OTE_DROME - dbPTM
OTE_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OTE_DROME
UniProt AC P20240
Protein Name Otefin {ECO:0000303|PubMed:2186029}
Gene Name Ote {ECO:0000303|PubMed:2186029, ECO:0000312|FlyBase:FBgn0266420}
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 424
Subcellular Localization Nucleus inner membrane
Peripheral membrane protein . Nucleus, nucleoplasm . Cytoplasm . Chromosome . Cytoplasm, cytoskeleton, spindle pole . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Component of the spindle envelope duri
Protein Description Inner nuclear membrane protein. [PubMed: 2186029]
Protein Sequence MADVDDFDSLSNAELRAKMLAQGLPNIPVTDSSRKVLVKRLRASIGGQASPAASPKKTNRRETLAPAPGAPSAPAAASTPVDKLDGNKVAPATKARRTITAAEAKEPVRRLPEEAIRRRPDEADRLRSEEPVAARKPTTAPAAQPVQTRRTSTSSGSERKVVEPLRKPETIVEQPASSKRADREENYLKVNSLIVLESDEEEDEQLVQAADLVEQEHAARQKTTKLASSGTTTYEYKSKVVEPPRRQVYEATAAPVLPPSVPSARAQTTSSTRSYDYASNPAPGRYSSFVRTAAQGYVTAEAPPVASYSSSYKRTYANELSDDTDSKEDQYESTFARNLARLRAERIGDRISPYSRRTLASGNAGSGSLGYEPRARRSLRPNDNSVSEAFNRWLNSLEQKYHIKSKLFIVLLVLLLIGVYYIFY
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
44PhosphorylationLVKRLRASIGGQASP
HHHHHHHHHCCCCCC		18.4819429919
50PhosphorylationASIGGQASPAASPKK
HHHCCCCCCCCCCCC		13.7421082442
54PhosphorylationGQASPAASPKKTNRR
CCCCCCCCCCCCCCC		39.0821082442
63PhosphorylationKKTNRRETLAPAPGA
CCCCCCCCCCCCCCC		26.8022817900
78PhosphorylationPSAPAAASTPVDKLD
CCCCCCCCCCCCCCC		28.6319429919
79PhosphorylationSAPAAASTPVDKLDG
CCCCCCCCCCCCCCC		23.7019429919
98PhosphorylationPATKARRTITAAEAK
CCHHHHHCCCHHHHC		19.6819429919
100PhosphorylationTKARRTITAAEAKEP
HHHHHCCCHHHHCHH		21.1419429919
128PhosphorylationDEADRLRSEEPVAAR
CHHHHHHCCCCCHHC		51.4022817900
152PhosphorylationPVQTRRTSTSSGSER
CCCCCCCCCCCCCCC		25.2022751930
192PhosphorylationENYLKVNSLIVLESD
HCCCEEEEEEEECCC		23.5923607784
198PhosphorylationNSLIVLESDEEEDEQ
EEEEEECCCHHHHHH		46.2721082442
287PhosphorylationNPAPGRYSSFVRTAA
CCCCCCCHHHHHHHC		18.8821082442
313UbiquitinationASYSSSYKRTYANEL
CCCCCCCCCCCCCCC		39.9631113955
321PhosphorylationRTYANELSDDTDSKE
CCCCCCCCCCCCCHH		27.5419429919
324PhosphorylationANELSDDTDSKEDQY
CCCCCCCCCCHHHHH		47.3519429919
326PhosphorylationELSDDTDSKEDQYES
CCCCCCCCHHHHHHH		39.7819429919
331PhosphorylationTDSKEDQYESTFARN
CCCHHHHHHHHHHHH		24.9523607784
333PhosphorylationSKEDQYESTFARNLA
CHHHHHHHHHHHHHH		24.7223607784
334PhosphorylationKEDQYESTFARNLAR
HHHHHHHHHHHHHHH		14.9023607784
352PhosphorylationERIGDRISPYSRRTL
HHHHCCCCCCCCCCC		20.7619429919
355PhosphorylationGDRISPYSRRTLASG
HCCCCCCCCCCCCCC		20.7625749252
358PhosphorylationISPYSRRTLASGNAG
CCCCCCCCCCCCCCC		26.0918327897
366PhosphorylationLASGNAGSGSLGYEP
CCCCCCCCCCCCCCC		23.8527626673
368PhosphorylationSGNAGSGSLGYEPRA
CCCCCCCCCCCCCCC		21.9627626673
378PhosphorylationYEPRARRSLRPNDNS
CCCCCCCCCCCCCCH		24.1519429919
385PhosphorylationSLRPNDNSVSEAFNR
CCCCCCCHHHHHHHH		29.8619429919
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
54SPhosphorylationKinaseCDK1P23572
GPS
54SPhosphorylationKinaseCDK7-PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OTE_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 OTE_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LAM0_DROMELamphysical
14605208
JMJD6_DROMEPSRphysical
22036573
Y2199_DROMECG2199physical
22036573
ORN_DROMECG10214physical
22036573
RFC1_DROMEGnf1physical
22036573
TBG1_DROMEgammaTub23Cphysical
22751930
LAM0_DROMELamphysical
22751930
LAM0_DROMELamphysical
9632815
TBG2_DROMEgammaTub37Cphysical
22751930
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of OTE_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-44; SER-50; SER-54;SER-192; SER-198; SER-321; THR-324; SER-326; THR-358; SER-378 ANDSER-385, AND MASS SPECTROMETRY.

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