PTH1R_HUMAN - dbPTM
PTH1R_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTH1R_HUMAN
UniProt AC Q03431
Protein Name Parathyroid hormone/parathyroid hormone-related peptide receptor
Gene Name PTH1R
Organism Homo sapiens (Human).
Sequence Length 593
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description 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..
Protein Sequence MGTARIAPGLALLLCCPVLSSAYALVDADDVMTKEEQIFLLHRAQAQCEKRLKEVLQRPASIMESDKGWTSASTSGKPRKDKASGKLYPESEEDKEAPTGSRYRGRPCLPEWDHILCWPLGAPGEVVAVPCPDYIYDFNHKGHAYRRCDRNGSWELVPGHNRTWANYSECVKFLTNETREREVFDRLGMIYTVGYSVSLASLTVAVLILAYFRRLHCTRNYIHMHLFLSFMLRAVSIFVKDAVLYSGATLDEAERLTEEELRAIAQAPPPPATAAAGYAGCRVAVTFFLYFLATNYYWILVEGLYLHSLIFMAFFSEKKYLWGFTVFGWGLPAVFVAVWVSVRATLANTGCWDLSSGNKKWIIQVPILASIVLNFILFINIVRVLATKLRETNAGRCDTRQQYRKLLKSTLVLMPLFGVHYIVFMATPYTEVSGTLWQVQMHYEMLFNSFQGFFVAIIYCFCNGEVQAEIKKSWSRWTLALDFKRKARSGSSSYSYGPMVSHTSVTNVGPRVGLGLPLSPRLLPTATTNGHPQLPGHAKPGTPALETLETTPPAMAAPKDDGFLNGSCSGLDEEASGPERPPALLQEEWETVM
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
23PhosphorylationCPVLSSAYALVDADD
HHHHHHHHHHCCHHH
11.47-
73PhosphorylationDKGWTSASTSGKPRK
CCCCCCCCCCCCCCC
23.91-
91PhosphorylationSGKLYPESEEDKEAP
CCCCCCCCHHCCCCC
41.6128857561
99PhosphorylationEEDKEAPTGSRYRGR
HHCCCCCCCCCCCCC
55.6316674116
101PhosphorylationDKEAPTGSRYRGRPC
CCCCCCCCCCCCCCC
28.7216674116
151N-linked_GlycosylationAYRRCDRNGSWELVP
CEEECCCCCCEEECC
35.28UniProtKB CARBOHYD
161N-linked_GlycosylationWELVPGHNRTWANYS
EEECCCCCCCCCCHH
49.33UniProtKB CARBOHYD
163PhosphorylationLVPGHNRTWANYSEC
ECCCCCCCCCCHHHH
33.9627732954
166N-linked_GlycosylationGHNRTWANYSECVKF
CCCCCCCCHHHHHHH
32.21UniProtKB CARBOHYD
167PhosphorylationHNRTWANYSECVKFL
CCCCCCCHHHHHHHH
9.7127732954
168PhosphorylationNRTWANYSECVKFLT
CCCCCCHHHHHHHHC
25.0727732954
176N-linked_GlycosylationECVKFLTNETREREV
HHHHHHCCCHHHHHH
51.28UniProtKB CARBOHYD
192PhosphorylationDRLGMIYTVGYSVSL
HHHCCCEECCCCHHH
9.13-
198PhosphorylationYTVGYSVSLASLTVA
EECCCCHHHHHHHHH
16.5728857561
201PhosphorylationGYSVSLASLTVAVLI
CCCHHHHHHHHHHHH
29.8428857561
203PhosphorylationSVSLASLTVAVLILA
CHHHHHHHHHHHHHH
12.1528857561
320PhosphorylationAFFSEKKYLWGFTVF
HHHCCCCCHHCEEEC
20.82-
387PhosphorylationNIVRVLATKLRETNA
HHHHHHHHHHHHCCC
26.84-
388UbiquitinationIVRVLATKLRETNAG
HHHHHHHHHHHCCCC
39.68-
392PhosphorylationLATKLRETNAGRCDT
HHHHHHHCCCCCCCH
24.76-
473PhosphorylationVQAEIKKSWSRWTLA
HHHHHHHHHHHEEEE
25.86-
484UbiquitinationWTLALDFKRKARSGS
EEEEEEHHHHHCCCC
53.29-
489PhosphorylationDFKRKARSGSSSYSY
EHHHHHCCCCCCCCC
48.1328857561
491PhosphorylationKRKARSGSSSYSYGP
HHHHCCCCCCCCCCC
19.8428857561
492PhosphorylationRKARSGSSSYSYGPM
HHHCCCCCCCCCCCC
36.5028857561
493PhosphorylationKARSGSSSYSYGPMV
HHCCCCCCCCCCCCC
21.5728857561
494PhosphorylationARSGSSSYSYGPMVS
HCCCCCCCCCCCCCC
14.0928857561
495PhosphorylationRSGSSSYSYGPMVSH
CCCCCCCCCCCCCCC
26.0928857561
496PhosphorylationSGSSSYSYGPMVSHT
CCCCCCCCCCCCCCE
19.60-
501PhosphorylationYSYGPMVSHTSVTNV
CCCCCCCCCEEEECC
18.1328857561
503PhosphorylationYGPMVSHTSVTNVGP
CCCCCCCEEEECCCC
19.8628857561
504PhosphorylationGPMVSHTSVTNVGPR
CCCCCCEEEECCCCC
22.8628857561
506PhosphorylationMVSHTSVTNVGPRVG
CCCCEEEECCCCCCC
24.7728857561
519PhosphorylationVGLGLPLSPRLLPTA
CCCCCCCCCCCCCCC
13.1626029660
547PhosphorylationPGTPALETLETTPPA
CCCCCHHHHCCCCCC
30.64-
550PhosphorylationPALETLETTPPAMAA
CCHHHHCCCCCCCCC
47.9522468782
551PhosphorylationALETLETTPPAMAAP
CHHHHCCCCCCCCCC
20.218703170
569PhosphorylationGFLNGSCSGLDEEAS
CCCCCCCCCCCCCCC
44.0522468782
576PhosphorylationSGLDEEASGPERPPA
CCCCCCCCCCCCCCH
59.1522468782

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
494YPhosphorylationKinaseIGF1RP08069
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTH1R_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10)
Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PTH1R_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PTHR_HUMANPTHLHphysical
9108031
PTHY_HUMANPTHphysical
9108031
NHRF2_HUMANSLC9A3R2physical
12075354
NHRF1_HUMANSLC9A3R1physical
12075354
DYLT1_MOUSEDynlt1bphysical
17202780
E41L2_MOUSEEpb4.1l2physical
17202780
DJC17_HUMANDNAJC17physical
26186194
MBOA7_HUMANMBOAT7physical
26186194
CUX1_HUMANCUX1physical
26186194
CASP_HUMANCUX1physical
26186194
AT12A_HUMANATP12Aphysical
26186194
PIGO_HUMANPIGOphysical
26186194
S12A9_HUMANSLC12A9physical
26186194
TMX2_HUMANTMX2physical
26186194
SRBP2_HUMANSREBF2physical
26186194
B3A2_HUMANSLC4A2physical
26186194
RETST_HUMANRETSATphysical
26186194
PLCC_HUMANAGPAT3physical
26186194
SPP2B_HUMANSPPL2Bphysical
26186194
S12A7_HUMANSLC12A7physical
26186194
S12A4_HUMANSLC12A4physical
26186194
ZNT1_HUMANSLC30A1physical
26186194
ABCA3_HUMANABCA3physical
26186194
SOAT1_HUMANSOAT1physical
26186194
CCPG1_HUMANCCPG1physical
26186194
CTL1_HUMANSLC44A1physical
26186194
ALG6_HUMANALG6physical
26186194
SIDT2_HUMANSIDT2physical
26186194
EVI5L_HUMANEVI5Lphysical
26186194
AT11C_HUMANATP11Cphysical
26186194
S47A1_HUMANSLC47A1physical
26186194
DEGS1_HUMANDEGS1physical
26186194
FADS1_HUMANFADS1physical
26186194
CLN3_HUMANCLN3physical
26186194
F118B_HUMANFAM118Bphysical
26186194
MOT8_HUMANSLC16A2physical
26186194
CERS6_HUMANCERS6physical
26186194
KCNJ8_HUMANKCNJ8physical
26186194
CA112_HUMANC1orf112physical
26186194
AT132_HUMANATP13A2physical
26186194
AG10A_HUMANALG10physical
26186194
S27A3_HUMANSLC27A3physical
26186194
PCX3_HUMANPCNXL3physical
26186194
ACD10_HUMANACAD10physical
26186194
SGPP1_HUMANSGPP1physical
26186194
PM34_HUMANSLC25A17physical
26186194
BRI3B_HUMANBRI3BPphysical
26186194
PIGM_HUMANPIGMphysical
26186194
DJC17_HUMANDNAJC17physical
28514442
SIDT2_HUMANSIDT2physical
28514442
CTL1_HUMANSLC44A1physical
28514442
S47A1_HUMANSLC47A1physical
28514442
S12A9_HUMANSLC12A9physical
28514442
ZNT1_HUMANSLC30A1physical
28514442
FADS1_HUMANFADS1physical
28514442
AT132_HUMANATP13A2physical
28514442
EVI5L_HUMANEVI5Lphysical
28514442
CCPG1_HUMANCCPG1physical
28514442
SOAT1_HUMANSOAT1physical
28514442
S12A4_HUMANSLC12A4physical
28514442
PCX3_HUMANPCNXL3physical
28514442
B3A2_HUMANSLC4A2physical
28514442
AT11C_HUMANATP11Cphysical
28514442
PIGO_HUMANPIGOphysical
28514442
F118B_HUMANFAM118Bphysical
28514442
TMX2_HUMANTMX2physical
28514442
DEGS1_HUMANDEGS1physical
28514442
AG10A_HUMANALG10physical
28514442
ACD10_HUMANACAD10physical
28514442
OPA1_HUMANOPA1physical
28514442
MBOA7_HUMANMBOAT7physical
28514442
SPP2B_HUMANSPPL2Bphysical
28514442
SGPP1_HUMANSGPP1physical
28514442
AT12A_HUMANATP12Aphysical
28514442

Drug and Disease Associations
Kegg Disease
H00479 Metaphyseal dysplasias, including: Metaphyseal dysplasia, Schmid type; Metaphyseal dysplasia, McKusi
H00495 Eiken dysplasia
H00508 Blomstrand syndrome; Blomstrand chondrodysplasia
H00680 Primary failure of tooth eruption
OMIM Disease
156400Jansen metaphyseal chondrodysplasia (JMC)
215045Chondrodysplasia Blomstrand type (BOCD)
166000Enchondromatosis multiple (ENCHOM)
600002Eiken skeletal dysplasia (EISD)
125350Primary failure of tooth eruption (PFE)
Kegg Drug
D03358 Teriparatide acetate (JAN); Human PHT (TN)
D05364 Parathyroid hormone (human) (USAN); Parathyroid hormone (INN); ALX 1-11; Parathormone; PTH
D06078 Teriparatide (genetical recombination) (JAN); Teriparatide (USAN/INN); Forteo (TN)
D06546 Teriparatide acetate (USAN); Teriparatide acetate hydrate; Parathar (TN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PTH1R_HUMAN

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Related Literatures of Post-Translational Modification

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