SMG_DROME - dbPTM
SMG_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMG_DROME
UniProt AC Q23972
Protein Name Protein Smaug
Gene Name smg
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 999
Subcellular Localization Cytoplasm . In the cytoplasm of syncytial embryos, accumulates in discrete foci.
Protein Description Translation regulator that binds to the 3'-UTR of specific mRNAs such as nanos (nos) and prevents their translation. Prevents translation of unlocalized nos in the bulk cytoplasm via the recruitment of cup..
Protein Sequence MKYATGTDNAMTSGISGQTNNSNSASNEMQPTTSTPTAAHKEATSTATTTATYANGNPNSNANPSQSQPSNALFCEQVTTVTNLFEKWNDCERTVVMYALLKRLRYPSLKFLQYSIDSNLTQNLGTSQTNLSSVVIDINANNPVYLQNLLNAYKTFQPCDLLDAMSSSSSDKDSMPCYGSDFQITTSAQCDERKLYARKEDILHEVLNMLPLLKPGNEEAKLIYLTLIPVAVKDTMQQIVPTELVQQIFSYLLIHPAITSEDRRSLNIWLRHLEDHIQAAAAGLTNRSYFLQPSPQLVAGGSSTGSGSCSSSATSSSTASCSSVASSSLCPASGSRSSRTNDWQTIAPPSKQLQNKLAGDWRGNGGGSSSGSINPLCDNLNGITLNELASSQNSLGLSLEGSSSLVNGVVAGAGSMLGIAGGDDHDTSFSKNGTEILDFDPVTADMGEACSLASSSLCGRNGGNPVEDRSQPPPNLQQQLLQPPPYASILMGNVGDQFGEINRWSLDSKIAALKTRRSNSLTTQTISSCSSSSNSSVITVNDNCSNSTENLAQFANKPRSFSLSIEHQRGALMNSGSDTRLDEFKPNYIKFHTRNVGMSGIGLWLKSLRLHKYIELFKNMTYEEMLLITEDFLQSVGVTKGASHKLALCIDKLKERANILNRVEQELLSGQMELSTAVEELTNIVLTPMKPLESPGPPEENIGLRFLKVIDIVTNTLQQDPYAVQDDETLGVLMWILDRSIHNEAFMNHASQLKDLKFKLSKMKISMVPKMHHVKPAGVGPNNGNINKPRWNGKTRKCDTKNGSNDRINNRKNSNDMLNFSLNCLPHPLPHHSQQAPPPLPQFDYNGYGGGPSHQPQYKSSSYPSFMGNPQQQPPPPPSSKSHHHPQQMQQMLQQHNHFPALPQQTPPQSHRRSLNNLILVAGGPQQPQQLIFKPGQGVLTNNGSNDNLVLERNQQSQQQQQQRKLSGGVSSAEQQPKKTMAAVVMENLAKFDQHFTLF
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
562PhosphorylationANKPRSFSLSIEHQR
CCCCCCEECEEEHHH
23.5822817900
564PhosphorylationKPRSFSLSIEHQRGA
CCCCEECEEEHHHCC
25.4022817900
575PhosphorylationQRGALMNSGSDTRLD
HHCCCCCCCCCCCHH
26.2118327897
682PhosphorylationSTAVEELTNIVLTPM
HHHHHHHHCCCCCCC
26.6122668510
687PhosphorylationELTNIVLTPMKPLES
HHHCCCCCCCCCCCC
15.5022668510
694PhosphorylationTPMKPLESPGPPEEN
CCCCCCCCCCCCHHH
42.7222668510
967PhosphorylationQQQQRKLSGGVSSAE
HHHHHHHHCCCCCHH
36.2122817900
972PhosphorylationKLSGGVSSAEQQPKK
HHHCCCCCHHHCCCH
33.1612820967

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 SMG_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SMG_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 SMG_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LIS1_DROMELis-1physical
14605208
CUP_DROMEcupphysical
14685270
NDUS1_DROMEND75physical
25816335
SDHB_DROMESdhBphysical
25816335
SDHA_DROMESdhAphysical
25816335
ATPK_DROMECG4692physical
25816335
ORB2_DROMEorb2physical
22284910
AGO2_DROMEAGO2physical
23184089
CAF1_DROMECaf1physical
17050620
NANOS_DROMEnosphysical
17050620
NANOS_DROMEnosphysical
10606265
NANOS_DROMEnosphysical
21081899
NANOS_DROMEnosphysical
8895661
NDUAA_DROMEND42physical
25816335
DHSD_DROMECG10219physical
25816335
ATPB_DROMEATPsyn-betaphysical
25816335
IF4E_DROMEeIF-4Ephysical
14685270
COX7A_DROMECG9603physical
25816335

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SMG_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-564; SER-575 ANDSER-972, AND MASS SPECTROMETRY.

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