GRM5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GRM5_HUMAN
• UniProt AC: P41594
• Protein Name: Metabotropic glutamate receptor 5
• Gene Name: GRM5
• Organism: Homo sapiens (Human).
• Sequence Length: 1212
• 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 activates a phosphatidylinositol-calcium second messenger system and generates a calcium-activated chloride current. Plays an important role in the regulation of synaptic plasticity and the modulation of the neural network activity..
• Protein Sequence: MVLLLILSVLLLKEDVRGSAQSSERRVVAHMPGDIIIGALFSVHHQPTVDKVHERKCGAVREQYGIQRVEAMLHTLERINSDPTLLPNITLGCEIRDSCWHSAVALEQSIEFIRDSLISSEEEEGLVRCVDGSSSSFRSKKPIVGVIGPGSSSVAIQVQNLLQLFNIPQIAYSATSMDLSDKTLFKYFMRVVPSDAQQARAMVDIVKRYNWTYVSAVHTEGNYGESGMEAFKDMSAKEGICIAHSYKIYSNAGEQSFDKLLKKLTSHLPKARVVACFCEGMTVRGLLMAMRRLGLAGEFLLLGSDGWADRYDVTDGYQREAVGGITIKLQSPDVKWFDDYYLKLRPETNHRNPWFQEFWQHRFQCRLEGFPQENSKYNKTCNSSLTLKTHHVQDSKMGFVINAIYSMAYGLHNMQMSLCPGYAGLCDAMKPIDGRKLLESLMKTNFTGVSGDTILFDENGDSPGRYEIMNFKEMGKDYFDYINVGSWDNGELKMDDDEVWSKKSNIIRSVCSEPCEKGQIKVIRKGEVSCCWTCTPCKENEYVFDEYTCKACQLGSWPTDDLTGCDLIPVQYLRWGDPEPIAAVVFACLGLLATLFVTVVFIIYRDTPVVKSSSRELCYIILAGICLGYLCTFCLIAKPKQIYCYLQRIGIGLSPAMSYSALVTKTNRIARILAGSKKKICTKKPRFMSACAQLVIAFILICIQLGIIVALFIMEPPDIMHDYPSIREVYLICNTTNLGVVTPLGYNGLLILSCTFYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNYKIITMCFSVSLSATVALGCMFVPKVYIILAKPERNVRSAFTTSTVVRMHVGDGKSSSAASRSSSLVNLWKRRGSSGETLRYKDRRLAQHKSEIECFTPKGSMGNGGRATMSSSNGKSVTWAQNEKSSRGQHLWQRLSIHINKKENPNQTAVIKPFPKSTESRGLGAGAGAGGSAGGVGATGGAGCAGAGPGGPESPDAGPKALYDVAEAEEHFPAPARPRSPSPISTLSHRAGSASRTDDDVPSLHSEPVARSSSSQGSLMEQISSVVTRFTANISELNSMMLSTAAPSPGVGAPLCSSYLIPKEIQLPTTMTTFAEIQPLPAIEVTGGAQPAAGAQAAGDAARESPAAGPEAAAAKPDLEELVALTPPSPFRDSVDSGSTTPNSPVSESALCIPSSPKYDTLIIRDYTQSSSSL

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
8	Phosphorylation	MVLLLILSVLLLKED CHHHHHHHHHHHHCC	12.06	-
23	Phosphorylation	VRGSAQSSERRVVAH CCCCCCCCCCHHHEE	24.04	-
88	N-linked_Glycosylation	SDPTLLPNITLGCEI CCCCCCCCCEECCEE	39.59	UniProtKB CARBOHYD
98	Phosphorylation	LGCEIRDSCWHSAVA ECCEECCCHHHHHHH	14.84	-
119	Phosphorylation	FIRDSLISSEEEEGL HHHHHCCCCCHHCCC	36.67	26699800
120	Phosphorylation	IRDSLISSEEEEGLV HHHHCCCCCHHCCCE	41.87	26699800
136	Phosphorylation	CVDGSSSSFRSKKPI ECCCCCCCCCCCCCE	26.99	22210691
183	Phosphorylation	SMDLSDKTLFKYFMR CCCCCHHHHHHHHHH	42.28	24275569
210	N-linked_Glycosylation	VDIVKRYNWTYVSAV HHHHHHCCCEEEEEE	28.75	UniProtKB CARBOHYD
250	Phosphorylation	AHSYKIYSNAGEQSF EEEEEECCCCCHHHH	24.55	-
256	Phosphorylation	YSNAGEQSFDKLLKK CCCCCHHHHHHHHHH	30.98	-
259	Ubiquitination	AGEQSFDKLLKKLTS CCHHHHHHHHHHHHH	54.42	-
266	Phosphorylation	KLLKKLTSHLPKARV HHHHHHHHCCCCHHH	33.20	-
282	Phosphorylation	ACFCEGMTVRGLLMA EHHCCCCCHHHHHHH	20.22	29052541
378	N-linked_Glycosylation	PQENSKYNKTCNSSL CCCCCCCCCCCCCCE	36.58	UniProtKB CARBOHYD
382	N-linked_Glycosylation	SKYNKTCNSSLTLKT CCCCCCCCCCEEEEE	39.61	UniProtKB CARBOHYD
384	Phosphorylation	YNKTCNSSLTLKTHH CCCCCCCCEEEEEEC	16.04	24719451
445	N-linked_Glycosylation	LESLMKTNFTGVSGD HHHHHHCCCCCCCCC	27.28	UniProtKB CARBOHYD
607	Phosphorylation	VFIIYRDTPVVKSSS HHHHHCCCCCCCCCH	14.69	-
619	Phosphorylation	SSSRELCYIILAGIC CCHHHHHHHHHHHHH	12.01	-
654	Phosphorylation	QRIGIGLSPAMSYSA HHHCCCCCCCCCHHH	12.85	-
664	Phosphorylation	MSYSALVTKTNRIAR CCHHHHHHCHHHHHH	32.76	22817900
666	Phosphorylation	YSALVTKTNRIARIL HHHHHHCHHHHHHHH	21.99	22817900
734	N-linked_Glycosylation	REVYLICNTTNLGVV CEEEEEECCCCCCCC	42.83	UniProtKB CARBOHYD
761	Phosphorylation	CTFYAFKTRNVPANF EEEEEECCCCCCCCC	22.48	26074081
773	Phosphorylation	ANFNEAKYIAFTMYT CCCCHHHHHHHHHHH	12.44	26074081
777	Phosphorylation	EAKYIAFTMYTTCII HHHHHHHHHHHHHHH	10.55	26074081
779	Phosphorylation	KYIAFTMYTTCIIWL HHHHHHHHHHHHHHH	8.88	26074081
780	Phosphorylation	YIAFTMYTTCIIWLA HHHHHHHHHHHHHHH	12.36	26074081
781	Phosphorylation	IAFTMYTTCIIWLAF HHHHHHHHHHHHHHH	5.57	26074081
828	Acetylation	KVYIILAKPERNVRS EEEEEEECCCCCHHH	43.92	7697057
840	Phosphorylation	VRSAFTTSTVVRMHV HHHCCEECEEEEEEE	19.02	15894802
841	Phosphorylation	RSAFTTSTVVRMHVG HHCCEECEEEEEEEC	22.41	9242710
861	Phosphorylation	SAASRSSSLVNLWKR CCHHHCHHHHHHHHH	37.27	25332170
869	Methylation	LVNLWKRRGSSGETL HHHHHHHCCCCCCHH	45.69	-
888	Phosphorylation	RRLAQHKSEIECFTP HHHHHCCCEEEEECC	41.50	-
894	Phosphorylation	KSEIECFTPKGSMGN CCEEEEECCCCCCCC	35.43	30576142
925	Methylation	AQNEKSSRGQHLWQR ECCCCCCCHHHHHHH	56.75	-
955	Phosphorylation	VIKPFPKSTESRGLG EEECCCCCCCCCCCC	37.33	28857561
956	Phosphorylation	IKPFPKSTESRGLGA EECCCCCCCCCCCCC	44.07	23532336
958	Phosphorylation	PFPKSTESRGLGAGA CCCCCCCCCCCCCCC	31.56	24275569
970	Phosphorylation	AGAGAGGSAGGVGAT CCCCCCCCCCCCCCC	23.87	24275569
977	Phosphorylation	SAGGVGATGGAGCAG CCCCCCCCCCCCCCC	30.16	28857561
992	Phosphorylation	AGPGGPESPDAGPKA CCCCCCCCCCCCHHH	31.08	23532336
1001	Phosphorylation	DAGPKALYDVAEAEE CCCHHHHHHHHHHHH	17.15	-
1018	Phosphorylation	PAPARPRSPSPISTL CCCCCCCCCCCCCCC	32.20	25332170
1020	Phosphorylation	PARPRSPSPISTLSH CCCCCCCCCCCCCCC	35.79	20886841
1031	Phosphorylation	TLSHRAGSASRTDDD CCCCCCCCCCCCCCC	23.30	25954137
1033	Phosphorylation	SHRAGSASRTDDDVP CCCCCCCCCCCCCCC	37.09	25954137
1041	Phosphorylation	RTDDDVPSLHSEPVA CCCCCCCCCCCCCCC	38.26	25954137
1044	Phosphorylation	DDVPSLHSEPVARSS CCCCCCCCCCCCCCC	49.22	25307156
1050	O-linked_Glycosylation	HSEPVARSSSSQGSL CCCCCCCCCCCCCCH	25.49	28657654
1051	Phosphorylation	SEPVARSSSSQGSLM CCCCCCCCCCCCCHH	28.58	25954137
1051	O-linked_Glycosylation	SEPVARSSSSQGSLM CCCCCCCCCCCCCHH	28.58	28657654
1052	Phosphorylation	EPVARSSSSQGSLME CCCCCCCCCCCCHHH	28.11	24076635
1053	Phosphorylation	PVARSSSSQGSLMEQ CCCCCCCCCCCHHHH	40.27	25954137
1056	Phosphorylation	RSSSSQGSLMEQISS CCCCCCCCHHHHHHH	19.53	25954137
1062	Phosphorylation	GSLMEQISSVVTRFT CCHHHHHHHHHHHHH	19.44	25954137
1066	Phosphorylation	EQISSVVTRFTANIS HHHHHHHHHHHHCHH	20.22	25954137
1143	Phosphorylation	AGDAARESPAAGPEA HHHHHHHCCCCCHHH	17.81	24076635
1164	Phosphorylation	LEELVALTPPSPFRD HHHHHCCCCCCCCCC	24.34	24076635
1172	Phosphorylation	PPSPFRDSVDSGSTT CCCCCCCCCCCCCCC	24.46	28270605
1175	Phosphorylation	PFRDSVDSGSTTPNS CCCCCCCCCCCCCCC	32.27	28270605
1177	Phosphorylation	RDSVDSGSTTPNSPV CCCCCCCCCCCCCCC	32.81	28270605
1178	Phosphorylation	DSVDSGSTTPNSPVS CCCCCCCCCCCCCCC	50.20	28270605
1179	Phosphorylation	SVDSGSTTPNSPVSE CCCCCCCCCCCCCCC	23.36	28270605
1182	Phosphorylation	SGSTTPNSPVSESAL CCCCCCCCCCCCCCE	28.07	28270605
1185	Phosphorylation	TTPNSPVSESALCIP CCCCCCCCCCCEECC	29.26	28270605
1187	Phosphorylation	PNSPVSESALCIPSS CCCCCCCCCEECCCC	21.02	28270605
1193	Phosphorylation	ESALCIPSSPKYDTL CCCEECCCCCCCCEE	39.08	28270605
1194	Phosphorylation	SALCIPSSPKYDTLI CCEECCCCCCCCEEE	21.76	24076635
1211	Phosphorylation	DYTQSSSSL------ ECCCCCCCC------	39.79	25332170

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
-	K	Ubiquitination	E3 ubiquitin ligase	SIAH1	Q8IUQ4	PMID:22199232

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of GRM5_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of GRM5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SIAH1_HUMAN	SIAH1	physical	23152621
HOME1_HUMAN	HOMER1	physical	11418862

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
• D04155: Fenobam (USAN)
• DrugBank
• There are no disease associations of PTM sites.