P13500 (CCL2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	99 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
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 process	Chemotaxis Inflammatory response
Cellular component	Secreted
Domain	Signal
Molecular function	Cytokine
PTM	Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	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: Compara 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 cellular calcium ion homeostasis Inferred from electronic annotation. Source: Compara cellular homeostasis Traceable author statement PubMed 18334747. Source: BHF-UCL 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 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: Compara cytokine-mediated signaling pathway Inferred from direct assay PubMed 12207323. Source: BHF-UCL cytoskeleton organization Inferred from direct assay PubMed 10072545. Source: UniProtKB 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: Compara macrophage chemotaxis Inferred from direct assay PubMed 12207323. Source: BHF-UCL maternal process involved in parturition Inferred from electronic annotation. Source: Compara monocyte chemotaxis Inferred from direct assay PubMed 12207323. Source: BHF-UCL negative regulation of angiogenesis Inferred from electronic annotation. Source: Compara negative regulation of 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 neutrophil chemotaxis Inferred from electronic annotation. Source: Compara organ morphogenesis Traceable author statement PubMed 9364936. Source: ProtInc organ regeneration Inferred from electronic annotation. Source: Compara 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: Compara positive regulation of immune complex clearance by monocytes and macrophages Inferred from electronic annotation. Source: Compara positive regulation of macrophage chemotaxis Inferred from electronic annotation. Source: Compara 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: Compara protein kinase B signaling cascade Inferred from mutant phenotype PubMed 21147091. Source: UniProtKB regulation of cell shape Inferred from direct assay PubMed 10072545. Source: UniProtKB regulation of vascular endothelial growth factor production Inferred from electronic annotation. Source: Compara response to activity Inferred from electronic annotation. Source: Compara response to amino acid stimulus Inferred from electronic annotation. Source: Compara response to antibiotic Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to ethanol Inferred from electronic annotation. Source: Compara response to gamma radiation Inferred from electronic annotation. Source: Compara response to glucocorticoid stimulus Inferred from electronic annotation. Source: Compara response to heat Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from electronic annotation. Source: Compara response to mechanical stimulus Inferred from electronic annotation. Source: Compara response to progesterone stimulus Inferred from electronic annotation. Source: Compara response to vitamin B3 Inferred from electronic annotation. Source: Compara transforming growth factor beta receptor signaling pathway Inferred from electronic annotation. Source: Compara vascular endothelial growth factor receptor signaling pathway Inferred from electronic annotation. Source: Compara viral genome replication Traceable author statement PubMed 10985244. Source: ProtInc
Cellular_component	cytoplasm Inferred from electronic annotation. Source: Compara extracellular space Traceable author statement PubMed 10942204. Source: ProtInc neuronal cell body Inferred from electronic annotation. Source: Compara
Molecular_function	CCR2 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: Compara protein kinase activity Traceable author statement PubMed 9973507. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Ref.15

Chain

24 – 99

76

C-C motif chemokine 2

PRO_0000005146

Sites

Site

31

1

Involved in dimerization

Site

36

1

Involved in dimerization, receptor binding and signaling

Site

41

1

Involved in GAG binding

Site

42

1

Involved in GAG binding

Site

47

1

Involved in GAG binding and receptor binding

Site

58

1

Involved in dimerization

Site

61

1

Involved in dimerization

Site

72

1

Involved in GAG binding and receptor binding

Site

81

1

Involved in GAG binding

Site

89

1

Involved in GAG binding

Amino acid modifications

Modified residue

24

1

Pyrrolidone carboxylic acid Ref.6

Glycosylation

37

1

N-linked (GlcNAc...) Potential

Disulfide bond

34 ↔ 59

Disulfide bond

35 ↔ 75

Experimental info

Mutagenesis

24 – 91

68

Missing: 83% reduction in activity.

Mutagenesis

24 – 85

62

Missing: 90% reduction in activity.

Mutagenesis

24

1

Missing: Loss of activity.

Mutagenesis

25 – 31

7

Missing: Loss of signaling. Ref.22 Ref.23

Mutagenesis

26

1

D → A: Reduction in activity. Ref.23

Mutagenesis

28

1

I → A: Slight reduction in activity. Ref.23

Mutagenesis

29

1

N → A: 50% reduction in activity. Ref.23

Mutagenesis

31

1

P → A: Loss of dimerization; slight reduction of activity. Ref.22 Ref.23

Mutagenesis

32

1

V → A: Slight reduction in activity. Ref.22 Ref.23

Mutagenesis

32

1

V → E: Slight reduction in affinity. Ref.22 Ref.23

Mutagenesis

33

1

T → A: Slight reduction in activity. Ref.22 Ref.23

Mutagenesis

33

1

T → E: Slight reduction in affinity. Ref.22 Ref.23

Mutagenesis

36

1

Y → A: Loss of activity. Ref.22

Mutagenesis

47

1

R → F: 95% reduction in activity; strong reduction of receptor binding.

Mutagenesis

50

1

S → Q: 40% reduction in activity.

Mutagenesis

51

1

Y → D: Loss of activity.

Mutagenesis

53

1

R → L: Loss of activity.

Mutagenesis

79

1

K → A: No effect on heparin binding.

Mutagenesis

81

1

K → A: Strongly reduces heparin binding. Ref.21

Mutagenesis

89

1

H → A: Strongly reduces heparin binding. Ref.21

Mutagenesis

91

1

D → L: 90% reduction in activity.

Mutagenesis

95 – 99

5

Missing: No effect on heparin binding. Ref.21

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

99

Helix Strand Turn

Details...

Helix

25 – 29

5

Beta strand

32 – 34

3

Helix

45 – 47

3

Beta strand

48 – 54

7

Beta strand

59 – 61

3

Beta strand

63 – 68

6

Beta strand

73 – 76

4

Helix

81 – 92

12

Beta strand

93 – 95

3

Sequences

	Sequence		Length	Mass (Da)
	P13500 [UniParc]. Last modified January 1, 1990. Version 1. Checksum: 45EC72361435302F	FASTA	99	11,025
	10 20 30 40 50 60 MKVSAALLCL LLIAATFIPQ GLAQPDAINA PVTCCYNFTN RKISVQRLAS YRRITSSKCP 70 80 90 KEAVIFKTIV AKEICADPKQ KWVQDSMDHL DKQTQTPKT

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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.
[27]	"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.
[28]	"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).
[29]	"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

Wikipedia

CCL2 entry

SeattleSNPs

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.

IPI

IPI00009308.

PIR

A60299. A35474.

RefSeq

NP_002973.1. NM_002982.3.

UniGene

Hs.303649.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DOK	X-ray	1.85	A/B	24-99	[»]
1DOL	X-ray	2.40	A	24-99	[»]
1DOM	NMR	-	A/B	24-99	[»]
1DON	NMR	-	A/B	24-99	[»]
1MCA	model	-	A/B	24-96	[»]
1ML0	X-ray	2.80	D	24-99	[»]
2BDN	X-ray	2.53	A	24-99	[»]
2NZ1	X-ray	2.50	D/E/Y	24-99	[»]
3IFD	X-ray	1.90	A	24-99	[»]
4DN4	X-ray	2.80	M	24-99	[»]

ProteinModelPortal

P13500.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5838N.

IntAct

P13500. 1 interaction.

MINT

MINT-103269.

STRING

9606.ENSP00000225831.

Polymorphism databases

DMDM

126842.

Proteomic databases

PaxDb

P13500.

PRIDE

P13500.

Protocols and materials databases

DNASU

6347.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000225831; ENSP00000225831; ENSG00000108691.

GeneID

6347.

KEGG

hsa:6347.

UCSC

uc002hhy.3. human.

Organism-specific databases

CTD

6347.

GeneCards

GC17P032582.

HGNC

HGNC:10618. CCL2.

HPA

CAB013676.
HPA019163.

MIM

158105. gene.
607948. phenotype.

neXtProt

NX_P13500.

PharmGKB

PA130413151.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG46819.

HOGENOM

HOG000036686.

HOVERGEN

HBG017871.

InParanoid

P13500.

KO

K14624.

OMA

MSYRRVT.

OrthoDB

EOG45DWR1.

PhylomeDB

P13500.

Enzyme and pathway databases

Pathway_Interaction_DB

il23pathway. IL23-mediated signaling events.

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.

Gene expression databases

ArrayExpress

P13500.

Bgee

P13500.

CleanEx

HS_CCL2.

Genevestigator

P13500.

GermOnline

ENSG00000108691. Homo sapiens.

Family and domain databases

InterPro

IPR000827. Chemokine_CC_CS.
IPR001811. Chemokine_IL8-like_dom.
[Graphical view]

Pfam

PF00048. IL8. 1 hit.
[Graphical view]

SMART

SM00199. SCY. 1 hit.
[Graphical view]

SUPFAM

SSF54117. Chemokine_IL8. 1 hit.

PROSITE

PS00472. SMALL_CYTOKINES_CC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1649052.

DrugBank

DB01076. Atorvastatin.
DB01406. Danazol.
DB01055. Mimosine.
DB00641. Simvastatin.

EvolutionaryTrace

P13500.

GenomeRNAi

6347.

NextBio

24660.

PMAP-CutDB

P13500.

SOURCE

Search...

Entry information

Entry name

CCL2_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 170 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.