2ABB_HUMAN - dbPTM
2ABB_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID 2ABB_HUMAN
UniProt AC Q00005
Protein Name Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform
Gene Name PPP2R2B
Organism Homo sapiens (Human).
Sequence Length 443
Subcellular Localization Isoform 1: Cytoplasm. Cytoplasm, cytoskeleton. Membrane.
Isoform 2: Cytoplasm. Mitochondrion. Mitochondrion outer membrane. Under basal conditions, localizes to both cytosolic and mitochondrial compartments. Relocalizes from the cytosolic to the mit
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. Within the PP2A holoenzyme complex, isoform 2 is required to promote proapoptotic activity (By similarity). Isoform 2 regulates neuronal survival through the mitochondrial fission and fusion balance (By similarity)..
Protein Sequence MEEDIDTRKINNSFLRDHSYATEADIISTVEFNHTGELLATGDKGGRVVIFQREQESKNQVHRRGEYNVYSTFQSHEPEFDYLKSLEIEEKINKIRWLPQQNAAYFLLSTNDKTVKLWKVSERDKRPEGYNLKDEEGRLRDPATITTLRVPVLRPMDLMVEATPRRVFANAHTYHINSISVNSDYETYMSADDLRINLWNFEITNQSFNIVDIKPANMEELTEVITAAEFHPHHCNTFVYSSSKGTIRLCDMRASALCDRHTKFFEEPEDPSNRSFFSEIISSISDVKFSHSGRYIMTRDYLTVKVWDLNMENRPIETYQVHDYLRSKLCSLYENDCIFDKFECVWNGSDSVIMTGSYNNFFRMFDRNTKRDVTLEASRENSKPRAILKPRKVCVGGKRRKDEISVDSLDFSKKILHTAWHPSENIIAVAATNNLYIFQDKVN
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
6 (in isoform 4)Phosphorylation-53.4325072903
10 (in isoform 4)Phosphorylation-5.4925072903
20 (in isoform 2)Phosphorylation-17.70-
21 (in isoform 2)Phosphorylation-11.28-
22 (in isoform 2)Phosphorylation-24.39-
64UbiquitinationSKNQVHRRGEYNVYS
CCCCCCCCCCCCHHH		27.6723503661
67UbiquitinationQVHRRGEYNVYSTFQ
CCCCCCCCCHHHCCC		16.8629967540
71UbiquitinationRGEYNVYSTFQSHEP
CCCCCHHHCCCCCCC		20.6129901268
73UbiquitinationEYNVYSTFQSHEPEF
CCCHHHCCCCCCCCC		6.0423503661
75UbiquitinationNVYSTFQSHEPEFDY
CHHHCCCCCCCCCCC		26.1529967540
80UbiquitinationFQSHEPEFDYLKSLE
CCCCCCCCCCHHHHC		12.5329901268
84UbiquitinationEPEFDYLKSLEIEEK
CCCCCCHHHHCHHHH		46.9221906983
87UbiquitinationFDYLKSLEIEEKINK
CCCHHHHCHHHHHHH		56.2823503661
90UbiquitinationLKSLEIEEKINKIRW
HHHHCHHHHHHHCEE		65.9723503661
91UbiquitinationKSLEIEEKINKIRWL
HHHCHHHHHHHCEEC		38.50-
94UbiquitinationEIEEKINKIRWLPQQ
CHHHHHHHCEECCCC		36.8029901268
97UbiquitinationEKINKIRWLPQQNAA
HHHHHCEECCCCCEE		18.8329901268
115UbiquitinationLSTNDKTVKLWKVSE
EECCCCEEEEEEECC		6.2129967540
125UbiquitinationWKVSERDKRPEGYNL
EEECCCCCCCCCCCC		75.8721906983
142UbiquitinationEEGRLRDPATITTLR
CCCCCCCCCEEEEEE		25.5223503661
149UbiquitinationPATITTLRVPVLRPM
CCEEEEEECCCCCCC		28.7129901268
150UbiquitinationATITTLRVPVLRPMD
CEEEEEECCCCCCCC		4.2923503661
157UbiquitinationVPVLRPMDLMVEATP
CCCCCCCCEEEECCC		34.0029901268
190UbiquitinationSDYETYMSADDLRIN
CCCCEEECHHHEEEE		20.3823503661
197UbiquitinationSADDLRINLWNFEIT
CHHHEEEEEEEEEEC		32.35-
226PhosphorylationEELTEVITAAEFHPH
HHHHHHHHHHHCCCH		25.6223879269
231UbiquitinationVITAAEFHPHHCNTF
HHHHHHCCCHHCCEE		16.58-
268UbiquitinationHTKFFEEPEDPSNRS
CHHHCCCCCCCCCCH		44.0630230243
275PhosphorylationPEDPSNRSFFSEIIS
CCCCCCCHHHHHHHH		34.5925627689
277UbiquitinationDPSNRSFFSEIISSI
CCCCCHHHHHHHHHH		7.2630230243
291UbiquitinationISDVKFSHSGRYIMT
HHCCEECCCCCEEEE		37.0930230243
294UbiquitinationVKFSHSGRYIMTRDY
CEECCCCCEEEEECE		22.3330230243
295PhosphorylationKFSHSGRYIMTRDYL
EECCCCCEEEEECEE		9.89-
298PhosphorylationHSGRYIMTRDYLTVK
CCCCEEEEECEEEEE		15.72-
301PhosphorylationRYIMTRDYLTVKVWD
CEEEEECEEEEEEEE		10.86-
331PhosphorylationYLRSKLCSLYENDCI
HHHHHHHHHHCCCCC		44.4127251275
346UbiquitinationFDKFECVWNGSDSVI
CCCEEEEEECCCEEE		18.3530230243
354UbiquitinationNGSDSVIMTGSYNNF
ECCCEEEEECCCCCC		3.0430230243
393UbiquitinationAILKPRKVCVGGKRR
EEECCCEEEECCCCC		3.1829967540
394UbiquitinationILKPRKVCVGGKRRK
EECCCEEEECCCCCC		2.36-
401AcetylationCVGGKRRKDEISVDS
EECCCCCCCCCEECH		64.8426051181
402UbiquitinationVGGKRRKDEISVDSL
ECCCCCCCCCEECHH		57.5629967540
416UbiquitinationLDFSKKILHTAWHPS
HCCHHHHHHHHCCCC		3.9429967540
419UbiquitinationSKKILHTAWHPSENI
HHHHHHHHCCCCCCE		7.5729967540
434UbiquitinationIAVAATNNLYIFQDK
EEEEEECCEEEEECC		29.84-
437PhosphorylationAATNNLYIFQDKVN-
EEECCEEEEECCCC-		2.55-
437 (in isoform 7)Phosphorylation-2.5527251275
471Ubiquitination-----------------------------------
-----------------------------------		29967540
479Ubiquitination-------------------------------------------
-------------------------------------------		29967540
519Ubiquitination-----------------------------------------------------------------------------------
-----------------------------------------------------------------------------------		29967540
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 2ABB_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of 2ABB_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 2ABB_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MTCL1_HUMANMTCL1physical
19156129
SKA2_HUMANSKA2physical
19156129
SKA3_HUMANSKA3physical
19156129
SKA1_HUMANSKA1physical
19156129
F122A_HUMANFAM122Aphysical
19156129
SRTD4_HUMANSERTAD4physical
19156129
CDCA4_HUMANCDCA4physical
19156129
IER5_HUMANIER5physical
19156129
ZBT21_HUMANZBTB21physical
19156129
SK2L2_HUMANSKIV2L2physical
19156129
TCPE_HUMANCCT5physical
19156129
TCPQ_HUMANCCT8physical
19156129
TCPB_HUMANCCT2physical
19156129
TCPD_HUMANCCT4physical
19156129
TCPH_HUMANCCT7physical
19156129
TIF1B_HUMANTRIM28physical
19156129
BAG2_HUMANBAG2physical
19156129
DYL1_HUMANDYNLL1physical
19156129
ZN136_HUMANZNF136physical
19156129
TCPG_HUMANCCT3physical
19156129
TCPA_HUMANTCP1physical
19156129
S10A9_HUMANS100A9physical
19156129
PERI_HUMANPRPHphysical
19156129
PP4C_HUMANPPP4Cphysical
19156129
2AAB_HUMANPPP2R1Bphysical
19156129
2AAA_HUMANPPP2R1Aphysical
19156129
PP2AB_HUMANPPP2CBphysical
19156129
PP2AA_HUMANPPP2CAphysical
19156129
MYO9A_HUMANMYO9Aphysical
19156129
TCPZ_HUMANCCT6Aphysical
19156129
CAPZB_HUMANCAPZBphysical
19156129
ZCCHV_HUMANZC3HAV1physical
19156129
ZCHC8_HUMANZCCHC8physical
19156129
ATX2L_HUMANATXN2Lphysical
19156129
IER2_HUMANIER2physical
19156129
EFTU_HUMANTUFMphysical
19156129
2AAA_HUMANPPP2R1Aphysical
23135275
PP2AA_HUMANPPP2CAphysical
23135275
KLH15_HUMANKLHL15physical
23135275
CUL3_HUMANCUL3physical
23135275
PP2AB_HUMANPPP2CBphysical
26344197
2AAA_HUMANPPP2R1Aphysical
26344197
SYNEM_HUMANSYNMphysical
22337773
Drug and Disease Associations
Kegg Disease
H00063 Spinocerebellar ataxia (SCA); Machado-Joseph disease (SCA3)
OMIM Disease
604326Spinocerebellar ataxia 12 (SCA12)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of 2ABB_HUMAN

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