2A5E_HUMAN - dbPTM
2A5E_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID 2A5E_HUMAN
UniProt AC Q16537
Protein Name Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit epsilon isoform
Gene Name PPP2R5E
Organism Homo sapiens (Human).
Sequence Length 467
Subcellular Localization Cytoplasm.
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 MSSAPTTPPSVDKVDGFSRKSVRKARQKRSQSSSQFRSQGKPIELTPLPLLKDVPSSEQPELFLKKLQQCCVIFDFMDTLSDLKMKEYKRSTLNELVDYITISRGCLTEQTYPEVVRMVSCNIFRTLPPSDSNEFDPEEDEPTLEASWPHLQLVYEFFIRFLESQEFQPSIAKKYIDQKFVLQLLELFDSEDPRERDYLKTVLHRIYGKFLGLRAFIRKQINNIFLRFVYETEHFNGVAELLEILGSIINGFALPLKAEHKQFLVKVLIPLHTVRSLSLFHAQLAYCIVQFLEKDPSLTEPVIRGLMKFWPKTCSQKEVMFLGELEEILDVIEPSQFVKIQEPLFKQIAKCVSSPHFQVAERALYYWNNEYIMSLIEENSNVILPIMFSSLYRISKEHWNPAIVALVYNVLKAFMEMNSTMFDELTATYKSDRQREKKKEKEREELWKKLEDLELKRGLRRDGIIPT
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------MSSAPTTPP
------CCCCCCCCC		34.9028450419
2Acetylation------MSSAPTTPP
------CCCCCCCCC		34.9022814378
3 (in isoform 3)Phosphorylation-36.6529116813
3Phosphorylation-----MSSAPTTPPS
-----CCCCCCCCCC		36.6528450419
5 (in isoform 3)Phosphorylation-38.4629116813
6Phosphorylation--MSSAPTTPPSVDK
--CCCCCCCCCCCCC		52.2123401153
7Phosphorylation-MSSAPTTPPSVDKV
-CCCCCCCCCCCCCC		31.9523401153
10PhosphorylationSAPTTPPSVDKVDGF
CCCCCCCCCCCCCCC		44.1229255136
13UbiquitinationTTPPSVDKVDGFSRK
CCCCCCCCCCCCCHH		39.8224816145
18PhosphorylationVDKVDGFSRKSVRKA
CCCCCCCCHHHHHHH		44.3124719451
21PhosphorylationVDGFSRKSVRKARQK
CCCCCHHHHHHHHHH		26.5026074081
30PhosphorylationRKARQKRSQSSSQFR
HHHHHHHHHCCHHHH		41.2626846344
32PhosphorylationARQKRSQSSSQFRSQ
HHHHHHHCCHHHHHC		32.9530266825
33PhosphorylationRQKRSQSSSQFRSQG
HHHHHHCCHHHHHCC		22.1130266825
34PhosphorylationQKRSQSSSQFRSQGK
HHHHHCCHHHHHCCC		38.2930266825
38PhosphorylationQSSSQFRSQGKPIEL
HCCHHHHHCCCCCCC		44.5730576142
41UbiquitinationSQFRSQGKPIELTPL
HHHHHCCCCCCCCCC		34.87-
41UbiquitinationSQFRSQGKPIELTPL
HHHHHCCCCCCCCCC		34.8723000965
46PhosphorylationQGKPIELTPLPLLKD
CCCCCCCCCCCCCCC		15.2526074081
65UbiquitinationEQPELFLKKLQQCCV
CCHHHHHHHHHHHHH		44.0733845483
97UbiquitinationRSTLNELVDYITISR
HCCHHHHHHHHHHCC		4.2422817900
98UbiquitinationSTLNELVDYITISRG
CCHHHHHHHHHHCCC		41.5622817900
99PhosphorylationTLNELVDYITISRGC
CHHHHHHHHHHCCCC		7.7727642862
101PhosphorylationNELVDYITISRGCLT
HHHHHHHHHCCCCCC		13.48-
103PhosphorylationLVDYITISRGCLTEQ
HHHHHHHCCCCCCCC		17.6124719451
173UbiquitinationEFQPSIAKKYIDQKF
CCCHHHHHHHCCHHH		44.43-
173UbiquitinationEFQPSIAKKYIDQKF
CCCHHHHHHHCCHHH		44.4322817900
173AcetylationEFQPSIAKKYIDQKF
CCCHHHHHHHCCHHH		44.4325953088
173MalonylationEFQPSIAKKYIDQKF
CCCHHHHHHHCCHHH		44.4326320211
174UbiquitinationFQPSIAKKYIDQKFV
CCHHHHHHHCCHHHH		38.1222817900
185UbiquitinationQKFVLQLLELFDSED
HHHHHHHHHHHCCCC		3.2929967540
200UbiquitinationPRERDYLKTVLHRIY
HHHHHHHHHHHHHHH		30.29-
209UbiquitinationVLHRIYGKFLGLRAF
HHHHHHHHHHCHHHH		22.05-
209UbiquitinationVLHRIYGKFLGLRAF
HHHHHHHHHHCHHHH		22.05-
261UbiquitinationLPLKAEHKQFLVKVL
CCCCHHHHHHHHHHH		33.9629967540
270UbiquitinationFLVKVLIPLHTVRSL
HHHHHHHHHHHHHHH		17.5829967540
297PhosphorylationQFLEKDPSLTEPVIR
HHHHHCCCCCHHHHH		59.04-
299PhosphorylationLEKDPSLTEPVIRGL
HHHCCCCCHHHHHHH		42.45-
308UbiquitinationPVIRGLMKFWPKTCS
HHHHHHHHHCCCCCC		49.69-
308UbiquitinationPVIRGLMKFWPKTCS
HHHHHHHHHCCCCCC		49.69-
320SulfoxidationTCSQKEVMFLGELEE
CCCHHHEEHHHHHHH		2.1130846556
346UbiquitinationKIQEPLFKQIAKCVS
CCCHHHHHHHHHHHC		48.7729967540
346UbiquitinationKIQEPLFKQIAKCVS
CCCHHHHHHHHHHHC		48.77-
365PhosphorylationQVAERALYYWNNEYI
HHHHHHHHHHCCHHH		12.8817053785
366PhosphorylationVAERALYYWNNEYIM
HHHHHHHHHCCHHHH		11.5117053785
373UbiquitinationYWNNEYIMSLIEENS
HHCCHHHHHHHHHCC		2.3329967540
380UbiquitinationMSLIEENSNVILPIM
HHHHHHCCCEEHHHH		35.4429967540
444UbiquitinationKKKEKEREELWKKLE
HHHHHHHHHHHHHHH		59.54-
444MethylationKKKEKEREELWKKLE
HHHHHHHHHHHHHHH		59.54-
449"N6,N6-dimethyllysine"EREELWKKLEDLELK
HHHHHHHHHHHHHHH		45.59-
449UbiquitinationEREELWKKLEDLELK
HHHHHHHHHHHHHHH		45.5929967540
449MethylationEREELWKKLEDLELK
HHHHHHHHHHHHHHH		45.5923644510
451UbiquitinationEELWKKLEDLELKRG
HHHHHHHHHHHHHHH		70.2329967540
451UbiquitinationEELWKKLEDLELKRG
HHHHHHHHHHHHHHH		70.23-
456UbiquitinationKLEDLELKRGLRRDG
HHHHHHHHHHHCCCC		34.7429967540
467PhosphorylationRRDGIIPT-------
CCCCCCCC-------		40.61-
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
-KUbiquitinationE3 ubiquitin ligaseKLHL42Q9P2K6
PMID:32071084
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of 2A5E_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 2A5E_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PP2AA_HUMANPPP2CAphysical
8703017
2AAB_HUMANPPP2R1Bphysical
8703017
A4_HUMANAPPphysical
21832049
SYAC_HUMANAARSphysical
22863883
SAE1_HUMANSAE1physical
22863883
TPD54_HUMANTPD52L2physical
22863883
RORG_HUMANRORCphysical
23555304
2A5E_HUMANPPP2R5Ephysical
23555304
API5_HUMANAPI5physical
26344197
RED_HUMANIKphysical
26344197
2A5G_HUMANPPP2R5Cphysical
26344197
2AAA_HUMANPPP2R1Aphysical
27173435
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 2A5E_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-7, AND MASSSPECTROMETRY.

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