CCNB_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CCNB_DROME
• UniProt AC: P20439
• Protein Name: G2/mitotic-specific cyclin-B
• Gene Name: CycB
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 530
• Protein Description: Essential for the control of the cell cycle at the G2/M (mitosis) transition..
• Protein Sequence: MVGTTLKMRGDENASENFKQVQLKKLTVPSMEATTKRAALGDLQNRGISRPIAAKDAAQKDSKDLKLTDALRNAKARVDSHWKKQPLGSTNGNGNGAVPPKVNEGGVSAFLRSNSVRNRVPTKTTVEPTKVTVKSSSSENVNEPTLKREDSNLSKKSLTKLRAALAKPVMGVSGIRREPVAVSRKEAETKKELPETKKDSLEVKKDATRMPLIRGNSAVTTTTSTMPTTMSLSSKRLAGIEDIDANDKENLVLVSEYVNDIYDYLYQVELEQPIHKDHLAGQKEVSHKMRAVLIDWINEVHLQFHLAAETFQLAVAIIDRYLQVVKDTKRTYLQLVGVTALFIATKYEELFPPAIGDFVFITDDTYTARQIRQMELQIFKAIDCNLSRPLPIHFLRRYSKAAGAEDEHHTMSKYFIELASVDYEMATYRPSEIAAASLFLSLHLLNGNHRAGTGFNDRHWTPTLTFYSRYSAAHLRPITRLIAKLARDAPQAKLKAIYNKYQGSKFQKIALRTELTGALMDSIVGQSQRK

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
135	Phosphorylation	PTKVTVKSSSSENVN CEEEEECCCCCCCCC	30.99	19429919
136	Phosphorylation	TKVTVKSSSSENVNE EEEEECCCCCCCCCC	31.97	19429919
137	Phosphorylation	KVTVKSSSSENVNEP EEEECCCCCCCCCCC	49.08	19429919
138	Phosphorylation	VTVKSSSSENVNEPT EEECCCCCCCCCCCC	34.83	29892262
145	Phosphorylation	SENVNEPTLKREDSN CCCCCCCCCCHHCCC	38.44	25749252
151	Phosphorylation	PTLKREDSNLSKKSL CCCCHHCCCCCHHHH	34.61	19429919
200	Phosphorylation	LPETKKDSLEVKKDA CCCCHHHCCCCCCCC	35.00	19429919
217	Phosphorylation	MPLIRGNSAVTTTTS CCEEECCCCEEECCC	27.26	25749252
229	Phosphorylation	TTSTMPTTMSLSSKR CCCCCCCEECCCCCC	10.01	21082442

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
-	K	Ubiquitination	E3 ubiquitin ligase	fzy	Q24044	PMID:22199232

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CCNB_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 CCNB_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FD3_DROME	fd59A	physical	14605208
MSIR6_DROME	Rbp6	physical	15575970
CDK1_DROME	cdc2	physical	22036573
CKS1_DROME	Cks30A	physical	22036573
CCNB3_DROME	CycB3	physical	22036573
RUX_DROME	rux	physical	22036573
SQH_DROME	sqh	genetic	12454065
CDC42_DROME	Cdc42	genetic	12454065
PROF_DROME	chic	genetic	12454065
CDK1_DROME	cdc2	genetic	11369230
CDK1_DROME	cdc2	genetic	12454065
QUAI_DROME	qua	genetic	12454065
DIA_DROME	dia	genetic	12454065
THR_DROME	thr	genetic	15772129
MYSN_DROME	zip	genetic	12454065
DYHC_DROME	Dhc64C	genetic	12454065
CCNA_DROME	CycA	genetic	12454065
DCTN1_DROME	Gl	genetic	12454065
ACTZ_DROME	Arp1	genetic	12454065
CDK1_DROME	cdc2	physical	16139207
CDK1_DROME	cdc2	physical	8156587

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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-137, AND MASSSPECTROMETRY.
PubMed: 18327897

"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-137, AND MASSSPECTROMETRY.
PubMed: 17372656