dbPTM

GRAP2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GRAP2_HUMAN
UniProt AC	O75791
Protein Name	GRB2-related adapter protein 2
Gene Name	GRAP2
Organism	Homo sapiens (Human).
Sequence Length	330
Subcellular Localization	Nucleus . Cytoplasm . Endosome .
Protein Description	Interacts with SLP-76 to regulate NF-AT activation. Binds to tyrosine-phosphorylated shc..
Protein Sequence	MEAVAKFDFTASGEDELSFHTGDVLKILSNQEEWFKAELGSQEGYVPKNFIDIQFPKWFHEGLSRHQAENLLMGKEVGFFIIRASQSSPGDFSISVRHEDDVQHFKVMRDNKGNYFLWTEKFPSLNKLVDYYRTNSISRQKQIFLRDRTREDQGHRGNSLDRRSQGGPHLSGAVGEEIRPSMNRKLSDHPPTLPLQQHQHQPQPPQYAPAPQQLQQPPQQRYLQHHHFHQERRGGSLDINDGHCGTGLGSEMNAALMHRRHTDPVQLQAAGRVRWARALYDFEALEDDELGFHSGEVVEVLDSSNPSWWTGRLHNKLGLFPANYVAPMTR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
36	Ubiquitination	SNQEEWFKAELGSQE CCCHHHHHHHHCCCC	41.86	-
41	Phosphorylation	WFKAELGSQEGYVPK HHHHHHCCCCCCCCC	37.37	29978859
45	Phosphorylation	ELGSQEGYVPKNFID HHCCCCCCCCCCEEE	16.90	15570572
48	Ubiquitination	SQEGYVPKNFIDIQF CCCCCCCCCEEEEEC	55.22	-
57	Ubiquitination	FIDIQFPKWFHEGLS EEEEECCHHHCCCHH	64.87	-
85	Phosphorylation	GFFIIRASQSSPGDF EEEEEEECCCCCCCE	22.27	23186163
87	Phosphorylation	FIIRASQSSPGDFSI EEEEECCCCCCCEEE	35.68	29978859
88	Phosphorylation	IIRASQSSPGDFSIS EEEECCCCCCCEEEE	25.84	23186163
93	Phosphorylation	QSSPGDFSISVRHED CCCCCCEEEEEECCC	20.77	23186163
95	Phosphorylation	SPGDFSISVRHEDDV CCCCEEEEEECCCCC	16.35	23186163
106	Acetylation	EDDVQHFKVMRDNKG CCCCCEEEEEECCCC	32.75	19608861
112	Ubiquitination	FKVMRDNKGNYFLWT EEEEECCCCCEEEEE	53.47	-
121	Ubiquitination	NYFLWTEKFPSLNKL CEEEEECCCCCHHHH	56.02	-
127	Ubiquitination	EKFPSLNKLVDYYRT CCCCCHHHHHHHHHH	56.00	-
131	Phosphorylation	SLNKLVDYYRTNSIS CHHHHHHHHHHCCHH	6.33	22798277
132	Phosphorylation	LNKLVDYYRTNSISR HHHHHHHHHHCCHHH	13.39	28509920
134	Phosphorylation	KLVDYYRTNSISRQK HHHHHHHHCCHHHCC	19.73	28509920
136	Phosphorylation	VDYYRTNSISRQKQI HHHHHHCCHHHCCEE	22.71	28509920
138	Phosphorylation	YYRTNSISRQKQIFL HHHHCCHHHCCEEEE	28.60	22798277
141	Ubiquitination	TNSISRQKQIFLRDR HCCHHHCCEEEECCC	44.22	-
159	Phosphorylation	DQGHRGNSLDRRSQG CCCCCCCCCCCHHCC	34.18	30576142
164	Phosphorylation	GNSLDRRSQGGPHLS CCCCCCHHCCCCCCC	33.79	28634120
171	Phosphorylation	SQGGPHLSGAVGEEI HCCCCCCCCCCCCCC	22.98	28111955
181	Phosphorylation	VGEEIRPSMNRKLSD CCCCCCHHHCCCCCC	20.88	-
187	Phosphorylation	PSMNRKLSDHPPTLP HHHCCCCCCCCCCCC	36.59	23401153
192	Phosphorylation	KLSDHPPTLPLQQHQ CCCCCCCCCCCCCCC	45.52	28796482
207	Phosphorylation	HQPQPPQYAPAPQQL CCCCCCCCCCCCHHH	21.96	28796482
222	Phosphorylation	QQPPQQRYLQHHHFH CCCCHHHHHHHHCCC	13.33	28796482
233	Methylation	HHFHQERRGGSLDIN HCCCCHHCCCCCCCC	53.74	-
236	Phosphorylation	HQERRGGSLDINDGH CCHHCCCCCCCCCCC	26.20	23401153
246	Phosphorylation	INDGHCGTGLGSEMN CCCCCCCCCCCHHHH	34.33	23401153
250	Phosphorylation	HCGTGLGSEMNAALM CCCCCCCHHHHHHHH	38.42	28464451
262	Phosphorylation	ALMHRRHTDPVQLQA HHHHCCCCCHHHHHH	39.94	23401153
324	Phosphorylation	LGLFPANYVAPMTR- CCCCCCHHCCCCCC-	10.49	23917254

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 GRAP2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GRAP2_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 GRAP2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GAB1_HUMAN	GAB1	physical	9878555
CCDB1_HUMAN	CCNDBP1	physical	10801854
ZBT7B_HUMAN	ZBTB7B	physical	16189514
BEND5_HUMAN	BEND5	physical	16189514
RBPMS_HUMAN	RBPMS	physical	16189514
KR412_HUMAN	KRTAP4-12	physical	16189514
STABP_HUMAN	STAMBP	physical	16189514
LCP2_HUMAN	LCP2	physical	10820259
SOS2_HUMAN	SOS2	physical	10820259
RACK1_HUMAN	GNB2L1	physical	10820259
KHDR1_HUMAN	KHDRBS1	physical	10820259
M4K1_HUMAN	MAP4K1	physical	11313918
M4K1_HUMAN	MAP4K1	genetic	11313918
CSF1R_HUMAN	CSF1R	physical	9857184
TNFL6_HUMAN	FASLG	physical	11741599
LAX1_HUMAN	LAX1	physical	12359715
LCP2_HUMAN	LCP2	physical	10021361
LAT_HUMAN	LAT	physical	10021361
LCP2_HUMAN	LCP2	physical	10224278
LAT_HUMAN	LAT	physical	10224278
UBP8_HUMAN	USP8	physical	12176364
GAB2_HUMAN	GAB2	physical	12176364
BLNK_HUMAN	BLNK	physical	12176364
LCP2_HUMAN	LCP2	physical	12176364
LCP2_HUMAN	LCP2	physical	12773374
LCP2_HUMAN	LCP2	physical	12496419
M4K1_HUMAN	MAP4K1	physical	12496419
CBL_HUMAN	CBL	physical	12496419
BLNK_HUMAN	BLNK	physical	12496419
LCP2_HUMAN	LCP2	physical	17235283
ERBB2_HUMAN	ERBB2	physical	16273093
SPY2_HUMAN	SPRY2	physical	25416956
GAB2_HUMAN	GAB2	physical	26186194
CDC27_HUMAN	CDC27	physical	26186194
STABP_HUMAN	STAMBP	physical	26186194
TNIP1_HUMAN	TNIP1	physical	26186194
ZSC21_HUMAN	ZSCAN21	physical	26186194
UBP8_HUMAN	USP8	physical	26186194
APC5_HUMAN	ANAPC5	physical	26186194
PTN23_HUMAN	PTPN23	physical	26186194
ITCH_HUMAN	ITCH	physical	26186194
GAB1_HUMAN	GAB1	physical	26186194
GARE1_HUMAN	GAREM	physical	26186194
TRI68_HUMAN	TRIM68	physical	26186194
SNX18_HUMAN	SNX18	physical	26186194
APC1_HUMAN	ANAPC1	physical	26186194
APC16_HUMAN	ANAPC16	physical	26186194
NAGK_HUMAN	NAGK	physical	26186194
CDC23_HUMAN	CDC23	physical	26186194
APC7_HUMAN	ANAPC7	physical	26186194
ANC2_HUMAN	ANAPC2	physical	26186194
GARE1_HUMAN	GAREM	physical	25814554
CBL_HUMAN	CBL	physical	25814554
CBLB_HUMAN	CBLB	physical	25814554
ABL1_HUMAN	ABL1	physical	9872323
CSF1R_HUMAN	CSF1R	physical	25241761
ERBB2_HUMAN	ERBB2	physical	25241761
UBP8_HUMAN	USP8	physical	28514442
GAB2_HUMAN	GAB2	physical	28514442
PTN23_HUMAN	PTPN23	physical	28514442
STABP_HUMAN	STAMBP	physical	28514442
GARE1_HUMAN	GAREM	physical	28514442
GAB1_HUMAN	GAB1	physical	28514442
ZSC21_HUMAN	ZSCAN21	physical	28514442
CDC27_HUMAN	CDC27	physical	28514442
TNIP1_HUMAN	TNIP1	physical	28514442
SNX18_HUMAN	SNX18	physical	28514442
TRI68_HUMAN	TRIM68	physical	28514442
ANC2_HUMAN	ANAPC2	physical	28514442
APC16_HUMAN	ANAPC16	physical	28514442
CDC23_HUMAN	CDC23	physical	28514442
ITCH_HUMAN	ITCH	physical	28514442
APC5_HUMAN	ANAPC5	physical	28514442

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 GRAP2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-106, AND MASS SPECTROMETRY.	19608861 [Abstract]
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-45 AND THR-262, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-262, AND MASSSPECTROMETRY.	18088087 [Abstract]
"Profiling of tyrosine phosphorylation pathways in human cells usingmass spectrometry."; Salomon A.R., Ficarro S.B., Brill L.M., Brinker A., Phung Q.T.,Ericson C., Sauer K., Brock A., Horn D.M., Schultz P.G., Peters E.C.; Proc. Natl. Acad. Sci. U.S.A. 100:443-448(2003). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-262, AND MASSSPECTROMETRY.	12522270 [Abstract]
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry."; Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.; Anal. Chem. 76:2763-2772(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-45, AND MASSSPECTROMETRY.	15144186 [Abstract]