BIB_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BIB_DROME
• UniProt AC: P23645
• Protein Name: Neurogenic protein big brain
• Gene Name: bib
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 696
• Subcellular Localization: Membrane ; Multi-pass membrane protein .
• Protein Description: Essential for proper differentiation of ectoderm. Acts synergistically with neurogenic locus proteins Notch and Delta during the separation of neural and epidermal cell lineages in response to the lateral inhibition signal. Voltage-insensitive monovalent cation channel. Ion transport is blocked by the presence of divalent cations..
• Protein Sequence: MADESLHTVPLEHNIDYHIVTLFERLEAMRKDSHGGGHGVNNRLSSTLQAPKRSMQAEIRTLEFWRSIISECLASFMYVFIVCGAAAGVGVGASVSSVLLATALASGLAMATLTQCFLHISGAHINPAVTLALCVVRSISPIRAAMYITAQCGGGIAGAALLYGVTVPGYQGNLQAAISHSAALAAWERFGVEFILTFLVVLCYFVSTDPMKKFMGNSAASIGCAYSACCFVSMPYLNPARSLGPSFVLNKWDSHWVYWFGPLVGGMASGLVYEYIFNSRNRNLRHNKGSIDNDSSSIHSEDELNYDMDMEKPNKYQQSQGTYPRGQSNGNGGGQAAGNGQHQAANMGQMPGVVANAGQGNYCQNLYTAPPLSSKYDQQQEPLYGGTRSLYCRSPTLTRSNLNRSQSVYAKSNTAINRDIVPRPGPLVPAQSLYPMRTQQQQQQQQQQQQQVAPAPQSSHLQNQNVQNQMQQRSESIYGMRGSMRGQQQPIQQQQQQQQQQQLQQQQPNMGVQQQQMQPPPQMMSDPQQQPQGFQPVYGTRTNPTPMDGNHKYDRRDPQQMYGVTGPRNRGQSAQSDDSSYGSYHGSAVTPPARHPSVEPSPPPPPMLMYAPPPQPNAAHPQPIRTQSERKVSAPVVVSQPAACAVTYTTSQGSAVTAQQQQQQQQQQQQQQQQQQQQMMMQQQQQHYGMLPLRPN

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
46	Phosphorylation	GVNNRLSSTLQAPKR CCHHHHHHHHCCCHH	37.42	22817900
47	Phosphorylation	VNNRLSSTLQAPKRS CHHHHHHHHCCCHHH	21.36	22817900
273	Phosphorylation	GMASGLVYEYIFNSR HHHHHHHHHHHHCCC	14.20	-
295	Phosphorylation	KGSIDNDSSSIHSED CCCCCCCCCCCCCHH	32.04	22817900
296	Phosphorylation	GSIDNDSSSIHSEDE CCCCCCCCCCCCHHH	35.85	22817900
297	Phosphorylation	SIDNDSSSIHSEDEL CCCCCCCCCCCHHHC	28.42	22817900
300	Phosphorylation	NDSSSIHSEDELNYD CCCCCCCCHHHCCCC	45.10	22817900
367	Phosphorylation	GNYCQNLYTAPPLSS CCCCCCCCCCCCCCC	14.38	-
384	Phosphorylation	DQQQEPLYGGTRSLY CCCCCCCCCCCCCEE	24.99	-
394	Phosphorylation	TRSLYCRSPTLTRSN CCCEEECCCCCCCCC	20.76	22817900
478	Phosphorylation	QQRSESIYGMRGSMR HHHHHHHHHHHHHHH	17.72	-
576	Phosphorylation	NRGQSAQSDDSSYGS CCCCCCCCCCCCCCC	43.00	22817900
610	Phosphorylation	PPPPMLMYAPPPQPN CCCCCEEECCCCCCC	16.40	-

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
273	Y	Phosphorylation	Kinase	SRC	-	Uniprot
367	Y	Phosphorylation	Kinase	ABL	P00522	Uniprot
384	Y	Phosphorylation	Kinase	SRC	-	Uniprot
478	Y	Phosphorylation	Kinase	SRC	-	Uniprot
610	Y	Phosphorylation	Kinase	ABL	P00522	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BIB_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 BIB_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NOTCH_DROME	N	genetic	9367444
NOTCH_DROME	N	genetic	8406001
DL_DROME	Dl	genetic	9367444

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-46; THR-47; SER-300;SER-394 AND SER-576, AND MASS SPECTROMETRY.
PubMed: 18327897