GRAP2_HUMAN - dbPTM
GRAP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
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 Orthologous
Protein Cluster
36UbiquitinationSNQEEWFKAELGSQE
CCCHHHHHHHHCCCC
41.86-
41PhosphorylationWFKAELGSQEGYVPK
HHHHHHCCCCCCCCC
37.3729978859
45PhosphorylationELGSQEGYVPKNFID
HHCCCCCCCCCCEEE
16.9015570572
48UbiquitinationSQEGYVPKNFIDIQF
CCCCCCCCCEEEEEC
55.22-
57UbiquitinationFIDIQFPKWFHEGLS
EEEEECCHHHCCCHH
64.87-
85PhosphorylationGFFIIRASQSSPGDF
EEEEEEECCCCCCCE
22.2723186163
87PhosphorylationFIIRASQSSPGDFSI
EEEEECCCCCCCEEE
35.6829978859
88PhosphorylationIIRASQSSPGDFSIS
EEEECCCCCCCEEEE
25.8423186163
93PhosphorylationQSSPGDFSISVRHED
CCCCCCEEEEEECCC
20.7723186163
95PhosphorylationSPGDFSISVRHEDDV
CCCCEEEEEECCCCC
16.3523186163
106AcetylationEDDVQHFKVMRDNKG
CCCCCEEEEEECCCC
32.7519608861
112UbiquitinationFKVMRDNKGNYFLWT
EEEEECCCCCEEEEE
53.47-
121UbiquitinationNYFLWTEKFPSLNKL
CEEEEECCCCCHHHH
56.02-
127UbiquitinationEKFPSLNKLVDYYRT
CCCCCHHHHHHHHHH
56.00-
131PhosphorylationSLNKLVDYYRTNSIS
CHHHHHHHHHHCCHH
6.3322798277
132PhosphorylationLNKLVDYYRTNSISR
HHHHHHHHHHCCHHH
13.3928509920
134PhosphorylationKLVDYYRTNSISRQK
HHHHHHHHCCHHHCC
19.7328509920
136PhosphorylationVDYYRTNSISRQKQI
HHHHHHCCHHHCCEE
22.7128509920
138PhosphorylationYYRTNSISRQKQIFL
HHHHCCHHHCCEEEE
28.6022798277
141UbiquitinationTNSISRQKQIFLRDR
HCCHHHCCEEEECCC
44.22-
159PhosphorylationDQGHRGNSLDRRSQG
CCCCCCCCCCCHHCC
34.1830576142
164PhosphorylationGNSLDRRSQGGPHLS
CCCCCCHHCCCCCCC
33.7928634120
171PhosphorylationSQGGPHLSGAVGEEI
HCCCCCCCCCCCCCC
22.9828111955
181PhosphorylationVGEEIRPSMNRKLSD
CCCCCCHHHCCCCCC
20.88-
187PhosphorylationPSMNRKLSDHPPTLP
HHHCCCCCCCCCCCC
36.5923401153
192PhosphorylationKLSDHPPTLPLQQHQ
CCCCCCCCCCCCCCC
45.5228796482
207PhosphorylationHQPQPPQYAPAPQQL
CCCCCCCCCCCCHHH
21.9628796482
222PhosphorylationQQPPQQRYLQHHHFH
CCCCHHHHHHHHCCC
13.3328796482
233MethylationHHFHQERRGGSLDIN
HCCCCHHCCCCCCCC
53.74-
236PhosphorylationHQERRGGSLDINDGH
CCHHCCCCCCCCCCC
26.2023401153
246PhosphorylationINDGHCGTGLGSEMN
CCCCCCCCCCCHHHH
34.3323401153
250PhosphorylationHCGTGLGSEMNAALM
CCCCCCCHHHHHHHH
38.4228464451
262PhosphorylationALMHRRHTDPVQLQA
HHHHCCCCCHHHHHH
39.9423401153
324PhosphorylationLGLFPANYVAPMTR-
CCCCCCHHCCCCCC-
10.4923917254

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 Domain-Domain Interactions
GAB1_HUMANGAB1physical
9878555
CCDB1_HUMANCCNDBP1physical
10801854
ZBT7B_HUMANZBTB7Bphysical
16189514
BEND5_HUMANBEND5physical
16189514
RBPMS_HUMANRBPMSphysical
16189514
KR412_HUMANKRTAP4-12physical
16189514
STABP_HUMANSTAMBPphysical
16189514
LCP2_HUMANLCP2physical
10820259
SOS2_HUMANSOS2physical
10820259
RACK1_HUMANGNB2L1physical
10820259
KHDR1_HUMANKHDRBS1physical
10820259
M4K1_HUMANMAP4K1physical
11313918
M4K1_HUMANMAP4K1genetic
11313918
CSF1R_HUMANCSF1Rphysical
9857184
TNFL6_HUMANFASLGphysical
11741599
LAX1_HUMANLAX1physical
12359715
LCP2_HUMANLCP2physical
10021361
LAT_HUMANLATphysical
10021361
LCP2_HUMANLCP2physical
10224278
LAT_HUMANLATphysical
10224278
UBP8_HUMANUSP8physical
12176364
GAB2_HUMANGAB2physical
12176364
BLNK_HUMANBLNKphysical
12176364
LCP2_HUMANLCP2physical
12176364
LCP2_HUMANLCP2physical
12773374
LCP2_HUMANLCP2physical
12496419
M4K1_HUMANMAP4K1physical
12496419
CBL_HUMANCBLphysical
12496419
BLNK_HUMANBLNKphysical
12496419
LCP2_HUMANLCP2physical
17235283
ERBB2_HUMANERBB2physical
16273093
SPY2_HUMANSPRY2physical
25416956
GAB2_HUMANGAB2physical
26186194
CDC27_HUMANCDC27physical
26186194
STABP_HUMANSTAMBPphysical
26186194
TNIP1_HUMANTNIP1physical
26186194
ZSC21_HUMANZSCAN21physical
26186194
UBP8_HUMANUSP8physical
26186194
APC5_HUMANANAPC5physical
26186194
PTN23_HUMANPTPN23physical
26186194
ITCH_HUMANITCHphysical
26186194
GAB1_HUMANGAB1physical
26186194
GARE1_HUMANGAREMphysical
26186194
TRI68_HUMANTRIM68physical
26186194
SNX18_HUMANSNX18physical
26186194
APC1_HUMANANAPC1physical
26186194
APC16_HUMANANAPC16physical
26186194
NAGK_HUMANNAGKphysical
26186194
CDC23_HUMANCDC23physical
26186194
APC7_HUMANANAPC7physical
26186194
ANC2_HUMANANAPC2physical
26186194
GARE1_HUMANGAREMphysical
25814554
CBL_HUMANCBLphysical
25814554
CBLB_HUMANCBLBphysical
25814554
ABL1_HUMANABL1physical
9872323
CSF1R_HUMANCSF1Rphysical
25241761
ERBB2_HUMANERBB2physical
25241761
UBP8_HUMANUSP8physical
28514442
GAB2_HUMANGAB2physical
28514442
PTN23_HUMANPTPN23physical
28514442
STABP_HUMANSTAMBPphysical
28514442
GARE1_HUMANGAREMphysical
28514442
GAB1_HUMANGAB1physical
28514442
ZSC21_HUMANZSCAN21physical
28514442
CDC27_HUMANCDC27physical
28514442
TNIP1_HUMANTNIP1physical
28514442
SNX18_HUMANSNX18physical
28514442
TRI68_HUMANTRIM68physical
28514442
ANC2_HUMANANAPC2physical
28514442
APC16_HUMANANAPC16physical
28514442
CDC23_HUMANCDC23physical
28514442
ITCH_HUMANITCHphysical
28514442
APC5_HUMANANAPC5physical
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

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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.
Phosphorylation
ReferencePubMed
"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.
"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.
"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.
"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.

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