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UniProtKB/Swiss-Prot entry P41597


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CCR2_HUMAN
Primary accession number P41597
Secondary accession numbers A0AVQ3 B2RMT0
Integrated into Swiss-Prot on November 1, 1995
Sequence was last modified on November 1, 1995 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 103)
Name and origin of the protein
Protein name C-C chemokine receptor type 2
Synonyms C-C CKR-2
CC-CKR-2
CCR-2
CCR2
Monocyte chemoattractant protein 1 receptor
MCP-1-R
CD192 antigen
Gene name
Name: CCR2
Synonyms: CMKBR2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1073/pnas.91.7.2752; PubMed=8146186 [NCBI, ExPASy, EBI, Israel, Japan]
Charo I.F., Myers S.J., Herman A., Franci C., Connolly A.J., Coughlin S.R.;
"Molecular cloning and functional expression of two monocyte chemoattractant protein 1 receptors reveals alternative splicing of the carboxyl-terminal tails.";
Proc. Natl. Acad. Sci. U.S.A. 91:2752-2756(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1006/bbrc.1994.2049; PubMed=8048929 [NCBI, ExPASy, EBI, Israel, Japan]
Yamagami S., Tokuda Y., Ishii K., Tamaka H., Endo N.;
"cDNA cloning and functional expression of a human monocyte chemoattractant protein 1 receptor.";
Biochem. Biophys. Res. Commun. 202:1156-1162(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1074/jbc.272.2.1038; PubMed=8995400 [NCBI, ExPASy, EBI, Israel, Japan]
Wong L.-M., Myers S.J., Tsou C.-L., Gosling J., Arai H., Charo I.F.;
"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.";
J. Biol. Chem. 272:1038-1045(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-64 AND GLU-355.
SeattleSNPs variation discovery resource;
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04728; PubMed=16641997 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
INTERACTION WITH HIV-1 TAT.
DOI=10.1073/pnas.95.22.13153; PubMed=9789057 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"HIV-1 Tat protein mimicry of chemokines.";
Proc. Natl. Acad. Sci. U.S.A. 95:13153-13158(1998).
[8]
SULFATION AT TYR-26, AND GLYCOSYLATION.
PubMed=11046064 [NCBI, ExPASy, EBI, Israel, Japan]
Preobrazhensky A.A., Dragan S., Kawano T., Gavrilin M.A., Gulina I.V., Chakravarty L., Kolattukudy P.E.;
"Monocyte chemotactic protein-1 receptor CCR2B is a glycoprotein that has tyrosine sulfation in a conserved extracellular N-terminal region.";
J. Immunol. 165:5295-5303(2000).
[9]
VARIANT ILE-64.
DOI=10.1126/science.277.5328.959; PubMed=9252328 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Contrasting genetic influence of CCR2 and CCR5 variants on HIV-1 infection and disease progression.";
Science 277:959-965(1997).
[10]
VARIANT ILE-64.
DOI=10.1038/nm0798-786; PubMed=9662369 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Genealogy of the CCR5 locus and chemokine system gene variants associated with altered rates of HIV-1 disease progression.";
Nat. Med. 4:786-793(1998).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U03882; AAA19119.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U03905; AAA19120.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D29984; BAA06253.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U80924; AAC51637.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U80924; AAC51636.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF545480; AAN16400.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U95626; AAB57791.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U95626; AAB57792.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC074751; AAH74751.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC126452; AAI26453.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC136396; AAI36397.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00015137; -.
IPI00218945; -.
PIR I38450; I38450.
JC2443; JC2443.
RefSeq NP_001116513.2; -.
UniGene Hs.511794
3D structure databases
PDB
1KAD; Model; -; A=1-343.[ExPASy / RCSB / EBI]
1KP1; Model; -; A=1-343.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1KAD; -.
1KP1; -.
ModBase P41597.
Protein-protein interaction databases
DIP DIP:5833N; -.
DIP:5839N; -.
Protein family/group databases
GPCRDB P41597; CCR2_HUMAN.
PTM databases
PhosphoSite P41597; -.
Enzyme and pathway databases
Reactome REACT_14797; Signaling by GPCR.
Organism-specific databases
GeneCards GC03P046373; -.
GC03P9K0042; -.
H-InvDB HIX0030863; -.
HIX0031336; -.
HGNC HGNC:1603; CCR2.
GenAtlas CCR2.
HPA CAB003793; -.
MIM 601267; gene. [NCBI / EBI]
609423; phenotype. [NCBI / EBI]
PharmGKB PA26167; -.
Gene expression databases
Bgee P41597; -.
CleanEx HS_CCR2; -.
GermOnline ENSG00000121807; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from MGI).
GO:0005887; Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0005625; Cellular component: soluble fraction (traceable author statement from ProtInc).
GO:0016493; Molecular function: C-C chemokine receptor activity (inferred from electronic annotation from InterPro).
GO:0031727; Molecular function: CCR2 chemokine receptor binding (inferred from direct assay from MGI).
GO:0006968; Biological process: cellular defense response (traceable author statement from ProtInc).
GO:0006935; Biological process: chemotaxis (traceable author statement from ProtInc).
GO:0019221; Biological process: cytokine-mediated signaling pathway (inferred from direct assay from MGI).
GO:0007204; Biological process: elevation of cytosolic calcium ion concentration (traceable author statement from ProtInc).
GO:0007186; Biological process: G-protein coupled receptor protein signaling pathway (inferred from electronic annotation from UniProtKB-KW).
GO:0006955; Biological process: immune response (traceable author statement from ProtInc).
GO:0006954; Biological process: inflammatory response (traceable author statement from ProtInc).
GO:0044419; Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0007259; Biological process: JAK-STAT cascade (traceable author statement from ProtInc).
GO:0007194; Biological process: negative regulation of adenylate cyclase activity (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000276; 7TM_GPCR_Rhodpsn.
IPR002237; CC_2_rcpt.
IPR002240; CC_5_rcpt.
IPR000355; Chmkine_rcpt.
IPR017452; GPCR_Rhodpsn_supfam.
Graphical view of domain structure.
PANTHER PTHR19264:SF204; CC_5_rcpt; 1.
Pfam PF00001; 7tm_1; 1.
Pfam graphical view of domain structure.
PRINTS PR00657; CCCHEMOKINER.
PR01107; CHEMOKINER2.
PR00237; GPCRRHODOPSN.
PROSITE PS00237; G_PROTEIN_RECEP_F1_1; 1.
PS50262; G_PROTEIN_RECEP_F1_2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P41597; -.
Genome annotation databases
Ensembl ENSG00000121807; Homo sapiens. [Contig view]
ENSG00000215782; Homo sapiens. [Contig view]
GeneID 729230; -.
KEGG hsa:1231; -.
hsa:729230; -.
Phylogenomic databases
HOGENOM P41597; -.
HOVERGEN P41597; -.
OMA P41597; NCESTSQ.
Other
NextBio 5019; -.
SOURCE CCR2; Homo sapiens.
GPCRDB-Snakes P41597.
ProtoNet P41597.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein; Host-virus interaction; Membrane; Polymorphism; Receptor; Sulfation; Transducer; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   374  374     C-C chemokine receptor type 2. PRO_0000069232
TOPO_DOM   1    42  42     Extracellular (Potential). 
TRANSMEM   43    70  28     1 (Potential). 
TOPO_DOM   71    80  10     Cytoplasmic (Potential). 
TRANSMEM   81   100  20     2 (Potential). 
TOPO_DOM   101   114  14     Extracellular (Potential). 
TRANSMEM   115   136  22     3 (Potential). 
TOPO_DOM   137   153  17     Cytoplasmic (Potential). 
TRANSMEM   154   178  25     4 (Potential). 
TOPO_DOM   179   206  28     Extracellular (Potential). 
TRANSMEM   207   226  20     5 (Potential). 
TOPO_DOM   227   243  17     Cytoplasmic (Potential). 
TRANSMEM   244   268  25     6 (Potential). 
TOPO_DOM   269   285  17     Extracellular (Potential). 
TRANSMEM   286   309  24     7 (Potential). 
TOPO_DOM   310   374  65     Cytoplasmic (Potential). 
MOD_RES   26    26        Sulfotyrosine. 
CARBOHYD   14    14        N-linked (GlcNAc...) (Potential). 
DISULFID   32   277         
DISULFID   113   190         
VAR_SEQ   314   374        SLFHIALGCRIAPLQKPVCGGPGVRPGKNVKVTTQGLLDG RGKGKSIGRAPEASLQDKEGA -> RYLSVFFRKHITKRFCKQCPVFYRETVDGVTSTNTPSTGE QEVSAGL (in isoform B). VSP_001893
VARIANT   45    45  1     L -> V (in dbSNP:rs4987052 [NCBI]). VAR_020066 
VARIANT   64    64  1     V -> I (confers relative resistance to infection by HIV-1; delay in disease progression in African Americans but not in Caucasians; dbSNP:rs1799864 [NCBI]). VAR_014339 
VARIANT   355   355  1     G -> E (in dbSNP:rs3918387 [NCBI]). VAR_014340 
TURN   2     6  5      
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      
STRAND   191   193  3      
HELIX   194   196  3      
HELIX   202   210  9      
HELIX   212   224  13      
STRAND   234   236  3      
HELIX   239   255  17      
HELIX   258   265  8      
STRAND   283   285  3      
HELIX   293   300  8      
HELIX   301   304  4      
HELIX   305   316  12      
HELIX   318   328  11      
STRAND   333   335  3      
HELIX   340   343  4      
Sequence information
Length: 374 AA [This is the length of the unprocessed precursor] Molecular weight: 41915 Da [This is the MW of the unprocessed precursor] CRC64: F865E0D39E74CF0F [This is a checksum on the sequence]
        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 

P41597 in FASTA format

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