ABRU_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ABRU_DROME
• UniProt AC: Q24174
• Protein Name: Protein abrupt
• Gene Name: ab
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 904
• Subcellular Localization: Nucleus.
• Protein Description: Expression is vital for development; may be involved in transcriptional regulation. In embryos, muscle specific expression is required for segmental nerve b (SNb) motoneuron target recognition within ventral longitudinal muscles. Has a role in establishing and maintaining embryonic muscle attachments, adult sensory cell formation (macrochaetae) and morphogenesis of adult appendages (legs, antenna aristae and male external genitalia). Has a role in the morphogenesis of the class I dendritic neurons: selective expression of ab in class I da neurons plays a pivotal role in forming dendritic arbors, which are characteristic of the class I cells. The development of more complex arbors of class II-IV neurons depends on the absence of ab..
• Protein Sequence: MTESTQLQTAENNNAGVVKMEPPPPATSSVSVSAAAAAHALSSLSSLTMAATGSALSPATPPPSLNLSHQQQQHQQHYALKWNDFQSSILSSFRHLRDEEDFVDVTLACDERSFTAHKVVLSACSPYFRRLLKANPCEHPIVILRDVRCDDVENLLSFMYNGEVNVSHEQLPDFLKTAHLLQIRGLADVNGGYPYSKALSAALSHNSSNNNNNNSSSNNSLSNNNNNNNNNAESSNHNKISSYLSPNQTSAACNNSSNSNSNNHSSSHNNSSSNNISGSLNSSLNSPFSAPQIPPPVTASSAAAAAAAAASLTAAVAAAAAATAASAGSSSSAASGQTSGTPAIQELKASSAASPVRNPNPNPSKASSSNHWDMGEMEGSRKSHLTPPPQKRIKSADLFRAQHGISPERLLLDREFPVAGQHPLTRNRSGRDTSKDRERNLELRESLLGQALENSNGQQANPKHELGQSAGEDSNSSDTEPSDRGDGQHDGTLDGIDNQRSHSFPNAFLGLQGIPGLLPGPSGINSDFVSRRSLEMRVRATDPRPCPKCGKIYRSAHTLRTHLEDKHTVCPGYRCVLCGTVAKSRNSLHSHMSRQHRGISTKDLPVLPMPSAFDPELASRLLAKAGVKISPAELRARASPTGGSGSSGGGGGGGSSQAKLDLSNASGGPMDDAEDSDDDPEDLTTGNGLYGMGGSSSDLSRYHESLLSNFGHARMRNEAAAVAATAAALGQPKDLGVQLPNSNAPGQSLLDTYLQFITENTFGMGMSQEQAAAAALRAKMAQLNAMGHSLDNLPPGLLPGQFDLSKLAAGNPAFGQSGPGLTIEPIMRHEQAAGNLSPNRPLALNSGGRMMGHDEMAENDGDMRREGSEPMDLGLDNNQSGSNHEVANSDAEENYSEDEGVHNT

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
395	Phosphorylation	PPQKRIKSADLFRAQ CCCHHCCHHHHHHHH	25.33	18327897
406	Phosphorylation	FRAQHGISPERLLLD HHHHHCCCHHHHHHC	25.87	18327897
474	Phosphorylation	GQSAGEDSNSSDTEP CCCCCCCCCCCCCCC	34.02	18327897
477	Phosphorylation	AGEDSNSSDTEPSDR CCCCCCCCCCCCCCC	53.45	18327897
837	Phosphorylation	EQAAGNLSPNRPLAL HHHCCCCCCCCCEEE	24.91	18327897
846	Phosphorylation	NRPLALNSGGRMMGH CCCEEECCCCCCCCC	43.40	18327897
868	Phosphorylation	GDMRREGSEPMDLGL CCCCCCCCCCCCCCC	33.50	18327897
889	Phosphorylation	SNHEVANSDAEENYS CCCCCCCCCHHHHCC	28.58	18327897
896	Phosphorylation	SDAEENYSEDEGVHN CCHHHHCCCCCCCCC	50.59	12537569

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ABRU_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 ABRU_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
OMB_DROME	bi	genetic	15073155
CUT_DROME	ct	genetic	15363392

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-474; SER-837; SER-846;SER-868; SER-889 AND SER-896, AND MASS SPECTROMETRY.
PubMed: 18327897