MESH1_HUMAN - dbPTM
MESH1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MESH1_HUMAN
UniProt AC Q8N4P3
Protein Name Guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase MESH1
Gene Name HDDC3
Organism Homo sapiens (Human).
Sequence Length 179
Subcellular Localization
Protein Description ppGpp hydrolyzing enzyme involved in starvation response..
Protein Sequence MGSEAAQLLEAADFAARKHRQQRRKDPEGTPYINHPIGVARILTHEAGITDIVVLQAALLHDTVEDTDTTLDEVELHFGAQVRRLVEEVTDDKTLPKLERKRLQVEQAPHSSPGAKLVKLADKLYNLRDLNRCTPEGWSEHRVQEYFEWAAQVVKGLQGTNRQLEEALKHLFKQRGLTI
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------MGSEAAQLL
------CCHHHHHHH
33.9119413330
3Phosphorylation-----MGSEAAQLLE
-----CCHHHHHHHH
23.82-
25UbiquitinationKHRQQRRKDPEGTPY
HHHHHHHCCCCCCCC
78.7224816145
25MalonylationKHRQQRRKDPEGTPY
HHHHHHHCCCCCCCC
78.7226320211
25AcetylationKHRQQRRKDPEGTPY
HHHHHHHCCCCCCCC
78.7219608861
90PhosphorylationRRLVEEVTDDKTLPK
HHHHHHHCCCCCCCH
41.5819664994
93AcetylationVEEVTDDKTLPKLER
HHHHCCCCCCCHHHH
55.5623954790
93UbiquitinationVEEVTDDKTLPKLER
HHHHCCCCCCCHHHH
55.5624816145
932-HydroxyisobutyrylationVEEVTDDKTLPKLER
HHHHCCCCCCCHHHH
55.56-
93MalonylationVEEVTDDKTLPKLER
HHHHCCCCCCCHHHH
55.5626320211
97AcetylationTDDKTLPKLERKRLQ
CCCCCCCHHHHHCCH
67.1219608861
97MalonylationTDDKTLPKLERKRLQ
CCCCCCCHHHHHCCH
67.1226320211
119UbiquitinationSPGAKLVKLADKLYN
CCCHHHHHHHHHHHC
48.6822817900
123AcetylationKLVKLADKLYNLRDL
HHHHHHHHHHCCHHH
47.4619608861
123UbiquitinationKLVKLADKLYNLRDL
HHHHHHHHHHCCHHH
47.4622817900
1232-HydroxyisobutyrylationKLVKLADKLYNLRDL
HHHHHHHHHHCCHHH
47.46-
123 (in isoform 1)Ubiquitination-47.4621890473
123 (in isoform 2)Ubiquitination-47.4621890473

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 MESH1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MESH1_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 MESH1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
VATC1_HUMANATP6V1C1physical
26344197

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 MESH1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-25; LYS-97 AND LYS-123, ANDMASS SPECTROMETRY.

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