2ABA_HUMAN - dbPTM
2ABA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID 2ABA_HUMAN
UniProt AC P63151
Protein Name Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
Gene Name PPP2R2A
Organism Homo sapiens (Human).
Sequence Length 447
Subcellular Localization
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 MAGAGGGNDIQWCFSQVKGAVDDDVAEADIISTVEFNHSGELLATGDKGGRVVIFQQEQENKIQSHSRGEYNVYSTFQSHEPEFDYLKSLEIEEKINKIRWLPQKNAAQFLLSTNDKTIKLWKISERDKRPEGYNLKEEDGRYRDPTTVTTLRVPVFRPMDLMVEASPRRIFANAHTYHINSISINSDYETYLSADDLRINLWHLEITDRSFNIVDIKPANMEELTEVITAAEFHPNSCNTFVYSSSKGTIRLCDMRASALCDRHSKLFEEPEDPSNRSFFSEIISSISDVKFSHSGRYMMTRDYLSVKIWDLNMENRPVETYQVHEYLRSKLCSLYENDCIFDKFECCWNGSDSVVMTGSYNNFFRMFDRNTKRDITLEASRENNKPRTVLKPRKVCASGKRKKDEISVDSLDFNKKILHTAWHPKENIIAVATTNNLYIFQDKVN
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------MAGAGGGND
------CCCCCCCCC		19.2822223895
33PhosphorylationAEADIISTVEFNHSG
HHCCEEEEEEECCCC		17.4120071362
62AcetylationFQQEQENKIQSHSRG
EECCCCCCCCCCCCC		41.1723236377
62UbiquitinationFQQEQENKIQSHSRG
EECCCCCCCCCCCCC		41.1721890473
62UbiquitinationFQQEQENKIQSHSRG
EECCCCCCCCCCCCC		41.1721890473
68MethylationNKIQSHSRGEYNVYS
CCCCCCCCCCCCHHH		36.22115488577
72UbiquitinationSHSRGEYNVYSTFQS
CCCCCCCCHHHCCCC		23.1921890473
72 (in isoform 2)Ubiquitination-23.19-
88AcetylationEPEFDYLKSLEIEEK
CCCCCCHHHHCHHHH		46.9220167786
88UbiquitinationEPEFDYLKSLEIEEK
CCCCCCHHHHCHHHH		46.9221890473
95UbiquitinationKSLEIEEKINKIRWL
HHHCHHHHHHHCCCC		38.50-
98AcetylationEIEEKINKIRWLPQK
CHHHHHHHCCCCCCC		36.8020167786
105AcetylationKIRWLPQKNAAQFLL
HCCCCCCCCHHHHHH		46.7625953088
105UbiquitinationKIRWLPQKNAAQFLL
HCCCCCCCCHHHHHH		46.7621890473
105UbiquitinationKIRWLPQKNAAQFLL
HCCCCCCCCHHHHHH		46.7621890473
115 (in isoform 2)Ubiquitination-45.46-
115UbiquitinationAQFLLSTNDKTIKLW
HHHHHCCCCCEEEEE		45.4621890473
117UbiquitinationFLLSTNDKTIKLWKI
HHHCCCCCEEEEEEE		54.9721890473
1172-HydroxyisobutyrylationFLLSTNDKTIKLWKI
HHHCCCCCEEEEEEE		54.97-
123UbiquitinationDKTIKLWKISERDKR
CCEEEEEEEECCCCC		46.95-
129UbiquitinationWKISERDKRPEGYNL
EEEECCCCCCCCCCC		75.8721890473
137UbiquitinationRPEGYNLKEEDGRYR
CCCCCCCCCCCCCCC		56.2521890473
143PhosphorylationLKEEDGRYRDPTTVT
CCCCCCCCCCCCCEE		25.5423917254
147PhosphorylationDGRYRDPTTVTTLRV
CCCCCCCCCEEEEEE		37.8820068231
148PhosphorylationGRYRDPTTVTTLRVP
CCCCCCCCEEEEEEE		22.6520068231
153PhosphorylationPTTVTTLRVPVFRPM
CCCEEEEEEEECCCH		28.7127642862
167PhosphorylationMDLMVEASPRRIFAN
HHEEEECCCCEEEEC		12.8721815630
230PhosphorylationEELTEVITAAEFHPN
HHHHHEEHHHHCCCC		25.6223879269
266PhosphorylationSALCDRHSKLFEEPE
HHHHHHHHHHHCCCC		31.7628348404
267UbiquitinationALCDRHSKLFEEPED
HHHHHHHHHHCCCCC		51.5821890473
267AcetylationALCDRHSKLFEEPED
HHHHHHHHHHCCCCC		51.5825953088
276PhosphorylationFEEPEDPSNRSFFSE
HCCCCCCCCCHHHHH		58.1425627689
277 (in isoform 2)Ubiquitination-49.34-
278MethylationEPEDPSNRSFFSEII
CCCCCCCCHHHHHHH		38.90115488585
279PhosphorylationPEDPSNRSFFSEIIS
CCCCCCCHHHHHHHH		34.5925627689
292UbiquitinationISSISDVKFSHSGRY
HHHHHCCEECCCCCE		46.25-
332UbiquitinationVHEYLRSKLCSLYEN
HHHHHHHHHHHHHCC		47.26-
335PhosphorylationYLRSKLCSLYENDCI
HHHHHHHHHHCCCCC		44.4127251275
355PhosphorylationCCWNGSDSVVMTGSY
EECCCCCEEEEECCC		20.50-
359PhosphorylationGSDSVVMTGSYNNFF
CCCEEEEECCCCCCE		16.03-
378PhosphorylationRNTKRDITLEASREN
CCCCCCEEEHHHHHC		23.8820068231
382PhosphorylationRDITLEASRENNKPR
CCEEEHHHHHCCCCC		30.6523401153
387UbiquitinationEASRENNKPRTVLKP
HHHHHCCCCCEEECC		47.67-
390PhosphorylationRENNKPRTVLKPRKV
HHCCCCCEEECCCEE		38.4228555341
397 (in isoform 2)Ubiquitination-3.30-
402AcetylationRKVCASGKRKKDEIS
CEECCCCCCCCCCEE		59.5615605981
404UbiquitinationVCASGKRKKDEISVD
ECCCCCCCCCCEEEC		68.9721890473
405UbiquitinationCASGKRKKDEISVDS
CCCCCCCCCCEEECC		65.70-
409PhosphorylationKRKKDEISVDSLDFN
CCCCCCEEECCCCCC		20.1620873877
412PhosphorylationKDEISVDSLDFNKKI
CCCEEECCCCCCHHH		27.9020873877
417AcetylationVDSLDFNKKILHTAW
ECCCCCCHHHHHHCC		40.9826051181
417UbiquitinationVDSLDFNKKILHTAW
ECCCCCCHHHHHHCC		40.9821890473
4172-HydroxyisobutyrylationVDSLDFNKKILHTAW
ECCCCCCHHHHHHCC		40.98-
418UbiquitinationDSLDFNKKILHTAWH
CCCCCCHHHHHHCCC		52.16-
440PhosphorylationVATTNNLYIFQDKVN
EEECCCEEEEECCCC		11.21-
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 2ABA_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of 2ABA_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 2ABA_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PP2AA_HUMANPPP2CAphysical
1328247
2AAB_HUMANPPP2R1Bphysical
1328247
4EBP1_HUMANEIF4EBP1physical
16899564
KS6B1_HUMANRPS6KB1physical
16899564
RRN3_HUMANRRN3physical
15004009
2ABD_HUMANPPP2R2Dphysical
19156129
CDCA4_HUMANCDCA4physical
19156129
SK2L2_HUMANSKIV2L2physical
19156129
TCPE_HUMANCCT5physical
19156129
TCPQ_HUMANCCT8physical
19156129
TCPB_HUMANCCT2physical
19156129
TCPD_HUMANCCT4physical
19156129
TCPH_HUMANCCT7physical
19156129
TBA4A_HUMANTUBA4Aphysical
19156129
TCPG_HUMANCCT3physical
19156129
TCPA_HUMANTCP1physical
19156129
2AAB_HUMANPPP2R1Bphysical
19156129
2AAA_HUMANPPP2R1Aphysical
19156129
PP2AB_HUMANPPP2CBphysical
19156129
PP2AA_HUMANPPP2CAphysical
19156129
FABP5_HUMANFABP5physical
19156129
DESP_HUMANDSPphysical
19156129
DSG1_HUMANDSG1physical
19156129
TCPZ_HUMANCCT6Aphysical
19156129
G3P_HUMANGAPDHphysical
19156129
PP2AA_HUMANPPP2CAphysical
22939629
HS74L_HUMANHSPA4Lphysical
22863883
NRDC_HUMANNRD1physical
22863883
PP2AA_HUMANPPP2CAphysical
26344197
PP2AB_HUMANPPP2CBphysical
26344197
2AAA_HUMANPPP2R1Aphysical
26344197
2AAB_HUMANPPP2R1Bphysical
26344197
FOXC1_HUMANFOXC1physical
26496610
FOXC2_HUMANFOXC2physical
26496610
VTDB_HUMANGCphysical
26496610
PP2AA_HUMANPPP2CAphysical
26496610
2AAA_HUMANPPP2R1Aphysical
26496610
2AAB_HUMANPPP2R1Bphysical
26496610
RS28_HUMANRPS28physical
26496610
SYYC_HUMANYARSphysical
26496610
RBM7_HUMANRBM7physical
26496610
RFIP5_HUMANRAB11FIP5physical
26496610
ECSIT_HUMANECSITphysical
26496610
CDCA4_HUMANCDCA4physical
26496610
F122A_HUMANFAM122Aphysical
26496610
FXL16_HUMANFBXL16physical
26496610
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 2ABA_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory