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Protein

C-C motif chemokine 5

Gene

CCL5

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

Functioni

Chemoattractant for blood monocytes, memory T-helper cells and eosinophils. Causes the release of histamine from basophils and activates eosinophils. May activate several chemokine receptors including CCR1, CCR3, CCR4 and CCR5. One of the major HIV-suppressive factors produced by CD8+ T-cells. Recombinant RANTES protein induces a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV). The processed form RANTES(3-68) acts as a natural chemotaxis inhibitor and is a more potent inhibitor of HIV-1-infection. The second processed form RANTES(4-68) exhibits reduced chemotactic and HIV-suppressive activity compared with RANTES(1-68) and RANTES(3-68) and is generated by an unidentified enzyme associated with monocytes and neutrophils (PubMed:16791620, PubMed:1380064, PubMed:8525373, PubMed:9516414, PubMed:15923218). May also be an agonist of the G protein-coupled receptor GPR75, stimulating inositol trisphosphate production and calcium mobilization through its activation. Together with GPR75, may play a role in neuron survival through activation of a downstream signaling pathway involving the PI3, Akt and MAP kinases. By activating GPR75 may also play a role in insulin secretion by islet cells (PubMed:23979485).7 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei25 – 262Cleavage; by DPP4

GO - Molecular functioni

  • CCR1 chemokine receptor binding Source: UniProtKB
  • CCR4 chemokine receptor binding Source: BHF-UCL
  • CCR5 chemokine receptor binding Source: BHF-UCL
  • chemoattractant activity Source: UniProtKB
  • chemokine activity Source: UniProtKB
  • chemokine receptor antagonist activity Source: BHF-UCL
  • chemokine receptor binding Source: BHF-UCL
  • heparin binding Source: Ensembl
  • phosphatidylinositol phospholipase C activity Source: UniProtKB
  • phospholipase activator activity Source: UniProtKB
  • protein homodimerization activity Source: BHF-UCL
  • protein kinase activity Source: UniProtKB
  • protein self-association Source: BHF-UCL
  • receptor signaling protein tyrosine kinase activator activity Source: BHF-UCL

GO - Biological processi

  • activation of phospholipase D activity Source: BHF-UCL
  • aging Source: Ensembl
  • calcium ion transport Source: UniProtKB
  • cell-cell signaling Source: BHF-UCL
  • cellular calcium ion homeostasis Source: UniProtKB
  • cellular protein complex assembly Source: BHF-UCL
  • cellular response to alkyl hydroperoxide Source: Ensembl
  • cellular response to amino acid stimulus Source: Ensembl
  • cellular response to ethanol Source: Ensembl
  • cellular response to fibroblast growth factor stimulus Source: UniProtKB
  • cellular response to high density lipoprotein particle stimulus Source: Ensembl
  • cellular response to interferon-gamma Source: UniProtKB
  • cellular response to interleukin-1 Source: UniProtKB
  • cellular response to morphine Source: Ensembl
  • cellular response to organic cyclic compound Source: UniProtKB
  • cellular response to transforming growth factor beta stimulus Source: Ensembl
  • cellular response to tumor necrosis factor Source: UniProtKB
  • cellular response to vitamin K Source: Ensembl
  • chemokine-mediated signaling pathway Source: UniProtKB
  • chemotaxis Source: UniProtKB
  • chronic inflammatory response Source: Ensembl
  • dendritic cell chemotaxis Source: BHF-UCL
  • dibenzo-p-dioxin metabolic process Source: Ensembl
  • eosinophil chemotaxis Source: BHF-UCL
  • exocytosis Source: UniProtKB
  • G-protein coupled receptor signaling pathway Source: UniProtKB
  • inflammatory response Source: UniProtKB
  • leukocyte cell-cell adhesion Source: BHF-UCL
  • lipopolysaccharide-mediated signaling pathway Source: UniProtKB
  • lymphocyte chemotaxis Source: Ensembl
  • macrophage chemotaxis Source: BHF-UCL
  • MAPK cascade Source: UniProtKB
  • monocyte chemotaxis Source: UniProtKB
  • negative regulation by host of viral transcription Source: UniProtKB
  • negative regulation of chemokine-mediated signaling pathway Source: GOC
  • negative regulation of G-protein coupled receptor protein signaling pathway Source: UniProtKB
  • negative regulation of macrophage apoptotic process Source: Ensembl
  • negative regulation of neuron death Source: Ensembl
  • negative regulation of T cell apoptotic process Source: BHF-UCL
  • negative regulation of viral genome replication Source: BHF-UCL
  • neutrophil activation Source: BHF-UCL
  • positive chemotaxis Source: GOC
  • positive regulation of activation of JAK2 kinase activity Source: BHF-UCL
  • positive regulation of angiogenesis Source: Ensembl
  • positive regulation of calcium ion transport Source: UniProtKB
  • positive regulation of cell adhesion Source: BHF-UCL
  • positive regulation of cell-cell adhesion mediated by integrin Source: BHF-UCL
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of cellular biosynthetic process Source: BHF-UCL
  • positive regulation of epithelial cell proliferation Source: Ensembl
  • positive regulation of fever generation Source: Ensembl
  • positive regulation of homotypic cell-cell adhesion Source: BHF-UCL
  • positive regulation of innate immune response Source: BHF-UCL
  • positive regulation of JAK-STAT cascade Source: BHF-UCL
  • positive regulation of macrophage chemotaxis Source: BHF-UCL
  • positive regulation of mast cell chemotaxis Source: Ensembl
  • positive regulation of monocyte chemotaxis Source: BHF-UCL
  • positive regulation of natural killer cell chemotaxis Source: UniProtKB
  • positive regulation of neuron differentiation Source: Ensembl
  • positive regulation of osteoclast differentiation Source: Ensembl
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: BHF-UCL
  • positive regulation of phosphorylation Source: BHF-UCL
  • positive regulation of protein tyrosine kinase activity Source: GOC
  • positive regulation of smooth muscle cell migration Source: BHF-UCL
  • positive regulation of smooth muscle cell proliferation Source: BHF-UCL
  • positive regulation of T cell apoptotic process Source: BHF-UCL
  • positive regulation of T cell chemotaxis Source: BHF-UCL
  • positive regulation of T cell migration Source: MGI
  • positive regulation of T cell proliferation Source: BHF-UCL
  • positive regulation of translational initiation Source: BHF-UCL
  • positive regulation of tyrosine phosphorylation of STAT protein Source: BHF-UCL
  • positive regulation of viral genome replication Source: BHF-UCL
  • protein kinase B signaling Source: UniProtKB
  • protein tetramerization Source: BHF-UCL
  • regulation of chronic inflammatory response Source: BHF-UCL
  • regulation of insulin secretion Source: UniProtKB
  • regulation of neuron death Source: UniProtKB
  • regulation of T cell activation Source: BHF-UCL
  • response to activity Source: Ensembl
  • response to cholesterol Source: Ensembl
  • response to drug Source: Ensembl
  • response to estrogen Source: Ensembl
  • response to glucocorticoid Source: Ensembl
  • response to insulin Source: Ensembl
  • response to salt stress Source: Ensembl
  • response to toxic substance Source: UniProtKB
  • response to virus Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Cytokine

Keywords - Biological processi

Chemotaxis, Inflammatory response

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
C-C motif chemokine 5
Alternative name(s):
EoCP
Eosinophil chemotactic cytokine
SIS-delta
Small-inducible cytokine A5
T cell-specific protein P228
Short name:
TCP228
T-cell-specific protein RANTES
Cleaved into the following 2 chains:
Gene namesi
Name:CCL5
Synonyms:D17S136E, SCYA5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:10632. CCL5.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35564.

Polymorphism and mutation databases

BioMutaiCCL5.
DMDMi6175077.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23232 PublicationsAdd
BLAST
Chaini24 – 9168C-C motif chemokine 5PRO_0000005175Add
BLAST
Chaini26 – 9166RANTES(3-68)PRO_0000005176Add
BLAST
Chaini27 – 9165RANTES(4-68)PRO_0000005177Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi27 – 271O-linked (GalNAc...); partial1 Publication
Glycosylationi28 – 281O-linked (GalNAc...); partial1 Publication
Disulfide bondi33 ↔ 57
Disulfide bondi34 ↔ 73
Modified residuei90 – 901Methionine sulfoxide1 Publication

Post-translational modificationi

N-terminal processed form RANTES(3-68) is produced by proteolytic cleavage, probably by DPP4, after secretion from peripheral blood leukocytes and cultured sarcoma cells.1 Publication
The identity of the O-linked saccharides at Ser-27 and Ser-28 are not reported in PubMed:1380064. They are assigned by similarity.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Oxidation

Proteomic databases

PaxDbiP13501.
PeptideAtlasiP13501.
PRIDEiP13501.

PTM databases

PhosphoSiteiP13501.

Miscellaneous databases

PMAP-CutDBP13501.

Expressioni

Tissue specificityi

T-cell and macrophage specific.

Inductioni

By mitogens.

Gene expression databases

BgeeiP13501.
CleanExiHS_CCL5.
ExpressionAtlasiP13501. baseline and differential.
GenevisibleiP13501. HS.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CCR5P516814EBI-2848366,EBI-489374

Protein-protein interaction databases

BioGridi112255. 16 interactions.
DIPiDIP-31N.
IntActiP13501. 24 interactions.
MINTiMINT-103226.
STRINGi9606.ENSP00000293272.

Structurei

Secondary structure

1
91
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi31 – 333Combined sources
Beta strandi35 – 406Combined sources
Helixi44 – 463Combined sources
Beta strandi47 – 526Combined sources
Beta strandi57 – 593Combined sources
Beta strandi62 – 665Combined sources
Beta strandi71 – 744Combined sources
Helixi79 – 8911Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B3AX-ray1.60A/B25-91[»]
1EQTX-ray1.60A/B26-91[»]
1HRJNMR-A/B24-91[»]
1RTNNMR-A/B24-91[»]
1RTONMR-A/B24-91[»]
1U4LX-ray2.00A/B24-91[»]
1U4MX-ray2.00A/B24-91[»]
1U4PX-ray1.70A/B24-91[»]
1U4RX-ray2.20A/B/C/D24-91[»]
2L9HOther-A/B/C/D24-91[»]
2VXWX-ray1.70A/B/C/D33-91[»]
ProteinModelPortaliP13501.
SMRiP13501. Positions 25-91.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13501.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG38896.
GeneTreeiENSGT00730000110278.
HOVERGENiHBG017871.
InParanoidiP13501.
OrthoDBiEOG7CVQ1F.
PhylomeDBiP13501.
TreeFamiTF334888.

Family and domain databases

InterProiIPR030595. CCL5.
IPR000827. Chemokine_CC_CS.
IPR001811. Chemokine_IL8-like_dom.
[Graphical view]
PANTHERiPTHR12015:SF82. PTHR12015:SF82. 1 hit.
PfamiPF00048. IL8. 1 hit.
[Graphical view]
SMARTiSM00199. SCY. 1 hit.
[Graphical view]
SUPFAMiSSF54117. SSF54117. 1 hit.
PROSITEiPS00472. SMALL_CYTOKINES_CC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P13501-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVSAAALAV ILIATALCAP ASASPYSSDT TPCCFAYIAR PLPRAHIKEY
60 70 80 90
FYTSGKCSNP AVVFVTRKNR QVCANPEKKW VREYINSLEM S
Length:91
Mass (Da):9,990
Last modified:July 15, 1999 - v3
Checksum:iFB0BFAF9A87C620F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71A → R in AAA36725 (PubMed:2456327).Curated
Sequence conflicti7 – 71A → R in AAF73070 (Ref. 5) Curated
Sequence conflicti14 – 141A → V in AAF73070 (Ref. 5) Curated

Mass spectrometryi

Molecular mass is 7515±1 Da from positions 27 - 91. Determined by SELDI. 1 Publication
Molecular mass is 7862.8±1.1 Da from positions 24 - 91. Determined by ESI. 1 Publication
Molecular mass is 8355±10 Da from positions 24 - 91. Determined by ESI. O-glycosylated.1 Publication

Polymorphismi

The variant Phe-24 is an antagonist of the chemokine receptors CCR1 and CCR3.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti24 – 241S → F.1 Publication
VAR_043043

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21121 mRNA. Translation: AAA36725.1.
AF088219 Genomic DNA. Translation: AAC63331.1.
DQ230537 mRNA. Translation: ABB69929.1.
AF043341 mRNA. Translation: AAC03541.1.
AF266753 mRNA. Translation: AAF73070.1.
DQ017060 Genomic DNA. Translation: AAY22177.1.
BC008600 mRNA. Translation: AAH08600.1.
CCDSiCCDS11300.1.
PIRiA28815.
RefSeqiNP_002976.2. NM_002985.2.
UniGeneiHs.514821.

Genome annotation databases

EnsembliENST00000603197; ENSP00000474412; ENSG00000271503.
ENST00000605140; ENSP00000475057; ENSG00000271503.
ENST00000613606; ENSP00000479894; ENSG00000274233.
GeneIDi6352.
UCSCiuc002hkf.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

RANTES entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21121 mRNA. Translation: AAA36725.1.
AF088219 Genomic DNA. Translation: AAC63331.1.
DQ230537 mRNA. Translation: ABB69929.1.
AF043341 mRNA. Translation: AAC03541.1.
AF266753 mRNA. Translation: AAF73070.1.
DQ017060 Genomic DNA. Translation: AAY22177.1.
BC008600 mRNA. Translation: AAH08600.1.
CCDSiCCDS11300.1.
PIRiA28815.
RefSeqiNP_002976.2. NM_002985.2.
UniGeneiHs.514821.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B3AX-ray1.60A/B25-91[»]
1EQTX-ray1.60A/B26-91[»]
1HRJNMR-A/B24-91[»]
1RTNNMR-A/B24-91[»]
1RTONMR-A/B24-91[»]
1U4LX-ray2.00A/B24-91[»]
1U4MX-ray2.00A/B24-91[»]
1U4PX-ray1.70A/B24-91[»]
1U4RX-ray2.20A/B/C/D24-91[»]
2L9HOther-A/B/C/D24-91[»]
2VXWX-ray1.70A/B/C/D33-91[»]
ProteinModelPortaliP13501.
SMRiP13501. Positions 25-91.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112255. 16 interactions.
DIPiDIP-31N.
IntActiP13501. 24 interactions.
MINTiMINT-103226.
STRINGi9606.ENSP00000293272.

Chemistry

BindingDBiP13501.
ChEMBLiCHEMBL1275217.

PTM databases

PhosphoSiteiP13501.

Polymorphism and mutation databases

BioMutaiCCL5.
DMDMi6175077.

Proteomic databases

PaxDbiP13501.
PeptideAtlasiP13501.
PRIDEiP13501.

Protocols and materials databases

DNASUi6352.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000603197; ENSP00000474412; ENSG00000271503.
ENST00000605140; ENSP00000475057; ENSG00000271503.
ENST00000613606; ENSP00000479894; ENSG00000274233.
GeneIDi6352.
UCSCiuc002hkf.3. human.

Organism-specific databases

CTDi6352.
GeneCardsiGC17M034198.
HGNCiHGNC:10632. CCL5.
MIMi187011. gene.
neXtProtiNX_P13501.
PharmGKBiPA35564.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG38896.
GeneTreeiENSGT00730000110278.
HOVERGENiHBG017871.
InParanoidiP13501.
OrthoDBiEOG7CVQ1F.
PhylomeDBiP13501.
TreeFamiTF334888.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP13501.
GeneWikiiCCL5.
GenomeRNAii6352.
NextBioi24676.
PMAP-CutDBP13501.
PROiP13501.
SOURCEiSearch...

Gene expression databases

BgeeiP13501.
CleanExiHS_CCL5.
ExpressionAtlasiP13501. baseline and differential.
GenevisibleiP13501. HS.

Family and domain databases

InterProiIPR030595. CCL5.
IPR000827. Chemokine_CC_CS.
IPR001811. Chemokine_IL8-like_dom.
[Graphical view]
PANTHERiPTHR12015:SF82. PTHR12015:SF82. 1 hit.
PfamiPF00048. IL8. 1 hit.
[Graphical view]
SMARTiSM00199. SCY. 1 hit.
[Graphical view]
SUPFAMiSSF54117. SSF54117. 1 hit.
PROSITEiPS00472. SMALL_CYTOKINES_CC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A human T cell-specific molecule is a member of a new gene family."
    Schall T.J., Jongstra J., Dyer B.J., Jorgensen J., Clayberger C., Davis M.M., Krensky A.M.
    J. Immunol. 141:1018-1025(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Organization of the chemokine gene cluster on human chromosome 17q11.2 containing the genes for CC chemokine MPIF-1, HCC-2, LEC, and RANTES."
    Nomiyama H., Fukuda S., Iio M., Tanase S., Miura R., Yoshie O.
    J. Interferon Cytokine Res. 19:227-234(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, VARIANT PHE-24.
    Tissue: Blood.
  4. Jang J.S., Kim B.E.
    Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Leukocyte.
  5. "The complete sequence of human beta-chemokine RANTES mRNA."
    Zeng Q.P., Yang R.Y., Fu L.C.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  6. NIEHS SNPs program
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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].
    Tissue: Brain.
  8. "Cytokine RANTES released by thrombin-stimulated platelets is a potent attractant for human eosinophils."
    Kameyoshi Y., Doerschner A., Mallet A.I., Christophers E., Schroeder J.-M.
    J. Exp. Med. 176:587-592(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-55, FUNCTION, MASS SPECTROMETRY, GLYCOSYLATION AT SER-27 AND SER-28, OXIDATION AT MET-90.
  9. "Platelets secrete an eosinophil-chemotactic cytokine which is a member of the C-C-chemokine family."
    Schroeder J.-M., Kameyoshi Y., Christophers E.
    Adv. Exp. Med. Biol. 351:119-128(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-55.
  10. "Identification of RANTES, MIP-1 alpha, and MIP-1 beta as the major HIV-suppressive factors produced by CD8+ T cells."
    Cocchi F., DeVico A.L., Garzino-Demo A., Arya S.K., Gallo R.C., Lusso P.
    Science 270:1811-1815(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 49-56; 71-79 AND 83-91, FUNCTION.
  11. "Amino-terminal truncation of chemokines by CD26/dipeptidyl-peptidase IV. Conversion of RANTES into a potent inhibitor of monocyte chemotaxis and HIV-1-infection."
    Proost P., De Meester I., Schols D., Struyf S., Lambeir A.-M., Wuyts A., Opdenakker G., De Clercq E., Scharpe S., Van Damme J.
    J. Biol. Chem. 273:7222-7227(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF RANTES(3-68), PROTEOLYTIC PROCESSING OF N-TERMINUS, FUNCTION.
  12. "Multiple pathways of amino terminal processing produce two truncated variants of RANTES/CCL5."
    Lim J.K., Burns J.M., Lu W., DeVico A.L.
    J. Leukoc. Biol. 78:442-452(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF RANTES(4-68), MASS SPECTROMETRY, FUNCTION.
  13. "RANTES stimulates Ca2+ mobilization and inositol trisphosphate (IP3) formation in cells transfected with G protein-coupled receptor 75."
    Ignatov A., Robert J., Gregory-Evans C., Schaller H.C.
    Br. J. Pharmacol. 149:490-497(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "The novel chemokine receptor, G-protein-coupled receptor 75, is expressed by islets and is coupled to stimulation of insulin secretion and improved glucose homeostasis."
    Liu B., Hassan Z., Amisten S., King A.J., Bowe J.E., Huang G.C., Jones P.M., Persaud S.J.
    Diabetologia 56:2467-2476(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "Proton NMR assignments and solution conformation of RANTES, a chemokine of the C-C type."
    Skelton N.J., Aspiras F., Ogez J., Schall T.J.
    Biochemistry 34:5329-5342(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.
  16. Cited for: STRUCTURE BY NMR.
  17. "Total chemical synthesis and high-resolution crystal structure of the potent anti-HIV protein AOP-RANTES."
    Wilken J., Hoover D., Thompson D.A., Barlow P.N., McSparron H., Picard L., Wlodawer A., Lubkowski J., Kent S.B.
    Chem. Biol. 6:43-51(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SYNTHESIS, X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
  18. "The crystal structure of Met-RANTES: comparison with native RANTES and AOP-RANTES."
    Hoover D.M., Shaw J., Gryczynski Z., Proudfoot A.E.I., Wells T.N.C., Lubkowski J.
    Protein Pept. Lett. 7:73-82(2000)
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).

Entry informationi

Entry nameiCCL5_HUMAN
AccessioniPrimary (citable) accession number: P13501
Secondary accession number(s): O43646
, Q0QVW8, Q4ZGJ1, Q9NYA2, Q9UBG2, Q9UC99
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: July 15, 1999
Last modified: July 22, 2015
This is version 170 of the entry and version 3 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.