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P49682

- CXCR3_HUMAN

UniProt

P49682 - CXCR3_HUMAN

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Protein

C-X-C chemokine receptor type 3

Gene

CXCR3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 (PubMed:12782716). Binds to CCL21. Probably promotes cell chemotaxis response.1 Publication
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 (PubMed:12782716). 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.1 Publication
Isoform 3: Mediates the activity of CXCL11.

GO - Molecular functioni

  1. chemokine binding Source: BHF-UCL
  2. chemokine receptor activity Source: ProtInc
  3. C-X-C chemokine binding Source: UniProtKB
  4. C-X-C chemokine receptor activity Source: Ensembl
  5. receptor activity Source: UniProtKB

GO - Biological processi

  1. angiogenesis Source: UniProtKB-KW
  2. apoptotic process Source: UniProtKB-KW
  3. calcium-mediated signaling Source: Ensembl
  4. cell adhesion Source: ProtInc
  5. cell surface receptor signaling pathway Source: BHF-UCL
  6. cellular component movement Source: ProtInc
  7. chemokine (C-C motif) ligand 11 production Source: UniProtKB
  8. chemotaxis Source: ProtInc
  9. G-protein coupled receptor signaling pathway Source: UniProtKB
  10. inflammatory response Source: InterPro
  11. negative regulation of angiogenesis Source: UniProtKB
  12. negative regulation of endothelial cell proliferation Source: UniProtKB
  13. negative regulation of execution phase of apoptosis Source: UniProtKB
  14. positive regulation of angiogenesis Source: UniProtKB
  15. positive regulation of cAMP-mediated signaling Source: UniProtKB
  16. positive regulation of cAMP metabolic process Source: UniProtKB
  17. positive regulation of cell proliferation Source: UniProtKB
  18. positive regulation of chemotaxis Source: UniProtKB
  19. positive regulation of cytosolic calcium ion concentration Source: ProtInc
  20. positive regulation of execution phase of apoptosis Source: UniProtKB
  21. positive regulation of release of sequestered calcium ion into cytosol Source: UniProtKB
  22. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  23. regulation of leukocyte migration Source: InterPro
  24. T cell chemotaxis Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Keywords - Biological processi

Angiogenesis, Apoptosis, Chemotaxis

Enzyme and pathway databases

ReactomeiREACT_15344. Chemokine receptors bind chemokines.
REACT_19231. G alpha (i) signalling events.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:CXCR3
Synonyms:GPR9
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:4540. CXCR3.

Subcellular locationi

Isoform 1 : Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication
Isoform 2 : Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. external side of plasma membrane Source: Ensembl
  3. integral component of plasma membrane Source: ProtInc
  4. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1 – 1616Missing: Reduces binding to CXCL10 and CXCL11, and reduces CXCL10- and CXCL11-induced chemotaxis and activation. Does not affect CXCL9-induced chemotaxis and activation. 1 PublicationAdd
BLAST
Mutagenesisi4 – 41E → K: Does not affect binding to CXCL9, CXCL10 and CXCL11 or activation. 1 Publication
Mutagenesisi21 – 211E → K: Reduces slightly CXCL9-, CXCL10- and CXCL11-induced chemotaxis. 1 Publication
Mutagenesisi27 – 293YDY → ADA: Abolishes binding to CXCL10 and CXCL11 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. 1 Publication
Mutagenesisi27 – 271Y → 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. 2 Publications
Mutagenesisi29 – 291Y → 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. 2 Publications
Mutagenesisi112 – 1121D → A: Abolishes binding to CXCL10 and CXCL11. Reduces CXCL9-, CXCL10- and CXCL11-induced chemotaxis. 1 Publication
Mutagenesisi112 – 1121D → K: Abolishes binding to CXCL10 and CXCL11 and CXCL10- and CXCL11-induced chemotaxis. Reduces CXCL9-induced chemotaxis. 1 Publication
Mutagenesisi197 – 1971R → A: Abolishes binding to CXCL10 and CXCL11 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Reduces ligand-induced receptor internalization. 1 Publication
Mutagenesisi212 – 2121R → A: Abolishes CXCL10-induced chemotaxis. Reduces CXCL9- and CXCL11-induced chemotaxis. Does not affect binding to CXCL10 and CXCL11. 1 Publication
Mutagenesisi216 – 2161R → A: Reduces CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Does not affect binding to CXCL10 and CXCL11 or receptor internalization. 1 Publication
Mutagenesisi278 – 2781D → A: Abolishes binding to CXCL10 and CXCL11 and CXCL11-induced chemotaxis. Reduces CXCL9 and CXCL10-induced chemotaxis. 1 Publication
Mutagenesisi278 – 2781D → K: Abolishes binding to CXCL10 and CXCL11 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. 1 Publication
Mutagenesisi282 – 2821D → A: Reduces binding to CXCL10 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. Abolishes binding to CXCL11. 1 Publication
Mutagenesisi282 – 2821D → K: Reduces binding to CXCL10 and CXCL11 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. 1 Publication
Mutagenesisi293 – 2931E → A: Reduces binding to CXCL10 and CXCL9- and CXCL11-induced chemotaxis. Abolishes binding to CXCL11 and CXCL10-induced chemotaxis. 1 Publication
Mutagenesisi293 – 2931E → K: Abolishes binding to CXCL10 and CXCL11 and CXCL9-, CXCL10- and CXCL11-induced chemotaxis. 1 Publication

Organism-specific databases

PharmGKBiPA35049.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 368368C-X-C chemokine receptor type 3PRO_0000069346Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi22 – 221N-linked (GlcNAc...)Sequence Analysis
Modified residuei27 – 271Sulfotyrosine2 Publications
Modified residuei29 – 291Sulfotyrosine1 Publication
Glycosylationi32 – 321N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi124 ↔ 203PROSITE-ProRule annotation

Post-translational modificationi

Sulfation on Tyr-27 and Tyr-29 is essential for CXCL10 binding and subsequent signal transduction induction.2 Publications
N-glycosylated.

Keywords - PTMi

Disulfide bond, Glycoprotein, Sulfation

Proteomic databases

PaxDbiP49682.
PRIDEiP49682.

PTM databases

PhosphoSiteiP49682.

Expressioni

Tissue specificityi

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).2 Publications

Gene expression databases

BgeeiP49682.
CleanExiHS_CXCR3.
GenevestigatoriP49682.

Organism-specific databases

HPAiCAB017820.

Interactioni

Subunit structurei

Homomer. Forms heteromers with ACKR4.1 Publication

Protein-protein interaction databases

BioGridi109094. 6 interactions.
DIPiDIP-5891N.
MINTiMINT-91399.
STRINGi9606.ENSP00000362795.

Structurei

3D structure databases

ProteinModelPortaliP49682.
SMRiP49682. Positions 50-326.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 5353ExtracellularSequence AnalysisAdd
BLAST
Topological domaini81 – 899CytoplasmicSequence Analysis
Topological domaini111 – 12515ExtracellularSequence AnalysisAdd
BLAST
Topological domaini148 – 16922CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini190 – 21223ExtracellularSequence AnalysisAdd
BLAST
Topological domaini234 – 25522CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini278 – 29821ExtracellularSequence AnalysisAdd
BLAST
Topological domaini322 – 36847CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei54 – 8027Helical; Name=1Sequence AnalysisAdd
BLAST
Transmembranei90 – 11021Helical; Name=2Sequence AnalysisAdd
BLAST
Transmembranei126 – 14722Helical; Name=3Sequence AnalysisAdd
BLAST
Transmembranei170 – 18920Helical; Name=4Sequence AnalysisAdd
BLAST
Transmembranei213 – 23321Helical; Name=5Sequence AnalysisAdd
BLAST
Transmembranei256 – 27722Helical; Name=6Sequence AnalysisAdd
BLAST
Transmembranei299 – 32123Helical; Name=7Sequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG150428.
GeneTreeiENSGT00760000118785.
HOGENOMiHOG000234122.
HOVERGENiHBG106917.
InParanoidiP49682.
KOiK04188.
OMAiAYCYARI.
OrthoDBiEOG7F5126.
PhylomeDBiP49682.
TreeFamiTF330966.

Family and domain databases

Gene3Di1.20.1070.10. 1 hit.
InterProiIPR004070. Chemokine_CXCR3.
IPR000355. Chemokine_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PANTHERiPTHR24227. PTHR24227. 1 hit.
PTHR24227:SF27. PTHR24227:SF27. 1 hit.
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00657. CCCHEMOKINER.
PR01532. CXCCHMKINER3.
PR00237. GPCRRHODOPSN.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P49682-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MVLEVSDHQV LNDAEVAALL ENFSSSYDYG ENESDSCCTS PPCPQDFSLN
60 70 80 90 100
FDRAFLPALY SLLFLLGLLG NGAVAAVLLS RRTALSSTDT FLLHLAVADT
110 120 130 140 150
LLVLTLPLWA VDAAVQWVFG SGLCKVAGAL FNINFYAGAL LLACISFDRY
160 170 180 190 200
LNIVHATQLY RRGPPARVTL TCLAVWGLCL LFALPDFIFL SAHHDERLNA
210 220 230 240 250
THCQYNFPQV GRTALRVLQL VAGFLLPLLV MAYCYAHILA VLLVSRGQRR
260 270 280 290 300
LRAMRLVVVV VVAFALCWTP YHLVVLVDIL MDLGALARNC GRESRVDVAK
310 320 330 340 350
SVTSGLGYMH CCLNPLLYAF VGVKFRERMW MLLLRLGCPN QRGLQRQPSS
360
SRRDSSWSET SEASYSGL
Length:368
Mass (Da):40,660
Last modified:November 1, 1997 - v2
Checksum:iF08A3B44B2BBAD04
GO
Isoform 2 (identifier: P49682-2) [UniParc]FASTAAdd to Basket

Also known as: CXCR3-B

The sequence of this isoform differs from the canonical sequence as follows:
     1-4: MVLE → MELRKYGPGRLAGTVIGGAAQSKSQTKSDSITKEFLPGLYTAPSSPFPPSQ

Show »
Length:415
Mass (Da):45,523
Checksum:i325C8A65982A43C4
GO
Isoform 3 (identifier: P49682-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:267
Mass (Da):28,715
Checksum:i8E5C6052A5A3E518
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 751A → R in CAB02143. 1 PublicationCurated
Sequence conflicti157 – 1571T → I in BAG36429. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti292 – 2921R → Q.1 Publication
Corresponds to variant rs139226823 [ dbSNP | Ensembl ].
VAR_016240
Natural varianti363 – 3631A → T.1 Publication
VAR_016241

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 44MVLE → MELRKYGPGRLAGTVIGGAA QSKSQTKSDSITKEFLPGLY TAPSSPFPPSQ in isoform 2. 2 PublicationsVSP_015684
Alternative sequencei210 – 368159VGRTA…SYSGL → GSSSGSGCGCCSCAWAAPTR EGSRGSHRLPAGIHPGLRPQ RPPTRACEAGIRAPLSPI in isoform 3. CuratedVSP_015685Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS14416.1. [P49682-1]
CCDS48135.1. [P49682-2]
RefSeqiNP_001136269.1. NM_001142797.1. [P49682-2]
NP_001495.1. NM_001504.1. [P49682-1]
UniGeneiHs.198252.

Genome annotation databases

EnsembliENST00000373691; ENSP00000362795; ENSG00000186810. [P49682-2]
ENST00000373693; ENSP00000362797; ENSG00000186810. [P49682-1]
GeneIDi2833.
KEGGihsa:2833.
UCSCiuc004eaf.3. human. [P49682-1]
uc011mpx.2. human. [P49682-2]

Polymorphism databases

DMDMi2829400.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
Wikipedia

CXC chemokine receptors entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS14416.1. [P49682-1 ]
CCDS48135.1. [P49682-2 ]
RefSeqi NP_001136269.1. NM_001142797.1. [P49682-2 ]
NP_001495.1. NM_001504.1. [P49682-1 ]
UniGenei Hs.198252.

3D structure databases

ProteinModelPortali P49682.
SMRi P49682. Positions 50-326.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109094. 6 interactions.
DIPi DIP-5891N.
MINTi MINT-91399.
STRINGi 9606.ENSP00000362795.

Chemistry

BindingDBi P49682.
ChEMBLi CHEMBL4441.
GuidetoPHARMACOLOGYi 70.

Protein family/group databases

GPCRDBi Search...

PTM databases

PhosphoSitei P49682.

Polymorphism databases

DMDMi 2829400.

Proteomic databases

PaxDbi P49682.
PRIDEi P49682.

Protocols and materials databases

DNASUi 2833.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000373691 ; ENSP00000362795 ; ENSG00000186810 . [P49682-2 ]
ENST00000373693 ; ENSP00000362797 ; ENSG00000186810 . [P49682-1 ]
GeneIDi 2833.
KEGGi hsa:2833.
UCSCi uc004eaf.3. human. [P49682-1 ]
uc011mpx.2. human. [P49682-2 ]

Organism-specific databases

CTDi 2833.
GeneCardsi GC0XM070835.
HGNCi HGNC:4540. CXCR3.
HPAi CAB017820.
MIMi 300574. gene.
neXtProti NX_P49682.
PharmGKBi PA35049.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG150428.
GeneTreei ENSGT00760000118785.
HOGENOMi HOG000234122.
HOVERGENi HBG106917.
InParanoidi P49682.
KOi K04188.
OMAi AYCYARI.
OrthoDBi EOG7F5126.
PhylomeDBi P49682.
TreeFami TF330966.

Enzyme and pathway databases

Reactomei REACT_15344. Chemokine receptors bind chemokines.
REACT_19231. G alpha (i) signalling events.

Miscellaneous databases

GeneWikii CXCR3.
GenomeRNAii 2833.
NextBioi 11181.
PROi P49682.
SOURCEi Search...

Gene expression databases

Bgeei P49682.
CleanExi HS_CXCR3.
Genevestigatori P49682.

Family and domain databases

Gene3Di 1.20.1070.10. 1 hit.
InterProi IPR004070. Chemokine_CXCR3.
IPR000355. Chemokine_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view ]
PANTHERi PTHR24227. PTHR24227. 1 hit.
PTHR24227:SF27. PTHR24227:SF27. 1 hit.
Pfami PF00001. 7tm_1. 1 hit.
[Graphical view ]
PRINTSi PR00657. CCCHEMOKINER.
PR01532. CXCCHMKINER3.
PR00237. GPCRRHODOPSN.
PROSITEi PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    , 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. Cited for: SUBUNIT, TISSUE SPECIFICITY.

Entry informationi

Entry nameiCXCR3_HUMAN
AccessioniPrimary (citable) accession number: P49682
Secondary accession number(s): B2R982
, O15185, Q7Z710, Q9P2T4, Q9P2T5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: November 1, 1997
Last modified: October 29, 2014
This is version 150 of the entry and version 2 of the sequence. [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

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Human cell differentiation molecules
    CD nomenclature of surface proteins of human leucocytes and list of entries
  3. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  4. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  5. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. SIMILARITY comments
    Index of protein domains and families

External Data

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