Y2199_DROME - dbPTM
Y2199_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID Y2199_DROME
UniProt AC Q8IRH5
Protein Name Zinc finger protein CG2199
Gene Name CG2199
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 733
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MRNILLCENMTKVQKEVRCDHCGTSQGSKSVFSGQKVFLGRKITDVLETITHRSIPSSLPIKICFVCTSTFMSSAALIEKVRETVDRVQEQPAKKTKVAEIEEPSTQESDKKAVKVPKKNTTLRQRSKSIAAFPPSFVNGANTNTEIEIISASPKKLDKTPKKQISRLFEDNLNDSVKLTPAKEVSSTKKAFLNLFGNGGNDAIEVLTESEEEEDSDKGPITINTNNFQCPECEFHAKFPKPYKEHLQKEHGLQRPRIYPCTLCIKTFGVLKTLKNHLRDTHSRTFESEAKTKAKESKEKEAKSGAKNKIDAKAKETNAVSQRKKPKEKKSKEKKTEIKCNVETKVVDEIDDQVNNKKGTDSEDADQTQATKIASFKALNESLMKKRMLENVIDSEYTFAINGSSASTPRADSNNFQCEICDCELMTAKQMQEHMKTVHSIDKPKVFKCHVCEKSLATKQSLKTHMTLHADGAEAPNSSKRKILQDEDEDVDILGTTQIENTAEKVEGPKKSQQSPTKAAKFTNRKILQEEDEVVEIVDAFKTDNTAEDDEGPAEEKIIRSRNNIQHQVDGGMIAPRSPAKKTKKTSHVDLSVSTTNGNSPAKSEKRKKQDKSEDTLPSSDVDIVEEINYNVRPHKKARLESIGDSTADESTLSCDRCGKFVKSRQRLDSHMEKKHAAKLQCTLCKEVYQNQMDYVAHFSNCGSEGGLPCGVANCKKVFTEANFLSSHLRKRH
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
105PhosphorylationVAEIEEPSTQESDKK
EEECCCCCCCHHHHC		46.1022668510
106PhosphorylationAEIEEPSTQESDKKA
EECCCCCCCHHHHCC		47.2527626673
109PhosphorylationEEPSTQESDKKAVKV
CCCCCCHHHHCCCCC		44.9317372656
127PhosphorylationNTTLRQRSKSIAAFP
CCCHHHHHHHCEECC		23.5522817900
129PhosphorylationTLRQRSKSIAAFPPS
CHHHHHHHCEECCHH		20.7823607784
136PhosphorylationSIAAFPPSFVNGANT
HCEECCHHHCCCCCC		41.9023607784
143PhosphorylationSFVNGANTNTEIEII
HHCCCCCCCCEEEEE		42.8823607784
145PhosphorylationVNGANTNTEIEIISA
CCCCCCCCEEEEEEC		35.9823607784
151PhosphorylationNTEIEIISASPKKLD
CCEEEEEECCHHCCC		28.4923607784
153PhosphorylationEIEIISASPKKLDKT
EEEEEECCHHCCCCC		30.3823607784
176PhosphorylationFEDNLNDSVKLTPAK
HHCCCCCCCCCCCHH		21.7819429919
180PhosphorylationLNDSVKLTPAKEVSS
CCCCCCCCCHHHCCC		18.5822817900
188PhosphorylationPAKEVSSTKKAFLNL
CHHHCCCCCHHHHHH		29.1118327897
360PhosphorylationQVNNKKGTDSEDADQ
HHHCCCCCCCCCCHH		45.2719429919
362PhosphorylationNNKKGTDSEDADQTQ
HCCCCCCCCCCHHHH		36.8925749252
368PhosphorylationDSEDADQTQATKIAS
CCCCCHHHHHHHHHH		22.2525749252
440PhosphorylationEHMKTVHSIDKPKVF
HHHHHHHHCCCCCEE		28.3119429919
578PhosphorylationGGMIAPRSPAKKTKK
CCCCCCCCCCCCCCC		28.3119429919
600PhosphorylationVSTTNGNSPAKSEKR
EECCCCCCCCHHHHH		27.8622668510
613PhosphorylationKRKKQDKSEDTLPSS
HHCCCCCCCCCCCCC		49.3319429919
616PhosphorylationKQDKSEDTLPSSDVD
CCCCCCCCCCCCCCH		36.2019429919
619PhosphorylationKSEDTLPSSDVDIVE
CCCCCCCCCCCHHHH		42.1319429919
620PhosphorylationSEDTLPSSDVDIVEE
CCCCCCCCCCHHHHH		39.4519429919
642PhosphorylationHKKARLESIGDSTAD
CCCHHHHHHCCCCCC		36.1419429919
646PhosphorylationRLESIGDSTADESTL
HHHHHCCCCCCCCCC		21.9319429919
647PhosphorylationLESIGDSTADESTLS
HHHHCCCCCCCCCCC		42.7519429919
654PhosphorylationTADESTLSCDRCGKF
CCCCCCCCCCCCCHH		17.6618327897
670PhosphorylationKSRQRLDSHMEKKHA
HHHHHHHHHHHHHHH		29.3522817900
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 Y2199_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of Y2199_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 Y2199_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RB97D_DROMERb97Dphysical
14605208
GCL_DROMEgclphysical
14605208
JRA_DROMEJraphysical
14605208
STX1A_DROMESyx1Aphysical
14605208
FOXO_DROMEfoxophysical
14605208
ELBOW_DROMEelBphysical
14605208
HSP23_DROMEHsp23physical
14605208
SRP68_DROMESrp68physical
14605208
AEF1_DROMEAef1physical
14605208
FMR1_DROMEFmr1physical
14605208
DCTD_DROMECG6951physical
14605208
DX39B_DROMEHel25Ephysical
14605208
DCTN2_DROMEDmnphysical
14605208
LARK_DROMElarkphysical
14605208
PGPLE_DROMEPGRP-LEphysical
14605208
ANX11_DROMEAnxB11physical
14605208
CPSF6_DROMECG7185physical
22036573
MED17_DROMEMED17physical
22036573
MED11_DROMEMED11physical
22036573
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of Y2199_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-109; SER-153; SER-176;THR-180; THR-188; SER-600; SER-642; SER-646; THR-647 AND SER-654, ANDMASS SPECTROMETRY.
"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells.";
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
Mol. Biosyst. 3:275-286(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND MASSSPECTROMETRY.

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