SRP_DROME - dbPTM
SRP_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SRP_DROME
UniProt AC P52172
Protein Name Box A-binding factor
Gene Name srp
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1264
Subcellular Localization Nucleus.
Protein Description May function as a transcriptional activator protein and may play a key role in the organogenesis of the fat body. Binds a sequence element (5'-[TA]GATAA-3') found in the larval promoters of all known alcohol dehydrogenase (ADH) genes. Acts as a homeotic gene downstream of the terminal gap gene HKB to promote morphogenesis and differentiation of anterior and posterior midgut..
Protein Sequence MTKTTKPKEKAAAGGAVIGSGSGLGSVTKAGGGSLLSNAADSKIRTAKSNNNKRQAGRAATALAATTTASALAATTTAGATGSNAAANETEIAIETENGEAATPTAAATAAAANLSSLESARSQALTSVVSETARQAVTTANASATSTSTVTAATEIATATASDTAATSEAAIDDDPSAINTNNNNNNSKAQNDASESVKTKVISYHQSEDQQQQQQQQAQIYEQQQQFLSQQLISHHQQEQHQQAQQQQHQQVVQEQHQASWLAYDLTSGSAAAAAAAAAAASHPHLFGQFSYPPSHHTPTQLYEHYPSTDPIMRNNFAFYSVYTGGGGGVGVGMTSHEHLAAAAAAAAAVAQGTTPNIDEVIQDTLKDECFEDGHSTDYHVLTSVSDMHTLKDSSPYALTHEQLHQQQHHHQQQLHHHQQQQQQLYHQQQQQQQQQQHHHHHNNSTSSAGGDSPSSSHALSTLQSFTQLTSATQRDSLSPENDAYFAAAQLGSSLQNSSVYAGSLLTQTANGIQYGMQSPNQTQAHLQQQHHQQQQQQHQQHQQQQLQQQQQQHHHNQHQHHNSSSSSPGPAGLHHSSSSAATAAAVAAATAAVNGHNSSLEDGYGSPRSSHSGGGGGGTLPAFQRIAYPNSGSVERYAPITNYRGQNDTWFDPLSYATSSSGQAQLGVGVGAGVVSNVIRNGRAISAANAAAAAAADGTTGRVDPGTFLSASASLSAMAAESGGDFYKPNSFNVGGGGRSKANTSGAASSYSCPGSNATSAATSAVASGTAATAATTLDEHVSRANSRRLSASKRAGLSCSNCHTTHTSLWRRNPAGEPVCNACGLYYKLHSVPRPLTMKKDTIQKRKRKPKGTKSEKSKSKSKNALNAIMESGSLVTNCHNVGVVLDSSQMDVNDDMKPQLDLKPYNSYSSQPQQQLPQYQQQQQLLMADQHSSAASSPHSMGSTSLSPSAMSHQHQTHPHQQQQQQLCSGLDMSPNSNYQMSPLNMQQHQQQQSCSMQHSPSTPTSIFNTPSPTHQLHNNNNNNNNSSIFNNNNNNNSSSNENNNKLIQKYLQAQQLSSSSNSGSTSDHQLLAQLLPNSITAAAAAAAAAAAAAIKTEALSLTSQANCSTASAGLMVTSTPTTASSTLSSLSHSNIISLQNPYHQAGMTLCKPTRPSPPYYLTPEEDEQPALIKMEEMDQSQQQQQQQQHQQQQHGEIMLSRSASLDEHYELAAFQRHQQQQQQLQQQTAALLGQHEQHVTNYAMHKFGVDRETVVKME
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 Orthologous
Protein Cluster
612PhosphorylationDGYGSPRSSHSGGGG
CCCCCCCCCCCCCCC
35.4719429919
613PhosphorylationGYGSPRSSHSGGGGG
CCCCCCCCCCCCCCC
23.9719429919
615PhosphorylationGSPRSSHSGGGGGGT
CCCCCCCCCCCCCCC
40.8719429919
622PhosphorylationSGGGGGGTLPAFQRI
CCCCCCCCCCCHHEE
32.6119429919
1159PhosphorylationGMTLCKPTRPSPPYY
CCCCCCCCCCCCCCC
40.4819429919
1162PhosphorylationLCKPTRPSPPYYLTP
CCCCCCCCCCCCCCC
34.9019429919
1206PhosphorylationQHGEIMLSRSASLDE
HHHHHHHCCCCCHHH
13.5522817900
1208PhosphorylationGEIMLSRSASLDEHY
HHHHHCCCCCHHHHH
20.8719429919
1210PhosphorylationIMLSRSASLDEHYEL
HHHCCCCCHHHHHHH
37.2819429919
1215PhosphorylationSASLDEHYELAAFQR
CCCHHHHHHHHHHHH
15.5823607784

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 SRP_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SRP_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 SRP_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LOZEN_DROMElzgenetic
14504400
LOZEN_DROMElzgenetic
14657024
USH_DROMEushgenetic
8946251
USH_DROMEushgenetic
14504400
KRUP_DROMEKrgenetic
22252491
RS29_DROMERpS29physical
25242320

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SRP_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-1208 AND SER-1210, ANDMASS SPECTROMETRY.

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