CDC37_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CDC37_DROME
• UniProt AC: Q24276
• Protein Name: Hsp90 co-chaperone Cdc37
• Gene Name: Cdc37
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 389
• Subcellular Localization: Cytoplasm.
• Protein Description: Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. Required for cytokinesis and chromosome segregation in mitosis and male meiosis..
• Protein Sequence: MVDYSKWKNIEISDDEDDTHPNIDTPSLFRWRHQARVERMAEMDHEKDELKKKRQSYQARLMDVKERISKKDGDEEALKKELEKIEAEGKELDRIESEMIKKEKKTPWNVDTISKPGFEKTVINKKAGRKPDENLSEEEREQRMKQFVKENEKLCQQYGMLRKYDDSKRFLQEHLHLVGEETANYLVIWSINLEMEEKHELMAHVAHQCICMQYILELAKQLDVDPRACVSSFFSKIQHCHPEYRAQFDSEIEGFKGRIQKRAQEKIQEAIAQAEEEERKERLGPGGLDPADVFESLPDELKACFESRDVELLQKTIAAMPVDVAKLHMKRCVDSGLWVPNAADLEGDKKEEDDSDDVAGGEEKTDDAKSESAAKEEPIYTGVSTEDVD

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
13	Phosphorylation	KWKNIEISDDEDDTH HCCCCCCCCCCCCCC	26.64	21082442
19	Phosphorylation	ISDDEDDTHPNIDTP CCCCCCCCCCCCCCH	52.10	19429919
25	Phosphorylation	DTHPNIDTPSLFRWR CCCCCCCCHHHHHHH	15.81	19429919
27	Phosphorylation	HPNIDTPSLFRWRHQ CCCCCCHHHHHHHHH	42.08	19429919
56	Phosphorylation	ELKKKRQSYQARLMD HHHHHHHHHHHHHHH	24.20	19429919
112	Phosphorylation	KTPWNVDTISKPGFE CCCCCCCCCCCCCCC	23.91	21082442
115	Acetylation	WNVDTISKPGFEKTV CCCCCCCCCCCCHHH	45.36	21791702
136	Phosphorylation	RKPDENLSEEEREQR CCCCCCCCHHHHHHH	55.32	22668510
296	Phosphorylation	DPADVFESLPDELKA CHHHHHHHCCHHHHH	33.46	22817900
316	Phosphorylation	DVELLQKTIAAMPVD CHHHHHHHHHHCCCC	11.68	22817900
355	Phosphorylation	DKKEEDDSDDVAGGE CCCCCCCCCCCCCCC	48.29	21082442
365	Phosphorylation	VAGGEEKTDDAKSES CCCCCCCCCCHHCHH	42.25	22668510
380	Phosphorylation	AAKEEPIYTGVSTED HHCCCCCCCCCCCCC	14.25	19429919
381	Phosphorylation	AKEEPIYTGVSTEDV HCCCCCCCCCCCCCC	31.65	19429919
385	Phosphorylation	PIYTGVSTEDVD--- CCCCCCCCCCCC---	33.52	22668510

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

Oops, there are no upstream regulatory protein records of CDC37_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CDC37_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 CDC37_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ESMD_DROME	E(spl)mdelta-HLH	physical	15575970
KAPC_DROME	Pka-C1	physical	15575970
BCD_DROME	bcd	physical	15575970
MOB2_DROME	Mob2	physical	15575970
HPS5_DROME	p	physical	15575970
SUDX_DROME	Su(dx)	physical	15575970
WARTS_DROME	wts	physical	15575970
ELYS_DROME	CG14215	physical	15575970
PYR1_DROME	r	physical	15575970

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-13; THR-19 AND SER-355,AND MASS SPECTROMETRY.
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-13 AND SER-296, AND MASSSPECTROMETRY.
PubMed: 17372656