BOREA_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: BOREA_DROME
• UniProt AC: Q9VLD6
• Protein Name: Borealin
• Gene Name: borr
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 315
• Subcellular Localization: Nucleus . Chromosome, centromere . Cytoplasm, cytoskeleton, spindle . Localizes on chromosome arms and inner centromeres from prophase through metaphase and then transferring to the spindle midzone and midbody from anaphase through cytokinesis. Coloc
• Protein Description: Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of embryonic mitosis. The CPC complex has essential functions at the centromere for ensuring sister chromatid cohesion, recruitment of the CPC to kinetochores, and chromosome alignment and segregation. There is no function in meiotic histone phosphorylation or spindle formation..
• Protein Sequence: MPRTKIPKNSKRNREVANREEKVRLYELKMDSRLISIDSLETKFLSAVDHQVKTLLGQVQKELANLKMPEVLRLFEELDRFSDFKASDQTQLLASMSMSGSAIEGHAPSATGSRNDEEDSSIGASGGSILAAHTGSLLRSTKAMRTPGPLHSARARRARRSRSACGDLNILHSAKPPSISSSSSSSRNSRSKLRTPMASRAKAFSADRTPLKQKQMRSGSPTTPPMAFLRYPKPGEVALSKYGSPMVAQVMPDKFANVNIPIRNGVLSLRPKKLDADEVESNLLENLDEDTLNQIKTLHENLQMIVNKASQAVFK

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
36	Phosphorylation	KMDSRLISIDSLETK CCCCCEEEHHHHCHH	25.57	25749252
97	Phosphorylation	TQLLASMSMSGSAIE HHHHHHHHCCCCCEE	13.80	21082442
99	Phosphorylation	LLASMSMSGSAIEGH HHHHHHCCCCCEECC	23.45	21082442
101	Phosphorylation	ASMSMSGSAIEGHAP HHHHCCCCCEECCCC	20.83	21082442
146	Phosphorylation	RSTKAMRTPGPLHSA HHCCCCCCCCCHHHH	21.36	22817900
152	Phosphorylation	RTPGPLHSARARRAR CCCCCHHHHHHHHHH	27.42	22817900
161	Phosphorylation	RARRARRSRSACGDL HHHHHHHHHHCCCCC	25.65	21082442
163	Phosphorylation	RRARRSRSACGDLNI HHHHHHHHCCCCCCC	29.20	19429919
173	Phosphorylation	GDLNILHSAKPPSIS CCCCCCCCCCCCCCC	34.24	22817900
180	Phosphorylation	SAKPPSISSSSSSSR CCCCCCCCCCCCCCC	28.62	21082442
195	Phosphorylation	NSRSKLRTPMASRAK CCCHHCCCCCHHHHH	28.05	22817900
205	Phosphorylation	ASRAKAFSADRTPLK HHHHHHHCCCCCCCC	33.83	19429919
209	Phosphorylation	KAFSADRTPLKQKQM HHHCCCCCCCCHHHH	33.26	25749252
218	Phosphorylation	LKQKQMRSGSPTTPP CCHHHHHCCCCCCCC	37.98	19429919
220	Phosphorylation	QKQMRSGSPTTPPMA HHHHHCCCCCCCCCE	21.96	19429919
222	Phosphorylation	QMRSGSPTTPPMAFL HHHCCCCCCCCCEEC	54.34	19429919
223	Phosphorylation	MRSGSPTTPPMAFLR HHCCCCCCCCCEECC	28.87	19429919
242	Phosphorylation	GEVALSKYGSPMVAQ CCEEHHHCCCCCEEE	21.33	22817900
244	Phosphorylation	VALSKYGSPMVAQVM EEHHHCCCCCEEECC	13.51	22817900
268	Phosphorylation	PIRNGVLSLRPKKLD EEECCCCCCCCCCCC	21.67	21082442

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of BOREA_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 BOREA_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
BOREA_DROME	borr	physical	18268101

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 THR-146; SER-152; SER-163;SER-205; THR-209; SER-218; SER-220 AND SER-244, AND MASS SPECTROMETRY.
PubMed: 18327897