dbPTM

GRM1_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GRM1_RAT
UniProt AC	P23385
Protein Name	Metabotropic glutamate receptor 1
Gene Name	Grm1
Organism	Rattus norvegicus (Rat).
Sequence Length	1199
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. May participate in the central action of glutamate in the CNS, such as long-term potentiation in the hippocampus and long-term depression in the cerebellum..
Protein Sequence	MVRLLLIFFPMIFLEMSILPRMPDRKVLLAGASSQRSVARMDGDVIIGALFSVHHQPPAEKVPERKCGEIREQYGIQRVEAMFHTLDKINADPVLLPNITLGSEIRDSCWHSSVALEQSIEFIRDSLISIRDEKDGLNRCLPDGQTLPPGRTKKPIAGVIGPGSSSVAIQVQNLLQLFDIPQIAYSATSIDLSDKTLYKYFLRVVPSDTLQARAMLDIVKRYNWTYVSAVHTEGNYGESGMDAFKELAAQEGLCIAHSDKIYSNAGEKSFDRLLRKLRERLPKARVVVCFCEGMTVRGLLSAMRRLGVVGEFSLIGSDGWADRDEVIEGYEVEANGGITIKLQSPEVRSFDDYFLKLRLDTNTRNPWFPEFWQHRFQCRLPGHLLENPNFKKVCTGNESLEENYVQDSKMGFVINAIYAMAHGLQNMHHALCPGHVGLCDAMKPIDGRKLLDFLIKSSFVGVSGEEVWFDEKGDAPGRYDIMNLQYTEANRYDYVHVGTWHEGVLNIDDYKIQMNKSGMVRSVCSEPCLKGQIKVIRKGEVSCCWICTACKENEFVQDEFTCRACDLGWWPNAELTGCEPIPVRYLEWSDIESIIAIAFSCLGILVTLFVTLIFVLYRDTPVVKSSSRELCYIILAGIFLGYVCPFTLIAKPTTTSCYLQRLLVGLSSAMCYSALVTKTNRIARILAGSKKKICTRKPRFMSAWAQVIIASILISVQLTLVVTLIIMEPPMPILSYPSIKEVYLICNTSNLGVVAPVGYNGLLIMSCTYYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNYKIITTCFAVSLSVTVALGCMFTPKMYIIIAKPERNVRSAFTTSDVVRMHVGDGKLPCRSNTFLNIFRRKKPGAGNANSNGKSVSWSEPGGRQAPKGQHVWQRLSVHVKTNETACNQTAVIKPLTKSYQGSGKSLTFSDASTKTLYNVEEEDNTPSAHFSPPSSPSMVVHRRGPPVATTPPLPPHLTAEETPLFLADSVIPKGLPPPLPQQQPQQPPPQQPPQQPKSLMDQLQGVVTNFGSGIPDFHAVLAGPGTPGNSLRSLYPPPPPPQHLQMLPLHLSTFQEESISPPGEDIDDDSERFKLLQEFVYEREGNTEEDELEEEEDLPTASKLTPEDSPALTPPSPFRDSVASGSSVPSSPVSESVLCTPPNVTYASVILRDYKQSSSTL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
33	Phosphorylation	KVLLAGASSQRSVAR CEEEECCCCCHHHHC	26.53	23984901
34	Phosphorylation	VLLAGASSQRSVARM EEEECCCCCHHHHCC	29.13	23984901
98	N-linked_Glycosylation	ADPVLLPNITLGSEI CCCCCCCCCCCCHHH	39.59	11069170
223	N-linked_Glycosylation	LDIVKRYNWTYVSAV HHHHHHCCCEEEEEE	28.75	11069170
397	N-linked_Glycosylation	FKKVCTGNESLEENY CCCCCCCCCCHHHHH	19.96	-
515	N-linked_Glycosylation	DDYKIQMNKSGMVRS HHCEEEECCCCCCEE	20.97	-
695	Phosphorylation	GSKKKICTRKPRFMS CCCCCCCCCCHHHHH	45.24	10823959
853	Phosphorylation	VRSAFTTSDVVRMHV HHCCCCCCCEEEEEE	25.92	-
871	Phosphorylation	KLPCRSNTFLNIFRR CCCCCCCCHHHEECC	30.64	25403869
892	Phosphorylation	NANSNGKSVSWSEPG CCCCCCCCCCCCCCC	23.84	27097102
894	Phosphorylation	NSNGKSVSWSEPGGR CCCCCCCCCCCCCCC	31.79	27097102
914	Phosphorylation	QHVWQRLSVHVKTNE CCCEEEEEEEEECCC	16.62	25403869
942	Ubiquitination	KSYQGSGKSLTFSDA CCCCCCCCCEECCCC	43.95	-
963	Phosphorylation	NVEEEDNTPSAHFSP EECCCCCCCCCCCCC	30.83	22673903
965	Phosphorylation	EEEDNTPSAHFSPPS CCCCCCCCCCCCCCC	32.13	22673903
969	Phosphorylation	NTPSAHFSPPSSPSM CCCCCCCCCCCCCCC	26.49	22673903
972	Phosphorylation	SAHFSPPSSPSMVVH CCCCCCCCCCCCEEE	59.26	22673903
973	Phosphorylation	AHFSPPSSPSMVVHR CCCCCCCCCCCEEEC	27.11	22673903
975	Phosphorylation	FSPPSSPSMVVHRRG CCCCCCCCCEEECCC	26.59	22673903
1098	Phosphorylation	TFQEESISPPGEDID HCCCCCCCCCCCCCC	34.03	-
1138	Phosphorylation	EEEEDLPTASKLTPE HHCCCCCCCCCCCCC	51.35	22673903
1140	Phosphorylation	EEDLPTASKLTPEDS CCCCCCCCCCCCCCC	30.58	22673903
1143	Phosphorylation	LPTASKLTPEDSPAL CCCCCCCCCCCCCCC	28.50	22673903
1147	Phosphorylation	SKLTPEDSPALTPPS CCCCCCCCCCCCCCC	15.48	22673903
1151	Phosphorylation	PEDSPALTPPSPFRD CCCCCCCCCCCCCCC	34.95	22673903
1154	Phosphorylation	SPALTPPSPFRDSVA CCCCCCCCCCCCCCC	37.56	-

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
695	T	Phosphorylation	Kinase	PRKCA	P05696	GPS
871	T	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
871	T	Phosphorylation	Kinase	CAMK2A	P11275	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GRM1_RAT !!

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 GRM1_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
SIAH1_RAT	Siah1	physical	10469171

Drug and Disease Associations

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

Regulatory Network of GRM1_RAT

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Structural basis of glutamate recognition by a dimeric metabotropicglutamate receptor."; Kunishima N., Shimada Y., Tsuji Y., Sato T., Yamamoto M., Kumasaka T.,Nakanishi S., Jingami H., Morikawa K.; Nature 407:971-977(2000). Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 33-522 ALONE AND IN COMPLEXWITH GLUTAMATE, SUBUNIT, GLYCOSYLATION AT ASN-98 AND ASN-223,GLUTAMATE-BINDING SITES, AND DISULFIDE BONDS.	11069170 [Abstract]