GRM3_HUMAN - dbPTM
GRM3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GRM3_HUMAN
UniProt AC Q14832
Protein Name Metabotropic glutamate receptor 3
Gene Name GRM3
Organism Homo sapiens (Human).
Sequence Length 879
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description G-protein coupled receptor for glutamate. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling inhibits adenylate cyclase activity..
Protein Sequence MKMLTRLQVLTLALFSKGFLLSLGDHNFLRREIKIEGDLVLGGLFPINEKGTGTEECGRINEDRGIQRLEAMLFAIDEINKDDYLLPGVKLGVHILDTCSRDTYALEQSLEFVRASLTKVDEAEYMCPDGSYAIQENIPLLIAGVIGGSYSSVSIQVANLLRLFQIPQISYASTSAKLSDKSRYDYFARTVPPDFYQAKAMAEILRFFNWTYVSTVASEGDYGETGIEAFEQEARLRNICIATAEKVGRSNIRKSYDSVIRELLQKPNARVVVLFMRSDDSRELIAAASRANASFTWVASDGWGAQESIIKGSEHVAYGAITLELASQPVRQFDRYFQSLNPYNNHRNPWFRDFWEQKFQCSLQNKRNHRRVCDKHLAIDSSNYEQESKIMFVVNAVYAMAHALHKMQRTLCPNTTKLCDAMKILDGKKLYKDYLLKINFTAPFNPNKDADSIVKFDTFGDGMGRYNVFNFQNVGGKYSYLKVGHWAETLSLDVNSIHWSRNSVPTSQCSDPCAPNEMKNMQPGDVCCWICIPCEPYEYLADEFTCMDCGSGQWPTADLTGCYDLPEDYIRWEDAWAIGPVTIACLGFMCTCMVVTVFIKHNNTPLVKASGRELCYILLFGVGLSYCMTFFFIAKPSPVICALRRLGLGSSFAICYSALLTKTNCIARIFDGVKNGAQRPKFISPSSQVFICLGLILVQIVMVSVWLILEAPGTRRYTLAEKRETVILKCNVKDSSMLISLTYDVILVILCTVYAFKTRKCPENFNEAKFIGFTMYTTCIIWLAFLPIFYVTSSDYRVQTTTMCISVSLSGFVVLGCLFAPKVHIILFQPQKNVVTHRLHLNRFSVSGTGTTYSQSSASTYVPTVCNGREVLDSTTSSL
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
11PhosphorylationLTRLQVLTLALFSKG
HHHHHHHHHHHHHHC
15.8923663014
16PhosphorylationVLTLALFSKGFLLSL
HHHHHHHHHCCHHHC
32.4923663014
209N-linked_GlycosylationAEILRFFNWTYVSTV
HHHHHHCCCEEEEEC
27.71UniProtKB CARBOHYD
243PhosphorylationLRNICIATAEKVGRS
HHCHHHHHHHHHCCC
18.5522985185
255PhosphorylationGRSNIRKSYDSVIRE
CCCHHHHHHHHHHHH
25.07-
266UbiquitinationVIRELLQKPNARVVV
HHHHHHCCCCCEEEE
39.96-
292N-linked_GlycosylationIAAASRANASFTWVA
HHHHHHCCCEEEEEE
34.70UniProtKB CARBOHYD
294PhosphorylationAASRANASFTWVASD
HHHHCCCEEEEEECC
24.0226853621
308PhosphorylationDGWGAQESIIKGSEH
CCCCCCCHHCCCCCC
19.9624719451
410PhosphorylationALHKMQRTLCPNTTK
HHHHHHHHHCCCHHH
18.8027174698
414N-linked_GlycosylationMQRTLCPNTTKLCDA
HHHHHCCCHHHHHHH
60.42UniProtKB CARBOHYD
415PhosphorylationQRTLCPNTTKLCDAM
HHHHCCCHHHHHHHH
15.5127174698
416PhosphorylationRTLCPNTTKLCDAMK
HHHCCCHHHHHHHHH
28.7627174698
439N-linked_GlycosylationKDYLLKINFTAPFNP
CEEEEEEEEECCCCC
26.99UniProtKB CARBOHYD
466PhosphorylationFGDGMGRYNVFNFQN
CCCCCCCEEEEEEEC
15.2222817900
478PhosphorylationFQNVGGKYSYLKVGH
EECCCCCEEEEEECC
13.0622817900
480PhosphorylationNVGGKYSYLKVGHWA
CCCCCEEEEEECCEE
13.8822817900
743PhosphorylationSMLISLTYDVILVIL
HHHHHHHHHHHHHHH
17.3217053785
754PhosphorylationLVILCTVYAFKTRKC
HHHHHHHHHHHCCCC
6.5417053785
758PhosphorylationCTVYAFKTRKCPENF
HHHHHHHCCCCCCCC
28.98-
810PhosphorylationMCISVSLSGFVVLGC
EEEEEECCCCHHEEH
23.7624719451
845DephosphorylationRLHLNRFSVSGTGTT
EEEECEEEEECCCCE
16.4914663150

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 GRM3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GRM3_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 GRM3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PPM1A_HUMANPPM1Aphysical
14663150
GRIP1_HUMANGRIP1physical
11891216
PICK1_HUMANPICK1physical
11891216
SDCB1_HUMANSDCBPphysical
11891216

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
D09008 Talaglumetad hydrochloride (USAN)
D09949 Pomaglumetad methionil (USAN/INN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GRM3_HUMAN

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Related Literatures of Post-Translational Modification

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