PNUT_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PNUT_DROME
• UniProt AC: P40797
• Protein Name: Protein peanut
• Gene Name: pnut
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 539
• Subcellular Localization: Apical cell membrane ; Peripheral membrane protein . Cleavage furrow . Cytoplasm, cell cortex . Localized to the cleavage furrow of dividing cells during cytokinesis and to the intercellular bridge connecting postmitotic daughter cells. Equally found
• Protein Description: Involved in cytokinesis and possibly cellularization. Also acts as an enhancer of the sina gene, thus having a role in photoreceptor development..
• Protein Sequence: MNSPRSNAVNGGSGGAISALPSTLAQLALRDKQQAASASASSATNGSSGSESLVGVGGRPPNQPPSVPVAASGKLDTSGGGASNGDSNKLTHDLQEKEHQQAQKPQKPPLPVRQKPMEIAGYVGFANLPNQVYRKAVKRGFEFTLMVVGASGLGKSTLINSMFLSDIYNAEQYPGPSLRKKKTVAVEATKVMLKENGVNLTLTVVDTPGFGDAVDNSNCWVPILEYVDSKYEEYLTAESRVYRKTISDSRVHCCLYFIAPSGHGLLPLDIACMQSLSDKVNLVPVIAKADTMTPDEVHLFKKQILNEIAQHKIKIYDFPATLEDAAEEAKTTQNLRSRVPFAVVGANTIIEQDGKKVRGRRYPWGLVEVENLTHCDFIALRNMVIRTHLQDLKDVTNNVHYENYRCRKLSELGLVDGKARLSNKNPLTQMEEEKREHEQKMKKMEAEMEQVFDMKVKEKMQKLRDSELELARRHEERKKALELQIRELEEKRREFEREKKEWEDVNHVTLEELKRRSLGANSSTDNVDGKKEKKKKGLF

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
3	Phosphorylation	-----MNSPRSNAVN -----CCCCCCCCCC	22.01	27794539
6	Phosphorylation	--MNSPRSNAVNGGS --CCCCCCCCCCCCC	32.31	17372656
13	Phosphorylation	SNAVNGGSGGAISAL CCCCCCCCCHHHHHH	35.14	19060867
18	Phosphorylation	GGSGGAISALPSTLA CCCCHHHHHHHHHHH	24.18	21082442
22	Phosphorylation	GAISALPSTLAQLAL HHHHHHHHHHHHHHH	36.58	21082442
23	Phosphorylation	AISALPSTLAQLALR HHHHHHHHHHHHHHH	24.95	21082442
52	Phosphorylation	NGSSGSESLVGVGGR CCCCCCCCCCCCCCC	30.01	21082442
410	Phosphorylation	NYRCRKLSELGLVDG CHHHCCHHHHCCCCC	33.53	21082442
422	Phosphorylation	VDGKARLSNKNPLTQ CCCCCCCCCCCCCHH	39.96	21082442
428	Phosphorylation	LSNKNPLTQMEEEKR CCCCCCCHHHHHHHH	27.42	22817900
466	Phosphorylation	KMQKLRDSELELARR HHHHHHHHHHHHHHH	37.33	22817900
517	Phosphorylation	LEELKRRSLGANSST HHHHHHHCCCCCCCC	34.88	21082442
522	Phosphorylation	RRSLGANSSTDNVDG HHCCCCCCCCCCCCC	33.80	19429919
523	Phosphorylation	RSLGANSSTDNVDGK HCCCCCCCCCCCCCC	39.32	19429919
524	Phosphorylation	SLGANSSTDNVDGKK CCCCCCCCCCCCCCH	31.26	19429919

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PNUT_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 PNUT_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SEPT2_DROME	Sep2	physical	22036573
F10A1_DROME	HIP-R	physical	22036573
F10A2_DROME	HIP-R	physical	22036573
SEPT1_DROME	Sep1	physical	24633326
SEPT1_DROME	Sep1	physical	23447705
SEPT1_DROME	Sep1	physical	25355953
SEPT1_DROME	Sep1	physical	8590810
SEPT1_DROME	Sep1	physical	8636235
PNUT_DROME	pnut	physical	11884525
ORC6_DROME	Orc6	physical	18987337
ORC6_DROME	Orc6	physical	25355953
SEPT2_DROME	Sep2	physical	24633326
SEPT2_DROME	Sep2	physical	23447705
SEPT2_DROME	Sep2	physical	25355953
SEPT2_DROME	Sep2	physical	8636235
SEPT2_DROME	Sep2	physical	11884525
TFP11_DROME	sip1	physical	11884525

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-517, 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-6 AND SER-13, AND MASSSPECTROMETRY.
PubMed: 17372656