber B., Loetscher P., Jones S.A., Piali L., Clark-Lewis I., Baggiolini M., Moser B.
J. Exp. Med. 184:963-969(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Blood.
[2]"An alternatively spliced variant of CXCR3 mediates the inhibition of endothelial cell growth induced by IP-10, Mig, and I-TAC, and acts as functional receptor for platelet factor 4."
Lasagni L., Francalanci M., Annunziato F., Lazzeri E., Giannini S., Cosmi L., Sagrinati C., Mazzinghi B., Orlando C., Maggi E., Marra F., Romagnani S., Serio M., Romagnani P.
J. Exp. Med. 197:1537-1549(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
[3]"Activation of p38(MAPK) mediates the angiostatic effect of the chemokine receptor CXCR3-B."
Petrai I., Rombouts K., Lasagni L., Annunziato F., Cosmi L., Romanelli R.G., Sagrinati C., Mazzinghi B., Pinzani M., Romagnani S., Romagnani P., Marra F.
Int. J. Biochem. Cell Biol. 40:1764-1774(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION.
Tissue: Endothelial cell and Thymus.
[4]Gutierrez J., Varona R., Zaballos A., Lind P., Marquez G.
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
[5]"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: Leukocyte.
[6]"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: Colon.
[7]"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: Brain, Lung and Testis.
[8]"Cloning and chromosomal mapping of three novel genes, GPR9, GPR10, and GPR14, encoding receptors related to interleukin 8, neuropeptide Y, and somatostatin receptors."
Marchese A., Heiber M., Nguyen T., Heng H.H.Q., Saldivia V.R., Cheng R., Murphy P.M., Tsui L.-C., Shi X., Gregor P., George S.R., O'Dowd B.F., Docherty J.M.
Genomics 29:335-344(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-368.
[9]"Single nucleotide polymorphisms in the coding regions of human CXC-chemokine receptors CXCR1, CXCR2 and CXCR3."
Kato H., Tsuchiya N., Tokunaga K.
Genes Immun. 1:330-337(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 278-368, VARIANTS GLN-292 AND THR-363.
[10]"Identification and partial characterization of a variant of human CXCR3 generated by posttranscriptional exon skipping."
Ehlert J.E., Addison C.A., Burdick M.D., Kunkel S.L., Strieter R.M.
J. Immunol. 173:6234-6240(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 3), FUNCTION.
[11]"Interferon-inducible T cell alpha chemoattractant (I-TAC): a novel non-ELR CXC chemokine with potent activity on activated T cells through selective high affinity binding to CXCR3."
Cole K.E., Strick C.A., Paradis T.J., Ogborne K.T., Loetscher M., Gladue R.P., Lin W., Boyd J.G., Moser B., Wood D.E., Sahagan B.G., Neote K.
J. Exp. Med. 187:2009-2021(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: LIGAND-BINDING.
Tissue: Fetal astrocyte.
[12]"CXCR3 requires tyrosine sulfation for ligand binding and a second extracellular loop arginine residue for ligand-induced chemotaxis."
Colvin R.A., Campanella G.S., Manice L.A., Luster A.D.
Mol. Cell. Biol. 26:5838-5849(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SULFATION AT TYR-27, MUTAGENESIS OF 1-MET--VAL-16; GLU-4; GLU-21; TYR-27; 27-TYR--TYR-29; TYR-29; ASP-112; ARG-197; ARG-212; ARG-216; ASP-278; ASP-282 AND GLU-293.
[13]"Sulfated tyrosines 27 and 29 in the N-terminus of human CXCR3 participate in binding native IP-10."
Gao J.M., Xiang R.L., Jiang L., Li W.H., Feng Q.P., Guo Z.J., Sun Q., Zeng Z.P., Fang F.D.
Acta Pharmacol. Sin. 30:193-201(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SULFATION AT TYR-27 AND TYR-29, MUTAGENESIS OF TYR-27 AND TYR-29.
[14]"CXCR3-B can mediate growth-inhibitory signals in human renal cancer cells by down-regulating the expression of heme oxygenase-1."
Datta D., Banerjee P., Gasser M., Waaga-Gasser A.M., Pal S.
J. Biol. Chem. 285:36842-36848(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"Inhibition of CXCR3-mediated chemotaxis by the human chemokine receptor-like protein CCX-CKR."
Vinet J., van Zwam M., Dijkstra I.M., Brouwer N., van Weering H.R., Watts A., Meijer M., Fokkens M.R., Kannan V., Verzijl D., Vischer H.F., Smit M.J., Leurs R., Biber K., Boddeke H.W.
Br. J. Pharmacol. 168:1375-1387(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X95876 mRNA. Translation: CAA65126.1.
AF469635 mRNA. Translation: AAP55851.1.
Z79783 Genomic DNA. Translation: CAB02143.1.
AY242128 mRNA. Translation: AAO92295.1.
AK313679 mRNA. Translation: BAG36429.1.
BC034403 mRNA. Translation: AAH34403.1.
U32674 Genomic DNA. Translation: AAC50505.1.
AB032735 Genomic DNA. Translation: BAA92297.1.
AB032736 Genomic DNA. Translation: BAA92298.1.
RefSeqNP_001136269.1. NM_001142797.1.
NP_001495.1. NM_001504.1.
UniGeneHs.198252.

3D structure databases

ProteinModelPortalP49682.
SMRP49682. Positions 60-326.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109094. 6 interactions.
DIPDIP-5891N.
MINTMINT-91399.
STRING9606.ENSP00000362795.

Chemistry

BindingDBP49682.
ChEMBLCHEMBL4441.
GuidetoPHARMACOLOGY70.

Protein family/group databases

GPCRDBSearch...

PTM databases

PhosphoSiteP49682.

Polymorphism databases

DMDM2829400.

Proteomic databases

PaxDbP49682.
PRIDEP49682.

Protocols and materials databases

DNASU2833.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373691; ENSP00000362795; ENSG00000186810. [P49682-2]
ENST00000373693; ENSP00000362797; ENSG00000186810. [P49682-1]
GeneID2833.
KEGGhsa:2833.
UCSCuc004eaf.3. human. [P49682-1]
uc011mpx.2. human. [P49682-2]

Organism-specific databases

CTD2833.
GeneCardsGC0XM070835.
HGNCHGNC:4540. CXCR3.
HPACAB017820.
MIM300574. gene.
neXtProtNX_P49682.
PharmGKBPA35049.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG150428.
HOGENOMHOG000234122.
HOVERGENHBG106917.
KOK04188.
OMAAYCYARI.
OrthoDBEOG7F5126.
PhylomeDBP49682.
TreeFamTF330966.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

BgeeP49682.
CleanExHS_CXCR3.
GenevestigatorP49682.

Family and domain databases

Gene3D1.20.1070.10. 1 hit.
InterProIPR004070. Chemokine_CXCR3.
IPR000355. Chemokine_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERPTHR24227. PTHR24227. 1 hit.
PTHR24227:SF27. PTHR24227:SF27. 1 hit.
PfamPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSPR00657. CCCHEMOKINER.
PR01532. CXCCHMKINER3.
PR00237. GPCRRHODOPSN.
PROSITEPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCXCR3.
GenomeRNAi2833.
NextBio11181.
PROP49682.
SOURCESearch...

Entry information

Entry nameCXCR3_HUMAN
AccessionPrimary (citable) accession number: P49682
Secondary accession number(s): B2R982 expand/collapse secondary AC list , O15185, Q7Z710, Q9P2T4, Q9P2T5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 145 of the entry and version 2 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

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

Human chromosome X: 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