P55G_HUMAN - dbPTM
P55G_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID P55G_HUMAN
UniProt AC Q92569
Protein Name Phosphatidylinositol 3-kinase regulatory subunit gamma
Gene Name PIK3R3
Organism Homo sapiens (Human).
Sequence Length 461
Subcellular Localization
Protein Description Binds to activated (phosphorylated) protein-tyrosine kinases through its SH2 domain and regulates their kinase activity. During insulin stimulation, it also binds to IRS-1..
Protein Sequence MYNTVWSMDRDDADWREVMMPYSTELIFYIEMDPPALPPKPPKPMTSAVPNGMKDSSVSLQDAEWYWGDISREEVNDKLRDMPDGTFLVRDASTKMQGDYTLTLRKGGNNKLIKIYHRDGKYGFSDPLTFNSVVELINHYHHESLAQYNPKLDVKLMYPVSRYQQDQLVKEDNIDAVGKKLQEYHSQYQEKSKEYDRLYEEYTRTSQEIQMKRTAIEAFNETIKIFEEQCHTQEQHSKEYIERFRREGNEKEIERIMMNYDKLKSRLGEIHDSKMRLEQDLKNQALDNREIDKKMNSIKPDLIQLRKIRDQHLVWLNHKGVRQKRLNVWLGIKNEDADENYFINEEDENLPHYDEKTWFVEDINRVQAEDLLYGKPDGAFLIRESSKKGCYACSVVADGEVKHCVIYSTARGYGFAEPYNLYSSLKELVLHYQQTSLVQHNDSLNVRLAYPVHAQMPSLCR
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
2Phosphorylation------MYNTVWSMD
------CCCCCCCCC		21.3822210691
7Phosphorylation-MYNTVWSMDRDDAD
-CCCCCCCCCCCCCC		13.3822210691
78UbiquitinationSREEVNDKLRDMPDG
CHHHHHHHHHCCCCC		39.97-
93PhosphorylationTFLVRDASTKMQGDY
CEEEEECCCCCCCEE		32.6127282143
94PhosphorylationFLVRDASTKMQGDYT
EEEEECCCCCCCEEE		32.0527282143
106AcetylationDYTLTLRKGGNNKLI
EEEEEEEECCCCCEE		74.437668773
111UbiquitinationLRKGGNNKLIKIYHR
EEECCCCCEEEEEEC		56.44-
114AcetylationGGNNKLIKIYHRDGK
CCCCCEEEEEECCCC		47.887668783
114UbiquitinationGGNNKLIKIYHRDGK
CCCCCEEEEEECCCC		47.88-
155UbiquitinationYNPKLDVKLMYPVSR
HCCCCCEEEEEECCH		27.48-
161O-linked_GlycosylationVKLMYPVSRYQQDQL
EEEEEECCHHHHHHH		22.2930379171
163PhosphorylationLMYPVSRYQQDQLVK
EEEECCHHHHHHHHC		11.7425159151
170UbiquitinationYQQDQLVKEDNIDAV
HHHHHHHCCCCHHHH		68.86-
180UbiquitinationNIDAVGKKLQEYHSQ
CHHHHHHHHHHHHHH		49.85-
184PhosphorylationVGKKLQEYHSQYQEK
HHHHHHHHHHHHHHH		8.2025884760
186PhosphorylationKKLQEYHSQYQEKSK
HHHHHHHHHHHHHHH		29.6726356563
188PhosphorylationLQEYHSQYQEKSKEY
HHHHHHHHHHHHHHH		22.9626356563
191UbiquitinationYHSQYQEKSKEYDRL
HHHHHHHHHHHHHHH		51.83-
192PhosphorylationHSQYQEKSKEYDRLY
HHHHHHHHHHHHHHH		29.9328331001
195PhosphorylationYQEKSKEYDRLYEEY
HHHHHHHHHHHHHHH		15.3128796482
199PhosphorylationSKEYDRLYEEYTRTS
HHHHHHHHHHHHHHH		13.9622322096
202PhosphorylationYDRLYEEYTRTSQEI
HHHHHHHHHHHHHHH		6.9221082442
203PhosphorylationDRLYEEYTRTSQEIQ
HHHHHHHHHHHHHHH		30.6528152594
222PhosphorylationAIEAFNETIKIFEEQ
HHHHHHHHHHHHHHH		28.7720068231
224UbiquitinationEAFNETIKIFEEQCH
HHHHHHHHHHHHHHC		49.08-
237PhosphorylationCHTQEQHSKEYIERF
HCCCHHHHHHHHHHH		27.2029496907
238UbiquitinationHTQEQHSKEYIERFR
CCCHHHHHHHHHHHH		53.03-
260PhosphorylationIERIMMNYDKLKSRL
HHHHHHCHHHHHHHH		9.14-
273PhosphorylationRLGEIHDSKMRLEQD
HHHHHHHHHHHHHHH		17.7528152594
274UbiquitinationLGEIHDSKMRLEQDL
HHHHHHHHHHHHHHH		33.81-
294UbiquitinationDNREIDKKMNSIKPD
HHHHHHHHHHHCCCC		39.30-
299UbiquitinationDKKMNSIKPDLIQLR
HHHHHHCCCCHHHHH		32.09-
319UbiquitinationHLVWLNHKGVRQKRL
CEEEECCCCCCHHHE		59.01-
341PhosphorylationNEDADENYFINEEDE
CCCCCCCCCCCCCCC		12.0922322096
373PhosphorylationVQAEDLLYGKPDGAF
HCHHHHHCCCCCCCE		30.3322817900
375UbiquitinationAEDLLYGKPDGAFLI
HHHHHCCCCCCCEEE		26.78-
388UbiquitinationLIRESSKKGCYACSV
EEEECCCCCEEEEEE		57.04-
407PhosphorylationEVKHCVIYSTARGYG
EEEEEEEEECCCCCC		4.6029496907
408PhosphorylationVKHCVIYSTARGYGF
EEEEEEEECCCCCCC		12.4129496907
422PhosphorylationFAEPYNLYSSLKELV
CCCCCHHHHHHHHHH		7.809461588
423PhosphorylationAEPYNLYSSLKELVL
CCCCHHHHHHHHHHH		32.1528348404
424PhosphorylationEPYNLYSSLKELVLH
CCCHHHHHHHHHHHH		29.8828348404
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
341YPhosphorylationKinaseINSRP06213
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of P55G_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 P55G_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PK3CA_HUMANPIK3CAphysical
9415396
NC2A_HUMANDRAP1physical
16189514
IGF1R_HUMANIGF1Rphysical
9415396
IRS1_HUMANIRS1physical
9415396
ABCB6_HUMANABCB6physical
18624398
RING1_HUMANRING1physical
18624398
AMBP_HUMANAMBPphysical
18624398
A1AG1_HUMANORM1physical
18624398
SERF1_HUMANSERF1Aphysical
18624398
VTDB_HUMANGCphysical
18624398
SYK_HUMANKARSphysical
21900206
MICA1_HUMANMICAL1physical
21900206
DSN1_HUMANDSN1physical
21900206
PFD3_HUMANVBP1physical
21900206
SYQ_HUMANQARSphysical
21900206
SYDC_HUMANDARSphysical
21900206
KLC2_HUMANKLC2physical
21900206
TRM2A_HUMANTRMT2Aphysical
21900206
PSME1_HUMANPSME1physical
21900206
FIBB_HUMANFGBphysical
21900206
CE126_HUMANKIAA1377physical
21900206
LC7L2_HUMANLUC7L2physical
21900206
FBN3_HUMANFBN3physical
21900206
MBIP1_HUMANMBIPphysical
19060904
TRI54_HUMANTRIM54physical
25416956
LMBL3_HUMANL3MBTL3physical
25416956
FSD2_HUMANFSD2physical
25416956
AR6P4_HUMANARL6IP4physical
25814554
PKHS1_HUMANPLEKHS1physical
25814554
CCD14_HUMANCCDC14physical
25814554
IQUB_HUMANIQUBphysical
25814554
OTU7B_HUMANOTUD7Bphysical
25814554
PAR6A_HUMANPARD6Aphysical
25814554
PCDB5_HUMANPCDHB5physical
25814554
PELI3_HUMANPELI3physical
25814554
PELO_HUMANPELOphysical
25814554
PLB1_HUMANPLB1physical
25814554
RET7_HUMANRBP7physical
25814554
SOCS4_HUMANSOCS4physical
25814554
SPSB2_HUMANSPSB2physical
25814554
UBP2_HUMANUSP2physical
25814554
MET27_HUMANWBSCR27physical
25814554
ZN281_HUMANZNF281physical
25814554
CBL_HUMANCBLphysical
25814554
BTK_HUMANBTKphysical
25814554
CRBA2_HUMANCRYBA2physical
25814554
E2F6_HUMANE2F6physical
25814554
EVI1_HUMANMECOMphysical
25814554
PPARA_HUMANPPARAphysical
25814554
TERA_HUMANVCPphysical
25814554
CQ053_HUMANC17orf53physical
25814554
AUNIP_HUMANAUNIPphysical
25814554
BRK1_HUMANBRK1physical
25814554
CEP19_HUMANCEP19physical
25814554
KCC1A_HUMANCAMK1physical
25814554
CCD33_HUMANCCDC33physical
25814554
CRBN_HUMANCRBNphysical
25814554
KLF15_HUMANKLF15physical
25814554
KMT2B_HUMANKMT2Bphysical
25814554
MTF2_HUMANMTF2physical
25814554
OLIG1_HUMANOLIG1physical
25814554
PACRL_HUMANPACRGLphysical
25814554
SOCS6_HUMANSOCS6physical
25814554
WDFY3_HUMANWDFY3physical
25814554
DCAF8_HUMANDCAF8physical
25814554
WRIP1_HUMANWRNIP1physical
25814554
ZMAT1_HUMANZMAT1physical
25814554
ZN451_HUMANZNF451physical
25814554
FOXO1_HUMANFOXO1physical
25814554
FYN_HUMANFYNphysical
25814554
PK3CA_HUMANPIK3CAphysical
25814554
PK3CB_HUMANPIK3CBphysical
25814554
MYPT2_HUMANPPP1R12Bphysical
25814554
FAK1_HUMANPTK2physical
25814554
TERF2_HUMANTERF2physical
25814554
TNNC2_HUMANTNNC2physical
25814554
HCK_HUMANHCKphysical
25814554
IRS1_HUMANIRS1physical
25814554
TSN2_HUMANTSPAN2physical
25814554
IRS2_HUMANIRS2physical
28514442
PK3CD_HUMANPIK3CDphysical
28514442
PK3CA_HUMANPIK3CAphysical
28514442
PK3CB_HUMANPIK3CBphysical
28514442
EHD2_HUMANEHD2physical
28514442
NISCH_HUMANNISCHphysical
28514442
P85A_HUMANPIK3R1physical
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
DB01064Isoprenaline
Regulatory Network of P55G_HUMAN

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Related Literatures of Post-Translational Modification
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-199, AND MASSSPECTROMETRY.

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