BICD_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BICD_DROME
• UniProt AC: P16568
• Protein Name: Protein bicaudal D
• Gene Name: BicD
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 782
• Subcellular Localization: Cytoplasm, cytoskeleton .
• Protein Description: This protein is essential for differentiation. It may play a role in localizing of Nanos (a maternal determinant) activity in oocytes. During oogenesis, plays a specific role, together with Rab6 but independently of Sec5, in the polarization of the oocyte microtubule cytoskeleton, in oskar mRNA localization and in the anterodorsal secretion of grk..
• Protein Sequence: MSSASNNGPSADQSVQDLQMEVERLTRELDQVSSASAQSAQYGLSLLEEKSALQQKCEELETLYDNTRHELDITQEALTKFQTSQKVTNKTGIEQEDALLNESAARETSLNLQIFDLENELKQLRHELERVRNERDRMLQENSDFGRDKSDSEADRLRLKSELKDLKFRETRMLSEYSELEEENISLQKQVSSLRSSQVEFEGAKHEIRRLTEEVELLNQQVDELANLKKIAEKQMEEALETLQGEREAKYALKKELDGHLNRESMYHISNLAYSIRSNMEDNASNNSDGEEENLALKRLEADLSTELKSPDGTKCDLFSEIHLNELKKLEKQLESMESEKTHLTANLREAQTSLDKSQNELQNFMSRLALLAAHVDALVQLKKQIDVKEQGKEGGQKKDELEQQLRALISQYANWFTLSAKEIDGLKTDIAELQKGLNYTDATTTLRNEVTNLKNKLLATEQKSLDLQSDVQTLTHISQNAGQSLGSARSTLVALSDDLAQLYHLVCTVNGETPTRVLLDHKTDDMSFENDSLTAIQSQFKSDVFIAKPQIVEDLQGLADSVEIKKYVDTVSDQIKYLKTAVEHTIDMNKHKIRSEGGDALEKVNTEEMEELQEQIVKLKSLLSVKREQIGTLRNVLKSNKQTAEVALTNLKSKYENEKIIVSDTMSKLRNELRLLKEDAATFSSLRAMFAARCEEYVTQVDDLNRQLEAAEEEKKTLNQLLRLAVQQKLALTQRLEEMEMDREMRHVRRPMPAQRGTSGKSSFSTRPSSRNPASSNANPF

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
103	Phosphorylation	EDALLNESAARETSL HHHHHCHHHHHHHHH	26.59	25749252
285	Phosphorylation	SNMEDNASNNSDGEE HCCCCCCCCCCCCHH	42.68	25749252
288	Phosphorylation	EDNASNNSDGEEENL CCCCCCCCCCHHHHH	51.77	19429919
305	Phosphorylation	KRLEADLSTELKSPD HHHHHHHCCCCCCCC	22.00	19429919
306	Phosphorylation	RLEADLSTELKSPDG HHHHHHCCCCCCCCC	53.27	19429919
310	Phosphorylation	DLSTELKSPDGTKCD HHCCCCCCCCCCCCC	40.63	19429919
314	Phosphorylation	ELKSPDGTKCDLFSE CCCCCCCCCCCCHHH	35.56	19429919
524	Phosphorylation	RVLLDHKTDDMSFEN EEEECCCCCCCCCCC	33.54	19429919
528	Phosphorylation	DHKTDDMSFENDSLT CCCCCCCCCCCCHHH	36.08	19429919
533	Phosphorylation	DMSFENDSLTAIQSQ CCCCCCCHHHHHHHH	38.92	19429919
535	Phosphorylation	SFENDSLTAIQSQFK CCCCCHHHHHHHHHH	26.18	19429919
622	Phosphorylation	EQIVKLKSLLSVKRE HHHHHHHHHHHCCHH	45.00	27626673

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BICD_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 BICD_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TFP11_DROME	sip1	physical	14605208
RENT1_DROME	Upf1	physical	22036573
RS27A_DROME	RpS27A	physical	14588248
LIS1_DROME	Lis-1	genetic	10559989
KINH_DROME	Khc	genetic	15077115
PABP_DROME	pAbp	genetic	21782810
SMG_DROME	smg	genetic	10488336
POLO_DROME	polo	genetic	16971474
SH3G3_DROME	EndoA	genetic	20111007
CLH_DROME	Chc	physical	20111007
CLH_DROME	Chc	physical	24718986
LAM0_DROME	Lam	physical	10350216
GRK_DROME	grk	physical	19515976
RAB6_DROME	Rab6	physical	23723415
RAB6_DROME	Rab6	physical	19515976
BICD_DROME	BicD	physical	23723415
BICD_DROME	BicD	physical	10350216
BICD_DROME	BicD	physical	19515976
PABP_DROME	pAbp	physical	21782810
DYHC_DROME	Dhc64C	physical	23723415
HAIR_DROME	h	physical	19515976
HAIR_DROME	h	physical	23918939
DYIN_DROME	sw	physical	23723415
K10_DROME	fs(1)K10	physical	19515976
K10_DROME	fs(1)K10	physical	23918939

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-103; SER-285; SER-288;SER-305; THR-306; SER-310 AND SER-528, 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-103, AND MASSSPECTROMETRY.
PubMed: 17372656