dbPTM

GRASP_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GRASP_HUMAN
UniProt AC	Q7Z6J2
Protein Name	General receptor for phosphoinositides 1-associated scaffold protein
Gene Name	GRASP
Organism	Homo sapiens (Human).
Sequence Length	395
Subcellular Localization	Cytoplasm, perinuclear region. Cell membrane Peripheral membrane protein Cytoplasmic side. Cell junction, synapse, postsynaptic cell membrane. Localized at postsynaptic membranes..
Protein Description	Plays a role in intracellular trafficking and contributes to the macromolecular organization of group 1 metabotropic glutamate receptors (mGluRs) at synapses..
Protein Sequence	MTLRRLRKLQQKEEAAATPDPAARTPDSEVAPAAPVPTPGPPAAAATPGPPADELYAALEDYHPAELYRALAVSGGTLPRRKGSGFRWKNLSQSPEQQRKVLTLEKEDNQTFGFEIQTYGLHHREEQRVEMVTFVCRVHESSPAQLAGLTPGDTIASVNGLNVEGIRHREIVDIIKASGNVLRLETLYGTSIRKAELEARLQYLKQTLYEKWGEYRSLMVQEQRLVHGLVVKDPSIYDTLESVRSCLYGAGLLPGSLPFGPLLAVPGRPRGGARRARGDADDAVYHTCFFGDSEPPALPPPPPPARAFGPGPAETPAVGPGPGPRAALSRSASVRCAGPGGGGGGGAPGALWTEAREQALCGPGLRKTKYRSFRRRLLKFIPGLNRSLEEEESQL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2 (in isoform 2)	Phosphorylation	-	29.04	30206219
6 (in isoform 2)	Phosphorylation	-	4.59	30206219
11 (in isoform 2)	Phosphorylation	-	66.61	30206219
12	Ubiquitination	RLRKLQQKEEAAATP HHHHHHHHHHHHCCC	44.56	-
14 (in isoform 2)	Phosphorylation	-	51.12	30206219
18	Phosphorylation	QKEEAAATPDPAART HHHHHHCCCCCCCCC	24.41	23403867
74	Phosphorylation	LYRALAVSGGTLPRR HHHHHHHCCCCCCCC	26.37	29255136
77	Phosphorylation	ALAVSGGTLPRRKGS HHHHCCCCCCCCCCC	36.79	29255136
84	Phosphorylation	TLPRRKGSGFRWKNL CCCCCCCCCCCCCCC	37.48	-
92	Phosphorylation	GFRWKNLSQSPEQQR CCCCCCCCCCHHHHH	37.70	23403867
94	Phosphorylation	RWKNLSQSPEQQRKV CCCCCCCCHHHHHCE	27.33	29255136
186	Phosphorylation	GNVLRLETLYGTSIR CCEEEEEEECCCCCH	29.85	20393185
203	Phosphorylation	ELEARLQYLKQTLYE HHHHHHHHHHHHHHH	22.06	30622161
207	Phosphorylation	RLQYLKQTLYEKWGE HHHHHHHHHHHHHHH	29.71	30622161
209	Phosphorylation	QYLKQTLYEKWGEYR HHHHHHHHHHHHHHH	20.89	30622161
235	Phosphorylation	GLVVKDPSIYDTLES CEEECCCHHHHHHHH	43.87	23403867
237	Phosphorylation	VVKDPSIYDTLESVR EECCCHHHHHHHHHH	13.76	19605366
239	Phosphorylation	KDPSIYDTLESVRSC CCCHHHHHHHHHHHH	18.56	23403867
270	Methylation	LAVPGRPRGGARRAR EECCCCCCCCCCCCC	55.61	-
285	Phosphorylation	GDADDAVYHTCFFGD CCHHHCCEECCCCCC	7.98	27642862
315	Phosphorylation	FGPGPAETPAVGPGP CCCCCCCCCCCCCCC	20.75	23612710
329	Phosphorylation	PGPRAALSRSASVRC CCHHHHHHCCCCEEE	21.33	28857561
331	Phosphorylation	PRAALSRSASVRCAG HHHHHHCCCCEEECC	22.86	28857561
353	Phosphorylation	GAPGALWTEAREQAL CCCCCHHHHHHHHHH	22.18	28857561
387	Phosphorylation	FIPGLNRSLEEEESQ HCCCCCCCHHHHHHC	38.77	29507054

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 GRASP_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PSD1_HUMAN	PSD	physical	22569042
SRC_HUMAN	SRC	physical	15173175
PTN11_HUMAN	PTPN11	physical	15173175
GRM1_HUMAN	GRM1	physical	15173175
KSYK_HUMAN	SYK	physical	15173175

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

Regulatory Network of GRASP_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-237, AND MASSSPECTROMETRY.	19690332 [Abstract]