SUWA_DROME - dbPTM
SUWA_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SUWA_DROME
UniProt AC P12297
Protein Name Protein suppressor of white apricot
Gene Name su(w[a])
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 963
Subcellular Localization Nucleus speckle. Speckled subnuclear compartment.
Protein Description Regulator of pre-mRNA splicing (and, possibly, of other RNA processing events). Regulate its own expression at the level of RNA processing..
Protein Sequence MLPYNVRNAGGGSVGGILRRTGQGSGTGSTILGNGNSPGALGAGKVSSSLENHRQPPLELLVFGYACKIFRDDEKAREMDHGKQLIPWMGDVNLKIDRYDVRGALCELAPHEAPPGGYGNRLEYLSAEEQRAEQLCEEERYLFLYNNEEELRLRQEEDLKRLQQETSGGCFSQVGFQYDGQSAASTSIGGSSTATSQLSPNSEESELPFVLPYTLMMAPPLDMQLPETMKQHAIIEKTARFIATQGAQMEILIKAKQANNTQFDFLTQGGHLQPYYRHLLAAIKAAKFPPAPQTPLDQQNTDKEAPSADDHSEEVAGGRRNPNQVVITVPTIKYKPSANCAYTQLISKIKGVPLQAVLQEDESSNPGNSQHSGGTASPALSCRSEGHNSQGGEFTPVLLQYNGSTFTHEEESSNREQQDDNDVNGGEPPQVELLKNTSALALAQNYSSESEEEEDQVQPEKEEEKKPEPVLTFPVPKDSLRHIIDKTATYVIKNGRQFEETLRTKSVDRFSFLLPANEYYPYYLYKVTGDVDAASKEEKTRKAAAVAAALMSKKGLSFGGAAAAVSGSNLDKAPVSFSIRARDDQCPLQHTLPQEASDEETSSNAAGVEHVRPGMPDSVQRAIKQVETQLLARTAGQKGNITASPSCSSPQKEQRQAEERVKDKLAQIAREKLNGMISREKQLQLERKRKALAFLNQIKGEGAIVGSAVPVVGPNPPESAAGAATADSGDESGDSVRSIPITYFGPDDDDEVGEQRPEMRLIGSTQKDEEDDDEEDGGDLEKYNLLNDDSTNTFTSKPVLPPTAAPPPAAVLLSDDDDVQLVATTSTRSSSSRHLKTHRRSRSRSKNVRSSDSSPSSRESSRRRRQKSSRLSREPSSNPPRKSQHSSTQRKKTPKKRRRSKSRSRSKSIRRSRSISILRNNRRSRSRSPSCRNAEQRRQQDRRRTPTKKSHKRHKRRRRSSSP
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
364PhosphorylationVLQEDESSNPGNSQH
EEECCCCCCCCCCCC
45.0221082442
437PhosphorylationQVELLKNTSALALAQ
HHHHHHHHHHHHHHH
17.5019429919
438PhosphorylationVELLKNTSALALAQN
HHHHHHHHHHHHHHH
30.5819429919
446PhosphorylationALALAQNYSSESEEE
HHHHHHHCCCCCHHH
11.0719429919
447PhosphorylationLALAQNYSSESEEEE
HHHHHHCCCCCHHHH
34.8719429919
448PhosphorylationALAQNYSSESEEEED
HHHHHCCCCCHHHHH
34.4819429919
450PhosphorylationAQNYSSESEEEEDQV
HHHCCCCCHHHHHCC
52.8619429919
597PhosphorylationHTLPQEASDEETSSN
CCCCCCCCCCCCCCC
44.8122668510
649PhosphorylationTASPSCSSPQKEQRQ
CCCCCCCCHHHHHHH
35.3619060867
678PhosphorylationEKLNGMISREKQLQL
HHHHHHCCHHHHHHH
26.0427626673
738PhosphorylationESGDSVRSIPITYFG
CCCCCCCEEEEEEEC
30.4719429919
742PhosphorylationSVRSIPITYFGPDDD
CCCEEEEEEECCCCC
13.8819429919
872PhosphorylationRQKSSRLSREPSSNP
HHHHHHHCCCCCCCC
33.2222817900
912PhosphorylationRSKSIRRSRSISILR
HCHHHHHHHHHHHHC
22.1125749252
914PhosphorylationKSIRRSRSISILRNN
HHHHHHHHHHHHCCC
23.1825749252
916PhosphorylationIRRSRSISILRNNRR
HHHHHHHHHHCCCCC
19.4722817900

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 SUWA_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SUWA_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 SUWA_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CFA20_DROMECG5343physical
14605208

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SUWA_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-438; SER-447; SER-448;SER-450; SER-649; SER-912; SER-914 AND SER-916, AND MASS SPECTROMETRY.

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