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P02778 (CXL10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
C-X-C motif chemokine 10
Alternative name(s):
10 kDa interferon gamma-induced protein
Short name=Gamma-IP10
Short name=IP-10
Small-inducible cytokine B10

Cleaved into the following chain:

  1. CXCL10(1-73)
Gene names
Name:CXCL10
Synonyms:INP10, SCYB10
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length98 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Chemotactic for monocytes and T-lymphocytes. Binds to CXCR3.

Subcellular location

Secreted.

Induction

By IFNG/IFN-gamma. A diverse population of cell types rapidly increases transcription of mRNA encoding this protein. This suggests that gamma-induced protein may be a key mediator of the IFNG/IFN-gamma response.

Post-translational modification

CXCL10(1-73) is produced by proteolytic cleavage after secretion from keratinocytes.

Sequence similarities

Belongs to the intercrine alpha (chemokine CxC) family.

Mass spectrometry

Molecular mass is 8641.8 Da from positions 22 - 98. Determined by ESI. Ref.5

Ontologies

Keywords
   Biological processChemotaxis
Inflammatory response
   Cellular componentSecreted
   DomainSignal
   Molecular functionCytokine
   PTMCitrullination
Disulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Inferred from mutant phenotype PubMed 12782716. Source: UniProtKB

T cell chemotaxis

Inferred from mutant phenotype Ref.6. Source: UniProt

blood circulation

Traceable author statement PubMed 8798675. Source: ProtInc

cell surface receptor signaling pathway

Traceable author statement PubMed 10903763. Source: ProtInc

cell-cell signaling

Traceable author statement Ref.1. Source: ProtInc

cellular response to heat

Inferred from electronic annotation. Source: Ensembl

chemokine-mediated signaling pathway

Inferred from mutant phenotype Ref.6. Source: UniProt

chemotaxis

Inferred from direct assay PubMed 12782716. Source: UniProtKB

defense response to virus

Inferred from electronic annotation. Source: Ensembl

immune response

Inferred from electronic annotation. Source: Ensembl

inflammatory response

Traceable author statement PubMed 10903763. Source: ProtInc

muscle organ development

Traceable author statement PubMed 8798675. Source: ProtInc

negative regulation of angiogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of cAMP metabolic process

Inferred from direct assay PubMed 12782716. Source: UniProtKB

positive regulation of cAMP-mediated signaling

Inferred from direct assay PubMed 12782716. Source: UniProtKB

positive regulation of cell proliferation

Traceable author statement PubMed 8798675. Source: ProtInc

positive regulation of leukocyte chemotaxis

Inferred from electronic annotation. Source: Ensembl

positive regulation of release of sequestered calcium ion into cytosol

Inferred from direct assay PubMed 12782716. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Traceable author statement PubMed 12782716. Source: UniProtKB

protein secretion

Inferred from electronic annotation. Source: Ensembl

regulation of cell proliferation

Inferred from direct assay PubMed 12782716. Source: UniProtKB

regulation of protein kinase activity

Traceable author statement PubMed 10903763. Source: GOC

response to auditory stimulus

Inferred from electronic annotation. Source: Ensembl

response to cold

Inferred from electronic annotation. Source: Ensembl

response to gamma radiation

Inferred from electronic annotation. Source: Ensembl

response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

response to vitamin D

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement PubMed 10201891. Source: ProtInc

   Cellular_componentexternal side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular region

Inferred from direct assay PubMed 20041150. Source: BHF-UCL

extracellular space

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionCXCR3 chemokine receptor binding

Inferred from direct assay PubMed 12782716. Source: UniProtKB

cAMP-dependent protein kinase regulator activity

Traceable author statement PubMed 10903763. Source: ProtInc

chemokine activity

Inferred from direct assay PubMed 12782716. Source: UniProtKB

heparin binding

Inferred from mutant phenotype Ref.6. Source: UniProt

receptor binding

Traceable author statement PubMed 10201891. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

DPP4P274872EBI-7815386,EBI-2871277

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Ref.3 Ref.4 Ref.5
Chain22 – 9877C-X-C motif chemokine 10
PRO_0000005101
Chain22 – 9473CXCL10(1-73)
PRO_0000005102

Amino acid modifications

Modified residue261Citrulline; by PAD2
Disulfide bond30 ↔ 57
Disulfide bond32 ↔ 74

Experimental info

Sequence conflict931R → M in CAA26370. Ref.1

Secondary structure

.............. 98
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P02778 [UniParc].

Last modified June 20, 2002. Version 2.
Checksum: 44AE51967C58DDFF

FASTA9810,881
        10         20         30         40         50         60 
MNQTAILICC LIFLTLSGIQ GVPLSRTVRC TCISISNQPV NPRSLEKLEI IPASQFCPRV 

        70         80         90 
EIIATMKKKG EKRCLNPESK AIKNLLKAVS KERSKRSP 

« Hide

References

« Hide 'large scale' references
[1]"Gamma-interferon transcriptionally regulates an early-response gene containing homology to platelet proteins."
Luster A.D., Unkeless J.C., Ravetch J.V.
Nature 315:672-676(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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].
Tissue: Prostate.
[3]"Identification of a novel granulocyte chemotactic protein (GCP-2) from human tumor cells. In vitro and in vivo comparison with natural forms of GRO, IP-10, and IL-8."
Proost P., de Wolf-Peeters C., Conings R., Opdenakker G., Billiau A., van Damme J.
J. Immunol. 150:1000-1010(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 22-51.
[4]"Human IP-9: a keratinocyte derived high affinity CXC-chemokine ligand for the IP-10/Mig receptor (CXCR3)."
Tensen C.P., Flier J., van der Raaij-Helmer E.M.H., Sampat-Sardjoepersad S., van der Schors R.C., Leurs R., Scheper R.J., Boorsma D.M., Willemze R.
J. Invest. Dermatol. 112:716-722(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 22-29.
Tissue: Keratinocyte.
[5]"Processing of natural and recombinant CXCR3-targeting chemokines and implications for biological activity."
Hensbergen P.J., van der Raaij-Helmer E.M.H., Dijkman R., van der Schors R.C., Werner-Felmayer G., Boorsma D.M., Scheper R.J., Willemze R., Tensen C.P.
Eur. J. Biochem. 268:4992-4999(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 22-27; 60-67 AND 79-98, MASS SPECTROMETRY, IDENTIFICATION OF CXCL10(1-73).
Tissue: Foreskin keratinocyte.
[6]"Citrullination of CXCL10 and CXCL11 by peptidylarginine deiminase: a naturally occurring posttranslational modification of chemokines and new dimension of immunoregulation."
Loos T., Mortier A., Gouwy M., Ronsse I., Put W., Lenaerts J.P., Van Damme J., Proost P.
Blood 112:2648-2656(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: CITRULLINATION AT ARG-26.
[7]"The CXCR3 binding chemokine IP-10/CXCL10: structure and receptor interactions."
Booth V., Keizer D.W., Kamphuis M.B., Clark-Lewis I., Sykes B.D.
Biochemistry 41:10418-10425(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 22-98.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X02530 mRNA. Translation: CAA26370.1.
BC010954 mRNA. Translation: AAH10954.1.
PIRTGHUGI. A03243.
RefSeqNP_001556.2. NM_001565.3.
UniGeneHs.632586.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1LV9NMR-A22-98[»]
1O7YX-ray3.00A/B/C/D22-98[»]
1O7ZX-ray1.92A/B22-98[»]
1O80X-ray2.00A/B22-98[»]
ProteinModelPortalP02778.
SMRP02778. Positions 30-89.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109839. 2 interactions.
DIPDIP-5893N.
IntActP02778. 2 interactions.
MINTMINT-91448.
STRING9606.ENSP00000305651.

PTM databases

PhosphoSiteP02778.

Polymorphism databases

DMDM21542456.

Proteomic databases

PaxDbP02778.
PRIDEP02778.

Protocols and materials databases

DNASU3627.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000306602; ENSP00000305651; ENSG00000169245.
GeneID3627.
KEGGhsa:3627.
UCSCuc003hjl.4. human.

Organism-specific databases

CTD3627.
GeneCardsGC04M076942.
HGNCHGNC:10637. CXCL10.
MIM147310. gene.
neXtProtNX_P02778.
PharmGKBPA35568.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG47968.
HOGENOMHOG000220915.
HOVERGENHBG107789.
InParanoidP02778.
KOK12671.
OMASCPRVEI.
OrthoDBEOG7HHWVH.
PhylomeDBP02778.
TreeFamTF333433.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

BgeeP02778.
CleanExHS_CXCL10.
GenevestigatorP02778.

Family and domain databases

InterProIPR001089. Chemokine_CXC.
IPR018048. Chemokine_CXC_CS.
IPR027220. Chemokine_CXCL10/11.
IPR001811. Chemokine_IL8-like_dom.
[Graphical view]
PANTHERPTHR10179. PTHR10179. 1 hit.
PTHR10179:SF5. PTHR10179:SF5. 1 hit.
PfamPF00048. IL8. 1 hit.
[Graphical view]
PRINTSPR00437. SMALLCYTKCXC.
SMARTSM00199. SCY. 1 hit.
[Graphical view]
SUPFAMSSF54117. SSF54117. 1 hit.
PROSITEPS00471. SMALL_CYTOKINES_CXC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP02778.
GeneWikiCXCL10.
GenomeRNAi3627.
NextBio14193.
PROP02778.
SOURCESearch...

Entry information

Entry nameCXL10_HUMAN
AccessionPrimary (citable) accession number: P02778
Secondary accession number(s): Q96QJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: June 20, 2002
Last modified: April 16, 2014
This is version 157 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM