P85A_RAT - dbPTM
P85A_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID P85A_RAT
UniProt AC Q63787
Protein Name Phosphatidylinositol 3-kinase regulatory subunit alpha
Gene Name Pik3r1
Organism Rattus norvegicus (Rat).
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. Modulates the cellular response to ER stress by promoting nuclear translocation of XBP1 in a ER stress- and/or insulin-dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement (By similarity)..
Protein Sequence MSAEGYQYRALYDYKKEREEDIDLHLGDILTVNKGSLVALGFSDGQEARPEDIGWLNGYNETTGERGDFPGTYVEYIGRKRISPPTPKPRPPRPLPVAPGSSKTEADTEQPVLTLPDLAEQFAPPDVAPPLLIKLLEAIEKKGLECSTLYRTQSSSNPAELRQLLDCDPPSVDLDVFDEHVLADAFKRYLADLPNPVIPVAVYNEMMSLAQEVPSSEDYIQLLKKLIRSPNIPHQYWLTLQYLLKHFFKLSQASSKNLLNARALSEIFSHVLFRFPAASSDNTEHLIKAVELLISAEWSERQPAPALPPKPPKPTSIANNSMNNNMSLQDAEWYWGDISREEVNEKLRDTADGTFLVRDASTKMHGDYTLTLRKGGNNKLIKIFHRDGKYGFSDPLTFNSVVELINHYRNESLAQYNPKLDVKLLYPVSKYQQDQVVKEDNIEAVGKKLHEYNTQFQEKSREYDRLYEEYTRTSQEIQMKRTAIEAFNDTIKIFEEQCHPQERYSKDYIEKFKREGNEKEIQRIMHNHDKLKSRISEIIDSRRRLEEDLKKQAAEYREIDKRMNSIKPDLIQLRKTRDQYLMWLTQKGVRQKKLNEWLGNENTEDQYSLVDDDEDLPHHDEKTWNVGSSNRNKAENLLRGKRDGTFLVRESSKQGCYACSVVVDGEVKHCVINKTATGYGFAEPYNLYSSLKELVLHYQHTSLVQHNDSLNVTLAYPVYAQQRR
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-
31PhosphorylationLHLGDILTVNKGSLV
EEHHCEEEECCCCEE
23.51-
152PhosphorylationECSTLYRTQSSSNPA
CCHHHEECCCCCCHH
21.1730181290
154PhosphorylationSTLYRTQSSSNPAEL
HHHEECCCCCCHHHH
34.8130181290
155PhosphorylationTLYRTQSSSNPAELR
HHEECCCCCCHHHHH
25.0730181290
156PhosphorylationLYRTQSSSNPAELRQ
HEECCCCCCHHHHHH
52.6730181290
279PhosphorylationLFRFPAASSDNTEHL
HHHCCCCCCCCHHHH
40.09-
416PhosphorylationRNESLAQYNPKLDVK
CCCHHHHHCCCCCEE
28.02-
426PhosphorylationKLDVKLLYPVSKYQQ
CCCEEEEEECCHHCC
16.42-
452PhosphorylationVGKKLHEYNTQFQEK
HHHHHHHHHHHHHHH
16.86-
467PhosphorylationSREYDRLYEEYTRTS
HHHHHHHHHHHHHHH
13.9622673903
470PhosphorylationYDRLYEEYTRTSQEI
HHHHHHHHHHHHHHH
6.9225575281
508PhosphorylationQERYSKDYIEKFKRE
CHHCCHHHHHHHHHC
18.0816565309
580PhosphorylationLRKTRDQYLMWLTQK
HHHCHHHHHHHHHHH
11.6527097102
608PhosphorylationENTEDQYSLVDDDED
CCCCCCCCCCCCCCC
19.1114729945
633AcetylationVGSSNRNKAENLLRG
CCCCCCHHHHHHHHC
54.5722902405

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 P85A_RAT !!

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

-

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_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
THA_RATThraphysical
16717100
IRS1_RATIrs1physical
7539611
IRS1_RATIrs1physical
9415395
IRS1_HUMANIRS1physical
25667086

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of P85A_RAT

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Related Literatures of Post-Translational Modification

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