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P13500 (CCL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 178. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
C-C motif chemokine 2
Alternative name(s):
HC11
Monocyte chemoattractant protein 1
Monocyte chemotactic and activating factor
Short name=MCAF
Monocyte chemotactic protein 1
Short name=MCP-1
Monocyte secretory protein JE
Small-inducible cytokine A2
Gene names
Name:CCL2
Synonyms:MCP1, SCYA2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length99 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Chemotactic factor that attracts monocytes and basophils but not neutrophils or eosinophils. Augments monocyte anti-tumor activity. Has been implicated in the pathogenesis of diseases characterized by monocytic infiltrates, like psoriasis, rheumatoid arthritis or atherosclerosis. May be involved in the recruitment of monocytes into the arterial wall during the disease process of atherosclerosis.

Subunit structure

Monomer or homodimer; in equilibrium. Binds to CCR2 and CCR4. Is tethered on endothelial cells by glycosaminoglycan (GAG) side chains of proteoglycans. Ref.20 Ref.22

Subcellular location

Secreted.

Induction

Up-regulated upon hypertonic conditions. Ref.26

Post-translational modification

Processing at the N-terminus can regulate receptor and target cell selectivity. Deletion of the N-terminal residue converts it from an activator of basophil to an eosinophil chemoattractant.

Polymorphism

Genetic variations in CCL2 determine Mycobacterium tuberculosis susceptibility [MIM:607948].

Sequence similarities

Belongs to the intercrine beta (chemokine CC) family.

Ontologies

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

Traceable author statement PubMed 10542238. Source: ProtInc

G-protein coupled receptor signaling pathway, coupled to cyclic nucleotide second messenger

Traceable author statement PubMed 10770925. Source: ProtInc

JAK-STAT cascade

Traceable author statement PubMed 9670957. Source: ProtInc

MAPK cascade

Inferred from mutant phenotype PubMed 21147091. Source: UniProtKB

activation of signaling protein activity involved in unfolded protein response

Traceable author statement. Source: Reactome

aging

Inferred from electronic annotation. Source: Ensembl

angiogenesis

Traceable author statement PubMed 18334747. Source: BHF-UCL

astrocyte cell migration

Inferred from direct assay PubMed 12271471. Source: BHF-UCL

cell adhesion

Traceable author statement PubMed 10198043. Source: ProtInc

cell surface receptor signaling pathway

Traceable author statement PubMed 9548499. Source: ProtInc

cellular calcium ion homeostasis

Inferred from electronic annotation. Source: Ensembl

cellular homeostasis

Traceable author statement PubMed 18334747. Source: BHF-UCL

cellular protein metabolic process

Traceable author statement. Source: Reactome

cellular response to fibroblast growth factor stimulus

Inferred from expression pattern PubMed 9407497. Source: UniProtKB

cellular response to interferon-gamma

Inferred from expression pattern PubMed 9407497. Source: UniProtKB

cellular response to interleukin-1

Inferred from expression pattern PubMed 9407497. Source: UniProtKB

cellular response to lipopolysaccharide

Inferred from sequence or structural similarity. Source: BHF-UCL

cellular response to organic cyclic compound

Inferred from direct assay PubMed 21147091. Source: UniProtKB

cellular response to tumor necrosis factor

Inferred from expression pattern PubMed 9407497. Source: UniProtKB

chemokine-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

chemotaxis

Traceable author statement PubMed 10623817. Source: ProtInc

cytokine-mediated signaling pathway

Inferred from direct assay PubMed 12207323. Source: BHF-UCL

cytoskeleton organization

Inferred from direct assay PubMed 10072545. Source: UniProtKB

endoplasmic reticulum unfolded protein response

Traceable author statement. Source: Reactome

helper T cell extravasation

Inferred from sequence or structural similarity. Source: BHF-UCL

humoral immune response

Traceable author statement PubMed 9548499. Source: ProtInc

inflammatory response

Inferred from direct assay PubMed 21147091. Source: UniProtKB

lipopolysaccharide-mediated signaling pathway

Inferred from direct assay PubMed 21147091. Source: UniProtKB

lymphocyte chemotaxis

Inferred from electronic annotation. Source: Ensembl

macrophage chemotaxis

Inferred from direct assay PubMed 12207323. Source: BHF-UCL

maternal process involved in parturition

Inferred from electronic annotation. Source: Ensembl

monocyte chemotaxis

Inferred from direct assay PubMed 12207323. Source: BHF-UCL

negative regulation of angiogenesis

Inferred from electronic annotation. Source: Ensembl

negative regulation of glial cell apoptotic process

Inferred from direct assay PubMed 12753088. Source: UniProtKB

negative regulation of natural killer cell chemotaxis

Inferred from direct assay PubMed 7545673. Source: UniProtKB

negative regulation of neuron apoptotic process

Inferred from direct assay PubMed 12753088. Source: UniProtKB

neutrophil chemotaxis

Inferred from electronic annotation. Source: Ensembl

organ morphogenesis

Traceable author statement PubMed 9364936. Source: ProtInc

organ regeneration

Inferred from electronic annotation. Source: Ensembl

positive regulation of T cell activation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of apoptotic cell clearance

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of endothelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of immune complex clearance by monocytes and macrophages

Inferred from electronic annotation. Source: Ensembl

positive regulation of macrophage chemotaxis

Inferred from electronic annotation. Source: Ensembl

positive regulation of nitric-oxide synthase biosynthetic process

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of synaptic transmission

Inferred from electronic annotation. Source: Ensembl

protein kinase B signaling

Inferred from mutant phenotype PubMed 21147091. Source: UniProtKB

protein phosphorylation

Traceable author statement PubMed 9670957. Source: ProtInc

regulation of cell shape

Inferred from direct assay PubMed 10072545. Source: UniProtKB

regulation of vascular endothelial growth factor production

Inferred from electronic annotation. Source: Ensembl

response to activity

Inferred from electronic annotation. Source: Ensembl

response to amino acid

Inferred from electronic annotation. Source: Ensembl

response to antibiotic

Inferred from electronic annotation. Source: Ensembl

response to bacterium

Inferred from expression pattern PubMed 16034137. Source: BHF-UCL

response to drug

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to gamma radiation

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

response to heat

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

response to progesterone

Inferred from electronic annotation. Source: Ensembl

response to vitamin B3

Inferred from electronic annotation. Source: Ensembl

signal transduction

Non-traceable author statement PubMed 10770925. Source: ProtInc

transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

vascular endothelial growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

viral genome replication

Traceable author statement PubMed 10985244. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

extracellular region

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

extracellular space

Traceable author statement PubMed 10942204. Source: ProtInc

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionCCR2 chemokine receptor binding

Inferred from sequence or structural similarity. Source: BHF-UCL

chemokine activity

Traceable author statement PubMed 10623817. Source: ProtInc

heparin binding

Inferred from electronic annotation. Source: Ensembl

protein kinase activity

Traceable author statement PubMed 9973507. Source: ProtInc

receptor binding

Traceable author statement PubMed 10542238. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.15
Chain24 – 9976C-C motif chemokine 2
PRO_0000005146

Sites

Site311Involved in dimerization
Site361Involved in dimerization, receptor binding and signaling
Site411Involved in GAG binding
Site421Involved in GAG binding
Site471Involved in GAG binding and receptor binding
Site581Involved in dimerization
Site611Involved in dimerization
Site721Involved in GAG binding and receptor binding
Site811Involved in GAG binding
Site891Involved in GAG binding

Amino acid modifications

Modified residue241Pyrrolidone carboxylic acid Ref.6
Glycosylation371N-linked (GlcNAc...) Potential
Disulfide bond34 ↔ 59
Disulfide bond35 ↔ 75

Experimental info

Mutagenesis24 – 9168Missing: 83% reduction in activity.
Mutagenesis24 – 8562Missing: 90% reduction in activity.
Mutagenesis241Missing: Loss of activity.
Mutagenesis25 – 317Missing: Loss of signaling. Ref.22 Ref.23
Mutagenesis261D → A: Reduction in activity. Ref.23
Mutagenesis281I → A: Slight reduction in activity. Ref.23
Mutagenesis291N → A: 50% reduction in activity. Ref.23
Mutagenesis311P → A: Loss of dimerization; slight reduction of activity. Ref.22 Ref.23
Mutagenesis321V → A: Slight reduction in activity. Ref.22 Ref.23
Mutagenesis321V → E: Slight reduction in affinity. Ref.22 Ref.23
Mutagenesis331T → A: Slight reduction in activity. Ref.22 Ref.23
Mutagenesis331T → E: Slight reduction in affinity. Ref.22 Ref.23
Mutagenesis361Y → A: Loss of activity. Ref.22
Mutagenesis471R → F: 95% reduction in activity; strong reduction of receptor binding.
Mutagenesis501S → Q: 40% reduction in activity.
Mutagenesis511Y → D: Loss of activity.
Mutagenesis531R → L: Loss of activity.
Mutagenesis791K → A: No effect on heparin binding.
Mutagenesis811K → A: Strongly reduces heparin binding. Ref.21
Mutagenesis891H → A: Strongly reduces heparin binding. Ref.21
Mutagenesis911D → L: 90% reduction in activity.
Mutagenesis95 – 995Missing: No effect on heparin binding. Ref.21

Secondary structure

................. 99
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13500 [UniParc].

Last modified January 1, 1990. Version 1.
Checksum: 45EC72361435302F

FASTA9911,025
        10         20         30         40         50         60 
MKVSAALLCL LLIAATFIPQ GLAQPDAINA PVTCCYNFTN RKISVQRLAS YRRITSSKCP 

        70         80         90 
KEAVIFKTIV AKEICADPKQ KWVQDSMDHL DKQTQTPKT 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequencing of the cDNA for human monocyte chemotactic and activating factor (MCAF)."
Furutani Y., Nomura H., Notake M., Oyamada Y., Fukui T., Yamada M., Larsen C.G., Oppenheim J.J., Matsushima K.
Biochem. Biophys. Res. Commun. 159:249-255(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The human homolog of the JE gene encodes a monocyte secretory protein."
Rollins B.J., Stier P., Ernst T., Wong G.G.
Mol. Cell. Biol. 9:4687-4695(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[3]"Human monocyte chemoattractant protein-1 (MCP-1). Full-length cDNA cloning, expression in mitogen-stimulated blood mononuclear leukocytes, and sequence similarity to mouse competence gene JE."
Yoshimura T., Yuhki N., Moore S.K., Appella E., Lerman M.I., Leonard E.J.
FEBS Lett. 244:487-493(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Glial tumor.
[4]"Cloning and expression of a gamma-interferon-inducible gene in monocytes: a new member of a cytokine gene family."
Chang H.C., Hsu F., Freeman G.J., Griffin J.D., Reinherz E.L.
Int. Immunol. 1:388-397(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]"Structure of human monocyte chemotactic protein gene and its regulation by TPA."
Shyy Y.J., Li Y.S., Kolattukudy P.E.
Biochem. Biophys. Res. Commun. 169:346-351(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Human monocyte chemoattractant protein-1 (MCP-1)."
Yoshimura T., Leonard E.J.
Adv. Exp. Med. Biol. 305:47-56(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[7]"The expression of monocyte chemotactic protein (MCP-1) in human vascular endothelium in vitro and in vivo."
Li Y.S., Shyy Y.J., Wright J.G., Valente A.J., Cornhill J.F., Kolattukudy P.E.
Mol. Cell. Biochem. 126:61-68(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[8]"Differential transcriptional regulation of the monocyte-chemoattractant protein-1 (MCP-1) gene in tumorigenic and non-tumorigenic HPV 18 positive cells: the role of the chromatin structure and AP-1 composition."
Finzer P., Soto U., Delius H., Patzelt A., Poustka A., Coy J.F., zur Hausen H., Roesl F.
Oncogene 19:3235-3244(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[9]"Protein with cytokine activity, recombinant DNA, expression vector and hosts for obtaining it."
Caput D., Ferrara P., Miloux B., Minty A., Vita N.
Patent number EP0488900, 03-JUN-1992
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[10]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[11]SeattleSNPs variation discovery resource
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[12]"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. expand/collapse author list , 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].
Tissue: Urinary bladder.
[13]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[14]"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: Pancreas.
[15]"Complete amino acid sequence of a human monocyte chemoattractant, a putative mediator of cellular immune reactions."
Robinson E.A., Yoshimura T., Leonard E.J., Tanaka S., Griffin P.R., Shabanowitz J., Hunt D.F., Appella E.
Proc. Natl. Acad. Sci. U.S.A. 86:1850-1854(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-99.
[16]"Identification of the monocyte chemotactic protein from human osteosarcoma cells and monocytes: detection of a novel N-terminally processed form."
Decock B., Conings R., Lenaerts J.-P., Biliau A., van Damme J.
Biochem. Biophys. Res. Commun. 167:904-909(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 29-53 AND 82-92.
[17]"Assignment of the human small inducible cytokine A2 gene, SCYA2 (encoding JE or MCP-1), to 17q11.2-12: evolutionary relatedness of cytokines clustered at the same locus."
Rollins B.J., Morton C.C., Ledbetter D.H., Eddy R.L. Jr., Shows T.B.
Genomics 10:489-492(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE STRUCTURE.
[18]"Structure/activity analysis of human monocyte chemoattractant protein-1 (MCP-1) by mutagenesis. Identification of a mutated protein that inhibits MCP-1-mediated monocyte chemotaxis."
Zhang Y.J., Rutledge B.J., Rollins B.J.
J. Biol. Chem. 269:15918-15924(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[19]"Deletion of the NH2-terminal residue converts monocyte chemotactic protein 1 from an activator of basophil mediator release to an eosinophil chemoattractant."
Weber M., Uguccioni M., Baggiolini M., Clark-Lewis I., Dahinden C.A.
J. Exp. Med. 183:681-685(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: EFFECT OF DELETION OF N-TERMINAL RESIDUES.
[20]"Structural characterization of a monomeric chemokine: monocyte chemoattractant protein-3."
Kim K.-S., Rajarathnam K., Clark-Lewis I., Sykes B.D.
FEBS Lett. 395:277-282(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[21]"Lysine 58 and histidine 66 at the C-terminal alpha-helix of monocyte chemoattractant protein-1 are essential for glycosaminoglycan binding."
Chakravarty L., Rogers L., Quach T., Breckenridge S., Kolattukudy P.E.
J. Biol. Chem. 273:29641-29647(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: GAG BINDING SITES LYS-81 AND HIS-89, MUTAGENESIS OF LYS-81; HIS-89 AND 95-GLN--THR-99.
[22]"Monomeric monocyte chemoattractant protein-1 (MCP-1) binds and activates the MCP-1 receptor CCR2B."
Paavola C.D., Hemmerich S., Grunberger D., Polsky I., Bloom A., Freedman R., Mulkins M., Bhakta S., McCarley D., Wiesent L., Wong B., Jarnagin K., Handel T.M.
J. Biol. Chem. 273:33157-33165(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: HOMODIMERIZATION, MUTAGENESIS OF PRO-31; VAL-32; THR-33 AND TYR-36.
[23]"Identification of surface residues of the monocyte chemotactic protein 1 that affect signaling through the receptor CCR2."
Jarnagin K., Grunberger D., Mulkins M., Wong B., Hemmerich S., Paavola C., Bloom A., Bhakta S., Diehl F., Freedman R., McCarley D., Polsky I., Ping-Tsou A., Kosaka A., Handel T.M.
Biochemistry 38:16167-16177(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF 25-PRO--PRO-31; ASP-26; ILE-28; ASN-29; PRO-31; VAL-32 AND THR-33.
[24]"Identification of residues in the monocyte chemotactic protein-1 that contact the MCP-1 receptor, CCR2."
Hemmerich S., Paavola C., Bloom A., Bhakta S., Freedman R., Grunberger D., Krstenansky J., Lee S., McCarley D., Mulkins M., Wong B., Pease J., Mizoue L., Mirzadegan T., Polsky I., Thompson K., Handel T.M., Jarnagin K.
Biochemistry 38:13013-13025(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: IMPORTANCE OF TYR-36; ARG-47; LYS-58; LYS-61 AND LYS-72 FOR RECEPTOR BINDING, MUTAGENESIS.
[25]"Identification of the glycosaminoglycan binding site of the CC chemokine, MCP-1: implications for structure and function in vivo."
Lau E.K., Paavola C.D., Johnson Z., Gaudry J.-P., Geretti E., Borlat F., Kungl A.J., Proudfoot A.E., Handel T.M.
J. Biol. Chem. 279:22294-22305(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: GAG BINDING SITES ARG-41; LYS-42 AND ARG-47, MUTAGENESIS.
[26]"Fat-specific protein 27 modulates nuclear factor of activated T cells 5 and the cellular response to stress."
Ueno M., Shen W.J., Patel S., Greenberg A.S., Azhar S., Kraemer F.B.
J. Lipid Res. 54:734-743(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION BY OSMOTIC STRESS.
[27]"Modeling the three-dimensional structure of the monocyte chemo-attractant and activating protein MCAF/MCP-1 on the basis of the solution structure of interleukin-8."
Gronenborn A.M., Clore G.M.
Protein Eng. 4:263-269(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
[28]"Heteronuclear (1H, 13C, 15N) NMR assignments and solution structure of the monocyte chemoattractant protein-1 (MCP-1) dimer."
Handel T.M., Domaille P.J.
Biochemistry 35:6569-6584(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[29]"The structure of MCP-1 in two crystal forms provides a rare example of variable quaternary interactions."
Lubkowski J., Bujacz G., Domaille P.J., Handel T.M., Wlodawer A.
Nat. Struct. Biol. 4:64-69(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
[30]"A functional promoter polymorphism in monocyte chemoattractant protein-1 is associated with increased susceptibility to pulmonary tuberculosis."
Flores-Villanueva P.O., Ruiz-Morales J.A., Song C.-H., Flores L.M., Jo E.-K., Montano M., Barnes P.F., Selman M., Granados J.
J. Exp. Med. 202:1649-1658(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MYCOBACTERIUM TUBERCULOSIS SUSCEPTIBILITY.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M24545 mRNA. Translation: AAA18164.1.
M28225, M28223, M28224 Genomic DNA. Translation: AAA60308.1.
M28226 mRNA. Translation: AAA60309.1.
M31626, M30816, M31625 Genomic DNA. Translation: AAA36330.1.
X14768 mRNA. Translation: CAA32876.1.
M37719 Genomic DNA. Translation: AAA18102.1.
S71513 mRNA. Translation: AAB20651.1.
S69738 mRNA. Translation: AAB29926.1.
Y18933 Genomic DNA. Translation: CAC14049.1.
A17786 mRNA. Translation: CAA01352.1.
BT007329 mRNA. Translation: AAP35993.1.
AF519531 Genomic DNA. Translation: AAM54046.1.
AK311960 mRNA. Translation: BAG34900.1.
CH471147 Genomic DNA. Translation: EAW80212.1.
BC009716 mRNA. Translation: AAH09716.1.
PIRA60299. A35474.
RefSeqNP_002973.1. NM_002982.3.
UniGeneHs.303649.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DOKX-ray1.85A/B24-99[»]
1DOLX-ray2.40A24-99[»]
1DOMNMR-A/B24-99[»]
1DONNMR-A/B24-99[»]
1MCAmodel-A/B24-96[»]
1ML0X-ray2.80D24-99[»]
2BDNX-ray2.53A24-99[»]
2NZ1X-ray2.50D/E/Y24-99[»]
3IFDX-ray1.90A24-99[»]
4DN4X-ray2.80M24-99[»]
ProteinModelPortalP13500.
SMRP13500. Positions 24-94.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112251. 15 interactions.
DIPDIP-5838N.
IntActP13500. 1 interaction.
MINTMINT-103269.
STRING9606.ENSP00000225831.

Chemistry

ChEMBLCHEMBL1649052.
DrugBankDB01076. Atorvastatin.
DB01406. Danazol.
DB01055. Mimosine.
DB00641. Simvastatin.

Polymorphism databases

DMDM126842.

Proteomic databases

PaxDbP13500.
PRIDEP13500.

Protocols and materials databases

DNASU6347.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000225831; ENSP00000225831; ENSG00000108691.
GeneID6347.
KEGGhsa:6347.
UCSCuc002hhy.3. human.

Organism-specific databases

CTD6347.
GeneCardsGC17P032582.
HGNCHGNC:10618. CCL2.
HPACAB013676.
HPA019163.
MIM158105. gene.
607948. phenotype.
neXtProtNX_P13500.
PharmGKBPA130413151.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG46819.
HOGENOMHOG000036686.
HOVERGENHBG017871.
InParanoidP13500.
KOK14624.
OMANKEICAD.
PhylomeDBP13500.
TreeFamTF334888.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressP13500.
BgeeP13500.
CleanExHS_CCL2.
GenevestigatorP13500.

Family and domain databases

InterProIPR000827. Chemokine_CC_CS.
IPR001811. Chemokine_IL8-like_dom.
[Graphical view]
PfamPF00048. IL8. 1 hit.
[Graphical view]
SMARTSM00199. SCY. 1 hit.
[Graphical view]
SUPFAMSSF54117. SSF54117. 1 hit.
PROSITEPS00472. SMALL_CYTOKINES_CC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP13500.
GeneWikiCCL2.
GenomeRNAi6347.
NextBio24660.
PMAP-CutDBP13500.
PROP13500.
SOURCESearch...

Entry information

Entry nameCCL2_HUMAN
AccessionPrimary (citable) accession number: P13500
Secondary accession number(s): B2R4V3, Q9UDF3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: April 16, 2014
This is version 178 of the entry and version 1 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 17

Human chromosome 17: entries, gene names and cross-references to MIM