Reviewed, UniProtKB/Swiss-Prot P13500 (CCL2_HUMAN)

Names and origin

Protein names

Recommended name:
    C-C motif chemokine 2
Alternative name(s):
    Small-inducible cytokine A2
    Monocyte chemoattractant protein 1
    Monocyte chemotactic protein 1
      Short name=MCP-1
    Monocyte chemotactic and activating factor
      Short name=MCAF
    Monocyte secretory protein JE
    HC11

Gene names

Name:	CCL2
Synonyms:	MCP1, SCYA2

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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
Gene Ontology (GO)
Biological process	G-protein signaling, coupled to cyclic nucleotide second messenger Traceable author statement. Source: ProtInc JAK-STAT cascade Traceable author statement. Source: ProtInc anti-apoptosis Inferred from direct assay. Source: UniProtKB cell adhesion Traceable author statement. Source: ProtInc cellular calcium ion homeostasis Traceable author statement. Source: ProtInc humoral immune response Traceable author statement. Source: ProtInc inflammatory response Inferred from electronic annotation. Source: UniProtKB-KW macrophage chemotaxis Inferred from direct assay. Source: UniProtKB monocyte chemotaxis Inferred from direct assay. Source: UniProtKB protein amino acid phosphorylation Traceable author statement. Source: ProtInc viral genome replication Traceable author statement. Source: ProtInc
Cellular component	extracellular space Traceable author statement. Source: ProtInc
Molecular function	CCR2 chemokine receptor binding Traceable author statement. Source: UniProtKB chemokine activity Traceable author statement. Source: ProtInc protein kinase activity Traceable author statement. Source: ProtInc signal transducer activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GAMMAHV.M3	O41925	1	EBI-1034732,EBI-1034728	From a different organism.

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

Sequences

	Sequence		Length	Mass (Da)
	P13500-1 [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: 2923622] [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: 2513477] [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: 2465924] [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: 2518726] [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: 2357211] [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: 1661560] [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: 8107690] [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: 10918580] [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: 14702039] [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: 15489334] [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: 2648385] [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: 2322286] [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: 2071154] [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: 8195247] [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: 8627182] [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: 8898111] [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: 9792674] [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: 9837883] [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: 10587439] [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: 10529171] [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: 15033992] [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: 1857712] [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: 8639605] [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: 8989326] [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: 16352737] [Abstract] Cited for: INVOLVEMENT IN MYCOBACTERIUM TUBERCULOSIS SUSCEPTIBILITY.
+	Additional computationally mapped references.

Web resources

Wikipedia

CCL2 entry

SeattleSNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

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 Unassigned DNA. Translation: AAA18102.1.
S71513 mRNA. Translation: AAB20651.1.
S69738 mRNA. Translation: AAB29926.1.
Y18933 Genomic DNA. Translation: CAC14049.1.
A17786 Unassigned RNA. 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.

UniGene

Hs.303649

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:5838N.

IntAct

P13500. 1 interaction.

STRING

P13500.

Genome annotation databases

Ensembl

ENST00000225831; ENSP00000225831; ENSG00000108691; Homo sapiens. [Genome view]

GeneID

6347.

KEGG

hsa:6347.

UCSC

uc002hhy.1. human.

Organism-specific databases

CTD

6347.

GeneCards

GC17P029606.

H-InvDB

HIX0013714.

HGNC

HGNC:10618. CCL2.

HPA

CAB013676.
HPA019163.

MIM

158105. gene.
607948. phenotype.

PharmGKB

PA130413151.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P13500.

HOVERGEN

P13500.

OMA

CCYTLTN

OrthoDB

EOG9FJBV0

Enzyme and pathway databases

Pathway_Interaction_DB

il23pathway. IL23-mediated signaling events.

Gene expression databases

ArrayExpress

P13500.

Bgee

P13500.

CleanEx

HS_CCL2.

Genevestigator

P13500.

GermOnline

ENSG00000108691. Homo sapiens.

Family and domain databases

InterPro

IPR000827. CC_chemkine_sml_CS.
IPR001811. Chemokine_IL8.
[Graphical view]

Pfam

PF00048. IL8. 1 hit.
[Graphical view]

SMART

SM00199. SCY. 1 hit.
[Graphical view]

PROSITE

PS00472. SMALL_CYTOKINES_CC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

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

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:	November 24, 2009
This is version 137 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.