ZWILC_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ZWILC_DROME
• UniProt AC: Q9VA00
• Protein Name: Protein zwilch
• Gene Name: Zwilch {ECO:0000312|FlyBase:FBgn0061476}
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 641
• Subcellular Localization: Cytoplasm . Chromosome, centromere, kinetochore . Cytoplasm, cytoskeleton, spindle . Dynamic pattern of localization during the cell cycle (PubMed:22685323). In most cells at interphase, present diffusely in the cytoplasm (PubMed:22685323). At metaph
• Protein Description: Essential component of the mitotic checkpoint, which prevents cells from prematurely exiting mitosis. [PubMed: 15886105]
• Protein Sequence: MSASANLANVYAELMRRCGESYTITYGAPPTYLVSMVGAAEAGKKIVLVFKEDRNGAVARLRTTPTRAAPKKEGSADLDLTGSPLKDDCLVDAIADLSIDLQLDHSNPWKLEEEYQRGIPVDKARSIVCSEFLQLAEGLGSVWFLCDGSDLGQTQLLQYEFNPTHFSRGILSYQGVRPAYLVTSQALVRHHGKTPDETLIENSYQVNPHMRLRCSWTSSAALPLLVNLNDCDVALNHTFRVGDCGPLTQDFMNQLRILVYIREDIVSYHTDVKQGVSRDPTYRCGSGIDMDELRESINQTMTDVSGLIGRYSISNAEFDIEDVVQRAKVRQLTDLTDKLWELLKCCHSYKDLKIAFSMLFQCAARCNIVNTPTNKNRLAKIITELANRRLAMPCLSGAEPLELLLEIGLEKLYKDYEFIYTESKMCSTNLLKDDSSGASMDDGSPQNLPQLRKSLHNAVRGDPTPGAGMRKTLLHHHGAVNSRSTKYAGSDDDAGFKNSHFDEHESTERISKLFQIHCTLEHLLMMHIHLNLANVYNDVCSELLKKPPKLVESIDDQLSDVMDIRLSAHYVRDHLDGKDPYSRHITMRSHNKFRELKTTFYFNSENICPPNLAQCFQCDDKEMVKERTYHSWIYHKIRSLK

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
66	Phosphorylation	ARLRTTPTRAAPKKE EEEEECCCCCCCCCC	30.74	22817900
75	Phosphorylation	AAPKKEGSADLDLTG CCCCCCCCCCCCCCC	21.50	19429919
83	Phosphorylation	ADLDLTGSPLKDDCL CCCCCCCCCCCCCHH	23.09	19429919
311	Phosphorylation	VSGLIGRYSISNAEF HHHHHHCCCCCCCCC	12.73	22817900
312	Phosphorylation	SGLIGRYSISNAEFD HHHHHCCCCCCCCCC	20.41	19429919
314	Phosphorylation	LIGRYSISNAEFDIE HHHCCCCCCCCCCHH	24.85	18511481
435	Phosphorylation	TNLLKDDSSGASMDD CCCCCCCCCCCCCCC	40.58	29892262
436	Phosphorylation	NLLKDDSSGASMDDG CCCCCCCCCCCCCCC	45.43	29892262
439	Phosphorylation	KDDSSGASMDDGSPQ CCCCCCCCCCCCCCC	26.69	19429919
444	Phosphorylation	GASMDDGSPQNLPQL CCCCCCCCCCCHHHH	30.24	19429919
454	Phosphorylation	NLPQLRKSLHNAVRG CHHHHHHHHHHHHCC	28.55	19429919
472	Phosphorylation	PGAGMRKTLLHHHGA CCCCHHHHHHHCCCC	24.96	21082442
482	Phosphorylation	HHHGAVNSRSTKYAG HCCCCCCCCCCCCCC	22.47	21082442
487	Phosphorylation	VNSRSTKYAGSDDDA CCCCCCCCCCCCCCC	19.11	27626673
490	Phosphorylation	RSTKYAGSDDDAGFK CCCCCCCCCCCCCCC	29.69	19429919

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ZWILC_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 ZWILC_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
HSP7D_DROME	Hsc70-4	physical	12686595
ZW10_DROME	Zw10	physical	12686595

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-312, AND MASSSPECTROMETRY.
PubMed: 17372656