P25106 (CXCR7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
C-X-C chemokine receptor type 7
Short name=CXC-R7
Short name=CXCR-7

Alternative name(s):
Chemokine orphan receptor 1
G-protein coupled receptor 159
G-protein coupled receptor RDC1 homolog
Short name=RDC-1

Gene names

Name:	CXCR7
Synonyms:	CMKOR1, GPR159, RDC1

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

General annotation (Comments)

Function	Receptor for chemokines CXCL12/SDF1 and CXCL11. Does not elicit classical chemokine receptor signaling; chemokine binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalization and activation of MAPK signaling pathway. Acts as a scavenger for CXCL12/SDF1 and, to a lesser extent, for CXCL11. Required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness. In glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis. Promotes cell growth and survival. Not involved in cell migration, adhesion or proliferation of normal hematopoietic progenitors but activated by CXCL11 in malignant hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration. Plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12. Required for heart valve development. Acts as coreceptor with CXCR4 for a restricted number of HIV isolates. Ref.9 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21
Subunit structure	Homodimer. Can form heterodimers with CXCR4; heterodimerization may regulate CXCR4 signaling activity. Ref.13 Ref.15 Ref.17
Subcellular location	Cell membrane; Multi-pass membrane protein. Cytoplasm › perinuclear region. Early endosome. Recycling endosome By similarity. Note: Localized mainly in perinuclear regions in neurons and in early endosomes in T-lymphocytes and some other cell types, with very low levels detected on the cell surface. May spontaneously cycle between the plasma membrane and endosomal compartments. Ref.14 Ref.20 Ref.22
Tissue specificity	Expressed in monocytes, basophils, B-cells, umbilical vein endothelial cells (HUVEC) and B-lymphoblastoid cells. Lower expression detected in CD4+ T-lymphocytes and natural killer cells. In the brain, detected in endothelial cells and capillaries, and in mature neurons of the frontal cortex and hippocampus. Expressed in tubular formation in the kidney. Highly expressed in astroglial tumor endothelial, microglial and glioma cells. Expressed at low levels in normal CD34+ progenitor cells, but at very high levels in several myeloid malignant cell lines. Expressed in breast carcinomas but not in normal breast tissue (at protein level). Ref.10 Ref.12 Ref.16 Ref.18 Ref.19 Ref.22
Induction	Up-regulated during cell differentiation in glioma cells. Ref.18
Sequence similarities	Belongs to the G-protein coupled receptor 1 family.
Caution	Was originally (Ref.1) thought to be the receptor for VIP.

Ontologies

Keywords
Biological process	Cell adhesion Host-virus interaction
Cellular component	Cell membrane Cytoplasm Endosome Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
Molecular function	Developmental protein G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	angiogenesis Inferred from electronic annotation. Source: InterPro cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW chemotaxis Inferred from electronic annotation. Source: InterPro negative regulation of apoptotic process Inferred from mutant phenotype Ref.18. Source: BHF-UCL vasculogenesis Inferred from electronic annotation. Source: InterPro virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	early endosome Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Non-traceable author statement. Source: UniProtKB perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Traceable author statement. Source: Reactome recycling endosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	C-X-C chemokine receptor activity Inferred from mutant phenotype Ref.18. Source: BHF-UCL coreceptor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 362	362	C-X-C chemokine receptor type 7		PRO_0000070101
Regions
	Topological domain	1 – 40	40	Extracellular Potential
	Transmembrane	41 – 61	21	Helical; Name=1; Potential
	Topological domain	62 – 81	20	Cytoplasmic Potential
	Transmembrane	82 – 102	21	Helical; Name=2; Potential
	Topological domain	103 – 118	16	Extracellular Potential
	Transmembrane	119 – 139	21	Helical; Name=3; Potential
	Topological domain	140 – 162	23	Cytoplasmic Potential
	Transmembrane	163 – 183	21	Helical; Name=4; Potential
	Topological domain	184 – 213	30	Extracellular Potential
	Transmembrane	214 – 234	21	Helical; Name=5; Potential
	Topological domain	235 – 252	18	Cytoplasmic Potential
	Transmembrane	253 – 273	21	Helical; Name=6; Potential
	Topological domain	274 – 296	23	Extracellular Potential
	Transmembrane	297 – 319	23	Helical; Name=7; Potential
	Topological domain	320 – 362	43	Cytoplasmic Potential
Amino acid modifications
	Glycosylation	13	1	N-linked (GlcNAc...) Potential
	Glycosylation	22	1	N-linked (GlcNAc...) Potential
	Glycosylation	39	1	N-linked (GlcNAc...) Potential
	Disulfide bond	117 ↔ 196		By similarity
Natural variations
	Natural variant	219	1	L → W. Corresponds to variant rs10183641 [ dbSNP | Ensembl ].		VAR_027477
Experimental info
	Mutagenesis	145	1	S → A: Does not result in CXCL12-inducible chemotaxis, calcium mobilization or ERK activation, and has no effect on CXCR7-mediated CXCL12 degradation; when associated with V-147. Ref.20
	Mutagenesis	147	1	T → V: Does not result in CXCL12-inducible chemotaxis, calcium mobilization or ERK activation, and has no effect on CXCR7-mediated CXCL12 degradation; when associated with A-145. Ref.20
	Sequence conflict	9	1	S → A in AAA62370. Ref.1
	Sequence conflict	130	1	G → S in AAA62370. Ref.1
	Sequence conflict	130	1	G → S in AAB16913. Ref.2
	Sequence conflict	130	1	G → S in AAB94130. Ref.3
	Sequence conflict	131	1	S → G in AAA62370. Ref.1
	Sequence conflict	228	1	I → V in AAH36661. Ref.8
	Sequence conflict	360 – 361	2	ST → NA in AAA62370. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P25106 [UniParc]. Last modified October 3, 2006. Version 3. Checksum: A863EC1AFB5B158B	FASTA	362	41,493
	10 20 30 40 50 60 MDLHLFDYSE PGNFSDISWP CNSSDCIVVD TVMCPNMPNK SVLLYTLSFI YIFIFVIGMI 70 80 90 100 110 120 ANSVVVWVNI QAKTTGYDTH CYILNLAIAD LWVVLTIPVW VVSLVQHNQW PMGELTCKVT 130 140 150 160 170 180 HLIFSINLFG SIFFLTCMSV DRYLSITYFT NTPSSRKKMV RRVVCILVWL LAFCVSLPDT 190 200 210 220 230 240 YYLKTVTSAS NNETYCRSFY PEHSIKEWLI GMELVSVVLG FAVPFSIIAV FYFLLARAIS 250 260 270 280 290 300 ASSDQEKHSS RKIIFSYVVV FLVCWLPYHV AVLLDIFSIL HYIPFTCRLE HALFTALHVT 310 320 330 340 350 360 QCLSLVHCCV NPVLYSFINR NYRYELMKAF IFKYSAKTGL TKLIDASRVS ETEYSALEQS TK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of the human vasoactive intestinal peptide receptor." Sreedharan S.P., Robichon A., Peterson K.E., Goetzl E.J. Proc. Natl. Acad. Sci. U.S.A. 88:4986-4990(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[2]	"Coding and 3'-noncoding sequence of human RDC1, an orphan G protein-coupled receptor." Oates E.L., Roos B.A., Howard G.A. Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Human RDC1 gene." Bi A., Yu L., Zhang Q., Tu Q., Xing Y., Zheng L. Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Isolation of cDNA coding for Homo sapiens chemokine orphan receptor 1 (CMKOR1)." Martin A.L., Kaighin V.A., Aronstam R.S. Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: Placenta.
[6]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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 (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]. Tissue: Testis.
[9]	"RDC1 may not be VIP receptor." Nagata S., Ishihara T., Robberecht P., Libert F., Parmentier M., Christophe J., Vassart G. Trends Pharmacol. Sci. 13:102-103(1992) [PubMed] [Europe PMC] [Abstract] Cited for: DOUBTS ON THE ORIGINAL FUNCTION.
[10]	"The chemokine SDF-1/CXCL12 binds to and signals through the orphan receptor RDC1 in T lymphocytes." Balabanian K., Lagane B., Infantino S., Chow K.Y., Harriague J., Moepps B., Arenzana-Seisdedos F., Thelen M., Bachelerie F. J. Biol. Chem. 280:35760-35766(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[11]	"A novel chemokine receptor for SDF-1 and I-TAC involved in cell survival, cell adhesion, and tumor development." Burns J.M., Summers B.C., Wang Y., Melikian A., Berahovich R., Miao Z., Penfold M.E., Sunshine M.J., Littman D.R., Kuo C.J., Wei K., McMaster B.E., Wright K., Howard M.C., Schall T.J. J. Exp. Med. 203:2201-2213(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[12]	"Expression and regulation of the orphan receptor RDC1 and its putative ligand in human dendritic and B cells." Infantino S., Moepps B., Thelen M. J. Immunol. 176:2197-2207(2006) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[13]	"Disrupted cardiac development but normal hematopoiesis in mice deficient in the second CXCL12/SDF-1 receptor, CXCR7." Sierro F., Biben C., Martinez-Munoz L., Mellado M., Ransohoff R.M., Li M., Woehl B., Leung H., Groom J., Batten M., Harvey R.P., Martinez-A C., Mackay C.R., Mackay F. Proc. Natl. Acad. Sci. U.S.A. 104:14759-14764(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, HETERODIMERIZATION.
[14]	"A crosstalk between intracellular CXCR7 and CXCR4 involved in rapid CXCL12-triggered integrin activation but not in chemokine-triggered motility of human T lymphocytes and CD34+ cells." Hartmann T.N., Grabovsky V., Pasvolsky R., Shulman Z., Buss E.C., Spiegel A., Nagler A., Lapidot T., Thelen M., Alon R. J. Leukoc. Biol. 84:1130-1140(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[15]	"CXCR7 heterodimerizes with CXCR4 and regulates CXCL12-mediated G protein signaling." Levoye A., Balabanian K., Baleux F., Bachelerie F., Lagane B. Blood 113:6085-6093(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT.
[16]	"Elucidation of CXCR7-mediated signaling events and inhibition of CXCR4-mediated tumor cell transendothelial migration by CXCR7 ligands." Zabel B.A., Wang Y., Lewen S., Berahovich R.D., Penfold M.E., Zhang P., Powers J., Summers B.C., Miao Z., Zhao B., Jalili A., Janowska-Wieczorek A., Jaen J.C., Schall T.J. J. Immunol. 183:3204-3211(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[17]	"AMD3100 is a CXCR7 ligand with allosteric agonist properties." Kalatskaya I., Berchiche Y.A., Gravel S., Limberg B.J., Rosenbaum J.S., Heveker N. Mol. Pharmacol. 75:1240-1247(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT.
[18]	"The chemokine receptor CXCR7 is highly expressed in human glioma cells and mediates antiapoptotic effects." Hattermann K., Held-Feindt J., Lucius R., Muerkoster S.S., Penfold M.E., Schall T.J., Mentlein R. Cancer Res. 70:3299-3308(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, INDUCTION.
[19]	"CXCR7: a new SDF-1-binding receptor in contrast to normal CD34(+) progenitors is functional and is expressed at higher level in human malignant hematopoietic cells." Tarnowski M., Liu R., Wysoczynski M., Ratajczak J., Kucia M., Ratajczak M.Z. Eur. J. Haematol. 85:472-483(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[20]	"CXCR7 functions as a scavenger for CXCL12 and CXCL11." Naumann U., Cameroni E., Pruenster M., Mahabaleshwar H., Raz E., Zerwes H.G., Rot A., Thelen M. PLoS ONE 5:E9175-E9175(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-145 AND THR-147.
[21]	"Beta-arrestin- but not G protein-mediated signaling by the 'decoy' receptor CXCR7." Rajagopal S., Kim J., Ahn S., Craig S., Lam C.M., Gerard N.P., Gerard C., Lefkowitz R.J. Proc. Natl. Acad. Sci. U.S.A. 107:628-632(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[22]	"CXCR7 protein expression in human adult brain and differentiated neurons." Shimizu S., Brown M., Sengupta R., Penfold M.E., Meucci O. PLoS ONE 6:E20680-E20680(2011) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Wikipedia

CXC chemokine receptors entry

Cross-references

Sequence databases
EMBL GenBank DDBJ	M64749 mRNA. Translation: AAA62370.1. U73141 Genomic DNA. Translation: AAB18130.1. U67784 mRNA. Translation: AAB16913.1. AF030297 mRNA. Translation: AAB94130.1. DQ822477 mRNA. Translation: ABH01258.1. AK291659 mRNA. Translation: BAF84348.1. AC079611 Genomic DNA. Translation: AAX93086.1. CH471063 Genomic DNA. Translation: EAW71092.1. BC036661 mRNA. Translation: AAH36661.1.
IPI	IPI00012733.
PIR	A39714.
RefSeq	NP_064707.1. NM_020311.2.
UniGene	Hs.471751.
3D structure databases
ProteinModelPortal	P25106.
ModBase	Search...
Protein-protein interaction databases
IntAct	P25106. 4 interactions.
STRING	9606.ENSP00000272928.
Protein family/group databases
GPCRDB	Search...
PTM databases
PhosphoSite	P25106.
Polymorphism databases
DMDM	115502380.
Proteomic databases
PaxDb	P25106.
PeptideAtlas	P25106.
PRIDE	P25106.
Protocols and materials databases
DNASU	57007.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000272928; ENSP00000272928; ENSG00000144476.
GeneID	57007.
KEGG	hsa:57007.
UCSC	uc002vwd.3. human.
Organism-specific databases
CTD	57007.
GeneCards	GC02P237476.
HGNC	HGNC:23692. CXCR7.
HPA	HPA049718.
MIM	610376. gene.
neXtProt	NX_P25106.
PharmGKB	PA162383053.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG306050.
HOGENOM	HOG000261660.
HOVERGEN	HBG106832.
InParanoid	P25106.
KO	K04304.
OMA	YIPFTCQ.
PhylomeDB	P25106.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction.
SignaLink	P25106.
Gene expression databases
Bgee	P25106.
CleanEx	HS_CXCR7.
Genevestigator	P25106.
GermOnline	ENSG00000144476. Homo sapiens.
Family and domain databases
InterPro	IPR001416. Chemokine_CXCR7. IPR000355. Chemokine_rcpt. IPR000276. GPCR_Rhodpsn. IPR017452. GPCR_Rhodpsn_7TM. [Graphical view]
PANTHER	PTHR24227. PTHR24227. 1 hit. PTHR24227:SF34. PTHR24227:SF34. 1 hit.
Pfam	PF00001. 7tm_1. 1 hit. [Graphical view]
PRINTS	PR00237. GPCRRHODOPSN. PR00646. RDC1ORPHANR.
PROSITE	PS00237. G_PROTEIN_RECEP_F1_1. 1 hit. PS50262. G_PROTEIN_RECEP_F1_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CXCR7. human.
GenomeRNAi	57007.
NextBio	62747.
SOURCE	Search...

Entry information

Entry name

CXCR7_HUMAN

Accession

Primary (citable) accession number: P25106
Secondary accession number(s): A8K6J4 , Q53RV4, Q8NE10, Q92938, Q92986

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	October 3, 2006
Last modified:	May 29, 2013
This is version 133 of the entry and version 3 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.