P41597 (CCR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
C-C chemokine receptor type 2
Short name=C-C CKR-2
Short name=CC-CKR-2
Short name=CCR-2
Short name=CCR2

Alternative name(s):
Monocyte chemoattractant protein 1 receptor
Short name=MCP-1-R
CD_antigen=CD192

Gene names

Name:	CCR2
Synonyms:	CMKBR2

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	374 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Receptor for the MCP-1, MCP-3 and MCP-4 chemokines. Transduces a signal by increasing the intracellular calcium ions level. Alternative coreceptor with CD4 for HIV-1 infection.
Subunit structure	Binds to HIV-1 Tat. Interacts with ARRB1. Ref.10 Ref.11
Subcellular location	Cell membrane; Multi-pass membrane protein Ref.13.
Induction	Up-regulated by CREB3. Ref.13
Post-translational modification	N-glycosylated. Ref.12
Polymorphism	Variations in CCR2 are associated with relative resistance to immunodeficiency virus type 1 (resistance to HIV-1) [MIM:609423].
Sequence similarities	Belongs to the G-protein coupled receptor 1 family.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Cell membrane Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein Phosphoprotein Sulfation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	JAK-STAT cascade Traceable author statement Ref.9. Source: ProtInc T-helper 17 cell chemotaxis Inferred from sequence or structural similarity. Source: BHF-UCL blood vessel remodeling Inferred from sequence or structural similarity. Source: BHF-UCL cellular defense response Traceable author statement PubMed 10201901. Source: ProtInc dendritic cell chemotaxis Traceable author statement PubMed 16621978. Source: BHF-UCL elevation of cytosolic calcium ion concentration Traceable author statement PubMed 9548499. Source: ProtInc inflammatory response Traceable author statement PubMed 10623817. Source: ProtInc innate immune response Traceable author statement. Source: Reactome negative regulation of adenylate cyclase activity Traceable author statement Ref.3. Source: ProtInc negative regulation of angiogenesis Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of eosinophil degranulation Inferred from sequence or structural similarity. Source: BHF-UCL negative regulation of type 2 immune response Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of CD8-positive, alpha-beta T cell extravasation Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of T cell chemotaxis Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of T-helper 1 type immune response Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of alpha-beta T cell proliferation Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of astrocyte chemotaxis Inferred from direct assay PubMed 12271471. Source: BHF-UCL positive regulation of hematopoietic stem cell migration Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of immune complex clearance by monocytes and macrophages Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of inflammatory response Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of interferon-gamma production Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of interleukin-2 production Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of monocyte chemotaxis Inferred from direct assay Ref.13. Source: UniProtKB positive regulation of monocyte extravasation Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of tumor necrosis factor biosynthetic process Inferred from sequence or structural similarity. Source: BHF-UCL regulation of vascular endothelial growth factor production Inferred from sequence or structural similarity. Source: BHF-UCL virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Inferred from sequence or structural similarity. Source: BHF-UCL dendrite Inferred from sequence or structural similarity. Source: BHF-UCL integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc perikaryon Inferred from sequence or structural similarity. Source: BHF-UCL perinuclear region of cytoplasm Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular_function	C-C chemokine receptor activity Inferred from electronic annotation. Source: InterPro CCR2 chemokine receptor binding Inferred from direct assay PubMed 15995708. Source: MGI chemokine receptor activity Traceable author statement PubMed 10623817. Source: ProtInc protein homodimerization activity Inferred from sequence or structural similarity. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform A (identifier: P41597-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform B (identifier: P41597-2)

The sequence of this isoform differs from the canonical sequence as follows:
     314-374: SLFHIALGCR...EASLQDKEGA → RYLSVFFRKH...TGEQEVSAGL

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 374

374

C-C chemokine receptor type 2

PRO_0000069232

Regions

Topological domain

1 – 42

42

Extracellular Potential

Transmembrane

43 – 70

28

Helical; Name=1; Potential

Topological domain

71 – 80

10

Cytoplasmic Potential

Transmembrane

81 – 100

20

Helical; Name=2; Potential

Topological domain

101 – 114

14

Extracellular Potential

Transmembrane

115 – 136

22

Helical; Name=3; Potential

Topological domain

137 – 153

17

Cytoplasmic Potential

Transmembrane

154 – 178

25

Helical; Name=4; Potential

Topological domain

179 – 206

28

Extracellular Potential

Transmembrane

207 – 226

20

Helical; Name=5; Potential

Topological domain

227 – 243

17

Cytoplasmic Potential

Transmembrane

244 – 268

25

Helical; Name=6; Potential

Topological domain

269 – 285

17

Extracellular Potential

Transmembrane

286 – 309

24

Helical; Name=7; Potential

Topological domain

310 – 374

65

Cytoplasmic Potential

Amino acid modifications

Modified residue

26

1

Sulfotyrosine Ref.12

Modified residue

139

1

Phosphotyrosine; by JAK2 Ref.9

Glycosylation

14

1

N-linked (GlcNAc...) Potential

Disulfide bond

32 ↔ 277

Disulfide bond

113 ↔ 190

Natural variations

Alternative sequence

314 – 374

61

SLFHI…DKEGA → RYLSVFFRKHITKRFCKQCP VFYRETVDGVTSTNTPSTGE QEVSAGL in isoform B.

VSP_001893

Natural variant

45

1

L → V.
Corresponds to variant rs4987052 [ dbSNP | Ensembl ].

VAR_020066

Natural variant

64

1

V → I Confers relative resistance to infection by HIV-1; delay in disease progression in African Americans but not in Caucasians. Ref.4 Ref.14 Ref.15
Corresponds to variant rs1799864 [ dbSNP | Ensembl ].

VAR_014339

Natural variant

355

1

G → E. Ref.4
Corresponds to variant rs3918387 [ dbSNP | Ensembl ].

VAR_014340

Secondary structure

1

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374

Helix Strand Turn

Details...

Turn

2 – 6

5

Beta strand

12 – 14

3

Turn

20 – 23

4

Turn

37 – 40

4

Helix

41 – 69

29

Helix

77 – 93

17

Helix

95 – 101

7

Helix

109 – 143

35

Turn

145 – 148

4

Helix

156 – 177

22

Turn

185 – 188

4

Beta strand

191 – 193

3

Helix

194 – 196

3

Helix

202 – 210

9

Helix

212 – 224

13

Beta strand

234 – 236

3

Helix

239 – 255

17

Helix

258 – 265

8

Beta strand

283 – 285

3

Helix

293 – 300

8

Helix

301 – 304

4

Helix

305 – 316

12

Helix

318 – 328

11

Beta strand

333 – 335

3

Helix

340 – 343

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified November 1, 1995. Version 1. Checksum: F865E0D39E74CF0F	FASTA	374	41,915
	10 20 30 40 50 60 MLSTSRSRFI RNTNESGEEV TTFFDYDYGA PCHKFDVKQI GAQLLPPLYS LVFIFGFVGN 70 80 90 100 110 120 MLVVLILINC KKLKCLTDIY LLNLAISDLL FLITLPLWAH SAANEWVFGN AMCKLFTGLY 130 140 150 160 170 180 HIGYFGGIFF IILLTIDRYL AIVHAVFALK ARTVTFGVVT SVITWLVAVF ASVPGIIFTK 190 200 210 220 230 240 CQKEDSVYVC GPYFPRGWNN FHTIMRNILG LVLPLLIMVI CYSGILKTLL RCRNEKKRHR 250 260 270 280 290 300 AVRVIFTIMI VYFLFWTPYN IVILLNTFQE FFGLSNCEST SQLDQATQVT ETLGMTHCCI 310 320 330 340 350 360 NPIIYAFVGE KFRSLFHIAL GCRIAPLQKP VCGGPGVRPG KNVKVTTQGL LDGRGKGKSI 370 GRAPEASLQD KEGA
	Isoform B [UniParc]. Checksum: EA352636D724D470	FASTA	360	41,064
	10 20 30 40 50 60 MLSTSRSRFI RNTNESGEEV TTFFDYDYGA PCHKFDVKQI GAQLLPPLYS LVFIFGFVGN 70 80 90 100 110 120 MLVVLILINC KKLKCLTDIY LLNLAISDLL FLITLPLWAH SAANEWVFGN AMCKLFTGLY 130 140 150 160 170 180 HIGYFGGIFF IILLTIDRYL AIVHAVFALK ARTVTFGVVT SVITWLVAVF ASVPGIIFTK 190 200 210 220 230 240 CQKEDSVYVC GPYFPRGWNN FHTIMRNILG LVLPLLIMVI CYSGILKTLL RCRNEKKRHR 250 260 270 280 290 300 AVRVIFTIMI VYFLFWTPYN IVILLNTFQE FFGLSNCEST SQLDQATQVT ETLGMTHCCI 310 320 330 340 350 360 NPIIYAFVGE KFRRYLSVFF RKHITKRFCK QCPVFYRETV DGVTSTNTPS TGEQEVSAGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and functional expression of two monocyte chemoattractant protein 1 receptors reveals alternative splicing of the carboxyl-terminal tails." Charo I.F., Myers S.J., Herman A., Franci C., Connolly A.J., Coughlin S.R. Proc. Natl. Acad. Sci. U.S.A. 91:2752-2756(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"cDNA cloning and functional expression of a human monocyte chemoattractant protein 1 receptor." Yamagami S., Tokuda Y., Ishii K., Tamaka H., Endo N. Biochem. Biophys. Res. Commun. 202:1156-1162(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Organization and differential expression of the human monocyte chemoattractant protein 1 receptor gene. Evidence for the role of the carboxyl-terminal tail in receptor trafficking." Wong L.-M., Myers S.J., Tsou C.-L., Gosling J., Arai H., Charo I.F. J. Biol. Chem. 272:1038-1045(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	SeattleSNPs variation discovery resource Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-64 AND GLU-355.
[5]	"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: Thymus and Trachea.
[6]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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] (ISOFORMS A AND B).
[9]	"The chemokine monocyte chemotactic protein 1 triggers Janus kinase 2 activation and tyrosine phosphorylation of the CCR2B receptor." Mellado M., Rodriguez-Frade J.M., Aragay A., del Real G., Martin A.M., Vila-Coro A.J., Serrano A., Mayor F. Jr., Martinez-A C. J. Immunol. 161:805-813(1998) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-139 BY JAK2.
[10]	"Monocyte chemoattractant protein-1-induced CCR2B receptor desensitization mediated by the G protein-coupled receptor kinase 2." Aragay A.M., Mellado M., Frade J.M., Martin A.M., Jimenez-Sainz M.C., Martinez-A C., Mayor F. Jr. Proc. Natl. Acad. Sci. U.S.A. 95:2985-2990(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ARRB1.
[11]	"HIV-1 Tat protein mimicry of chemokines." Albini A., Ferrini S., Benelli R., Sforzini S., Giunciuglio D., Aluigi M.G., Proudfoot A.E.I., Alouani S., Wells T.N.C., Mariani G., Rabin R.L., Farber J.M., Noonan D.M. Proc. Natl. Acad. Sci. U.S.A. 95:13153-13158(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HIV-1 TAT.
[12]	"Monocyte chemotactic protein-1 receptor CCR2B is a glycoprotein that has tyrosine sulfation in a conserved extracellular N-terminal region." Preobrazhensky A.A., Dragan S., Kawano T., Gavrilin M.A., Gulina I.V., Chakravarty L., Kolattukudy P.E. J. Immunol. 165:5295-5303(2000) [PubMed] [Europe PMC] [Abstract] Cited for: SULFATION AT TYR-26, GLYCOSYLATION.
[13]	"Human LZIP induces monocyte CC chemokine receptor 2 expression leading to enhancement of monocyte chemoattractant protein 1/CCL2-induced cell migration." Sung H.J., Kim Y.S., Kang H., Ko J. Exp. Mol. Med. 40:332-338(2008) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INDUCTION.
[14]	"Contrasting genetic influence of CCR2 and CCR5 variants on HIV-1 infection and disease progression." Smith M.W., Dean M., Carrington M., Winkler C., Huttley G.A., Lomb D.A., Goedert J.J., O'Brien T.R., Jacobson L.P., Kaslow R., Buchbinder S., Vittinghoff E., Vlahov D., Hoots K., Hilgartner M.W., O'Brien S.J. Science 277:959-965(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ILE-64.
[15]	"Genealogy of the CCR5 locus and chemokine system gene variants associated with altered rates of HIV-1 disease progression." Mummidi S., Ahuja S.S., Gonzalez E., Anderson S.A., Santiago E.N., Stephan K.T., Craig F.E., O'Connell P., Tryon V., Clark R.A., Dolan M.J., Ahuja S.K. Nat. Med. 4:786-793(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ILE-64.
+	Additional computationally mapped references.

Web resources

Wikipedia

CC chemokine receptors entry

SeattleSNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U03882 mRNA. Translation: AAA19119.1.
U03905 mRNA. Translation: AAA19120.1.
D29984 mRNA. Translation: BAA06253.1.
U80924 Genomic DNA. Translation: AAC51637.1.
U80924 Genomic DNA. Translation: AAC51636.1.
AF545480 Genomic DNA. Translation: AAN16400.1.
AK292685 mRNA. Translation: BAF85374.1.
AK292920 mRNA. Translation: BAF85609.1.
U95626 Genomic DNA. Translation: AAB57791.1.
U95626 Genomic DNA. Translation: AAB57792.1.
CH471055 Genomic DNA. Translation: EAW64760.1.
BC074751 mRNA. Translation: AAH74751.1.
BC095540 mRNA. Translation: AAH95540.1.
BC126452 mRNA. Translation: AAI26453.1.
BC136396 mRNA. Translation: AAI36397.1.

IPI

IPI00015137.
IPI00218945.

PIR

I38450.
JC2443.

RefSeq

NP_001116513.2. NM_001123041.2.
NP_001116868.1. NM_001123396.1.

UniGene

Hs.511794.
Hs.705362.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KAD	model	-	A	1-343	[»]
1KP1	model	-	A	1-343	[»]

ProteinModelPortal

P41597.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-5833N.
DIP-5839N.

STRING

9606.ENSP00000292301.

Protein family/group databases

GPCRDB

Search...

PTM databases

PhosphoSite

P41597.

Polymorphism databases

DMDM

1168965.

Proteomic databases

PaxDb

P41597.

PRIDE

P41597.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000292301; ENSP00000292301; ENSG00000121807.
ENST00000400888; ENSP00000383681; ENSG00000121807.
ENST00000445132; ENSP00000399285; ENSG00000121807.

GeneID

729230.

KEGG

hsa:729230.

UCSC

uc003cpn.4. human.

Organism-specific databases

CTD

729230.

GeneCards

GC03P046356.

HGNC

HGNC:1603. CCR2.

HPA

CAB003793.

MIM

601267. gene.
609423. phenotype.

neXtProt

NX_P41597.

PharmGKB

PA26167.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG148353.

HOGENOM

HOG000234122.

HOVERGEN

HBG106917.

InParanoid

P41597.

KO

K04177.

OMA

CPVFYRE.

PhylomeDB

P41597.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P41597.

Bgee

P41597.

CleanEx

HS_CCR2.

Genevestigator

P41597.

GermOnline

ENSG00000121807. Homo sapiens.

Family and domain databases

InterPro

IPR002237. Chemokine_CCR2.
IPR000355. Chemokine_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]

Pfam

PF00001. 7tm_1. 1 hit.
[Graphical view]

PRINTS

PR00657. CCCHEMOKINER.
PR01107. CHEMOKINER2.
PR00237. GPCRRHODOPSN.

PROSITE

PS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P41597.

ChEMBL

CHEMBL4015.

GenomeRNAi

729230.

NextBio

129620.

SOURCE

Search...

Entry information

Entry name

CCR2_HUMAN

Accession

Primary (citable) accession number: P41597
Secondary accession number(s): A0AVQ3, B2RMT0, Q4VBL2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	May 1, 2013
This is version 141 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.