2ABG_HUMAN - dbPTM
2ABG_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID 2ABG_HUMAN
UniProt AC Q9Y2T4
Protein Name Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B gamma isoform
Gene Name PPP2R2C
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 MGEDTDTRKINHSFLRDHSYVTEADIISTVEFNHTGELLATGDKGGRVVIFQREPESKNAPHSQGEYDVYSTFQSHEPEFDYLKSLEIEEKINKIKWLPQQNAAHSLLSTNDKTIKLWKITERDKRPEGYNLKDEEGKLKDLSTVTSLQVPVLKPMDLMVEVSPRRIFANGHTYHINSISVNSDCETYMSADDLRINLWHLAITDRSFNIVDIKPANMEDLTEVITASEFHPHHCNLFVYSSSKGSLRLCDMRAAALCDKHSKLFEEPEDPSNRSFFSEIISSVSDVKFSHSGRYMLTRDYLTVKVWDLNMEARPIETYQVHDYLRSKLCSLYENDCIFDKFECAWNGSDSVIMTGAYNNFFRMFDRNTKRDVTLEASRESSKPRAVLKPRRVCVGGKRRRDDISVDSLDFTKKILHTAWHPAENIIAIAATNNLYIFQDKVNSDMH
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
46UbiquitinationLATGDKGGRVVIFQR
EEECCCCCEEEEEEC
25.5824816145
67UbiquitinationAPHSQGEYDVYSTFQ
CCCCCCCCCHHHCCC
19.9623503661
70UbiquitinationSQGEYDVYSTFQSHE
CCCCCCHHHCCCCCC
10.0923503661
74UbiquitinationYDVYSTFQSHEPEFD
CCHHHCCCCCCCCCC
43.9229901268
77UbiquitinationYSTFQSHEPEFDYLK
HHCCCCCCCCCCHHH
52.3429901268
84UbiquitinationEPEFDYLKSLEIEEK
CCCCCHHHHHCHHHH
46.9229901268
91UbiquitinationKSLEIEEKINKIKWL
HHHCHHHHHHHCCCC
38.5029901268
108 (in isoform 3)Ubiquitination-7.1321906983
108UbiquitinationQNAAHSLLSTNDKTI
CCHHHHHHCCCCCEE
7.1324816145
125UbiquitinationWKITERDKRPEGYNL
EEEECCCCCCCCCCC
75.8721906983
125 (in isoform 2)Ubiquitination-75.8721906983
125 (in isoform 1)Ubiquitination-75.8721906983
246 (in isoform 3)Ubiquitination-17.6621906983
246UbiquitinationVYSSSKGSLRLCDMR
EEECCCCCEEECHHH
17.6624816145
249UbiquitinationSSKGSLRLCDMRAAA
CCCCCEEECHHHHHH
3.3524816145
256UbiquitinationLCDMRAAALCDKHSK
ECHHHHHHHHHHHHH
14.0324816145
263UbiquitinationALCDKHSKLFEEPED
HHHHHHHHHCCCCCC
57.8424816145
263 (in isoform 2)Ubiquitination-57.8421906983
263 (in isoform 1)Ubiquitination-57.8421906983
272PhosphorylationFEEPEDPSNRSFFSE
CCCCCCCCCCHHHHH
58.1425627689
318PhosphorylationMEARPIETYQVHDYL
CCCCCCEEECHHHHH
21.70-
328UbiquitinationVHDYLRSKLCSLYEN
HHHHHHHHHHHHHCC
47.26-
331PhosphorylationYLRSKLCSLYENDCI
HHHHHHHHHHCCCCC
44.4127251275
349PhosphorylationFECAWNGSDSVIMTG
CEECCCCCCCEEEEC
24.4122210691
351PhosphorylationCAWNGSDSVIMTGAY
ECCCCCCCEEEECCC
18.4222210691
374PhosphorylationRNTKRDVTLEASRES
CCCCCCEEHHHHHHC
24.1429083192
378PhosphorylationRDVTLEASRESSKPR
CCEEHHHHHHCCCCC
27.4929083192
381PhosphorylationTLEASRESSKPRAVL
EHHHHHHCCCCCEEE
42.4229083192
382PhosphorylationLEASRESSKPRAVLK
HHHHHHCCCCCEEEC
41.7629083192
389AcetylationSKPRAVLKPRRVCVG
CCCCEEECCCEEEEC
29.8526051181
405PhosphorylationKRRRDDISVDSLDFT
CCCCCCCCCCHHHCH
27.2016674116
408PhosphorylationRDDISVDSLDFTKKI
CCCCCCCHHHCHHHH
27.9016674116

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 2ABG_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of 2ABG_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 2ABG_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TCPA_HUMANTCP1physical
18782753
TCPB_HUMANCCT2physical
18782753
2AAA_HUMANPPP2R1Aphysical
18782753
TCPZ_HUMANCCT6Aphysical
18782753
TCPE_HUMANCCT5physical
18782753
TCPH_HUMANCCT7physical
18782753
TCPD_HUMANCCT4physical
18782753
TCPQ_HUMANCCT8physical
18782753
TCPG_HUMANCCT3physical
18782753
PP2AA_HUMANPPP2CAphysical
18782753
2AAB_HUMANPPP2R1Bphysical
18782753
TCPZ_HUMANCCT6Aphysical
19156129
CDCA4_HUMANCDCA4physical
19156129
TCPE_HUMANCCT5physical
19156129
TCPQ_HUMANCCT8physical
19156129
TCPB_HUMANCCT2physical
19156129
TCPD_HUMANCCT4physical
19156129
TCPH_HUMANCCT7physical
19156129
BAG2_HUMANBAG2physical
19156129
TCPG_HUMANCCT3physical
19156129
TCPA_HUMANTCP1physical
19156129
2ABB_HUMANPPP2R2Bphysical
19156129
2AAB_HUMANPPP2R1Bphysical
19156129
2AAA_HUMANPPP2R1Aphysical
19156129
PP2AA_HUMANPPP2CAphysical
19156129
MPCP_HUMANSLC25A3physical
19156129
CH60_HUMANHSPD1physical
19156129
TCPG_HUMANCCT3physical
26186194
TCPZ_HUMANCCT6Aphysical
26186194
TCPB_HUMANCCT2physical
26186194
TCPH_HUMANCCT7physical
26186194
RPC1_HUMANPOLR3Aphysical
26186194
SIK2_HUMANSIK2physical
26186194
TCPA_HUMANTCP1physical
26186194
IQGA1_HUMANIQGAP1physical
26186194
2AAB_HUMANPPP2R1Bphysical
26186194
2AAA_HUMANPPP2R1Aphysical
26186194
STRN_HUMANSTRNphysical
26186194
STRN3_HUMANSTRN3physical
26186194
STRN4_HUMANSTRN4physical
26186194
2ABB_HUMANPPP2R2Bphysical
26186194
ZCHC8_HUMANZCCHC8physical
26186194
PP2AA_HUMANPPP2CAphysical
26186194
PHLP_HUMANPDCLphysical
26186194
SKA1_HUMANSKA1physical
26186194
RBM7_HUMANRBM7physical
26186194
ZN746_HUMANZNF746physical
26186194
SKA3_HUMANSKA3physical
26186194
F122B_HUMANFAM122Bphysical
26186194
DCA10_HUMANDCAF10physical
26186194
IER5_HUMANIER5physical
26186194
MTCL1_HUMANMTCL1physical
26186194
F122A_HUMANFAM122Aphysical
26186194
SRTD4_HUMANSERTAD4physical
26186194
CDCA4_HUMANCDCA4physical
26186194
REPI1_HUMANREPIN1physical
26186194
SIK2_HUMANSIK2physical
24841198
2AAA_HUMANPPP2R1Aphysical
24841198
PP2AA_HUMANPPP2CAphysical
24841198
SKA3_HUMANSKA3physical
28514442
CDCA4_HUMANCDCA4physical
28514442
SRTD4_HUMANSERTAD4physical
28514442
F122B_HUMANFAM122Bphysical
28514442
2ABB_HUMANPPP2R2Bphysical
28514442
SIK2_HUMANSIK2physical
28514442
ZN746_HUMANZNF746physical
28514442
PP2AA_HUMANPPP2CAphysical
28514442
IER5_HUMANIER5physical
28514442
MTCL1_HUMANMTCL1physical
28514442
F122A_HUMANFAM122Aphysical
28514442
2AAB_HUMANPPP2R1Bphysical
28514442
TCPB_HUMANCCT2physical
28514442
RBM7_HUMANRBM7physical
28514442
REPI1_HUMANREPIN1physical
28514442
TCPH_HUMANCCT7physical
28514442
DCA10_HUMANDCAF10physical
28514442
SKA1_HUMANSKA1physical
28514442
TCPZ_HUMANCCT6Aphysical
28514442
TCPG_HUMANCCT3physical
28514442
TCPA_HUMANTCP1physical
28514442
2AAA_HUMANPPP2R1Aphysical
28514442
TCPE_HUMANCCT5physical
28514442
ZCHC8_HUMANZCCHC8physical
28514442

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 2ABG_HUMAN

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Related Literatures of Post-Translational Modification

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