ESA1_SCHPO - dbPTM
ESA1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ESA1_SCHPO
UniProt AC O94446
Protein Name Histone acetyltransferase mst1
Gene Name mst1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 463
Subcellular Localization Nucleus .
Protein Description Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z. Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, and histone H2A to form H2AK4ac and H2AK7ac. Acetylation of histone H4 is essential for DNA double-strand break repair through homologous recombination. Involved in cell cycle progression. Recruitment to promoters depends on H3K4me (By similarity)..
Protein Sequence MSNDVDDESKIETKSYEAKDIVYKSKVFAFKDGEYRKAEILMIQKRTRGVVYYVHYNDYNKRLDEWITIDNIDLSKGIEYPPPEKPKKAHGKGKSSKRPKAVDRRRSITAPSKTEPSTPSTEKPEPSTPSGESDHGSNAGNESLPLLEEDHKPESLSKEQEVERLRFSGSMVQNPHEIARIRNINKICIGDHEIEPWYFSPYPKEFSEVDIVYICSFCFCYYGSERQFQRHREKCTLQHPPGNEIYRDDYISFFEIDGRKQRTWCRNICLLSKLFLDHKMLYYDVDPFLFYCMCRRDEYGCHLVGYFSKEKESSENYNLACILTLPQYQRHGYGKLLIQFSYELTKREHKHGSPEKPLSDLGLISYRAYWAEQIINLVLGMRTETTIDELANKTSMTTNDVLHTLQALNMLKYYKGQFIICISDGIEQQYERLKNKKRRRINGDLLADWQPPVFHPSQLRFGW
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
107PhosphorylationKAVDRRRSITAPSKT
CHHCCCCCCCCCCCC
23.6029996109
279AcetylationSKLFLDHKMLYYDVD
HHHHHCCCCEEECCC
30.21-

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 ESA1_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ESA1_SCHPO !!

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 ESA1_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FAT1_SCHPObud6physical
18505873
CBH1_SCHPOcbh1physical
18505873
HIR1_SCHPOhip1physical
18505873
MSC1_SCHPOmsc1physical
18505873
RAD22_SCHPOrad52physical
18505873
RES2_SCHPOres2physical
18505873
SEC18_SCHPOsec18physical
18505873
SKB1_SCHPOskb1physical
18505873
T111_SCHPOtaf111physical
18505873
H2AZ_SCHPOpht1physical
19915592
MCM2_SCHPOmcm2genetic
18505873
MCM7_SCHPOmcm7genetic
18505873
ORC1_SCHPOorc1genetic
18505873
DPOA_SCHPOpol1genetic
18505873
HSK1_SCHPOhsk1genetic
18505873
RAD50_SCHPOrad50genetic
18505873
CLR3_SCHPOclr3genetic
18505873
CLR4_SCHPOclr4genetic
18505873
SWI6_SCHPOswi6genetic
18505873
ING1_SCHPOpng1physical
20299455
RAD22_SCHPOrad52genetic
20299455
ARP4_SCHPOalp5physical
15483052
EPL1_SCHPOepl1physical
23695164
EPL1_SCHPOepl1physical
26771498

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ESA1_SCHPO

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Related Literatures of Post-Translational Modification

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