GRIA3_HUMAN - dbPTM
GRIA3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GRIA3_HUMAN
UniProt AC P42263
Protein Name Glutamate receptor 3
Gene Name GRIA3
Organism Homo sapiens (Human).
Sequence Length 894
Subcellular Localization Cell membrane
Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane
Multi-pass membrane protein. Interaction with CNIH2 and CNIH3 promotes cell surface expression..
Protein Description Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. Binding of the excitatory neurotransmitter L-glutamate induces a conformation change, leading to the opening of the cation channel, and thereby converts the chemical signal to an electrical impulse. The receptor then desensitizes rapidly and enters a transient inactive state, characterized by the presence of bound agonist. In the presence of CACNG4 or CACNG7 or CACNG8, shows resensitization which is characterized by a delayed accumulation of current flux upon continued application of glutamate..
Protein Sequence MARQKKMGQSVLRAVFFLVLGLLGHSHGGFPNTISIGGLFMRNTVQEHSAFRFAVQLYNTNQNTTEKPFHLNYHVDHLDSSNSFSVTNAFCSQFSRGVYAIFGFYDQMSMNTLTSFCGALHTSFVTPSFPTDADVQFVIQMRPALKGAILSLLGHYKWEKFVYLYDTERGFSILQAIMEAAVQNNWQVTARSVGNIKDVQEFRRIIEEMDRRQEKRYLIDCEVERINTILEQVVILGKHSRGYHYMLANLGFTDILLERVMHGGANITGFQIVNNENPMVQQFIQRWVRLDEREFPEAKNAPLKYTSALTHDAILVIAEAFRYLRRQRVDVSRRGSAGDCLANPAVPWSQGIDIERALKMVQVQGMTGNIQFDTYGRRTNYTIDVYEMKVSGSRKAGYWNEYERFVPFSDQQISNDSASSENRTIVVTTILESPYVMYKKNHEQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGARDPETKIWNGMVGELVYGRADIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHLEDNNEEPRDPQSPPDPPNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKSAEPSVFTKTTADGVARVRKSKGKFAFLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSALRNAVNLAVLKLNEQGLLDKLKNKWWYDKGECGSGGGDSKDKTSALSLSNVAGVFYILVGGLGLAMMVALIEFCYKSRAESKRMKLTKNTQNFKPAPATNTQNYATYREGYNVYGTESVKI
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
63N-linked_GlycosylationQLYNTNQNTTEKPFH
EEECCCCCCCCCCEE		51.54UniProtKB CARBOHYD
151PhosphorylationALKGAILSLLGHYKW
HHHHHHHHHHCHHHH		18.5517322306
165PhosphorylationWEKFVYLYDTERGFS
HHEEEEEEECCCCHH		11.79-
238AcetylationEQVVILGKHSRGYHY
HHHHHHCCCCCCCHH		34.657662369
266N-linked_GlycosylationRVMHGGANITGFQIV
HHHCCCCCCEEEEEE		35.31UniProtKB CARBOHYD
380N-linked_GlycosylationDTYGRRTNYTIDVYE
ECCCCCCCEEEEEEE		30.09UniProtKB CARBOHYD
415N-linked_GlycosylationFSDQQISNDSASSEN
CCCCCCCCCCCCCCC		49.22UniProtKB CARBOHYD
422N-linked_GlycosylationNDSASSENRTIVVTT
CCCCCCCCCEEEEEE		48.63UniProtKB CARBOHYD
424PhosphorylationSASSENRTIVVTTIL
CCCCCCCEEEEEEEE		29.7023612710
428PhosphorylationENRTIVVTTILESPY
CCCEEEEEEEECCCE		9.3824719451
429PhosphorylationNRTIVVTTILESPYV
CCEEEEEEEECCCEE		16.3824719451
433PhosphorylationVVTTILESPYVMYKK
EEEEEECCCEEEEEC		20.34-
435PhosphorylationTTILESPYVMYKKNH
EEEECCCEEEEECCH		13.7123612710
438PhosphorylationLESPYVMYKKNHEQL
ECCCEEEEECCHHHH		14.5723612710
451PhosphorylationQLEGNERYEGYCVDL
HHCCCCCCCCCHHHH		13.9218083107
460PhosphorylationGYCVDLAYEIAKHVR
CCHHHHHHHHHHHCC		18.3722817900
499PhosphorylationGMVGELVYGRADIAV
CCCCHHHHCCCCEEE		17.3322817900
522PhosphorylationREEVIDFSKPFMSLG
EHHHHCCCCCCHHCC		35.35-
527PhosphorylationDFSKPFMSLGISIMI
CCCCCCHHCCEEEEE		24.6724719451
531PhosphorylationPFMSLGISIMIKKPQ
CCHHCCEEEEEECCC		12.3320860994
567PhosphorylationVFAYIGVSVVLFLVS
HHHHHHHHHHHHHHH		10.9922210691
621S-palmitoylationGAFMQQGCDISPRSL
HHHHHCCCCCCCCCC		3.50-
663PhosphorylationLTVERMVSPIESAED
HCHHHCCCCCCCHHH		15.717877986
694PhosphorylationTKEFFRRSKIAVYEK
CHHHHHHHHHHHHHH		24.9426074081
699PhosphorylationRRSKIAVYEKMWSYM
HHHHHHHHHHHHHHH		10.7926074081
704PhosphorylationAVYEKMWSYMKSAEP
HHHHHHHHHHHHCCC		16.3226074081
705PhosphorylationVYEKMWSYMKSAEPS
HHHHHHHHHHHCCCC		7.9526074081
708PhosphorylationKMWSYMKSAEPSVFT
HHHHHHHHCCCCCCE		22.7226074081
712PhosphorylationYMKSAEPSVFTKTTA
HHHHCCCCCCEEECC		22.7426074081
715PhosphorylationSAEPSVFTKTTADGV
HCCCCCCEEECCCHH		25.8926074081
728PhosphorylationGVARVRKSKGKFAFL
HHHHHHHCCCCEEEE		35.76-
761PhosphorylationKVGGNLDSKGYGVAT
EECCCCCCCCCCCCC		31.0122210691
820PhosphorylationKDKTSALSLSNVAGV
CCCCCCHHHHHHHHH		29.4822210691
829PhosphorylationSNVAGVFYILVGGLG
HHHHHHHHHHHCHHH		7.3122210691
847S-palmitoylationMVALIEFCYKSRAES
HHHHHHHHHHHHHHH		2.44-
877PhosphorylationPATNTQNYATYREGY
CCCCCCCCEEECCCC		7.1819658100
884PhosphorylationYATYREGYNVYGTES
CEEECCCCCEECCCC		9.1927196784
887PhosphorylationYREGYNVYGTESVKI
ECCCCCEECCCCCCC		18.0727196784
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 GRIA3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
621CPalmitoylation

-
847CPalmitoylation

-
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 GRIA3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PICK1_HUMANPICK1physical
11891216
GRIP1_HUMANGRIP1physical
11891216
SDCB1_HUMANSDCBPphysical
11891216
GRIA4_HUMANGRIA4physical
28514442
GLRB_HUMANGLRBphysical
28514442
CCPG1_HUMANCCPG1physical
28514442
CLH2_HUMANCLTCL1physical
28514442
DNJB9_HUMANDNAJB9physical
28514442
GLBL2_HUMANGLB1L2physical
28514442
SEM4F_HUMANSEMA4Fphysical
28514442
FA69A_HUMANFAM69Aphysical
28514442
ALG9_HUMANALG9physical
28514442
TMPPE_HUMANTMPPEphysical
28514442
LMF2_HUMANLMF2physical
28514442
MAP2_HUMANMETAP2physical
28514442
HLAF_HUMANHLA-Fphysical
28514442
E2AK3_HUMANEIF2AK3physical
28514442
Drug and Disease Associations
Kegg Disease
H00577 Syndromic X-linked mental retardation with epilepsy or seizures, including: West syndrome (WS); Part
OMIM Disease
300699Mental retardation, X-linked 94 (MRX94)
Kegg Drug
D00537 Topiramate (JAN/USAN/INN); Topamax (TN); Trokendi xr (TN)
D02696 Talampanel (INN)
D04131 Farampator (USAN/INN); Org 24448
D06656 Tezampanel (USAN); Tezampanel hydrate
D08964 Perampanel (USAN); Fycompa (TN)
D09035 Zonampanel (INN/USAN)
D09931 Mibampator (USAN/INN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GRIA3_HUMAN

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Related Literatures of Post-Translational Modification

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