dbPTM

GRM1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GRM1_HUMAN
UniProt AC	Q13255
Protein Name	Metabotropic glutamate receptor 1
Gene Name	GRM1
Organism	Homo sapiens (Human).
Sequence Length	1194
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	MVGLLLFFFPAIFLEVSLLPRSPGRKVLLAGASSQRSVARMDGDVIIGALFSVHHQPPAEKVPERKCGEIREQYGIQRVEAMFHTLDKINADPVLLPNITLGSEIRDSCWHSSVALEQSIEFIRDSLISIRDEKDGINRCLPDGQSLPPGRTKKPIAGVIGPGSSSVAIQVQNLLQLFDIPQIAYSATSIDLSDKTLYKYFLRVVPSDTLQARAMLDIVKRYNWTYVSAVHTEGNYGESGMDAFKELAAQEGLCIAHSDKIYSNAGEKSFDRLLRKLRERLPKARVVVCFCEGMTVRGLLSAMRRLGVVGEFSLIGSDGWADRDEVIEGYEVEANGGITIKLQSPEVRSFDDYFLKLRLDTNTRNPWFPEFWQHRFQCRLPGHLLENPNFKRICTGNESLEENYVQDSKMGFVINAIYAMAHGLQNMHHALCPGHVGLCDAMKPIDGSKLLDFLIKSSFIGVSGEEVWFDEKGDAPGRYDIMNLQYTEANRYDYVHVGTWHEGVLNIDDYKIQMNKSGVVRSVCSEPCLKGQIKVIRKGEVSCCWICTACKENEYVQDEFTCKACDLGWWPNADLTGCEPIPVRYLEWSNIESIIAIAFSCLGILVTLFVTLIFVLYRDTPVVKSSSRELCYIILAGIFLGYVCPFTLIAKPTTTSCYLQRLLVGLSSAMCYSALVTKTNRIARILAGSKKKICTRKPRFMSAWAQVIIASILISVQLTLVVTLIIMEPPMPILSYPSIKEVYLICNTSNLGVVAPLGYNGLLIMSCTYYAFKTRNVPANFNEAKYIAFTMYTTCIIWLAFVPIYFGSNYKIITTCFAVSLSVTVALGCMFTPKMYIIIAKPERNVRSAFTTSDVVRMHVGDGKLPCRSNTFLNIFRRKKAGAGNANSNGKSVSWSEPGGGQVPKGQHMWHRLSVHVKTNETACNQTAVIKPLTKSYQGSGKSLTFSDTSTKTLYNVEEEEDAQPIRFSPPGSPSMVVHRRVPSAATTPPLPSHLTAEETPLFLAEPALPKGLPPPLQQQQQPPPQQKSLMDQLQGVVSNFSTAIPDFHAVLAGPGGPGNGLRSLYPPPPPPQHLQMLPLQLSTFGEELVSPPADDDDDSERFKLLQEYVYEHEREGNTEEDELEEEEEDLQAASKLTPDDSPALTPPSPFRDSVASGSSVPSSPVSESVLCTPPNVSYASVILRDYKQSSSTL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
74	Phosphorylation	CGEIREQYGIQRVEA HHHHHHHHCHHHHHH	16.08	26699800
98	N-linked_Glycosylation	ADPVLLPNITLGSEI CCCCCCCCCCCCHHH	39.59	UniProtKB CARBOHYD
103	Phosphorylation	LPNITLGSEIRDSCW CCCCCCCHHHHHHCC	32.72	21815630
126	Phosphorylation	SIEFIRDSLISIRDE HHHHHHHHHHHCCCC	20.11	27174698
129	Phosphorylation	FIRDSLISIRDEKDG HHHHHHHHCCCCCCC	19.50	27174698
188	Phosphorylation	PQIAYSATSIDLSDK CHHHCCCEECCCCCC	21.92	-
223	N-linked_Glycosylation	LDIVKRYNWTYVSAV HHHHHHCCCEEEEEE	28.75	UniProtKB CARBOHYD
263	Phosphorylation	AHSDKIYSNAGEKSF EECCCCCCCCCHHHH	24.55	23898821
339	Phosphorylation	VEANGGITIKLQSPE EEECCCEEEEECCCC	18.48	27050516
361	Phosphorylation	FLKLRLDTNTRNPWF EEEEEECCCCCCCCC	42.98	22985185
397	N-linked_Glycosylation	FKRICTGNESLEENY CCCCCCCCCCHHHHH	19.96	UniProtKB CARBOHYD
510	Phosphorylation	GVLNIDDYKIQMNKS CCCCCHHCEEEECCC	13.27	27273156
515	N-linked_Glycosylation	DDYKIQMNKSGVVRS HHCEEEECCCCCCEE	20.97	UniProtKB CARBOHYD
620	Phosphorylation	IFVLYRDTPVVKSSS HHHHHCCCHHHCCCH	14.69	-
632	Phosphorylation	SSSRELCYIILAGIF CCHHHHHHHHHHHHH	12.01	-
672	Phosphorylation	GLSSAMCYSALVTKT HHHHHHHHHHHHHHH	5.49	22817900
673	Phosphorylation	LSSAMCYSALVTKTN HHHHHHHHHHHHHHH	15.36	22461510
677	Phosphorylation	MCYSALVTKTNRIAR HHHHHHHHHHHHHHH	32.76	18187866
679	Phosphorylation	YSALVTKTNRIARIL HHHHHHHHHHHHHHH	21.99	18187866
695	Phosphorylation	GSKKKICTRKPRFMS CCCCCCCCCCHHHHH	45.24	10823959
740	Methylation	ILSYPSIKEVYLICN CCCCCCCCEEEEEEC	45.52	-
774	Phosphorylation	CTYYAFKTRNVPANF EEEEEECCCCCCCCC	22.48	26074081
786	Phosphorylation	ANFNEAKYIAFTMYT CCCCHHHHHHHHHHH	12.44	26074081
790	Phosphorylation	EAKYIAFTMYTTCII HHHHHHHHHHHHHHH	10.55	26074081
792	Phosphorylation	KYIAFTMYTTCIIWL HHHHHHHHHHHHHHH	8.88	26074081
793	Phosphorylation	YIAFTMYTTCIIWLA HHHHHHHHHHHHHHH	12.36	26074081
794	Phosphorylation	IAFTMYTTCIIWLAF HHHHHHHHHHHHHHH	5.57	26074081
853	Phosphorylation	VRSAFTTSDVVRMHV CCCCCCCCCEEEEEE	25.92	-
869	Phosphorylation	DGKLPCRSNTFLNIF CCCCCCCCCCHHHHH	47.11	-
871	Phosphorylation	KLPCRSNTFLNIFRR CCCCCCCCHHHHHHH	30.64	-
891	Ubiquitination	GNANSNGKSVSWSEP CCCCCCCCCCCCCCC	52.51	-
894	Phosphorylation	NSNGKSVSWSEPGGG CCCCCCCCCCCCCCC	31.79	-
969	Phosphorylation	DAQPIRFSPPGSPSM CCCCCCCCCCCCCCC	21.97	24076635
1091	Phosphorylation	TFGEELVSPPADDDD CCCCCCCCCCCCCCC	37.48	-
1109	Phosphorylation	RFKLLQEYVYEHERE HHHHHHHHHHHHHCC	8.72	17053785
1111	Phosphorylation	KLLQEYVYEHEREGN HHHHHHHHHHHCCCC	15.63	17053785
1142	Phosphorylation	SKLTPDDSPALTPPS HHCCCCCCCCCCCCC	21.32	-
1146	Phosphorylation	PDDSPALTPPSPFRD CCCCCCCCCCCCCCC	34.95	-
1149	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
627	S	Phosphorylation	Kinase	CAMK2-FAMILY	-	GPS
695	T	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
695	T	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GRM1_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 GRM1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GRM1_HUMAN	GRM1	physical	10945991
AA1R_HUMAN	ADORA1	physical	11278325
GRM1_HUMAN	GRM1	physical	10349865
OPTN_HUMAN	OPTN	physical	16091361
ARBK1_HUMAN	ADRBK1	physical	16091361
HD_HUMAN	HTT	physical	16091361
HOME1_HUMAN	HOMER1	physical	11418862
SRC_HUMAN	SRC	physical	15173175
FYN_HUMAN	FYN	physical	15173175
KSYK_HUMAN	SYK	physical	15173175

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614831	Spinocerebellar ataxia, autosomal recessive, 13 (SCAR13)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of GRM1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-672, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling."; Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.; EMBO J. 25:5058-5070(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1109 AND TYR-1111, ANDMASS SPECTROMETRY.	17053785 [Abstract]