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P13501

- CCL5_HUMAN

UniProt

P13501 - CCL5_HUMAN

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Protein

C-C motif chemokine 5

Gene

CCL5

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. CCR1 chemokine receptor binding Source: UniProtKB
  2. CCR4 chemokine receptor binding Source: BHF-UCL
  3. CCR5 chemokine receptor binding Source: BHF-UCL
  4. chemoattractant activity Source: UniProtKB
  5. chemokine activity Source: UniProtKB
  6. chemokine receptor antagonist activity Source: BHF-UCL
  7. chemokine receptor binding Source: BHF-UCL
  8. phosphatidylinositol phospholipase C activity Source: UniProtKB
  9. phospholipase activator activity Source: UniProtKB
  10. protein homodimerization activity Source: BHF-UCL
  11. protein kinase activity Source: UniProtKB
  12. protein self-association Source: BHF-UCL
  13. receptor signaling protein tyrosine kinase activator activity Source: BHF-UCL

GO - Biological processi

  1. activation of phospholipase D activity Source: BHF-UCL
  2. calcium ion transport Source: UniProtKB
  3. cell-cell signaling Source: BHF-UCL
  4. cellular calcium ion homeostasis Source: UniProtKB
  5. cellular protein complex assembly Source: BHF-UCL
  6. cellular response to fibroblast growth factor stimulus Source: UniProtKB
  7. cellular response to interferon-gamma Source: UniProtKB
  8. cellular response to interleukin-1 Source: UniProtKB
  9. cellular response to organic cyclic compound Source: UniProtKB
  10. cellular response to tumor necrosis factor Source: UniProtKB
  11. chemokine-mediated signaling pathway Source: UniProtKB
  12. chemotaxis Source: UniProtKB
  13. dendritic cell chemotaxis Source: BHF-UCL
  14. eosinophil chemotaxis Source: BHF-UCL
  15. exocytosis Source: UniProtKB
  16. G-protein coupled receptor signaling pathway Source: UniProtKB
  17. inflammatory response Source: UniProtKB
  18. leukocyte cell-cell adhesion Source: BHF-UCL
  19. lipopolysaccharide-mediated signaling pathway Source: UniProtKB
  20. macrophage chemotaxis Source: BHF-UCL
  21. MAPK cascade Source: UniProtKB
  22. monocyte chemotaxis Source: UniProtKB
  23. negative regulation by host of viral transcription Source: UniProtKB
  24. negative regulation of chemokine-mediated signaling pathway Source: GOC
  25. negative regulation of G-protein coupled receptor protein signaling pathway Source: UniProtKB
  26. negative regulation of T cell apoptotic process Source: BHF-UCL
  27. negative regulation of viral genome replication Source: BHF-UCL
  28. neutrophil activation Source: BHF-UCL
  29. positive chemotaxis Source: GOC
  30. positive regulation of activation of JAK2 kinase activity Source: BHF-UCL
  31. positive regulation of calcium ion transport Source: UniProtKB
  32. positive regulation of cell adhesion Source: BHF-UCL
  33. positive regulation of cell-cell adhesion mediated by integrin Source: BHF-UCL
  34. positive regulation of cell migration Source: UniProtKB
  35. positive regulation of cellular biosynthetic process Source: BHF-UCL
  36. positive regulation of homotypic cell-cell adhesion Source: BHF-UCL
  37. positive regulation of innate immune response Source: BHF-UCL
  38. positive regulation of JAK-STAT cascade Source: BHF-UCL
  39. positive regulation of macrophage chemotaxis Source: BHF-UCL
  40. positive regulation of monocyte chemotaxis Source: BHF-UCL
  41. positive regulation of natural killer cell chemotaxis Source: UniProtKB
  42. positive regulation of phosphatidylinositol 3-kinase signaling Source: BHF-UCL
  43. positive regulation of phosphorylation Source: BHF-UCL
  44. positive regulation of protein tyrosine kinase activity Source: GOC
  45. positive regulation of smooth muscle cell migration Source: BHF-UCL
  46. positive regulation of smooth muscle cell proliferation Source: BHF-UCL
  47. positive regulation of T cell apoptotic process Source: BHF-UCL
  48. positive regulation of T cell chemotaxis Source: BHF-UCL
  49. positive regulation of T cell migration Source: MGI
  50. positive regulation of T cell proliferation Source: BHF-UCL
  51. positive regulation of translational initiation Source: BHF-UCL
  52. positive regulation of tyrosine phosphorylation of STAT protein Source: BHF-UCL
  53. positive regulation of viral genome replication Source: BHF-UCL
  54. protein kinase B signaling Source: UniProtKB
  55. protein phosphorylation Source: GOC
  56. protein tetramerization Source: BHF-UCL
  57. regulation of chronic inflammatory response Source: BHF-UCL
  58. regulation of insulin secretion Source: UniProtKB
  59. regulation of neuron death Source: UniProtKB
  60. regulation of T cell activation Source: BHF-UCL
  61. response to toxic substance Source: UniProtKB
  62. 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: Chromosome 17

Organism-specific databases

HGNCiHGNC:10632. CCL5.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35564.

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. differential.
GenevestigatoriP13501.

Interactioni

Binary interactionsi

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

Protein-protein interaction databases

BioGridi112255. 16 interactions.
DIPiDIP-31N.
IntActiP13501. 13 interactions.
MINTiMINT-103226.
STRINGi9606.ENSP00000293272.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
GeneTreeiENSGT00760000120402.
HOVERGENiHBG017871.
InParanoidiP13501.
KOiK12499.
OrthoDBiEOG7CVQ1F.
PhylomeDBiP13501.
TreeFamiTF334888.

Family and domain databases

InterProiIPR000827. Chemokine_CC_CS.
IPR001811. Chemokine_IL8-like_dom.
[Graphical view]
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. 1 PublicationCurated
Sequence conflicti14 – 141A → V in AAF73070. 1 PublicationCurated

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:
EMBL
GenBank
DDBJ
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.
GeneIDi6352.
KEGGihsa:6352.
UCSCiuc002hkf.3. human.

Polymorphism databases

DMDMi6175077.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Wikipedia

RANTES entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS11300.1.
PIRi A28815.
RefSeqi NP_002976.2. NM_002985.2.
UniGenei Hs.514821.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B3A X-ray 1.60 A/B 25-91 [» ]
1EQT X-ray 1.60 A/B 26-91 [» ]
1HRJ NMR - A/B 24-91 [» ]
1RTN NMR - A/B 24-91 [» ]
1RTO NMR - A/B 24-91 [» ]
1U4L X-ray 2.00 A/B 24-91 [» ]
1U4M X-ray 2.00 A/B 24-91 [» ]
1U4P X-ray 1.70 A/B 24-91 [» ]
1U4R X-ray 2.20 A/B/C/D 24-91 [» ]
2L9H Other - A/B/C/D 24-91 [» ]
2VXW X-ray 1.70 A/B/C/D 33-91 [» ]
ProteinModelPortali P13501.
SMRi P13501. Positions 25-91.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112255. 16 interactions.
DIPi DIP-31N.
IntActi P13501. 13 interactions.
MINTi MINT-103226.
STRINGi 9606.ENSP00000293272.

Chemistry

BindingDBi P13501.
ChEMBLi CHEMBL1275217.

PTM databases

PhosphoSitei P13501.

Polymorphism databases

DMDMi 6175077.

Proteomic databases

PaxDbi P13501.
PeptideAtlasi P13501.
PRIDEi P13501.

Protocols and materials databases

DNASUi 6352.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000603197 ; ENSP00000474412 ; ENSG00000271503 .
ENST00000605140 ; ENSP00000475057 ; ENSG00000271503 .
GeneIDi 6352.
KEGGi hsa:6352.
UCSCi uc002hkf.3. human.

Organism-specific databases

CTDi 6352.
GeneCardsi GC17M034198.
HGNCi HGNC:10632. CCL5.
MIMi 187011. gene.
neXtProti NX_P13501.
PharmGKBi PA35564.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG38896.
GeneTreei ENSGT00760000120402.
HOVERGENi HBG017871.
InParanoidi P13501.
KOi K12499.
OrthoDBi EOG7CVQ1F.
PhylomeDBi P13501.
TreeFami TF334888.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTracei P13501.
GeneWikii CCL5.
GenomeRNAii 6352.
NextBioi 24676.
PMAP-CutDB P13501.
PROi P13501.
SOURCEi Search...

Gene expression databases

Bgeei P13501.
CleanExi HS_CCL5.
ExpressionAtlasi P13501. differential.
Genevestigatori P13501.

Family and domain databases

InterProi IPR000827. Chemokine_CC_CS.
IPR001811. Chemokine_IL8-like_dom.
[Graphical view ]
Pfami PF00048. IL8. 1 hit.
[Graphical view ]
SMARTi SM00199. SCY. 1 hit.
[Graphical view ]
SUPFAMi SSF54117. SSF54117. 1 hit.
PROSITEi PS00472. SMALL_CYTOKINES_CC. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 165 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