GRIK5_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GRIK5_RAT
• UniProt AC: Q63273
• Protein Name: Glutamate receptor ionotropic, kainate 5
• Gene Name: Grik5
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 979
• Subcellular Localization: Cell membrane; Multi-pass membrane protein. Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein.
• Protein Description: Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds kainate > quisqualate > glutamate >> AMPA..
• Protein Sequence: MPAELLLLLIVAFANPSCQVLSSLRMAAILDDQTVCGRGERLALALAREQINGIIEVPAKARVEVDIFELQRDSQYETTDTMCQILPKGVVSVLGPSSSPASASTVSHICGEKEIPHIKVGPEETPRLQYLRFASVSLYPSNEDVSLAVSRILKSFNYPSASLICAKAECLLRLEELVRGFLISKETLSVRMLDDSRDPTPLLKEIRDDKVSTIIIDANASISHLVLRKASELGMTSAFYKYILTTMDFPILHLDGIVEDSSNILGFSMFNTSHPFYPEFVRSLNMSWRENCEASTYPGPALSAALMFDAVHVVVSAVRELNRSQEIGVKPLACTSANIWPHGTSLMNYLRMVEYDGLTGRVEFNSKGQRTNYTLRILEKSRQGHREIGVWYSNRTLAMNATTLDINLSQTLANKTLVVTTILENPYVMRRPNFQALSGNERFEGFCVDMLRELAELLRFRYRLRLVEDGLYGAPEPNGSWTGMVGELINRKADLAVAAFTITAEREKVIDFSKPFMTLGISILYRVHMGRKPGYFSFLDPFSPAVWLFMLLAYLAVSCVLFLAARLSPYEWYNPHPCLRARPHILENQYTLGNSLWFPVGGFMQQGSEIMPRALSTRCVSGVWWAFTLIIISSYTANLAAFLTVQRMEVPVESADDLADQTNIEYGTIHAGSTMTFFQNSRYQTYQRMWNYMQSKQPSVFVKSTEEGIARVLNSRYAFLLESTMNEYHRRLNCNLTQIGGLLDTKGYGIGMPLGSPFRDEITLAILQLQENNRLEILKRKWWEGGRCPKEEDHRAKGLGMENIGGIFVVLICGLIIAVFVAVMEFIWSTRRSAESEEVSVCQEMLQELRHAVSCRKTSRSRRRRRPGGPSRALLSLRAVREMRLSNGKLYSAGAGGDAGAHGGPQRLLDDPGPPGGPRPQAPTPCTHVRVCQECRRIQALRASGAGAPPRGLGTPAEATSPPRPRPGPTGPRELTEHE

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
23	Phosphorylation	PSCQVLSSLRMAAIL CHHHHHHHHHHHHHC	18.81	21630457
219	N-linked_Glycosylation	STIIIDANASISHLV CEEEEECCCCHHHHH	30.39	20951142
271	N-linked_Glycosylation	ILGFSMFNTSHPFYP CCCEECCCCCCCCCH	31.84	20951142
285	N-linked_Glycosylation	PEFVRSLNMSWRENC HHHHHHCCCHHHHCC	24.56	20951142
322	N-linked_Glycosylation	VSAVRELNRSQEIGV HHHHHHHCCCCCCCC	36.48	20951142
372	N-linked_Glycosylation	NSKGQRTNYTLRILE CCCCCCCEEEEEEHH	29.95	20951142
394	N-linked_Glycosylation	EIGVWYSNRTLAMNA EEEEEECCCEEEECC	25.84	-
400	N-linked_Glycosylation	SNRTLAMNATTLDIN CCCEEEECCEEECEE	28.64	-
407	N-linked_Glycosylation	NATTLDINLSQTLAN CCEEECEEHHHHHCC	33.05	-
414	N-linked_Glycosylation	NLSQTLANKTLVVTT EHHHHHCCCEEEEEE	40.74	-
478	N-linked_Glycosylation	LYGAPEPNGSWTGMV CCCCCCCCCCCCHHH	56.31	-
735	N-linked_Glycosylation	YHRRLNCNLTQIGGL HHHHHCCCCCCCCCC	45.08	-
833	Phosphorylation	FIWSTRRSAESEEVS HHHHHCCCCCCHHHH	32.85	-
836	Phosphorylation	STRRSAESEEVSVCQ HHCCCCCCHHHHHHH	38.48	-
840	Phosphorylation	SAESEEVSVCQEMLQ CCCCHHHHHHHHHHH	22.06	-
859	Phosphorylation	AVSCRKTSRSRRRRR HHHCCCCCCCCCCCC	31.15	-
886	Phosphorylation	AVREMRLSNGKLYSA HHHHHHHHCCCEEEC	32.92	-
891	Phosphorylation	RLSNGKLYSAGAGGD HHHCCCEEECCCCCC	10.44	-
892	Phosphorylation	LSNGKLYSAGAGGDA HHCCCEEECCCCCCC	30.57	-
976	Phosphorylation	PTGPRELTEHE---- CCCCCCCCCCC----	30.46	-

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
859	S	Phosphorylation	Kinase	CAMK2A	P11275	PSP
892	S	Phosphorylation	Kinase	CAMK2A	P11275	PSP
976	T	Phosphorylation	Kinase	CAMK2A	P11275	PSP

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of GRIK5_RAT !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of GRIK5_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of GRIK5_RAT !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.