2A5G_HUMAN - dbPTM
2A5G_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID 2A5G_HUMAN
UniProt AC Q13362
Protein Name Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform
Gene Name PPP2R5C
Organism Homo sapiens (Human).
Sequence Length 524
Subcellular Localization Nucleus. Chromosome, centromere.
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. The PP2A-PPP2R5C holoenzyme may specifically dephosphorylate and activate TP53 and play a role in DNA damage-induced inhibition of cell proliferation. PP2A-PPP2R5C may also regulate the ERK signaling pathway through ERK dephosphorylation..
Protein Sequence MLTCNKAGSRMVVDAANSNGPFQPVVLLHIRDVPPADQEKLFIQKLRQCCVLFDFVSDPLSDLKWKEVKRAALSEMVEYITHNRNVITEPIYPEVVHMFAVNMFRTLPPSSNPTGAEFDPEEDEPTLEAAWPHLQLVYEFFLRFLESPDFQPNIAKKYIDQKFVLQLLELFDSEDPRERDFLKTTLHRIYGKFLGLRAYIRKQINNIFYRFIYETEHHNGIAELLEILGSIINGFALPLKEEHKIFLLKVLLPLHKVKSLSVYHPQLAYCVVQFLEKDSTLTEPVVMALLKYWPKTHSPKEVMFLNELEEILDVIEPSEFVKIMEPLFRQLAKCVSSPHFQVAERALYYWNNEYIMSLISDNAAKILPIMFPSLYRNSKTHWNKTIHGLIYNALKLFMEMNQKLFDDCTQQFKAEKLKEKLKMKEREEAWVKIENLAKANPQYTVYSQASTMSIPVAMETDGPLFEDVQMLRKTVKDEAHQAQKDPKKDRPLARRKSELPQDPHTKKALEAHCRADELASQDGR
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
1Acetylation-------MLTCNKAG
-------CCCCCCCC		6.7122814378
6Ubiquitination--MLTCNKAGSRMVV
--CCCCCCCCCEEEE		57.16-
9PhosphorylationLTCNKAGSRMVVDAA
CCCCCCCCEEEEECC		23.28-
39 (in isoform 5)Phosphorylation-52.88-
39 (in isoform 4)Phosphorylation-52.8825849741
40 (in isoform 5)Phosphorylation-42.96-
45UbiquitinationQEKLFIQKLRQCCVL
HHHHHHHHHHHHHHH		40.60-
45AcetylationQEKLFIQKLRQCCVL
HHHHHHHHHHHHHHH		40.6026051181
68 (in isoform 4)Phosphorylation-4.5228102081
69 (in isoform 4)Phosphorylation-37.0928102081
72 (in isoform 4)Phosphorylation-18.6928102081
74PhosphorylationEVKRAALSEMVEYIT
HHHHHHHHHHHHHHH		20.9422210691
74 (in isoform 4)Phosphorylation-20.9428102081
79PhosphorylationALSEMVEYITHNRNV
HHHHHHHHHHCCCCC		10.33-
81UbiquitinationSEMVEYITHNRNVIT
HHHHHHHHCCCCCCC		16.5222817900
82UbiquitinationEMVEYITHNRNVITE
HHHHHHHCCCCCCCC		22.9922817900
87UbiquitinationITHNRNVITEPIYPE
HHCCCCCCCCCCCHH		4.0523503661
88PhosphorylationTHNRNVITEPIYPEV
HCCCCCCCCCCCHHH		31.27-
127UbiquitinationPEEDEPTLEAAWPHL
CCCCCCCHHHHHHHH		6.5329901268
132UbiquitinationPTLEAAWPHLQLVYE
CCHHHHHHHHHHHHH		17.3722817900
133UbiquitinationTLEAAWPHLQLVYEF
CHHHHHHHHHHHHHH		18.5922817900
138UbiquitinationWPHLQLVYEFFLRFL
HHHHHHHHHHHHHHH		18.6623503661
140UbiquitinationHLQLVYEFFLRFLES
HHHHHHHHHHHHHHC		3.7022817900
141UbiquitinationLQLVYEFFLRFLESP
HHHHHHHHHHHHHCC		2.9822817900
146UbiquitinationEFFLRFLESPDFQPN
HHHHHHHHCCCCCCC		58.4723503661
147UbiquitinationFFLRFLESPDFQPNI
HHHHHHHCCCCCCCH		31.7322817900
148UbiquitinationFLRFLESPDFQPNIA
HHHHHHCCCCCCCHH		36.7422817900
150UbiquitinationRFLESPDFQPNIAKK
HHHHCCCCCCCHHHH		17.2422817900
151UbiquitinationFLESPDFQPNIAKKY
HHHCCCCCCCHHHHH		37.1922817900
153UbiquitinationESPDFQPNIAKKYID
HCCCCCCCHHHHHCC		35.7523503661
156UbiquitinationDFQPNIAKKYIDQKF
CCCCCHHHHHCCHHH		42.1722817900
156MalonylationDFQPNIAKKYIDQKF
CCCCCHHHHHCCHHH		42.1726320211
156AcetylationDFQPNIAKKYIDQKF
CCCCCHHHHHCCHHH		42.1725953088
156 (in isoform 1)Ubiquitination-42.1721906983
156 (in isoform 2)Ubiquitination-42.1721906983
156 (in isoform 3)Ubiquitination-42.1721906983
157UbiquitinationFQPNIAKKYIDQKFV
CCCCHHHHHCCHHHH		38.1222817900
162UbiquitinationAKKYIDQKFVLQLLE
HHHHCCHHHHHHHHH		33.4223503661
174UbiquitinationLLELFDSEDPRERDF
HHHHHCCCCHHHHHH		74.0933845483
175UbiquitinationLELFDSEDPRERDFL
HHHHCCCCHHHHHHH		52.0522817900
180UbiquitinationSEDPRERDFLKTTLH
CCCHHHHHHHHHHHH		48.7723503661
183UbiquitinationPRERDFLKTTLHRIY
HHHHHHHHHHHHHHH		39.18-
187UbiquitinationDFLKTTLHRIYGKFL
HHHHHHHHHHHHHHH		16.4022817900
188UbiquitinationFLKTTLHRIYGKFLG
HHHHHHHHHHHHHHC		27.2622817900
192UbiquitinationTLHRIYGKFLGLRAY
HHHHHHHHHHCHHHH		22.05-
193UbiquitinationLHRIYGKFLGLRAYI
HHHHHHHHHCHHHHH		5.9323503661
202UbiquitinationGLRAYIRKQINNIFY
CHHHHHHHHHHHHHH		46.0729901268
209PhosphorylationKQINNIFYRFIYETE
HHHHHHHHHHHHCCC		10.79-
211UbiquitinationINNIFYRFIYETEHH
HHHHHHHHHHCCCCC		4.8022817900
212UbiquitinationNNIFYRFIYETEHHN
HHHHHHHHHCCCCCC		1.9422817900
216UbiquitinationYRFIYETEHHNGIAE
HHHHHCCCCCCCHHH		31.0733845483
217UbiquitinationRFIYETEHHNGIAEL
HHHHCCCCCCCHHHH		27.4222817900
220UbiquitinationYETEHHNGIAELLEI
HCCCCCCCHHHHHHH		19.0023503661
222UbiquitinationTEHHNGIAELLEILG
CCCCCCHHHHHHHHH		11.6323503661
233UbiquitinationEILGSIINGFALPLK
HHHHHHHCCCCCCCC		37.5529901268
249UbiquitinationEHKIFLLKVLLPLHK
HHHHHHHHHHHHHHH		32.7433845483
256UbiquitinationKVLLPLHKVKSLSVY
HHHHHHHHCCCCCCC		60.07-
257UbiquitinationVLLPLHKVKSLSVYH
HHHHHHHCCCCCCCC		3.3829901268
258UbiquitinationLLPLHKVKSLSVYHP
HHHHHHCCCCCCCCH		50.9424816145
262UbiquitinationHKVKSLSVYHPQLAY
HHCCCCCCCCHHHHH		6.5429901268
267UbiquitinationLSVYHPQLAYCVVQF
CCCCCHHHHHHHHHH		4.2823503661
271UbiquitinationHPQLAYCVVQFLEKD
CHHHHHHHHHHHHCC		2.1723503661
275UbiquitinationAYCVVQFLEKDSTLT
HHHHHHHHHCCCCCC		4.4623503661
279UbiquitinationVQFLEKDSTLTEPVV
HHHHHCCCCCCHHHH		36.0623503661
280UbiquitinationQFLEKDSTLTEPVVM
HHHHCCCCCCHHHHH		48.0833845483
282UbiquitinationLEKDSTLTEPVVMAL
HHCCCCCCHHHHHHH		38.0323503661
285UbiquitinationDSTLTEPVVMALLKY
CCCCCHHHHHHHHHH		3.6023503661
286UbiquitinationSTLTEPVVMALLKYW
CCCCHHHHHHHHHHC		2.4523503661
289UbiquitinationTEPVVMALLKYWPKT
CHHHHHHHHHHCCCC		1.9823503661
291UbiquitinationPVVMALLKYWPKTHS
HHHHHHHHHCCCCCC		46.2333845483
291 (in isoform 2)Ubiquitination-46.23-
295UbiquitinationALLKYWPKTHSPKEV
HHHHHCCCCCCCHHH		44.7323503661
298PhosphorylationKYWPKTHSPKEVMFL
HHCCCCCCCHHHHHH		42.7919366811
304UbiquitinationHSPKEVMFLNELEEI
CCCHHHHHHHHHHHH		8.8333845483
309UbiquitinationVMFLNELEEILDVIE
HHHHHHHHHHHHHCC		36.4933845483
313UbiquitinationNELEEILDVIEPSEF
HHHHHHHHHCCHHHH		45.0423503661
317UbiquitinationEILDVIEPSEFVKIM
HHHHHCCHHHHHHHH		28.2124816145
322UbiquitinationIEPSEFVKIMEPLFR
CCHHHHHHHHHHHHH		41.4733845483
324UbiquitinationPSEFVKIMEPLFRQL
HHHHHHHHHHHHHHH		3.4424816145
326UbiquitinationEFVKIMEPLFRQLAK
HHHHHHHHHHHHHHH		21.3023503661
327UbiquitinationFVKIMEPLFRQLAKC
HHHHHHHHHHHHHHH		3.3524816145
333UbiquitinationPLFRQLAKCVSSPHF
HHHHHHHHHHCCCCH		43.7024816145
336PhosphorylationRQLAKCVSSPHFQVA
HHHHHHHCCCCHHHH		47.8529978859
337PhosphorylationQLAKCVSSPHFQVAE
HHHHHHCCCCHHHHH		11.2929978859
346UbiquitinationHFQVAERALYYWNNE
CHHHHHHHHHHCCCH		7.4533845483
348PhosphorylationQVAERALYYWNNEYI
HHHHHHHHHCCCHHH		12.8817053785
349PhosphorylationVAERALYYWNNEYIM
HHHHHHHHCCCHHHH		11.5117053785
350UbiquitinationAERALYYWNNEYIMS
HHHHHHHCCCHHHHH		6.3923503661
351UbiquitinationERALYYWNNEYIMSL
HHHHHHCCCHHHHHH		18.4833845483
354PhosphorylationLYYWNNEYIMSLISD
HHHCCCHHHHHHHCC		12.2117053785
355UbiquitinationYYWNNEYIMSLISDN
HHCCCHHHHHHHCCC		0.9223503661
357PhosphorylationWNNEYIMSLISDNAA
CCCHHHHHHHCCCHH		17.0029978859
360PhosphorylationEYIMSLISDNAAKIL
HHHHHHHCCCHHHHH		30.0629978859
364UbiquitinationSLISDNAAKILPIMF
HHHCCCHHHHHHHCC		12.9924816145
373PhosphorylationILPIMFPSLYRNSKT
HHHHCCHHHHHCCCC		27.1121406692
375PhosphorylationPIMFPSLYRNSKTHW
HHCCHHHHHCCCCHH		16.4621406692
385PhosphorylationSKTHWNKTIHGLIYN
CCCHHHHHHHHHHHH		18.2620873877
388UbiquitinationHWNKTIHGLIYNALK
HHHHHHHHHHHHHHH		15.2124816145
393UbiquitinationIHGLIYNALKLFMEM
HHHHHHHHHHHHHHH		6.7924816145
401UbiquitinationLKLFMEMNQKLFDDC
HHHHHHHHHHHHHHH		23.6424816145
403UbiquitinationLFMEMNQKLFDDCTQ
HHHHHHHHHHHHHHH		46.23-
413UbiquitinationDDCTQQFKAEKLKEK
HHHHHHHHHHHHHHH		51.8329967540
413MalonylationDDCTQQFKAEKLKEK
HHHHHHHHHHHHHHH		51.8326320211
413AcetylationDDCTQQFKAEKLKEK
HHHHHHHHHHHHHHH		51.8325953088
432UbiquitinationEREEAWVKIENLAKA
HHHHHHHHHHHHHHH		33.3329967540
444UbiquitinationAKANPQYTVYSQAST
HHHCCCEEEEEECCC		14.0229967540
452UbiquitinationVYSQASTMSIPVAME
EEEECCCCCCCEEEE		2.9524816145
460UbiquitinationSIPVAMETDGPLFED
CCCEEEECCCCCHHH		32.9224816145
463UbiquitinationVAMETDGPLFEDVQM
EEEECCCCCHHHHHH		36.3629967540
467UbiquitinationTDGPLFEDVQMLRKT
CCCCCHHHHHHHHHH		28.7224816145
468UbiquitinationDGPLFEDVQMLRKTV
CCCCHHHHHHHHHHH		2.5829967540
470UbiquitinationPLFEDVQMLRKTVKD
CCHHHHHHHHHHHHH		3.8224816145
476UbiquitinationQMLRKTVKDEAHQAQ
HHHHHHHHHHHHHHH		55.9024816145
487AcetylationHQAQKDPKKDRPLAR
HHHHHCCCCCCCCHH		76.947662415
494UbiquitinationKKDRPLARRKSELPQ
CCCCCCHHCHHCCCC		55.0024816145
497PhosphorylationRPLARRKSELPQDPH
CCCHHCHHCCCCCHH		42.4223401153
505PhosphorylationELPQDPHTKKALEAH
CCCCCHHHHHHHHHH		39.3623403867
507UbiquitinationPQDPHTKKALEAHCR
CCCHHHHHHHHHHHH		60.4024816145
520PhosphorylationCRADELASQDGR---
HHHHHHHHCCCC---		41.2421460856
528 (in isoform 5)Phosphorylation-27251275
531UbiquitinationR--------------
C--------------		24816145
536Ubiquitination-------------------
-------------------		24816145
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
298SPhosphorylationKinasePRKAA1Q13131
GPS
336SPhosphorylationKinasePRKAA1Q13131
GPS
520SPhosphorylationKinaseATMQ13315
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of 2A5G_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 2A5G_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PP2AA_HUMANPPP2CAphysical
8703017
2AAB_HUMANPPP2R1Bphysical
8703017
CHK2_HUMANCHEK2physical
15380617
2AAA_HUMANPPP2R1Aphysical
15380617
PP2AA_HUMANPPP2CAphysical
15380617
MBP_HUMANMBPphysical
15380617
A4_HUMANAPPphysical
21832049
IEX1_HUMANIER3physical
16456541
PP2AA_HUMANPPP2CAphysical
16456541
PSMG3_HUMANPSMG3physical
22863883
SWP70_HUMANSWAP70physical
22863883
API5_HUMANAPI5physical
26344197
LSM6_HUMANLSM6physical
26344197
LSM7_HUMANLSM7physical
26344197
2AAA_HUMANPPP2R1Aphysical
26344197
2AAB_HUMANPPP2R1Bphysical
26344197
2ABA_HUMANPPP2R2Aphysical
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 2A5G_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-348; TYR-349 ANDTYR-354, AND MASS SPECTROMETRY.

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