GRPR_HUMAN - dbPTM
GRPR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GRPR_HUMAN
UniProt AC P30550
Protein Name Gastrin-releasing peptide receptor
Gene Name GRPR
Organism Homo sapiens (Human).
Sequence Length 384
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description Receptor for gastrin-releasing peptide (GRP). [PubMed: 1655761 Signals via association with G proteins that activate a phosphatidylinositol-calcium second messenger system, resulting in Akt phosphorylation. Contributes to the regulation of food intake. Contributes to the perception of prurient stimuli and transmission of itch signals in the spinal cord that promote scratching behavior, but does not play a role in the perception of pain. Contributes primarily to nonhistaminergic itch sensation. Contributes to long-term fear memory, but not normal spatial memory (By similarity]
Protein Sequence MALNDCFLLNLEVDHFMHCNISSHSADLPVNDDWSHPGILYVIPAVYGVIILIGLIGNITLIKIFCTVKSMRNVPNLFISSLALGDLLLLITCAPVDASRYLADRWLFGRIGCKLIPFIQLTSVGVSVFTLTALSADRYKAIVRPMDIQASHALMKICLKAAFIWIISMLLAIPEAVFSDLHPFHEESTNQTFISCAPYPHSNELHPKIHSMASFLVFYVIPLSIISVYYYFIAKNLIQSAYNLPVEGNIHVKKQIESRKRLAKTVLVFVGLFAFCWLPNHVIYLYRSYHYSEVDTSMLHFVTSICARLLAFTNSCVNPFALYLLSKSFRKQFNTQLLCCQPGLIIRSHSTGRSTTCMTSLKSTNPSVATFSLINGNICHERYV
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
20N-linked_GlycosylationVDHFMHCNISSHSAD
CCEEECCCCCCCCCC
23.62UniProtKB CARBOHYD
127PhosphorylationQLTSVGVSVFTLTAL
EEECCCEEEEHHHHC
12.94-
328PhosphorylationALYLLSKSFRKQFNT
HHHHHCHHHHHHCCH
27.2329759185
335PhosphorylationSFRKQFNTQLLCCQP
HHHHHCCHHEEEECC
23.1429759185
339S-palmitoylationQFNTQLLCCQPGLII
HCCHHEEEECCCEEE
2.49-
348PhosphorylationQPGLIIRSHSTGRST
CCCEEEEECCCCCCC
16.0430108239
350PhosphorylationGLIIRSHSTGRSTTC
CEEEEECCCCCCCCE
33.5330108239
351PhosphorylationLIIRSHSTGRSTTCM
EEEEECCCCCCCCEE
31.0630108239
354PhosphorylationRSHSTGRSTTCMTSL
EECCCCCCCCEECCC
29.4330108239
355PhosphorylationSHSTGRSTTCMTSLK
ECCCCCCCCEECCCC
23.7430108239
356PhosphorylationHSTGRSTTCMTSLKS
CCCCCCCCEECCCCC
11.0930108239
359PhosphorylationGRSTTCMTSLKSTNP
CCCCCEECCCCCCCC
32.8130108239
360PhosphorylationRSTTCMTSLKSTNPS
CCCCEECCCCCCCCC
13.6030108239
362AcetylationTTCMTSLKSTNPSVA
CCEECCCCCCCCCCE
55.817367235
363PhosphorylationTCMTSLKSTNPSVAT
CEECCCCCCCCCCEE
38.4228348404
364PhosphorylationCMTSLKSTNPSVATF
EECCCCCCCCCCEEE
49.9528348404
367PhosphorylationSLKSTNPSVATFSLI
CCCCCCCCCEEEEEE
26.8428348404
370PhosphorylationSTNPSVATFSLINGN
CCCCCCEEEEEECCC
16.1728348404
372PhosphorylationNPSVATFSLINGNIC
CCCCEEEEEECCCCC
24.8028348404

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

Oops, there are no upstream regulatory protein records of GRPR_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GRPR_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 GRPR_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PAR1_HUMANF2Rphysical
28514442
AVR2B_HUMANACVR2Bphysical
28514442
CXG1_HUMANGJC1physical
28514442
MRCKB_HUMANCDC42BPBphysical
28514442
UBP30_HUMANUSP30physical
28514442
CCHL_HUMANHCCSphysical
28514442
SC6A8_HUMANSLC6A8physical
28514442
ASPH2_HUMANASPHD2physical
28514442
ARL8B_HUMANARL8Bphysical
28514442
RAB4A_HUMANRAB4Aphysical
28514442
TAP1_HUMANTAP1physical
28514442
MFSD5_HUMANMFSD5physical
28514442
FADS1_HUMANFADS1physical
28514442
MTG1_HUMANMTG1physical
28514442
MTR1L_HUMANGPR50physical
28514442
S35G2_HUMANSLC35G2physical
28514442
RAB3B_HUMANRAB3Bphysical
28514442
DUSTY_HUMANDSTYKphysical
28514442
ADCK1_HUMANADCK1physical
28514442
LMBR1_HUMANLMBR1physical
28514442
DPH6_HUMANDPH6physical
28514442
F213A_HUMANFAM213Aphysical
28514442
RAB32_HUMANRAB32physical
28514442
MD2L2_HUMANMAD2L2physical
28514442
ATLA3_HUMANATL3physical
28514442
GNPAT_HUMANGNPATphysical
28514442
PANX1_HUMANPANX1physical
28514442
ABCB6_HUMANABCB6physical
28514442
TTK_HUMANTTKphysical
28514442
RAP1B_HUMANRAP1Bphysical
28514442
AT12A_HUMANATP12Aphysical
28514442
FND3A_HUMANFNDC3Aphysical
28514442
RETR2_HUMANFAM134Aphysical
28514442
ARF5_HUMANARF5physical
28514442
DHRS7_HUMANDHRS7physical
28514442
CDS1_HUMANCDS1physical
28514442
MET7B_HUMANMETTL7Bphysical
28514442
ARV1_HUMANARV1physical
28514442
MBLC2_HUMANMBLAC2physical
28514442
S19A2_HUMANSLC19A2physical
28514442
ARL5B_HUMANARL5Bphysical
28514442
LMBD2_HUMANLMBRD2physical
28514442
BTAF1_HUMANBTAF1physical
28514442
ATP7B_HUMANATP7Bphysical
28514442
CIA30_HUMANNDUFAF1physical
28514442
FACR2_HUMANFAR2physical
28514442
MIPEP_HUMANMIPEPphysical
28514442
PTH2_HUMANPTRH2physical
28514442
COX1_HUMANCOX1physical
28514442
GRP_HUMANGRPphysical
12021405

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GRPR_HUMAN

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Related Literatures of Post-Translational Modification

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