Q03431 (PTH1R_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Parathyroid hormone/parathyroid hormone-related peptide receptor

Alternative name(s):
PTH/PTHrP type I receptor
Short name=PTH/PTHr receptor
Parathyroid hormone 1 receptor
Short name=PTH1 receptor

Gene names

Name:	PTH1R
Synonyms:	PTHR, PTHR1

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	593 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	This is a receptor for parathyroid hormone and for parathyroid hormone-related peptide. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase and also a phosphatidylinositol-calcium second messenger system. Ref.10 Ref.12
Subunit structure	Interacts (via N-terminal extracellular domain) with PTHLH and PTH. Homodimer in the absence of bound ligand. Peptide hormone binding leads to dissociation of the homodimer. Interacts (via C-terminus) with the heterodimer formed by GNG2 and GNB1. Ref.10 Ref.12
Subcellular location	Cell membrane; Multi-pass membrane protein Ref.12.
Tissue specificity	Expressed in most tissues. Most abundant in kidney, bone and liver.
Involvement in disease	Jansen metaphyseal chondrodysplasia (JMC) [MIM:156400]: Rare autosomal dominant disorder characterized by a short-limbed dwarfism associated with hypercalcemia and normal or low serum concentrations of the two parathyroid hormones. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13 Ref.14 Ref.15 Ref.17 Ref.20 Chondrodysplasia Blomstrand type (BOCD) [MIM:215045]: Severe skeletal dysplasia. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16 Enchondromatosis multiple (ENCHOM) [MIM:166000]: A condition characterized by multiple formation of enchondromas, benign neoplasms derived from mesodermal cells that form cartilage. Enchondromas remain within the substance of a cartilage or bone. Clinical problems caused by enchondromas include skeletal deformity and the potential for malignant change to osteosarcoma. Note: The disease may be caused by mutations affecting the gene represented in this entry. Ref.18 Ref.19 Eiken skeletal dysplasia (EISD) [MIM:600002]: A rare skeletal dysplasia characterized by severely retarded ossification, principally of the epiphyses, pelvis, hands and feet, as well as by abnormal modeling of the bones in hands and feet, abnormal persistence of cartilage in the pelvis and mild growth retardation. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21 Primary failure of tooth eruption (PFE) [MIM:125350]: Rare condition that has high penetrance and variable expressivity and in which tooth retention occurs without evidence of any obvious mechanical interference. Instead, malfunction of the eruptive mechanism itself appears to cause nonankylosed permanent teeth to fail to erupt, although the eruption pathway has been cleared by bone resorption. Note: The disease is caused by mutations affecting the gene represented in this entry.
Sequence similarities	Belongs to the G-protein coupled receptor 2 family.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Disease	Disease mutation Dwarfism
Domain	Signal Transmembrane Transmembrane helix
Molecular function	G-protein coupled receptor Receptor Transducer
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adenylate cyclase-activating G-protein coupled receptor signaling pathway Inferred from sequence or structural similarity. Source: BHF-UCL aging Inferred from electronic annotation. Source: Compara bone mineralization Inferred from electronic annotation. Source: Compara bone resorption Inferred from electronic annotation. Source: Compara cell maturation Inferred from electronic annotation. Source: Compara chondrocyte differentiation Inferred from electronic annotation. Source: Compara elevation of cytosolic calcium ion concentration Inferred from electronic annotation. Source: Compara negative regulation of cell proliferation Inferred from electronic annotation. Source: Compara osteoblast development Inferred from electronic annotation. Source: Compara phospholipase C-activating G-protein coupled receptor signaling pathway Inferred by curator PubMed 19608645. Source: BHF-UCL positive regulation of cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of inositol phosphate biosynthetic process Inferred from sequence or structural similarity. Source: BHF-UCL skeletal system development Traceable author statement Ref.16. Source: ProtInc
Cellular_component	apical plasma membrane Inferred from sequence or structural similarity. Source: BHF-UCL basolateral plasma membrane Inferred from sequence or structural similarity. Source: BHF-UCL brush border membrane Inferred from electronic annotation. Source: Compara cytoplasm Traceable author statement PubMed 10709993. Source: ProtInc integral to plasma membrane Inferred from direct assay Ref.11. Source: UniProtKB nucleus Traceable author statement PubMed 10709993. Source: ProtInc receptor complex Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular_function	parathyroid hormone receptor activity Inferred from direct assay Ref.11. Source: UniProtKB peptide hormone binding Inferred from direct assay Ref.11. Source: UniProtKB protein self-association Inferred from direct assay Ref.11. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

26

Potential

Chain

27 – 593

567

Parathyroid hormone/parathyroid hormone-related peptide receptor

PRO_0000012845

Regions

Topological domain

27 – 188

162

Extracellular Potential

Transmembrane

189 – 212

24

Helical; Name=1; Potential

Topological domain

213 – 219

7

Cytoplasmic Potential

Transmembrane

220 – 239

20

Helical; Name=2; Potential

Topological domain

240 – 282

43

Extracellular Potential

Transmembrane

283 – 306

24

Helical; Name=3; Potential

Topological domain

307 – 320

14

Cytoplasmic Potential

Transmembrane

321 – 342

22

Helical; Name=4; Potential

Topological domain

343 – 361

19

Extracellular Potential

Transmembrane

362 – 382

21

Helical; Name=5; Potential

Topological domain

383 – 409

27

Cytoplasmic Potential

Transmembrane

410 – 428

19

Helical; Name=6; Potential

Topological domain

429 – 440

12

Extracellular Potential

Transmembrane

441 – 463

23

Helical; Name=7; Potential

Topological domain

464 – 593

130

Cytoplasmic Potential

Motif

474 – 477

4

Important for interaction with G proteins

Amino acid modifications

Glycosylation

151

1

N-linked (GlcNAc...) Potential

Glycosylation

161

1

N-linked (GlcNAc...) Potential

Glycosylation

166

1

N-linked (GlcNAc...) Potential

Glycosylation

176

1

N-linked (GlcNAc...) Potential

Disulfide bond

48 ↔ 117

Ref.7 Ref.9 Ref.11

Disulfide bond

108 ↔ 148

Ref.7 Ref.9 Ref.11

Disulfide bond

131 ↔ 170

Ref.7 Ref.9 Ref.11

Natural variations

Natural variant

132

1

P → L in BOCD. Ref.16

VAR_016062

Natural variant

150

1

R → C in ENCHOM; Ollier type; unclear pathogenicity. Ref.18 Ref.19

VAR_016063

Natural variant

223

1

H → R in JMC; constitutively activated. Ref.13 Ref.14 Ref.15

VAR_003582

Natural variant

410

1

T → P in JMC; constitutively activated. Ref.14 Ref.15

VAR_003583

Natural variant

410

1

T → R in JMC; leads to agonist-independent cAMP formation which is less pronounced than that observed with the Pro-410 mutant. Ref.20

VAR_038811

Natural variant

458

1

I → R in JMC. Ref.17

VAR_016064

Experimental info

Mutagenesis

135

1

I → K: Abolishes hormone binding and homodimerization. Ref.12

Mutagenesis

137

1

D → A: Abolishes hormone binding. No effect on homodimerization. Ref.12

Mutagenesis

474

1

W → A: Strongly reduced interaction with G protein subunits GNB1 and GNG2; when associated with A-477. Ref.10

Mutagenesis

477

1

W → A: Strongly reduced interaction with G protein subunits GNB1 and GNG2; when associated with A-474. Ref.10

Sequence conflict

471

1

K → N Ref.2

Sequence conflict

473

1

S → C Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

593

Helix Strand Turn

Details...

Helix

34 – 55

22

Beta strand

126 – 130

5

Beta strand

143 – 148

6

Beta strand

152 – 154

3

Beta strand

160 – 163

4

Turn

168 – 173

6

Helix

180 – 185

6

Helix

188 – 196

9

Sequences

	Sequence		Length	Mass (Da)
	Q03431 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: DA1400640A6C7F2B	FASTA	593	66,361
	10 20 30 40 50 60 MGTARIAPGL ALLLCCPVLS SAYALVDADD VMTKEEQIFL LHRAQAQCEK RLKEVLQRPA 70 80 90 100 110 120 SIMESDKGWT SASTSGKPRK DKASGKLYPE SEEDKEAPTG SRYRGRPCLP EWDHILCWPL 130 140 150 160 170 180 GAPGEVVAVP CPDYIYDFNH KGHAYRRCDR NGSWELVPGH NRTWANYSEC VKFLTNETRE 190 200 210 220 230 240 REVFDRLGMI YTVGYSVSLA SLTVAVLILA YFRRLHCTRN YIHMHLFLSF MLRAVSIFVK 250 260 270 280 290 300 DAVLYSGATL DEAERLTEEE LRAIAQAPPP PATAAAGYAG CRVAVTFFLY FLATNYYWIL 310 320 330 340 350 360 VEGLYLHSLI FMAFFSEKKY LWGFTVFGWG LPAVFVAVWV SVRATLANTG CWDLSSGNKK 370 380 390 400 410 420 WIIQVPILAS IVLNFILFIN IVRVLATKLR ETNAGRCDTR QQYRKLLKST LVLMPLFGVH 430 440 450 460 470 480 YIVFMATPYT EVSGTLWQVQ MHYEMLFNSF QGFFVAIIYC FCNGEVQAEI KKSWSRWTLA 490 500 510 520 530 540 LDFKRKARSG SSSYSYGPMV SHTSVTNVGP RVGLGLPLSP RLLPTATTNG HPQLPGHAKP 550 560 570 580 590 GTPALETLET TPPAMAAPKD DGFLNGSCSG LDEEASGPER PPALLQEEWE TVM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identical complementary deoxyribonucleic acids encode a human renal and bone parathyroid hormone (PTH)/PTH-related peptide receptor." Schipani E., Karga H., Karaplis A.C., Potts J.T. Jr., Kronenberg H.M., Abou-Samra A.-B., Segre G.V., Jueppner H. Endocrinology 132:2157-2165(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[2]	"Cloning and functional expression of a human parathyroid hormone receptor." Schneider H., Feyen J.-H., Rao Movva N. Eur. J. Pharmacol. 246:149-155(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[3]	"Pseudohypoparathyroidism type Ib is not caused by mutations in the coding exons of the human parathyroid hormone (PTH)/PTH-related peptide receptor gene." Schipani E., Weinstein L.S., Bergwitz C., Iida-Klein A., Kong X.F., Stuhrmann M., Kruse K., Whyte M.P., Murray T., Schmidtke J., Dop C., Brickman A.S., Crawford J.D., Potts J.T. Jr., Kronenberg H.M., Abou-Samra A.-B., Segre G.V., Jueppner H. J. Clin. Endocrinol. Metab. 80:1611-1621(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Characterization of cDNA and genomic DNA encoding the human PTH/PTHrP receptor." Levine M.A. Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[5]	"Isolation of cDNA coding for parathyroid hormone receptor 1 (PTHR1)." King M.M., Aronstam R.S., Sharma S.V. Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lung.
[6]	"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: Cerebellum.
[7]	"The N-terminal fragment of human parathyroid hormone receptor 1 constitutes a hormone binding domain and reveals a distinct disulfide pattern." Grauschopf U., Lilie H., Honold K., Wozny M., Reusch D., Esswein A., Schafer W., Rucknagel K.P., Rudolph R. Biochemistry 39:8878-8887(2000) [PubMed] [Europe PMC] [Abstract] Cited for: DISULFIDE BONDS IN EXTRACELLULAR DOMAIN.
[8]	"Binding domain of human parathyroid hormone receptor: from conformation to function." Pellegrini M., Bisello A., Rosenblatt M., Chorev M., Mierke D.F. Biochemistry 37:12737-12743(1998) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 168-198.
[9]	"Molecular recognition of parathyroid hormone by its G protein-coupled receptor." Pioszak A.A., Xu H.E. Proc. Natl. Acad. Sci. U.S.A. 105:5034-5039(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 29-187 IN COMPLEX WITH PTH, DISULFIDE BONDS.
[10]	"Structure of the parathyroid hormone receptor C terminus bound to the G-protein dimer Gbeta1gamma2." Johnston C.A., Kimple A.J., Giguere P.M., Siderovski D.P. Structure 16:1086-1094(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 474-481 IN COMPLEX WITH GNG2 AND GNB1, FUNCTION, SUBUNIT, MUTAGENESIS OF TRP-474 AND TRP-477.
[11]	"Structural basis for parathyroid hormone-related protein binding to the parathyroid hormone receptor and design of conformation-selective peptides." Pioszak A.A., Parker N.R., Gardella T.J., Xu H.E. J. Biol. Chem. 284:28382-28391(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 29-187 IN COMPLEX WITH PTHLH, DISULFIDE BONDS.
[12]	"Dimeric arrangement of the parathyroid hormone receptor and a structural mechanism for ligand-induced dissociation." Pioszak A.A., Harikumar K.G., Parker N.R., Miller L.J., Xu H.E. J. Biol. Chem. 285:12435-12444(2010) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.24 ANGSTROMS) OF 29-187, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF ILE-135 AND ASP-137.
[13]	"A constitutively active mutant PTH-PTHrP receptor in Jansen-type metaphyseal chondrodysplasia." Schipani E., Kruse K., Jueppner H. Science 268:98-100(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT JMC ARG-223.
[14]	"Constitutively activated receptors for parathyroid hormone and parathyroid hormone-related peptide in Jansen's metaphyseal chondrodysplasia." Schipani E., Langman C.B., Parfitt A.M., Jensen G.S., Kikuchi S., Kooh S.W., Cole W.G., Jueppner H. N. Engl. J. Med. 335:708-714(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS JMC ARG-223 AND PRO-410.
[15]	"Constitutive activation of the cyclic adenosine 3',5'-monophosphate signaling pathway by parathyroid hormone (PTH)/PTH-related peptide receptors mutated at the two loci for Jansen's metaphyseal chondrodysplasia." Schipani E., Jensen G.S., Pincus J., Nissenson R.A., Gardella T.J., Jueppner H. Mol. Endocrinol. 11:851-858(1997) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS JMC ARG-223 AND PRO-410.
[16]	"A homozygous inactivating mutation in the parathyroid hormone/parathyroid hormone-related peptide receptor causing Blomstrand chondrodysplasia." Zhang P., Jobert A.-S., Couvineau A., Silve C. J. Clin. Endocrinol. Metab. 83:3365-3368(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT BOCD LEU-132.
[17]	"A novel parathyroid hormone (PTH)/PTH-related peptide receptor mutation in Jansen's metaphyseal chondrodysplasia." Schipani E., Langman C.B., Hunzelman J., Le Merrer M., Loke K.Y., Dillon M.J., Silve C., Jueppner H. J. Clin. Endocrinol. Metab. 84:3052-3057(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT JMC ARG-458.
[18]	"A mutant PTH/PTHrP type I receptor in enchondromatosis." Hopyan S., Gokgoz N., Poon R., Gensure R.C., Yu C., Cole W.G., Bell R.S., Jueppner H., Andrulis I.L., Wunder J.S., Alman B.A. Nat. Genet. 30:306-310(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ENCHOM CYS-150.
[19]	"Enchondromatosis (Ollier disease, Maffucci syndrome) is not caused by the PTHR1 mutation p.R150C." Rozeman L.B., Sangiorgi L., Briaire-de Bruijn I.H., Mainil-Varlet P., Bertoni F., Cleton-Jansen A.-M., Hogendoorn P.C.W., Bovee J.V.M.G. Hum. Mutat. 24:466-473(2004) [PubMed] [Europe PMC] [Abstract] Cited for: DISCUSSION OF THE ASSOCIATION OF CYS-150 WITH ENCHOM.
[20]	"A form of Jansen's metaphyseal chondrodysplasia with limited metabolic and skeletal abnormalities is caused by a novel activating parathyroid hormone (PTH)/PTH-related peptide receptor mutation." Bastepe M., Raas-Rothschild A., Silver J., Weissman I., Wientroub S., Jueppner H., Gillis D. J. Clin. Endocrinol. Metab. 89:3595-3600(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT JMC ARG-410, CHARACTERIZATION OF VARIANT JMC ARG-410.
[21]	"Recessive mutations in PTHR1 cause contrasting skeletal dysplasias in Eiken and Blomstrand syndromes." Duchatelet S., Ostergaard E., Cortes D., Lemainque A., Julier C. Hum. Mol. Genet. 14:1-5(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN EISD.
[22]	"PTHR1 loss-of-function mutations in familial, nonsyndromic primary failure of tooth eruption." Decker E., Stellzig-Eisenhauer A., Fiebig B.S., Rau C., Kress W., Saar K., Rueschendorf F., Hubner N., Grimm T., Weber B.H.F. Am. J. Hum. Genet. 83:781-786(2008) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN PRIMARY FAILURE OF TOOTH ERUPTION.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L04308 mRNA. Translation: AAA36525.1.
X68596 mRNA. Translation: CAA48589.1.
U22409 , U22401, U22402, U22403, U22404, U22405, U22406, U22407, U22408 Genomic DNA. Translation: AAB60657.1.
U17418 mRNA. Translation: AAA56774.1.
AY449732 mRNA. Translation: AAR18076.1.
BC112221 mRNA. Translation: AAI12222.1.
BC112247 mRNA. Translation: AAI12248.1.

IPI

IPI00010732.

PIR

A49191. I38139.

RefSeq

NP_000307.1. NM_000316.2.
NP_001171673.1. NM_001184744.1.

UniGene

Hs.1019.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BL1	NMR	-	A	168-197	[»]
1ET2	model	-	S	168-469	[»]
1ET3	model	-	S	168-469	[»]
3C4M	X-ray	1.95	A/B	29-187	[»]
3H3G	X-ray	1.94	A	29-187	[»]
3KJ5	X-ray	3.00	C	474-481	[»]
3L2J	X-ray	3.24	A/B	29-187	[»]

ProteinModelPortal

Q03431.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q03431. 1 interaction.

MINT

MINT-258057.

STRING

9606.ENSP00000321999.

Protein family/group databases

GPCRDB

Search...

PTM databases

PhosphoSite

Q03431.

Polymorphism databases

DMDM

417555.

2D gel databases

REPRODUCTION-2DPAGE

Q03431.

Proteomic databases

PaxDb

Q03431.

PRIDE

Q03431.

Protocols and materials databases

DNASU

5745.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000313049; ENSP00000321999; ENSG00000160801.
ENST00000418619; ENSP00000411424; ENSG00000160801.
ENST00000430002; ENSP00000413774; ENSG00000160801.
ENST00000449590; ENSP00000402723; ENSG00000160801.

GeneID

5745.

KEGG

hsa:5745.

UCSC

uc003cqm.3. human.

Organism-specific databases

CTD

5745.

GeneCards

GC03P046895.

HGNC

HGNC:9608. PTH1R.

HPA

CAB016053.
HPA007978.

MIM

125350. phenotype.
156400. phenotype.
166000. phenotype.
168468. gene.
215045. phenotype.
600002. phenotype.

neXtProt

NX_Q03431.

Orphanet

50945. Chondrodysplasia, Blomstrand type.
1077. Dental ankylosis.
79106. Eiken syndrome.
296. Enchondromatosis.
163634. Maffucci syndrome.
33067. Metaphyseal chondrodysplasia, Jansen type.

PharmGKB

PA33953.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG293423.

HOGENOM

HOG000008248.

HOVERGEN

HBG008318.

KO

K04585.

OMA

WIIQVPI.

OrthoDB

EOG4XWFXR.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

Q03431.

Bgee

Q03431.

CleanEx

HS_PTH1R.

Genevestigator

Q03431.

GermOnline

ENSG00000160801. Homo sapiens.

Family and domain databases

InterPro

IPR017981. GPCR_2-like.
IPR001879. GPCR_2_extracellular_dom.
IPR002170. GPCR_2_parathyroid_rcpt.
IPR000832. GPCR_2_secretin-like.
IPR017983. GPCR_2_secretin-like_CS.
[Graphical view]

PANTHER

PTHR12011:SF24. PTHR12011:SF24. 1 hit.

Pfam

PF00002. 7tm_2. 1 hit.
PF02793. HRM. 1 hit.
[Graphical view]

PRINTS

PR00249. GPCRSECRETIN.
PR00393. PTRHORMONER.

SMART

SM00008. HormR. 1 hit.
[Graphical view]

PROSITE

PS00649. G_PROTEIN_RECEP_F2_1. 1 hit.
PS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
PS50227. G_PROTEIN_RECEP_F2_3. 1 hit.
PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q03431.

ChEMBL

CHEMBL1793.

EvolutionaryTrace

Q03431.

GenomeRNAi

5745.

NextBio

22372.

PMAP-CutDB

Q03431.

SOURCE

Search...

Entry information

Entry name

PTH1R_HUMAN

Accession

Primary (citable) accession number: Q03431
Secondary accession number(s): Q2M1U3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	May 1, 2013
This is version 139 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.