PPP6_HUMAN - dbPTM
PPP6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PPP6_HUMAN
UniProt AC O00743
Protein Name Serine/threonine-protein phosphatase 6 catalytic subunit
Gene Name PPP6C
Organism Homo sapiens (Human).
Sequence Length 305
Subcellular Localization Mitochondrion . Cytoplasm .
Protein Description Catalytic subunit of protein phosphatase 6 (PP6). PP6 is a component of a signaling pathway regulating cell cycle progression in response to IL2 receptor stimulation. N-terminal domain restricts G1 to S phase progression in cancer cells, in part through control of cyclin D1. Downregulates MAP3K7 kinase activation of the IL1 signaling pathway by dephosphorylation of MAP3K7. Participates also in the innate immune defense against viruses by desphosphorylating RIG-I/DDX58, an essential step that triggers RIG-I/DDX58-mediated signaling activation..
Protein Sequence MAPLDLDKYVEIARLCKYLPENDLKRLCDYVCDLLLEESNVQPVSTPVTVCGDIHGQFYDLCELFRTGGQVPDTNYIFMGDFVDRGYYSLETFTYLLALKAKWPDRITLLRGNHESRQITQVYGFYDECQTKYGNANAWRYCTKVFDMLTVAALIDEQILCVHGGLSPDIKTLDQIRTIERNQEIPHKGAFCDLVWSDPEDVDTWAISPRGAGWLFGAKVTNEFVHINNLKLICRAHQLVHEGYKFMFDEKLVTVWSAPNYCYRCGNIASIMVFKDVNTREPKLFRAVPDSERVIPPRTTTPYFL
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-------MAPLDLDK
-------CCCCCHHH
8.6022814378
8UbiquitinationMAPLDLDKYVEIARL
CCCCCHHHHHHHHHH
59.5021890473
8 (in isoform 2)Ubiquitination-59.5021890473
8 (in isoform 1)Ubiquitination-59.5021890473
8UbiquitinationMAPLDLDKYVEIARL
CCCCCHHHHHHHHHH
59.5021890473
8 (in isoform 3)Ubiquitination-59.50-
17UbiquitinationVEIARLCKYLPENDL
HHHHHHHHHCCHHHH
55.18-
17AcetylationVEIARLCKYLPENDL
HHHHHHHHHCCHHHH
55.1826051181
17 (in isoform 3)Ubiquitination-55.18-
18PhosphorylationEIARLCKYLPENDLK
HHHHHHHHCCHHHHH
26.8826437602
25AcetylationYLPENDLKRLCDYVC
HCCHHHHHHHHHHHH
46.3025953088
25UbiquitinationYLPENDLKRLCDYVC
HCCHHHHHHHHHHHH
46.30-
111MethylationPDRITLLRGNHESRQ
CCCEEEECCCCCHHH
47.16115488633
120PhosphorylationNHESRQITQVYGFYD
CCCHHHHHEEEEECH
12.0230631047
123PhosphorylationSRQITQVYGFYDECQ
HHHHHEEEEECHHHH
7.5330631047
131PhosphorylationGFYDECQTKYGNANA
EECHHHHHHCCCCHH
37.5830631047
132UbiquitinationFYDECQTKYGNANAW
ECHHHHHHCCCCHHH
25.8621906983
178PhosphorylationKTLDQIRTIERNQEI
HHHHHHHCHHHCCCC
28.9028348404
188UbiquitinationRNQEIPHKGAFCDLV
HCCCCCCCCCCCCEE
46.72-
192GlutathionylationIPHKGAFCDLVWSDP
CCCCCCCCCEEECCH
3.8122555962
197PhosphorylationAFCDLVWSDPEDVDT
CCCCEEECCHHHCCC
35.4928464451
208PhosphorylationDVDTWAISPRGAGWL
HCCCEEECCCCCCCC
10.78-
209 (in isoform 2)Ubiquitination-32.3921890473
219UbiquitinationAGWLFGAKVTNEFVH
CCCCCCEEEECCEEE
50.39-
231 (in isoform 1)Ubiquitination-37.6221890473
231AcetylationFVHINNLKLICRAHQ
EEEECHHHHHHHHHH
37.6226051181
231UbiquitinationFVHINNLKLICRAHQ
EEEECHHHHHHHHHH
37.622189047
234PhosphorylationINNLKLICRAHQLVH
ECHHHHHHHHHHHHH
4.5727251275
244PhosphorylationHQLVHEGYKFMFDEK
HHHHHCCCCCCCCCC
9.6928102081
245AcetylationQLVHEGYKFMFDEKL
HHHHCCCCCCCCCCE
41.0126051181
245UbiquitinationQLVHEGYKFMFDEKL
HHHHCCCCCCCCCCE
41.01-
254PhosphorylationMFDEKLVTVWSAPNY
CCCCCEEEEECCCCC
27.0520068231
257PhosphorylationEKLVTVWSAPNYCYR
CCEEEEECCCCCCCC
29.5220068231
261PhosphorylationTVWSAPNYCYRCGNI
EEECCCCCCCCCCCE
6.9820090780
263PhosphorylationWSAPNYCYRCGNIAS
ECCCCCCCCCCCEEE
9.8920068231
268UbiquitinationYCYRCGNIASIMVFK
CCCCCCCEEEEEEEE
1.6121890473
268 (in isoform 3)Ubiquitination-1.61-
275AcetylationIASIMVFKDVNTREP
EEEEEEEECCCCCCC
49.7226051181
283UbiquitinationDVNTREPKLFRAVPD
CCCCCCCCEEEECCC
56.35-
301PhosphorylationVIPPRTTTPYFL---
CCCCCCCCCCCC---
18.51-

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 PPP6_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PPP6_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 PPP6_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
IGBP1_HUMANIGBP1physical
9647778
PP6R3_HUMANPPP6R3physical
21187329
PP6R1_HUMANPPP6R1physical
21187329
PP6R2_HUMANPPP6R2physical
21187329
ANR52_HUMANANKRD52physical
21187329
ANR28_HUMANANKRD28physical
21187329
ANR44_HUMANANKRD44physical
21187329
PRKDC_HUMANPRKDCphysical
20065038
PP6R1_HUMANPPP6R1physical
20065038
PP6R2_HUMANPPP6R2physical
20065038
PP6R3_HUMANPPP6R3physical
20065038
M3K7_HUMANMAP3K7physical
19955178
TAB2_HUMANTAB2physical
19955178
PP6R3_HUMANPPP6R3physical
22939629
M3K7_HUMANMAP3K7physical
17079228
ANR28_HUMANANKRD28physical
24255178
ANR44_HUMANANKRD44physical
24255178
ANR52_HUMANANKRD52physical
24255178
ARHG2_HUMANARHGEF2physical
24255178
IGBP1_HUMANIGBP1physical
24255178
PP6R1_HUMANPPP6R1physical
24255178
PP6R2_HUMANPPP6R2physical
24255178
PP6R3_HUMANPPP6R3physical
24255178
PRKDC_HUMANPRKDCphysical
24255178
TIPRL_HUMANTIPRLphysical
24255178
TBB6_HUMANTUBB6physical
24255178
ACLY_HUMANACLYphysical
22863883
KC1D_HUMANCSNK1Dphysical
23864707
ZNRF2_HUMANZNRF2physical
27244671
ANR28_HUMANANKRD28physical
27880917
ANR52_HUMANANKRD52physical
27880917
ARHG2_HUMANARHGEF2physical
27880917
IGBP1_HUMANIGBP1physical
27880917
K2C8_HUMANKRT8physical
27880917
PP6R1_HUMANPPP6R1physical
27880917
PP6R2_HUMANPPP6R2physical
27880917
PP6R3_HUMANPPP6R3physical
27880917
TIPRL_HUMANTIPRLphysical
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 PPP6_HUMAN

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Related Literatures of Post-Translational Modification

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