DPOA2_DROME - dbPTM
DPOA2_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DPOA2_DROME
UniProt AC Q9VB62
Protein Name DNA polymerase alpha subunit B
Gene Name DNApol-alpha73
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 609
Subcellular Localization Nucleus.
Protein Description May play an essential role at the early stage of chromosomal DNA replication by coupling the polymerase alpha/primase complex to the cellular replication machinery..
Protein Sequence MEEELKQQFDEMGVEPADAVLGRCAELAITYNIHDATEFVEQWMAFSLSHLQGEDPAIENLGDFERKVLQLRKDKAGYKATGQKAKSYGSPSVQDTSSLATYGVMEDDPMLDDYVSESAVDSSALHTPKAKKQSDRTANLKGAALFSPASYTPQSAKRKAGLETPSNSVAGKPGDIVDTFGHPKLLAGSSWQSQMEHTVPVTQKLLHNDAPLTIANLGYMNDLLTDRCHNLRVRFNQTGPALVDKKLGQAGAAECIWYPQDRQVLQSAGGLHAVGMIHSEDDGPLDAHSAFMAVLDDDVEDEMDPTLTLNFSRVKSASIFPGQVVLAKGFIPRGKTFMVEEIHTERKLTPATPLQIDRELQFVVASGPFTDSTDLFYEPLHDLLKYLKDHRPDVLVLTGPFLDADHKMVGELAETFDTFFEKMIGGIMESIGSHTAVLVVTSQKDAMALSVYPTPPPALRRTYPNLYMLPDPSLVDLDGFTLGVTSTDVVDHLLSHEFAVNAGERMHRAINHLFHQGSFYPLYPPADEDMAYDSQLALKYAQLKQLPNVLILPSDQRHFIRLVNDCLVINPGRVADKKGGTFARFLVAPSVPGKAANMFNSVACQVQRI
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
122PhosphorylationVSESAVDSSALHTPK
CCHHHCCHHHCCCCC
15.7718327897
147PhosphorylationLKGAALFSPASYTPQ
CCCEECCCCCCCCCH
22.0228490779
150PhosphorylationAALFSPASYTPQSAK
EECCCCCCCCCHHHH
32.6828490779
151PhosphorylationALFSPASYTPQSAKR
ECCCCCCCCCHHHHH
25.2528490779
152PhosphorylationLFSPASYTPQSAKRK
CCCCCCCCCHHHHHH
16.6221082442
155PhosphorylationPASYTPQSAKRKAGL
CCCCCCHHHHHHCCC
36.6428490779
164PhosphorylationKRKAGLETPSNSVAG
HHHCCCCCCCCCCCC
36.7419429919
166PhosphorylationKAGLETPSNSVAGKP
HCCCCCCCCCCCCCC
49.5119429919
168PhosphorylationGLETPSNSVAGKPGD
CCCCCCCCCCCCCCC
20.0619429919
199PhosphorylationQSQMEHTVPVTQKLL
HHHHCCCCCCHHHHH
3.7618327897
208PhosphorylationVTQKLLHNDAPLTIA
CHHHHHCCCCCEEEE
47.2918327897
210PhosphorylationQKLLHNDAPLTIANL
HHHHCCCCCEEEEEC
13.3018327897
212PhosphorylationLLHNDAPLTIANLGY
HHCCCCCEEEEECHH
6.0818327897

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 DPOA2_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DPOA2_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 DPOA2_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DPOLA_DROMEDNApol-alpha180physical
14605208
PRI1_DROMEDNApol-alpha50physical
6403945
DPOLA_DROMEDNApol-alpha180physical
6403945
PRI2_DROMEDNApol-alpha60physical
6403945

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DPOA2_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-155; THR-164; SER-166AND SER-168, AND MASS SPECTROMETRY.

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