PHO_DROME - dbPTM
PHO_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PHO_DROME
UniProt AC Q8ST83
Protein Name Polycomb protein PHO
Gene Name pho
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 520
Subcellular Localization Nucleus .
Protein Description Polycomb group (PcG) protein that binds to the 5'-CNGCCATNNNNG-3' sequence found in the regulatory regions of many genes. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. They probably act via the methylation of histones, rendering chromatin heritably changed in its expressibility. Probably targets the Esc/E(z) complex to DNA. Necessary but not sufficient to recruit a functional PcG repressive complex that represses target genes, suggesting that the recruitment of the distinct PRC1 complex is also required to allow a subsequent repression.; Proposed core component of the chromatin remodeling Ino80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair..
Protein Sequence MAYERFGIILQSEQYDEDIGNTKVNQKMNEGNHYDLHRKNAFDRIIHSESKKGDNVINYNIHENDKIKAADNIFSSKLKMNPNMSYEMNINCFKNIGYGENQETSKVLTNSLSNNDINTEESGVVDKNSPFLTLGTTILNSNGKSRRWEQKLVHIKTMEGEFSVTMWASGISDDEYSGSDQIVGASDLLKGKEEFGIDGFTSQQNKEYQKMESKFTNAQTLEMPHPISSVQIMDHLIKERGNLSQENNISERILSKTTLSFEEPILLPDSSSIELVNETAAMTINNHRTLSNHTGNTGDLHALPSSVPFRIGLHEGQVNDCLSTISQSTHQDNTDSTGCGEMNLSEVTVSYTNDKKIACPHKGCNKHFRDSSAMRKHLHTHGPRVHVCAECGKAFVESSKLKRHQLVHTGEKPFQCTFEGCGKRFSLDFNLRTHVRIHTGDRPFVCPFDACNKKFAQSTNLKSHILTHAKAKRNTSISGKSGCSNAESNSQSEDTSANYVKVELQDSVTENHVPFVVYAD
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
337PhosphorylationHQDNTDSTGCGEMNL
CCCCCCCCCCCEEEC
39.0222668510
409PhosphorylationKRHQLVHTGEKPFQC
CCCCCCCCCCCCEEE
39.2919429919

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 PHO_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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 PHO_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A6_DROMEa6physical
14605208
INO80_DROMEIno80physical
16618800
SMBT_DROMESfmbtphysical
16618800
ARP5_DROMEArp5physical
16618800
ARP8_DROMEArp8physical
16618800
RUVB2_DROMEreptphysical
16618800
RUVB1_DROMEpontphysical
16618800
ACT1_DROMEAct5Cphysical
16618800
ESC_DROMEescphysical
11581156
ESC_DROMEescphysical
15175158
SMBT_DROMESfmbtphysical
21415365
SMBT_DROMESfmbtphysical
24186981
EZ_DROMEE(z)physical
11581156
EZ_DROMEE(z)physical
15175158
PC_DROMEPcphysical
11581156
PC_DROMEPcphysical
21415365
SF3B5_DROMECG11985physical
25242320
SOSSC_DROMECG42374physical
25242320

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

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Related Literatures of Post-Translational Modification

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