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Protein

Type-2 angiotensin II receptor

Gene

AGTR2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Receptor for angiotensin II. Cooperates with MTUS1 to inhibit ERK2 activation and cell proliferation.1 Publication

GO - Molecular functioni

  1. angiotensin type II receptor activity Source: BHF-UCL
  2. peptide hormone binding Source: Ensembl
  3. receptor antagonist activity Source: BHF-UCL

GO - Biological processi

  1. aldosterone secretion Source: Ensembl
  2. angiotensin-activated signaling pathway Source: GOC
  3. blood vessel remodeling Source: BHF-UCL
  4. brain development Source: BHF-UCL
  5. brain renin-angiotensin system Source: Ensembl
  6. cell growth involved in cardiac muscle cell development Source: Ensembl
  7. cell surface receptor signaling pathway Source: BHF-UCL
  8. cellular response to dexamethasone stimulus Source: Ensembl
  9. cellular sodium ion homeostasis Source: Ensembl
  10. cerebellar cortex development Source: Ensembl
  11. dopamine biosynthetic process Source: Ensembl
  12. exploration behavior Source: Ensembl
  13. extracellular negative regulation of signal transduction Source: GOC
  14. G-protein coupled receptor signaling pathway Source: BHF-UCL
  15. G-protein coupled receptor signaling pathway coupled to cGMP nucleotide second messenger Source: BHF-UCL
  16. inflammatory response Source: Ensembl
  17. intracellular signal transduction Source: BHF-UCL
  18. negative regulation of blood vessel endothelial cell migration Source: BHF-UCL
  19. negative regulation of cell growth Source: BHF-UCL
  20. negative regulation of fibroblast proliferation Source: Ensembl
  21. negative regulation of heart rate Source: BHF-UCL
  22. negative regulation of icosanoid secretion Source: Ensembl
  23. negative regulation of neurotrophin TRK receptor signaling pathway Source: BHF-UCL
  24. negative regulation of norepinephrine secretion Source: Ensembl
  25. nitric oxide mediated signal transduction Source: BHF-UCL
  26. positive regulation of branching involved in ureteric bud morphogenesis Source: Ensembl
  27. positive regulation of cell proliferation Source: Ensembl
  28. positive regulation of cytokine secretion Source: Ensembl
  29. positive regulation of extrinsic apoptotic signaling pathway Source: BHF-UCL
  30. positive regulation of metanephric glomerulus development Source: Ensembl
  31. positive regulation of nitric oxide biosynthetic process Source: BHF-UCL
  32. positive regulation of nitric-oxide synthase activity Source: BHF-UCL
  33. positive regulation of phosphoprotein phosphatase activity Source: BHF-UCL
  34. positive regulation of renal sodium excretion Source: Ensembl
  35. positive regulation of transcription, DNA-templated Source: Ensembl
  36. positive regulation of vasodilation Source: BHF-UCL
  37. regulation of blood pressure Source: ProtInc
  38. regulation of metanephros size Source: Ensembl
  39. regulation of systemic arterial blood pressure by circulatory renin-angiotensin Source: BHF-UCL
  40. regulation of transcription factor import into nucleus Source: Ensembl
  41. renin-angiotensin regulation of aldosterone production Source: Ensembl
  42. response to organonitrogen compound Source: Ensembl
  43. vasodilation by angiotensin involved in regulation of systemic arterial blood pressure Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

G-protein coupled receptor, Receptor, Transducer

Enzyme and pathway databases

ReactomeiREACT_14819. Peptide ligand-binding receptors.
REACT_19231. G alpha (i) signalling events.

Names & Taxonomyi

Protein namesi
Recommended name:
Type-2 angiotensin II receptor
Alternative name(s):
Angiotensin II type-2 receptor
Short name:
AT2
Gene namesi
Name:AGTR2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:338. AGTR2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4545ExtracellularSequence AnalysisAdd
BLAST
Transmembranei46 – 7126Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini72 – 809CytoplasmicSequence Analysis
Transmembranei81 – 10222Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini103 – 11917ExtracellularSequence AnalysisAdd
BLAST
Transmembranei120 – 14021Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini141 – 16020CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei161 – 17919Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini180 – 20829ExtracellularSequence AnalysisAdd
BLAST
Transmembranei209 – 23426Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini235 – 25622CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei257 – 27822Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini279 – 29719ExtracellularSequence AnalysisAdd
BLAST
Transmembranei298 – 31821Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini319 – 36345CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular region Source: GOC
  2. integral component of plasma membrane Source: BHF-UCL
  3. perinuclear region of cytoplasm Source: Ensembl
  4. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

Orphaneti777. X-linked non-syndromic intellectual disability.
PharmGKBiPA44.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 363363Type-2 angiotensin II receptorPRO_0000069167Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi4 – 41N-linked (GlcNAc...)Sequence Analysis
Glycosylationi13 – 131N-linked (GlcNAc...)Sequence Analysis
Glycosylationi24 – 241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi29 – 291N-linked (GlcNAc...)Sequence Analysis
Glycosylationi34 – 341N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi35 ↔ 290PROSITE-ProRule annotation
Disulfide bondi117 ↔ 195PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP50052.
PRIDEiP50052.

PTM databases

PhosphoSiteiP50052.

Expressioni

Tissue specificityi

In adult, highly expressed in myometrium with lower levels in adrenal gland and fallopian tube. Expressed in the cerebellum. Very highly expressed in fetal kidney and intestine.1 Publication

Gene expression databases

BgeeiP50052.
CleanExiHS_AGTR2.
ExpressionAtlasiP50052. baseline and differential.
GenevestigatoriP50052.

Organism-specific databases

HPAiHPA029592.

Interactioni

Subunit structurei

Interacts with MTUS1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
AGTP010192EBI-1748067,EBI-2927577
TIMP3P356257EBI-1748067,EBI-1748085

Protein-protein interaction databases

BioGridi106692. 5 interactions.
IntActiP50052. 3 interactions.
STRINGi9606.ENSP00000360973.

Structurei

3D structure databases

ProteinModelPortaliP50052.
SMRiP50052. Positions 46-336.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the G-protein coupled receptor 1 family.PROSITE-ProRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG311643.
GeneTreeiENSGT00760000119055.
HOGENOMiHOG000234122.
HOVERGENiHBG104998.
InParanoidiP50052.
KOiK04167.
OMAiNCSHKPS.
OrthoDBiEOG7TQV1F.
PhylomeDBiP50052.
TreeFamiTF330024.

Family and domain databases

InterProiIPR000147. ATII_AT2_rcpt.
IPR000248. ATII_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00241. ANGIOTENSINR.
PR00636. ANGIOTENSN2R.
PR00237. GPCRRHODOPSN.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P50052-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKGNSTLATT SKNITSGLHF GLVNISGNNE STLNCSQKPS DKHLDAIPIL
60 70 80 90 100
YYIIFVIGFL VNIVVVTLFC CQKGPKKVSS IYIFNLAVAD LLLLATLPLW
110 120 130 140 150
ATYYSYRYDW LFGPVMCKVF GSFLTLNMFA SIFFITCMSV DRYQSVIYPF
160 170 180 190 200
LSQRRNPWQA SYIVPLVWCM ACLSSLPTFY FRDVRTIEYL GVNACIMAFP
210 220 230 240 250
PEKYAQWSAG IALMKNILGF IIPLIFIATC YFGIRKHLLK TNSYGKNRIT
260 270 280 290 300
RDQVLKMAAA VVLAFIICWL PFHVLTFLDA LAWMGVINSC EVIAVIDLAL
310 320 330 340 350
PFAILLGFTN SCVNPFLYCF VGNRFQQKLR SVFRVPITWL QGKRESMSCR
360
KSSSLREMET FVS
Length:363
Mass (Da):41,184
Last modified:September 30, 1996 - v1
Checksum:iFDD7D4E6F9B43E60
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti269 – 2691W → C (PubMed:7999093).Curated
Sequence conflicti272 – 2721F → L in AAA50762 (PubMed:8185599).Curated
Sequence conflicti323 – 3231N → G in AAA50762 (PubMed:8185599).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211G → V Rare variant found in patients with X-linked mental retardation; unknown pathological significance. 2 Publications
Corresponds to variant rs121917810 [ dbSNP | Ensembl ].
VAR_065946
Natural varianti231 – 2311Y → H.
Corresponds to variant rs3729977 [ dbSNP | Ensembl ].
VAR_049374
Natural varianti248 – 2481R → K.1 Publication
Corresponds to variant rs5191 [ dbSNP | Ensembl ].
VAR_011849
Natural varianti268 – 2681C → W.
Corresponds to variant rs1042860 [ dbSNP | Ensembl ].
VAR_011850
Natural varianti324 – 3241R → Q Rare variant found in patients with X-linked mental retardation; unknown pathological significance. 2 Publications
Corresponds to variant rs35474657 [ dbSNP | Ensembl ].
VAR_065947
Natural varianti337 – 3371I → V Rare variant found in patients with X-linked mental retardation; unknown pathological significance. 1 Publication
VAR_065948

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20860 Genomic DNA. Translation: AAA85851.1.
L34579 Genomic DNA. Translation: AAA98990.1.
U10273 Genomic DNA. Translation: AAA61794.1.
U15592 Genomic DNA. Translation: AAA50762.1.
U16957 mRNA. Translation: AAA67753.1.
U27478 Genomic DNA. Translation: AAA84900.1.
AY536522 Genomic DNA. Translation: AAS45437.1.
AY322542 Genomic DNA. Translation: AAP84355.1.
AY324607 Genomic DNA. Translation: AAP72969.1.
CR541969 mRNA. Translation: CAG46767.1.
AK313927 mRNA. Translation: BAG36648.1.
AL732602 Genomic DNA. Translation: CAI40984.1.
CH471234 Genomic DNA. Translation: EAW51502.1.
BC095504 mRNA. Translation: AAH95504.1.
X87723 mRNA. Translation: CAA61022.1.
CCDSiCCDS14569.1.
PIRiJC2543.
RefSeqiNP_000677.2. NM_000686.4.
UniGeneiHs.405348.

Genome annotation databases

EnsembliENST00000371906; ENSP00000360973; ENSG00000180772.
GeneIDi186.
KEGGihsa:186.
UCSCiuc004eqh.4. human.

Polymorphism databases

DMDMi1703214.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U20860 Genomic DNA. Translation: AAA85851.1.
L34579 Genomic DNA. Translation: AAA98990.1.
U10273 Genomic DNA. Translation: AAA61794.1.
U15592 Genomic DNA. Translation: AAA50762.1.
U16957 mRNA. Translation: AAA67753.1.
U27478 Genomic DNA. Translation: AAA84900.1.
AY536522 Genomic DNA. Translation: AAS45437.1.
AY322542 Genomic DNA. Translation: AAP84355.1.
AY324607 Genomic DNA. Translation: AAP72969.1.
CR541969 mRNA. Translation: CAG46767.1.
AK313927 mRNA. Translation: BAG36648.1.
AL732602 Genomic DNA. Translation: CAI40984.1.
CH471234 Genomic DNA. Translation: EAW51502.1.
BC095504 mRNA. Translation: AAH95504.1.
X87723 mRNA. Translation: CAA61022.1.
CCDSiCCDS14569.1.
PIRiJC2543.
RefSeqiNP_000677.2. NM_000686.4.
UniGeneiHs.405348.

3D structure databases

ProteinModelPortaliP50052.
SMRiP50052. Positions 46-336.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106692. 5 interactions.
IntActiP50052. 3 interactions.
STRINGi9606.ENSP00000360973.

Chemistry

BindingDBiP50052.
ChEMBLiCHEMBL2094256.
DrugBankiDB01349. Tasosartan.
GuidetoPHARMACOLOGYi35.

Protein family/group databases

GPCRDBiSearch...

PTM databases

PhosphoSiteiP50052.

Polymorphism databases

DMDMi1703214.

Proteomic databases

PaxDbiP50052.
PRIDEiP50052.

Protocols and materials databases

DNASUi186.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371906; ENSP00000360973; ENSG00000180772.
GeneIDi186.
KEGGihsa:186.
UCSCiuc004eqh.4. human.

Organism-specific databases

CTDi186.
GeneCardsiGC0XP115216.
H-InvDBHIX0213472.
HGNCiHGNC:338. AGTR2.
HPAiHPA029592.
MIMi300034. gene.
neXtProtiNX_P50052.
Orphaneti777. X-linked non-syndromic intellectual disability.
PharmGKBiPA44.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG311643.
GeneTreeiENSGT00760000119055.
HOGENOMiHOG000234122.
HOVERGENiHBG104998.
InParanoidiP50052.
KOiK04167.
OMAiNCSHKPS.
OrthoDBiEOG7TQV1F.
PhylomeDBiP50052.
TreeFamiTF330024.

Enzyme and pathway databases

ReactomeiREACT_14819. Peptide ligand-binding receptors.
REACT_19231. G alpha (i) signalling events.

Miscellaneous databases

GeneWikiiAngiotensin_II_receptor_type_2.
GenomeRNAii186.
NextBioi764.
PROiP50052.
SOURCEiSearch...

Gene expression databases

BgeeiP50052.
CleanExiHS_AGTR2.
ExpressionAtlasiP50052. baseline and differential.
GenevestigatoriP50052.

Family and domain databases

InterProiIPR000147. ATII_AT2_rcpt.
IPR000248. ATII_rcpt.
IPR000276. GPCR_Rhodpsn.
IPR017452. GPCR_Rhodpsn_7TM.
[Graphical view]
PfamiPF00001. 7tm_1. 1 hit.
[Graphical view]
PRINTSiPR00241. ANGIOTENSINR.
PR00636. ANGIOTENSN2R.
PR00237. GPCRRHODOPSN.
PROSITEiPS00237. G_PROTEIN_RECEP_F1_1. 1 hit.
PS50262. G_PROTEIN_RECEP_F1_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The sequence and genomic organization of the human type 2 angiotensin II receptor."
    Martin M.M., Elton T.S.
    Biochem. Biophys. Res. Commun. 209:554-562(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Liver.
  2. "Assignment of the human angiotensin II type 2 receptor gene (AGTR2) to chromosome Xq22-q23 by fluorescence in situ hybridization."
    Chassagne C., Beatty B.G., Meloche S.
    Genomics 25:601-603(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  3. "Human type 2 angiotensin II receptor gene: cloned, mapped to the X chromosome, and its mRNA is expressed in the human lung."
    Koike G., Horiuchi M., Yamada T., Szpirer C., Jacob H.J., Dzau V.J.
    Biochem. Biophys. Res. Commun. 203:1842-1850(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Blood.
  4. "Molecular cloning and expression of the gene encoding human angiotensin II type 2 receptor."
    Tsuzuki S., Ichiki T., Nakakubo H., Kitami Y., Guo D.F., Shirai H., Inagami T.
    Biochem. Biophys. Res. Commun. 200:1449-1454(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  5. "Molecular cloning of the human angiotensin II type 2 receptor cDNA."
    Martin M.M., Su B., Elton T.S.
    Biochem. Biophys. Res. Commun. 205:645-651(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lung.
  6. "Molecular characterization and chromosome localization of a human angiotensin II AT2 receptor gene highly expressed in fetal tissues."
    Lazard D., Briend-Sutren M.M., Villageois P., Mattei M.-G., Strosberg A.D., Nahmias C.
    Recept. Channels 2:271-280(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  7. "Sequence of the AGTR2 gene in Cantonese."
    Zhang M., Ma H., Wang B., Zhao Y.
    Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  8. "Isolation of complete coding sequence for angiotensin II receptor, type 2 (AGTR2)."
    Kopatz S.A., Aronstam R.S., Sharma S.V.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  9. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  10. Rieder M.J., da Ponte S.H., Kuldanek S.A., Rajkumar N., Smith J.D., Toth E.J., Nickerson D.A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  11. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  12. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  13. 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  15. Katsuya T., Dzau V.J.
    Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE OF 1-22.
    Tissue: Blood.
  16. Warnecke C.H., Holzmeister J., Regitz-Zagrosek V., Fleck E.
    Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE OF 1-16.
    Tissue: Uterus.
  17. Cited for: TISSUE SPECIFICITY, VARIANTS VAL-21; LYS-248; GLN-324 AND VAL-337, POSSIBLE ASSOCIATION OF VARIANTS VAL-21; GLN-324 AND VAL-337 WITH X-LINKED MENTAL RETARDATION.
  18. "Trans-inactivation of receptor tyrosine kinases by novel angiotensin II AT2 receptor-interacting protein, ATIP."
    Nouet S., Amzallag N., Li J.-M., Louis S., Seitz I., Cui T.-X., Alleaume A.-M., Di Benedetto M., Boden C., Masson M., Strosberg A.D., Horiuchi M., Couraud P.-O., Nahmias C.
    J. Biol. Chem. 279:28989-28997(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MTUS1, FUNCTION.
  19. "XLID-causing mutations and associated genes challenged in light of data from large-scale human exome sequencing."
    Piton A., Redin C., Mandel J.L.
    Am. J. Hum. Genet. 93:368-383(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: LACK OF ASSOCIATION VARIANTS VAL-21; GLN-324 AND VAL-337 WITH X-LINKED MENTAL RETARDATION.

Entry informationi

Entry nameiAGTR2_HUMAN
AccessioniPrimary (citable) accession number: P50052
Secondary accession number(s): B2R9V1, Q13016, Q6FGY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 30, 1996
Last sequence update: September 30, 1996
Last modified: February 3, 2015
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Caution

Although AGTR2 has been reported to be involved in X-linked mental retardation (PubMed:12089445), its pathological role is questionable (PubMed:23871722).2 Publications

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 7-transmembrane G-linked receptors
    List of 7-transmembrane G-linked receptor entries
  2. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.