ECO_DROME - dbPTM
ECO_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ECO_DROME
UniProt AC Q9VS50
Protein Name N-acetyltransferase eco
Gene Name eco
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1052
Subcellular Localization Nucleus.
Protein Description Acetyltransferase required for the establishment of sister chromatid cohesion and couple the processes of cohesion and DNA replication to ensure that only sister chromatids become paired together. In contrast to the structural cohesins, the deposition and establishment factors are required only during S phase..
Protein Sequence METPTGSGRPSRMATPRLSERKRQLFGSPRSRLRQINDDEDDADVDSLGVLPLKTHVAANRKGRSLFAAVPGKSSSSANSSPETNKENKKTRGGVMTATAEQLPQLFTATMRLNSNSSSNSRNSSPRQTRVQRKRADSSMSSPTSSSEGTPSSRARNSIRRSPRTFSAQKDPDAFSSPESFQTRLSKVAAMLMKGQDSRSMLEKSKKKHNHSLKTTAQVHTTKPKKTSPAEESQSDDEKPSSSKNSRKNTEVRETRSSQIISPKTRNRRRPFTSADINCKTLKAAAHLHENMRSYDEEKTAAVKLENSRSRSKSPVEVFKSNDDAVKRNTGNTNNKTAKSSEVATAKRPESPGSSMKIDVEVPESDEEASNHKPQKRQHPETSTPVAPSADADSGSPQSKMRKVTLSSSIPTMAFYSHSGEAVTKSRRRPSISKNSLKQPTKISPTSRPLLGINKGVHHKIRKRHGFANRLPATDMDNILNSLSNERLKNLITTKREERAKVEEVHQILRNAKDPIKMAKPLSVIEADDANNNNNLPATAWQETSADFSDLSDVEDIDPIIEVEPIIPIIRHEPVQKSPTAEPADLSKRKFFKSGRRSSTCMEVRITDNIRASVSQGKIELVQTIRRKPRQVRVKSATIFSAEQATVDAILKNLDDTVVDEIVEANPVVQATPIDAEETTMETESLPDIIEYAPEANDVEIDPFAEFRQRLPYQTDDPNVVEQQQILLEFLISNNICTEKNFEIFIANPDDYKDEANQIVDNLYMVVNSEEAAQLAQMETVENTAVAIAPKQDAPAVEEVQPKLFPIFTQRLQPVVQKSLRRRPDTSMRLLTAAGGSNQYQIDAGQKAFGARQCQQCGLVYTVHEPEEELLHREYHNSIHVLRFKGWIDEDIVSVYPEWASDGRIIRINERAPTARLDRLRDLIGVVDKELGYSSYIVPKIFVAFIAVRKQQIVGFCLVQPLSQAHRFIQVDGTDYFSEESYPASCGVSRIWVSPLQRRSGIASKLLRVVQCHTVLGQEIARECIAFSTPTDDGRALARQFTGLDNFLTYDQ
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
28PhosphorylationRKRQLFGSPRSRLRQ
HHHHHHCCCHHHHHC		15.1419429919
80PhosphorylationKSSSSANSSPETNKE
CCCCCCCCCCCCCCC		47.1630478224
81PhosphorylationSSSSANSSPETNKEN
CCCCCCCCCCCCCCC		26.9430478224
121PhosphorylationNSNSSSNSRNSSPRQ
CCCCCCCCCCCCCCH		34.4827626673
176PhosphorylationQKDPDAFSSPESFQT
CCCCCCCCCCHHHHH		46.8619429919
177PhosphorylationKDPDAFSSPESFQTR
CCCCCCCCCHHHHHH		26.6619429919
180PhosphorylationDAFSSPESFQTRLSK
CCCCCCHHHHHHHHH		26.4919429919
233PhosphorylationKTSPAEESQSDDEKP
CCCCCHHCCCCCCCC		26.8719429919
235PhosphorylationSPAEESQSDDEKPSS
CCCHHCCCCCCCCCC		57.2019429919
241PhosphorylationQSDDEKPSSSKNSRK
CCCCCCCCCCCCCCC		59.3119429919
242PhosphorylationSDDEKPSSSKNSRKN
CCCCCCCCCCCCCCC		54.5919429919
243PhosphorylationDDEKPSSSKNSRKNT
CCCCCCCCCCCCCCH		39.9519429919
246PhosphorylationKPSSSKNSRKNTEVR
CCCCCCCCCCCHHHH		48.6619429919
262PhosphorylationTRSSQIISPKTRNRR
HHHHHCCCCCCCCCC		23.2125749252
310PhosphorylationVKLENSRSRSKSPVE
HCCCCCCCCCCCCEE		40.5022817900
312PhosphorylationLENSRSRSKSPVEVF
CCCCCCCCCCCEEEE		38.4419429919
314PhosphorylationNSRSRSKSPVEVFKS
CCCCCCCCCEEEECC		35.1119429919
351PhosphorylationATAKRPESPGSSMKI
CCCCCCCCCCCCCEE		36.9219429919
354PhosphorylationKRPESPGSSMKIDVE
CCCCCCCCCCEEEEE		30.5522668510
365PhosphorylationIDVEVPESDEEASNH
EEEECCCCCHHHHCC		44.2319429919
370PhosphorylationPESDEEASNHKPQKR
CCCCHHHHCCCCCCC		42.6225749252
396PhosphorylationSADADSGSPQSKMRK
CCCCCCCCCCHHHCE		24.5830478224
578PhosphorylationRHEPVQKSPTAEPAD
CCCCCCCCCCCCCCC		15.4719429919
580PhosphorylationEPVQKSPTAEPADLS
CCCCCCCCCCCCCCC		51.2319429919
587PhosphorylationTAEPADLSKRKFFKS
CCCCCCCCCCHHHHC		30.8419429919
599PhosphorylationFKSGRRSSTCMEVRI
HHCCCCCCCCEEEEE		24.6621082442
636PhosphorylationPRQVRVKSATIFSAE
CCCEECEEEEEEECH		27.9921082442
638PhosphorylationQVRVKSATIFSAEQA
CEECEEEEEEECHHH		29.6421082442
818AcetylationRLQPVVQKSLRRRPD
HHHHHHHHHHHCCCC		39.5921791702
929AcetylationDLIGVVDKELGYSSY
HHHHHHCHHHCCCCC		43.1421791702
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 ECO_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ECO_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 ECO_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ECO_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-176; SER-177; SER-310;SER-312 AND SER-314, AND MASS SPECTROMETRY.

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