dbPTM

BAB2_DROME - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	BAB2_DROME
UniProt AC	Q9W0K4
Protein Name	Protein bric-a-brac 2
Gene Name	bab2
Organism	Drosophila melanogaster (Fruit fly).
Sequence Length	1067
Subcellular Localization	Nucleus .
Protein Description	Probably acts as a transcriptional regulator. Required for the specification of the tarsal segment. Also involved in antenna development..
Protein Sequence	MDMTKQIVDFEIKSELIGEIDQFEASDYTMAPPEEPKMVEESPQLGHLEDQNRKYSPEREVEPTLQDPSEVVDQMQKDTESVGEVKSPEKDVETELVKSKASPMNDQALTPPPRPLTSSEVVGLRDPEHTELRMCLEAKKSRSLPVSPQPQPNLKLAGSALFEFGQRSSPVETKIKTNPETKPPRRKIVPPSGEGQQFCLRWNNYQSNLTNVFDELLQSESFVDVTLSCEGHSIKAHKMVLSACSPYFQALFYDNPCQHPIIIMRDVSWSDLKALVEFMYKGEINVCQDQINPLLKVAETLKIRGLAEVSAGRGEGGASALPMSAFDDEDEEEELASATAILQQDGDADPDEEMKAKRPRLLPEGVLDLNQRQRKRSRDGSYATPSPSLQGGESEISERGSSGTPGQSQSQPLAMTTSTIVRNPFASPNPQTLEGRNSAMNAVANQRKSPAPTATGHSNGNSGAAMHSPPGGVAVQSALPPHMAAIVPPPPSAMHHHAQQLAAQHQLAHSHAMASALAAAAAGAGAAGAGGAGSGSGSGASAPTGGTGVAGSGAGAAVGSHHDDMEIKPEIAEMIREEERAKMIESGGHGGWMGAAAAATGAASVAADSYQYQLQSMWQKCWNTNQQNLVQQLRFRERGPLKSWRPEAMAEAIFSVLKEGLSLSQAARKFDIPYPTFVLYANRVHNMLGPSLDGGADPRPKARGRPQRILLGMWPEELIRSVIKAVVFRDYREIKEDMSAHQYANGQGHGTYIGGGTTTNGYHSAAAAKLAAQNAALAPPDAGSPLSSMTETLRRQILSQQQQHQQHHQQQAHHQQQPSHHQQQSPHAQSMNMYKSPAYLQRSEIEDQVSAAAAVAAAAAKHQQQQGERRGSENLPDLSALGLMGLPGLNVMPSRGSGGGSGGAAPNSAASYARELSRERERDRERERERELSRQYGSQSRGSSSGSGSAKSLTASQRPGAASPYSAAHYAKHQASAYNKRFLESLPAGIDLEAFANGLLQKSVNKSPRFEDFFPGPGQDMSELFANPDASAAAAAAAYAPPGAIRESPLMKIKLEQQHATELPHED

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
55	Phosphorylation	LEDQNRKYSPEREVE CCCCCCCCCCCCCCC	26.65	18327897
56	Phosphorylation	EDQNRKYSPEREVEP CCCCCCCCCCCCCCC	24.26	22817900
87	Phosphorylation	ESVGEVKSPEKDVET CCCCCCCCCCHHHHH	43.39	22817900
141	Phosphorylation	MCLEAKKSRSLPVSP HHHHHHHHCCCCCCC	26.79	27794539
143	Phosphorylation	LEAKKSRSLPVSPQP HHHHHHCCCCCCCCC	44.08	25749252
147	Phosphorylation	KSRSLPVSPQPQPNL HHCCCCCCCCCCCCC	18.84	25749252
169	Phosphorylation	FEFGQRSSPVETKIK HHCCCCCCCCCCCCC	34.84	27794539
177	Phosphorylation	PVETKIKTNPETKPP CCCCCCCCCCCCCCC	60.52	22817900
181	Phosphorylation	KIKTNPETKPPRRKI CCCCCCCCCCCCCCC	50.54	22817900
377	Phosphorylation	NQRQRKRSRDGSYAT HHHHHHHCCCCCCCC	37.45	22817900
384	Phosphorylation	SRDGSYATPSPSLQG CCCCCCCCCCCCCCC	18.96	22817900
386	Phosphorylation	DGSYATPSPSLQGGE CCCCCCCCCCCCCCC	23.83	22817900

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
Oops, there are no upstream regulatory protein records of BAB2_DROME !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of BAB2_DROME !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of BAB2_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of BAB2_DROME !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of BAB2_DROME

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 TYR-55; SER-56; SER-87;SER-147; SER-377 AND THR-384, AND MASS SPECTROMETRY.	18327897 [Abstract]