CCL5

CCL5 (C-C Motif Chemokine Ligand 5) is a Protein Coding gene. Diseases associated with CCL5 include Ulcer Of Lower Limbs and Periapical Granuloma. Among its related pathways are PEDF Induced Signaling and Toll-like receptor signaling pathway. Gene Ontology (GO) annotations related to this gene include protein homodimerization activity and chemokine activity. An important paralog of this gene is CCL3L3.

C-C Motif Chemokine Ligand 5

Activation of phospholipase D activity Source: BHF-UCL
Calcium ion transport Source: UniProtKB
Cell-cell signaling Source: BHF-UCL
Cellular calcium ion homeostasis Source: UniProtKB
Cellular response to fibroblast growth factor stimulus Source: UniProtKB
Cellular response to interferon-gamma Source: UniProtKB
Cellular response to interleukin-1 Source: UniProtKB
Cellular response to organic cyclic compound Source: UniProtKB
Cellular response to tumor necrosis factor Source: UniProtKB
Cellular response to virus Source: ARUK-UCL
Chemokine-mediated signaling pathway Source: UniProtKB
Chemotaxis Source: UniProtKB
Cytokine-mediated signaling pathway Source: Reactome
Dendritic cell chemotaxis Source: BHF-UCL
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: GO_Central
Macrophage chemotaxis Source: BHF-UCL
MAPK cascade Source: UniProtKB
Monocyte chemotaxis Source: GO_Central
Negative regulation by host of viral transcription Source: UniProtKB
Negative regulation of G protein-coupled receptor signaling pathway Source: UniProtKB
Negative regulation of T cell apoptotic process Source: BHF-UCL
Negative regulation of viral genome replication Source: BHF-UCL
Neutrophil activation Source: BHF-UCL
Neutrophil chemotaxis Source: GO_Central
Positive regulation of activation of Janus kinase activity Source: BHF-UCL
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 ERK1 and ERK2 cascade Source: GO_Central
Positive regulation of GTPase activity Source: GO_Central
Positive regulation of homotypic cell-cell adhesion Source: BHF-UCL
Positive regulation of innate immune response Source: BHF-UCL
Positive regulation of macrophage chemotaxis Source: BHF-UCL
Positive regulation of monocyte chemotaxis Source: BHF-UCL
Positive regulation of natural killer cell chemotaxis Source: UniProtKB
Positive regulation of phosphatidylinositol 3-kinase signaling Source: BHF-UCL
Positive regulation of phosphorylation Source: BHF-UCL
Positive regulation of receptor signaling pathway via JAK-STAT Source: BHF-UCL
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
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 toxic substance Source: UniProtKB
Response to virus Source: BHF-UCL

Secreted

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.
The identity of the O-linked saccharides at Ser-27 and Ser-28 are not reported in PubMed:1380064. They are assigned by similarity.