2A5B_HUMAN - dbPTM
2A5B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID 2A5B_HUMAN
UniProt AC Q15173
Protein Name Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform
Gene Name PPP2R5B
Organism Homo sapiens (Human).
Sequence Length 497
Subcellular Localization Cytoplasm .
Protein Description As the regulatory component of the serine/threonine-protein phosphatase 2A (PP2A) holoenzyme, modulates substrate specificity, subcellular localization, and responsiveness to phosphorylation. The phosphorylated form mediates the interaction between PP2A and AKT1, leading to AKT1 dephosphorylation..
Protein Sequence METKLPPASTPTSPSSPGLSPVPPPDKVDGFSRRSLRRARPRRSHSSSQFRYQSNQQELTPLPLLKDVPASELHELLSRKLAQCGVMFDFLDCVADLKGKEVKRAALNELVECVGSTRGVLIEPVYPDIIRMISVNIFRTLPPSENPEFDPEEDEPNLEPSWPHLQLVYEFFLRFLESPDFQPSVAKRYVDQKFVLMLLELFDSEDPREREYLKTILHRVYGKFLGLRAYIRKQCNHIFLRFIYEFEHFNGVAELLEILGSIINGFALPLKTEHKQFLVRVLIPLHSVKSLSVFHAQLAYCVVQFLEKDATLTEHVIRGLLKYWPKTCTQKEVMFLGEMEEILDVIEPSQFVKIQEPLFKQVARCVSSPHFQVAERALYFWNNEYILSLIEDNCHTVLPAVFGTLYQVSKEHWNQTIVSLIYNVLKTFMEMNGKLFDELTASYKLEKQQEQQKAQERQELWQGLEELRLRRLQGTQGAKEAPLQRLTPQVAASGGQS
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
9PhosphorylationETKLPPASTPTSPSS
CCCCCCCCCCCCCCC
40.4723186163
10PhosphorylationTKLPPASTPTSPSSP
CCCCCCCCCCCCCCC
32.4623186163
12PhosphorylationLPPASTPTSPSSPGL
CCCCCCCCCCCCCCC
54.0523186163
13PhosphorylationPPASTPTSPSSPGLS
CCCCCCCCCCCCCCC
24.8025850435
15PhosphorylationASTPTSPSSPGLSPV
CCCCCCCCCCCCCCC
49.2725850435
16PhosphorylationSTPTSPSSPGLSPVP
CCCCCCCCCCCCCCC
26.7725850435
20PhosphorylationSPSSPGLSPVPPPDK
CCCCCCCCCCCCCCC
29.7525159151
32PhosphorylationPDKVDGFSRRSLRRA
CCCCCCCCHHHHHHC
32.1121329884
35PhosphorylationVDGFSRRSLRRARPR
CCCCCHHHHHHCCCC
25.7221329884
44PhosphorylationRRARPRRSHSSSQFR
HHCCCCCCCCCHHHC
29.0621329884
46PhosphorylationARPRRSHSSSQFRYQ
CCCCCCCCCHHHCCC
32.6921329884
47PhosphorylationRPRRSHSSSQFRYQS
CCCCCCCCHHHCCCC
23.8021329884
48PhosphorylationPRRSHSSSQFRYQSN
CCCCCCCHHHCCCCC
36.0321329884
52PhosphorylationHSSSQFRYQSNQQEL
CCCHHHCCCCCCCCC
19.9930177828
54PhosphorylationSSQFRYQSNQQELTP
CHHHCCCCCCCCCCC
27.8928857561
78PhosphorylationSELHELLSRKLAQCG
HHHHHHHHHHHHHCC
39.7424719451
126PhosphorylationGVLIEPVYPDIIRMI
CEEEEECCHHHHHHH
13.10-
187MalonylationDFQPSVAKRYVDQKF
CCCHHHHHHHCCHHH
41.9526320211
327PhosphorylationLLKYWPKTCTQKEVM
HHHHCCCCCCHHHHH
19.3929978859
329PhosphorylationKYWPKTCTQKEVMFL
HHCCCCCCHHHHHHH
48.1629978859
349PhosphorylationILDVIEPSQFVKIQE
HHHHCCHHHCCCCCH
24.3829978859
368PhosphorylationQVARCVSSPHFQVAE
HHHHHHCCCCHHHHH
11.2917200115
406PhosphorylationPAVFGTLYQVSKEHW
HHHHHHHHHHCHHHH
13.5026074081
409PhosphorylationFGTLYQVSKEHWNQT
HHHHHHHCHHHHHHH
19.4626074081
479UbiquitinationLQGTQGAKEAPLQRL
HHCCCCHHHCCHHHH
62.32-

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
32SPhosphorylationKinaseCLK2P49760
Uniprot
35SPhosphorylationKinaseCLK2P49760
Uniprot
44SPhosphorylationKinaseCLK2P49760
Uniprot
46SPhosphorylationKinaseCLK2P49760
Uniprot
47SPhosphorylationKinaseCLK2P49760
Uniprot
48SPhosphorylationKinaseCLK2P49760
Uniprot
-KUbiquitinationE3 ubiquitin ligaseKLHL15Q96M94
PMID:23135275

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of 2A5B_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 2A5B_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PP2AA_HUMANPPP2CAphysical
8703017
2AAB_HUMANPPP2R1Bphysical
8703017
IEX1_HUMANIER3physical
16456541
PP2AA_HUMANPPP2CAphysical
16456541
PIM1_HUMANPIM1physical
17297438

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 2A5B_HUMAN

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Related Literatures of Post-Translational Modification

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