SUZ12_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SUZ12_DROME
• UniProt AC: Q9NJG9
• Protein Name: Polycomb protein Su(z)12
• Gene Name: Su(z)12
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 900
• Subcellular Localization: Nucleus.
• Protein Description: Polycomb group (PcG) protein. While PcG proteins are generally required to maintain the transcriptionally repressive state of homeotic genes throughout development, this protein is specifically required during the first 6 hours of embryogenesis to establish the repressed state. Component of the Esc/E(z) complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. The Esc/E(z) complex is necessary but not sufficient for the repression of homeotic target genes, suggesting that the recruitment of the distinct PRC1 complex is also required..
• Protein Sequence: MAPAKKREKDSNPDGSAANGIIGLTHGAPDASNAGSTVPPTAEGQVKLNGHQQEQELFLQAFEKPTQIYRYLRNRHETNPIFLNRTLSYMKERMSRNNKKRISFQVNSMLESITQKSEAVSQNYLHVIYDSLHEKLPARLDNESGEDLLQEQLLCEAGESVSVETTLYKITRSKRKDSTLDFQELLSKCSQIVYNPKDRVGEHATISIPLQTMRPMGEQHTLYKLLFRIKVLSPSTCNDENAETPPNKRSRPNEKMFGSELILYEKSSGFITEGEYEAMLQPLNSTSIKSFSPKKCTWETMPDSYIPLSLTYDVYQQSPMLKFHLTLSNEQLPEMISAPELQRYVQHLDAVAEMNYNNNNYNNNNNCSGLKNGSGGGNSTVCKTTPEHIQIVYNFMYSNNTRQQTEYTQELNCPWCGLDCLRLYALLKHLKLCHARFNFTYQPAGSGARIDVTINDAYDGSYAGSPYDLAGPSGSSFARTCGPVRRTSVTSLMVCRPRRQKTCLDEFLELDEDEISNQRSYITGHNRLYHHTETCLPVHPKELDIDSEGESDPLWLRQKTIQMIDEFSDVNEGEKELMKLWNLHVMRHGFVGDCQLPIACEMFLDAKGTEIVRKNLYRNFILHMCSLFDYGLIAAETVYKTVQKLQGLLSKYAAGQELMQRQREEQLKYWLDVGMHKKQEDPKTLKSPQKPAPPADQASTSSASTSGSGSGSSSMQPPKRMPAHLKRGSAASSPGVQSKGTENGTNGSNSSSSNSKNVAKKSADQPLSTLANTRERRSEYGQKRNVSGSRLAATPASKRKLSSKDNTVLNKRQRYSDGSPGTGIGNGHGGGSGSGANRNKSNNHSLPATSNNASSSSSNSKRAIARRRSTSERTKASGSTGGGAGGVRTRLSVPAKYERR

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
244	Phosphorylation	CNDENAETPPNKRSR CCCCCCCCCCCCCCC	41.45	27626673
547	Phosphorylation	PKELDIDSEGESDPL CHHCCCCCCCCCCCH	48.08	21082442
729	Phosphorylation	PAHLKRGSAASSPGV CCHHHCCCCCCCCCC	25.37	21082442
733	Phosphorylation	KRGSAASSPGVQSKG HCCCCCCCCCCCCCC	22.43	21082442
778	Phosphorylation	ANTRERRSEYGQKRN HHHHHHHHHHHCCCC	41.20	22817900
819	Phosphorylation	RQRYSDGSPGTGIGN CCCCCCCCCCCCCCC	25.75	30478224

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of SUZ12_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SUZ12_DROME !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of SUZ12_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EZ_DROME	E(z)	physical	12697833
HDAC1_DROME	Rpd3	physical	12697833
PCL_DROME	Pcl	physical	12697833
EZ_DROME	E(z)	physical	12408864
ESC_DROME	esc	physical	12408864
PIWI_DROME	piwi	physical	26780607
ESC_DROME	esc	physical	15776017
EZ_DROME	E(z)	physical	15776017
EZ_DROME	E(z)	physical	22493065
CAF1_DROME	Caf1	physical	15776017
CAF1_DROME	Caf1	physical	21550984

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells.";
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
Mol. Biosyst. 3:275-286(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-547, AND MASSSPECTROMETRY.
PubMed: 17372656