STC_DROME - dbPTM
STC_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STC_DROME
UniProt AC P40798
Protein Name Protein shuttle craft
Gene Name stc
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1106
Subcellular Localization Nucleus.
Protein Description Plays an essential role during the late stages of embryonic neurogenesis. May either fine-tune the guidance or the spatial maintenance of the migrating SNB and in nerve roots, which are composed of axons originating from distinct groups of motor neurons and may be required to either guide or maintain the position of these nerves along a direct and straight path to their ultimate targets in particular muscle fields. May play a role in egg chamber development and/or may confer essential maternal contributions to the early embryo..
Protein Sequence MAEYWQQLTNGAGEAGPGNESSAMADCNGGHESAAVGGSCNRHSNNNYVNFNQFIMQHNLGGGAPSNATSTMQHPVGSSYTNFSLGGGGGAFGLNPPVASASTSHFANVSHQSPNFYSQAMIPTYQNGDGIARVTVTSSYGSVNPSNSNFSSFYTPFGNNPFDFSASKLQASAPEFVPNFAKLSLEETPAAATTNGNSTASLETAINETRPRTLRAQEPAERGANNQCSNHNYERERERERDRDRDRERDRDRDRDRDRDRDRDRDRDSRPGNTRQQRRSDYRDDREDRYERSDRRRPQKQQRYDNHRSNKRRDDWNRNRDRINGFPRAVDDLDTSNESAHPSPEKQSQLQQISPRRGPPLPPADNEKLSQREKLVRDIEQRRLECLVCVEAIKSHQPTWSCRNCYHMLHLKCTITWASSSKSEVGWRCPACQNVLQDLPRDYLCFCGKLKNPPVSRTELAHSCGEVCCRIEGCSHACTLLCHPGPCPPCQANVVRSCGCGRSTKTMQCAMKEEVLCGEICDKLLNCGEHRCQAECHSGKCAACSEQVVQQCHCGKQERKVPCTRESQDKRTYSCKDSCGQPLPCGHHKCKDSCHAGSCRPCKLSPEQITSCPCGKMPVPAGQRSSCLDPIPTCEGICSRTLRCGKPAHPHQCGSKCHLGQCPPCPKQTGVKCRCGHMDQMIKCRQLCNRADDARCKRRCTKKRSCGKHKCNVECCIDIDHDCPLPCNRTLSCGKHKCDQPCHRGNCPPCYRSSFEELYCECGAEVIYPPVPCGTKKPICKLPCSRIHPCDHPPQHNCHSGPTCPPCMIFTTKLCHGNHELRKTIPCSQPNFSCGMACGKPLPCGGHKCIKPCHEGPCQSAGEICRQSCTKPRPTCGHKCAAACHEGACPETPCKELVEVQCECGNRKQNRSCQELAREHSRIATIQLASSMAEMSRGNYMELSEILAPAKKSNKTLDCNDECRLLERNRRLAAALSSGNSDTKQKCLTKYSEFVRGFAKKNPALTKSVYETLTDLVKLAKESKQRSRSHSFPTMNREKRQLVHELCEVFGIESVSYDKEPNRNVVATAHKDRCWFPATSIMEVLARESGQRRVPVPSNNAWGLKK
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
167PhosphorylationNPFDFSASKLQASAP
CCCCCCHHHHHHCCC
32.4721082442
172PhosphorylationSASKLQASAPEFVPN
CHHHHHHCCCCCCCC
31.2525749252
280PhosphorylationNTRQQRRSDYRDDRE
CHHHHHHHHHHCCHH
40.9822817900
335PhosphorylationRAVDDLDTSNESAHP
CHHHCCCCCCCCCCC
40.5225749252
336PhosphorylationAVDDLDTSNESAHPS
HHHCCCCCCCCCCCC
37.9625749252
339PhosphorylationDLDTSNESAHPSPEK
CCCCCCCCCCCCHHH
35.8125749252
343PhosphorylationSNESAHPSPEKQSQL
CCCCCCCCHHHHHHH
35.5122817900
354PhosphorylationQSQLQQISPRRGPPL
HHHHHHCCCCCCCCC
14.1721082442
930PhosphorylationIATIQLASSMAEMSR
HHHHHHHHHHHHHHC
29.2821082442

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 STC_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STC_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 STC_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NU214_DROMENup214physical
14605208
NU153_DROMENup153physical
14605208
NUP58_DROMENup58physical
14605208

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STC_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 THR-335; SER-336; SER-339;SER-343 AND SER-354, AND MASS SPECTROMETRY.

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