PDP2_HUMAN - dbPTM
PDP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PDP2_HUMAN
UniProt AC Q9P2J9
Protein Name [Pyruvate dehydrogenase [acetyl-transferring]]-phosphatase 2, mitochondrial
Gene Name PDP2
Organism Homo sapiens (Human).
Sequence Length 529
Subcellular Localization Mitochondrion matrix.
Protein Description Catalyzes the dephosphorylation and concomitant reactivation of the alpha subunit of the E1 component of the pyruvate dehydrogenase complex..
Protein Sequence MSSTVSYWILNSTRNSIATLQGGRRLYSRYVSNRNKLKWRLFSRVPPTLNSSPCGGFTLCKAYRHTSTEEDDFHLQLSPEQINEVLRAGETTHKILDLESRVPNSVLRFESNQLAANSPVEDRRGVASCLQTNGLMFGIFDGHGGHACAQAVSERLFYYVAVSLMSHQTLEHMEGAMESMKPLLPILHWLKHPGDSIYKDVTSVHLDHLRVYWQELLDLHMEMGLSIEEALMYSFQRLDSDISLEIQAPLEDEVTRNLSLQVAFSGATACMAHVDGIHLHVANAGDCRAILGVQEDNGMWSCLPLTRDHNAWNQAELSRLKREHPESEDRTIIMEDRLLGVLIPCRAFGDVQLKWSKELQRSILERGFNTEALNIYQFTPPHYYTPPYLTAEPEVTYHRLRPQDKFLVLASDGLWDMLSNEDVVRLVVGHLAEADWHKTDLAQRPANLGLMQSLLLQRKASGLHEADQNAATRLIRHAIGNNEYGEMEAERLAAMLTLPEDLARMYRDDITVTVVYFNSESIGAYYKGG
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------MSSTVSYWI
------CCCCCEEEH
34.4123663014
3Phosphorylation-----MSSTVSYWIL
-----CCCCCEEEHH
31.3723663014
4Phosphorylation----MSSTVSYWILN
----CCCCCEEEHHH
13.2323663014
6Phosphorylation--MSSTVSYWILNST
--CCCCCEEEHHHCC
18.1623663014
7Phosphorylation-MSSTVSYWILNSTR
-CCCCCEEEHHHCCC
7.6723663014
12PhosphorylationVSYWILNSTRNSIAT
CEEEHHHCCCCEEEE
25.8725404012
13PhosphorylationSYWILNSTRNSIATL
EEEHHHCCCCEEEEH
32.5629759185
28PhosphorylationQGGRRLYSRYVSNRN
HCCHHHHHHHHCCCC
23.0224719451
32PhosphorylationRLYSRYVSNRNKLKW
HHHHHHHCCCCCCCE
22.5730631047
43PhosphorylationKLKWRLFSRVPPTLN
CCCEEECCCCCCCCC
36.64-
58PhosphorylationSSPCGGFTLCKAYRH
CCCCCCEEEEEEECC
34.22-
66PhosphorylationLCKAYRHTSTEEDDF
EEEEECCCCCCCCCC
28.4826471730
67PhosphorylationCKAYRHTSTEEDDFH
EEEECCCCCCCCCCE
27.9125884760
68PhosphorylationKAYRHTSTEEDDFHL
EEECCCCCCCCCCEE
44.5426471730
94UbiquitinationRAGETTHKILDLESR
HCCCCCHHHHCCHHC
42.76-
357UbiquitinationDVQLKWSKELQRSIL
CCCHHHCHHHHHHHH
62.42-
438UbiquitinationLAEADWHKTDLAQRP
HHHCCHHCCCHHHCC
39.2121890473
459UbiquitinationQSLLLQRKASGLHEA
HHHHHHHHHCCCCHH
33.6620972266

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 PDP2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PDP2_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 PDP2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AFG32_HUMANAFG3L2physical
27880917
CLPX_HUMANCLPXphysical
27880917
UBR2_HUMANUBR2physical
27880917
YMEL1_HUMANYME1L1physical
27880917

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 PDP2_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP