2A5A_HUMAN - dbPTM
2A5A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID 2A5A_HUMAN
UniProt AC Q15172
Protein Name Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform
Gene Name PPP2R5A
Organism Homo sapiens (Human).
Sequence Length 486
Subcellular Localization Cytoplasm . Nucleus . Chromosome, centromere . From mitotic prophase to metaphase, localizes at the inner centromere between a pair of sister kinetochores. Decreased expression at the onset of anaphase.
Protein Description The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment..
Protein Sequence MSSSSPPAGAASAAISASEKVDGFTRKSVRKAQRQKRSQGSSQFRSQGSQAELHPLPQLKDATSNEQQELFCQKLQQCCILFDFMDSVSDLKSKEIKRATLNELVEYVSTNRGVIVESAYSDIVKMISANIFRTLPPSDNPDFDPEEDEPTLEASWPHIQLVYEFFLRFLESPDFQPSIAKRYIDQKFVQQLLELFDSEDPRERDFLKTVLHRIYGKFLGLRAFIRKQINNIFLRFIYETEHFNGVAELLEILGSIINGFALPLKAEHKQFLMKVLIPMHTAKGLALFHAQLAYCVVQFLEKDTTLTEPVIRGLLKFWPKTCSQKEVMFLGEIEEILDVIEPTQFKKIEEPLFKQISKCVSSSHFQVAERALYFWNNEYILSLIEENIDKILPIMFASLYKISKEHWNPTIVALVYNVLKTLMEMNGKLFDDLTSSYKAERQREKKKELEREELWKKLEELKLKKALEKQNSAYNMHSILSNTSAE
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------MSSSSPPAG
------CCCCCCCCH		38.6425850435
2Acetylation------MSSSSPPAG
------CCCCCCCCH		38.6422223895
3Phosphorylation-----MSSSSPPAGA
-----CCCCCCCCHH		33.2725850435
4Phosphorylation----MSSSSPPAGAA
----CCCCCCCCHHH		39.2925850435
5Phosphorylation---MSSSSPPAGAAS
---CCCCCCCCHHHH		36.5325850435
12PhosphorylationSPPAGAASAAISASE
CCCCHHHHHHHHHHH		20.0725850435
16PhosphorylationGAASAAISASEKVDG
HHHHHHHHHHHHCCC		22.4828270605
18PhosphorylationASAAISASEKVDGFT
HHHHHHHHHHCCCCC		31.0328270605
25PhosphorylationSEKVDGFTRKSVRKA
HHHCCCCCHHHHHHH		42.5924719451
28PhosphorylationVDGFTRKSVRKAQRQ
CCCCCHHHHHHHHHH		24.7022817900
38PhosphorylationKAQRQKRSQGSSQFR
HHHHHHHHCCCHHHH		46.0225159151
41PhosphorylationRQKRSQGSSQFRSQG
HHHHHCCCHHHHHCC		17.2126846344
42PhosphorylationQKRSQGSSQFRSQGS
HHHHCCCHHHHHCCC		39.9126846344
46PhosphorylationQGSSQFRSQGSQAEL
CCCHHHHHCCCCCEE		39.9325159151
49PhosphorylationSQFRSQGSQAELHPL
HHHHHCCCCCEECCC		20.6925159151
100PhosphorylationSKEIKRATLNELVEY
CHHHHHHHHHHHHHH		33.8626074081
107PhosphorylationTLNELVEYVSTNRGV
HHHHHHHHHHCCCCE		7.6926074081
109PhosphorylationNELVEYVSTNRGVIV
HHHHHHHHCCCCEEE		21.0426074081
110PhosphorylationELVEYVSTNRGVIVE
HHHHHHHCCCCEEEC		20.9226074081
118PhosphorylationNRGVIVESAYSDIVK
CCCEEECCHHHHHHH		22.9326074081
120PhosphorylationGVIVESAYSDIVKMI
CEEECCHHHHHHHHH		19.0226074081
121PhosphorylationVIVESAYSDIVKMIS
EEECCHHHHHHHHHH		22.1526074081
181MalonylationDFQPSIAKRYIDQKF
CCCHHHHHHHCCHHH		44.0326320211
181AcetylationDFQPSIAKRYIDQKF
CCCHHHHHHHCCHHH		44.0325953088
217UbiquitinationVLHRIYGKFLGLRAF
HHHHHHHHHHCHHHH		22.05-
259UbiquitinationILGSIINGFALPLKA
HHHHHHHCCCCCCCH		9.9721890473
263UbiquitinationIINGFALPLKAEHKQ
HHHCCCCCCCHHHHH		28.5222817900
281PhosphorylationKVLIPMHTAKGLALF
HHHHHHHHHHHHHHH		24.6626434552
316UbiquitinationPVIRGLLKFWPKTCS
HHHHHHHHHCCCCCC		50.8821890473
316UbiquitinationPVIRGLLKFWPKTCS
HHHHHHHHHCCCCCC		50.8821890473
320UbiquitinationGLLKFWPKTCSQKEV
HHHHHCCCCCCCHHE		53.4022817900
361PhosphorylationKQISKCVSSSHFQVA
HHHHHHCCCHHHHHH		35.2829083192
362PhosphorylationQISKCVSSSHFQVAE
HHHHHCCCHHHHHHH		13.8729083192
363PhosphorylationISKCVSSSHFQVAER
HHHHCCCHHHHHHHH		22.3329083192
381UbiquitinationFWNNEYILSLIEENI
HHCCHHHHHHHHHCH		3.1429967540
412UbiquitinationEHWNPTIVALVYNVL
HHCCHHHHHHHHHHH		3.5629967540
421PhosphorylationLVYNVLKTLMEMNGK
HHHHHHHHHHHHCCH		27.4624719451
438UbiquitinationDDLTSSYKAERQREK
HHHHHHHHHHHHHHH		45.8029967540
457UbiquitinationEREELWKKLEELKLK
HHHHHHHHHHHHHHH		49.93-
469UbiquitinationKLKKALEKQNSAYNM
HHHHHHHHCCCCHHH		56.4829967540
472PhosphorylationKALEKQNSAYNMHSI
HHHHHCCCCHHHHHH		29.6320068231
474PhosphorylationLEKQNSAYNMHSILS
HHHCCCCHHHHHHHH		16.9120068231
478PhosphorylationNSAYNMHSILSNTSA
CCCHHHHHHHHCCCC		17.9225159151
481PhosphorylationYNMHSILSNTSAE--
HHHHHHHHCCCCC--		36.0720068231
484PhosphorylationHSILSNTSAE-----
HHHHHCCCCC-----		34.35-
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
28SPhosphorylationKinaseEIF2AK2P19525
GPS
41SPhosphorylationKinasePRKCAP17252
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of 2A5A_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 2A5A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
2A5G_HUMANPPP2R5Cphysical
11929880
2AAA_HUMANPPP2R1Aphysical
18782753
PP2AA_HUMANPPP2CAphysical
18782753
2AAB_HUMANPPP2R1Bphysical
18782753
AXIN1_HUMANAXIN1physical
11297546
PP2AA_HUMANPPP2CAphysical
8703017
2AAB_HUMANPPP2R1Bphysical
8703017
CCNG1_MOUSECcng1physical
11983168
PTTG1_HUMANPTTG1physical
24781523
DAPK1_HUMANDAPK1physical
20220139
PP2AA_HUMANPPP2CAphysical
20220139
2AAA_HUMANPPP2R1Aphysical
20220139
2ABD_HUMANPPP2R2Dphysical
20220139
2A5D_HUMANPPP2R5Dphysical
26344197
PP2AA_HUMANPPP2CAphysical
26811472
BUB1B_HUMANBUB1Bphysical
26811472
CDC20_HUMANCDC20physical
26811472
UBE2S_HUMANUBE2Sphysical
26811472
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 2A5A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-42, AND MASSSPECTROMETRY.

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