P85A_MOUSE - dbPTM
P85A_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID P85A_MOUSE
UniProt AC P26450
Protein Name Phosphatidylinositol 3-kinase regulatory subunit alpha
Gene Name Pik3r1
Organism Mus musculus (Mouse).
Sequence Length 724
Subcellular Localization
Protein Description Binds to activated (phosphorylated) protein-Tyr kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Necessary for the insulin-stimulated increase in glucose uptake and glycogen synthesis in insulin-sensitive tissues. Plays an important role in signaling in response to FGFR1, FGFR2, FGFR3, FGFR4, KITLG/SCF, KIT, PDGFRA and PDGFRB. Likewise, plays a role in ITGB2 signaling (By similarity). Modulates the cellular response to ER stress by promoting nuclear translocation of XBP1 isoform 2 in a ER stress- and/or insulin-dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement. [PubMed: 20348926]
Protein Sequence MSAEGYQYRALYDYKKEREEDIDLHLGDILTVNKGSLVALGFSDGQEARPEDIGWLNGYNETTGERGDFPGTYVEYIGRKRISPPTPKPRPPRPLPVAPGSSKTEADTEQQALPLPDLAEQFAPPDVAPPLLIKLLEAIEKKGLECSTLYRTQSSSNPAELRQLLDCDAASVDLEMIDVHVLADAFKRYLADLPNPVIPVAVYNEMMSLAQELQSPEDCIQLLKKLIRLPNIPHQCWLTLQYLLKHFFKLSQASSKNLLNARVLSEIFSPVLFRFPAASSDNTEHLIKAIEILISTEWNERQPAPALPPKPPKPTTVANNSMNNNMSLQDAEWYWGDISREEVNEKLRDTADGTFLVRDASTKMHGDYTLTLRKGGNNKLIKIFHRDGKYGFSDPLTFNSVVELINHYRNESLAQYNPKLDVKLLYPVSKYQQDQVVKEDNIEAVGKKLHEYNTQFQEKSREYDRLYEEYTRTSQEIQMKRTAIEAFNETIKIFEEQCQTQERYSKEYIEKFKREGNEKEIQRIMHNHDKLKSRISEIIDSRRRLEEDLKKQAAEYREIDKRMNSIKPDLIQLRKTRDQYLMWLTQKGVRQKKLNEWLGNENTEDQYSLVEDDEDLPHHDEKTWNVGSSNRNKAENLLRGKRDGTFLVRESSKQGCYACSVVVDGEVKHCVINKTATGYGFAEPYNLYSSLKELVLHYQHTSLVQHNDSLNVTLAYPVYAQQRR
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
2Acetylation------MSAEGYQYR
------CCCCCCHHH
34.72-
2Phosphorylation------MSAEGYQYR
------CCCCCCHHH
34.7230635358
6Phosphorylation--MSAEGYQYRALYD
--CCCCCCHHHHHHC
8.2229514104
83PhosphorylationYIGRKRISPPTPKPR
EECCCCCCCCCCCCC
28.9429472430
86PhosphorylationRKRISPPTPKPRPPR
CCCCCCCCCCCCCCC
47.5329472430
150PhosphorylationGLECSTLYRTQSSSN
CCCCHHHEECCCCCC
16.2329514104
154PhosphorylationSTLYRTQSSSNPAEL
HHHEECCCCCCHHHH
34.8121825134
279PhosphorylationLFRFPAASSDNTEHL
HCCCCCCCCCCHHHH
40.09-
354PhosphorylationLRDTADGTFLVRDAS
HHHCCCCCEEEEECC
17.8428285833
361PhosphorylationTFLVRDASTKMHGDY
CEEEEECCCCCCCEE
32.6121825134
362PhosphorylationFLVRDASTKMHGDYT
EEEEECCCCCCCEEE
33.8228059163
382UbiquitinationGGNNKLIKIFHRDGK
CCCCCEEEEEECCCC
50.1622790023
426PhosphorylationKLDVKLLYPVSKYQQ
CCCEEEEEECCHHCC
16.42-
431PhosphorylationLLYPVSKYQQDQVVK
EEEECCHHCCCCCCC
12.1426026062
452PhosphorylationVGKKLHEYNTQFQEK
HHHHHHHHHHHHHHH
16.8622817900
463PhosphorylationFQEKSREYDRLYEEY
HHHHHHHHHHHHHHH
12.7822499769
467PhosphorylationSREYDRLYEEYTRTS
HHHHHHHHHHHHHHH
13.9625177544
470PhosphorylationYDRLYEEYTRTSQEI
HHHHHHHHHHHHHHH
6.9222499769
471PhosphorylationDRLYEEYTRTSQEIQ
HHHHHHHHHHHHHHH
30.65-
504PhosphorylationQCQTQERYSKEYIEK
HHHHHHHHHHHHHHH
24.2829514104
505PhosphorylationCQTQERYSKEYIEKF
HHHHHHHHHHHHHHH
25.8229514104
508PhosphorylationQERYSKEYIEKFKRE
HHHHHHHHHHHHHHH
20.3722499769
556PhosphorylationLKKQAAEYREIDKRM
HHHHHHHHHHHHHHH
14.6022817900
576PhosphorylationDLIQLRKTRDQYLMW
CHHHHHHCHHHHHHH
32.8026643407
580PhosphorylationLRKTRDQYLMWLTQK
HHHCHHHHHHHHHHH
11.6521082442
603PhosphorylationEWLGNENTEDQYSLV
HHHCCCCCHHHHCCC
34.4630635358
607PhosphorylationNENTEDQYSLVEDDE
CCCCHHHHCCCCCCC
19.1222817900
608PhosphorylationENTEDQYSLVEDDED
CCCHHHHCCCCCCCC
21.9522817900
651PhosphorylationGTFLVRESSKQGCYA
CCEEEEECCCCCEEE
32.0730635358
652PhosphorylationTFLVRESSKQGCYAC
CEEEEECCCCCEEEE
25.0121825134
657PhosphorylationESSKQGCYACSVVVD
ECCCCCEEEEEEEEC
19.9130635358
679PhosphorylationINKTATGYGFAEPYN
ECCCCCCCCCCCCCC
12.5222817900
690PhosphorylationEPYNLYSSLKELVLH
CCCCHHHHHHHHHHH
29.8822342344

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
508YPhosphorylationKinasePDGFRBP05622
PSP
508YPhosphorylationKinasePGFRBP05622
PhosphoELM
652SPhosphorylationKinasePRKD1Q15139
PSP
690SPhosphorylationKinaseCHUKO15111
GPS
690SPhosphorylationKinaseIKKBO14920
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
608SPhosphorylation

9312046

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 P85A_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CBL_MOUSECblphysical
9174058
IRS1_MOUSEIrs1physical
15380067
IRS2_MOUSEIrs2physical
15380067
CBL_MOUSECblphysical
9013636
GRB10_MOUSEGrb10physical
12783867
CBL_MOUSECblphysical
10940298
CBL_MOUSECblphysical
10391678
CBL_MOUSECblphysical
20133944
KIT_MOUSEKitphysical
22378847
PSN1_MOUSEPsen1physical
15192701
CADH1_MOUSECdh1physical
15192701
CADH2_MOUSECdh2physical
15192701
THB_MOUSEThrbphysical
17606624
RASH_MOUSEHrasphysical
24470255
PLAK_MOUSEJupphysical
24567360
AKT1_MOUSEAkt1physical
24567360
PA2G4_MOUSEPa2g4physical
24651434
JAK2_MOUSEJak2physical
8702385
OSTP_MOUSESpp1physical
25436971
ABI1_MOUSEAbi1physical
12515821
CYFP1_MOUSECyfip1physical
21946561
NCKP1_MOUSENckap1physical
21946561
CSF1R_MOUSECsf1rphysical
8947469
PK3CA_MOUSEPik3caphysical
8947469
CBL_MOUSECblphysical
8947469
GRB2_MOUSEGrb2physical
10995764
SHC1_MOUSEShc1physical
10995764
PTN11_MOUSEPtpn11physical
10995764
RET_MOUSERetphysical
10995764

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of P85A_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-467, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-467 AND TYR-607, ANDMASS SPECTROMETRY.

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