SGF11_DROME - dbPTM
SGF11_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SGF11_DROME
UniProt AC Q9VVR6
Protein Name SAGA-associated factor 11 homolog {ECO:0000255|HAMAP-Rule:MF_03047}
Gene Name Sgf11 {ECO:0000255|HAMAP-Rule:MF_03047}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 196
Subcellular Localization Nucleus, nucleoplasm . Nucleus, nuclear pore complex . Cytoplasm . Localizes to nuclear periphery, in contact with the nuclear pore complex (NPC).
Protein Description Component of the transcription regulatory histone acetylation (HAT) complex SAGA, a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates histone H2B. The SAGA complex is recruited to specific gene promoters by activators, where it is required for transcription. Required for nuclear receptor-mediated transactivation. Binds independently on SAGA to promoters in an RNA-dependent manner. Binds to mRNA and is essential for total mRNA export from the nucleus. Required to counteract heterochromatin silencing. Controls the development of neuronal connectivity in visual system by being required for accurate axon targeting in the optic lobe. Required for expression of ecdysone-induced genes such as br/broad..
Protein Sequence MSAANMPTTTGAQGSGNQVPTTSTTIVNHFRELIKEPKNLDEAANYLYQSLLDDAVVGIFNETHHLRKSGNLAALDGVPEDSTYRMCEMPNLDIFGISTAKKPMDCTCPNCDRLVAAARFAPHLEKCMGMGRISSRIASRRLATKEGATSAHLHSSGNTGGTDDEDDVDWSSDKRRKKSNQNSRNNGSKKNNGKTF
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
162PhosphorylationSSGNTGGTDDEDDVD
CCCCCCCCCCCCCCC
41.4422817900
172PhosphorylationEDDVDWSSDKRRKKS
CCCCCCCHHHHHHHC
42.7818327897

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 SGF11_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SGF11_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 SGF11_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ENY2B_DROMEe(y)2bphysical
14605208
RS13_DROMERpS13physical
14605208
NDKA_DROMEawdphysical
14605208
RLA2_DROMERpLP2physical
14605208
CH15_DROMECp15physical
14605208
PP2A_DROMEmtsphysical
14605208
GBLP_DROMERack1physical
14605208
RS29_DROMERpS29physical
14605208
CSN2_DROMEalienphysical
14605208
TAD2B_DROMEAda2bphysical
18188155
UBIQP_DROMEUbi-p63Ephysical
24493646
NOT_DROMEnotphysical
24493646
ENY2_DROMEe(y)2physical
24493646
TBB1_DROMEbetaTub56Dphysical
22989713
RAS2_DROMERas64Bphysical
22989713
NOT_DROMEnotphysical
22989713
XMAS2_DROMExmas-2physical
22989713
NCBP1_DROMECbp80physical
22989713
HSP71_DROMEHsp70Abphysical
22989713
HSP70_DROMEHsp70Abphysical
22989713
HSP72_DROMEHsp70Baphysical
22989713
ENY2_DROMEe(y)2physical
22989713
HSP75_DROMEHsp70Bbphysical
22989713
HSP73_DROMEHsp70Bbphysical
22989713
HSP74_DROMEHsp70Bbbphysical
22989713

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SGF11_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, AND MASSSPECTROMETRY.

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