HYD_DROME - dbPTM
HYD_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HYD_DROME
UniProt AC P51592
Protein Name E3 ubiquitin-protein ligase hyd
Gene Name hyd
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 2885
Subcellular Localization Nucleus .
Protein Description E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (By similarity). Required for regulation of cell proliferation in imaginal disks and germ cells. Acts as a negative regulator of hh, ci and dpp expression in the anterior of the eye disk..
Protein Sequence MVSMQFVLQPLPGSDDQFIERIREVSDKVNRFGYGSHRIFEQLKIPVKEVVIGPAHIGVLLEDGKAFRVSFSINSEKLDLTKSDAKCSTSGGSGTASASKAPSSSRPMARSRARLLRATGRSNSTGQGSGSRSTGVIIGGSTSSRPLVTVPATYVPEELISQAEVVLQGKSRNLIIRELQRTNLDVNLAVNNLLSRDDEEAEDTEEGADNYVPEDLISLLDNGFSGDNNSVIIDPSDGLFSEEIFSNYSSIRNLLFDRIRSERSNANANAADSNQSTTRSTSSGTALTGNSGLSAQISVNADREAFSRWRDRQYYGPRRWISKDDYTWEKDADSKKKEPSPMLSPIWISEELQPWPEKSSVRFKTIGALYSEFIALSESGDLYQWRWSDAEPYKSETENVYHPKTVSLNIVERVELISANFIRCSVVTETNRVATWMDEQLGYIGAKLEHSCCAFNEFISDSITKIYVCSLYTVVKTESNNIYWWGVLPFDQRRFLWDKFRTKTKKPFKVVATDINVGAQVIMKKCPMYQSGSIGFTCSNGVPKVGQLLNSVWTFTDVCRMKIININTNSGVDKSQAAGNNLNAHGITPDKDLPKSTAMPSTGSSKNGQSFSNSKESTDRIDMPPPPSPASSTCSDTGSVTSHKRTKRATTKEDSNAPQEGRKDEELWEVKDVVFVEDKVGPVGKVLKVDGDFVAVRFPAINAAAVAAAAAATSSTSNTASTSKEEGKEDDWQQCRLLRREDVQIFRTAMSTRGPDWLQKQPKKINVGGDAAGAQILTLAVDSRGIHVIKKVLGKIHYSLYNLYNCKQEQNCLFPTDCNSFIGSTPGNILMACNDDCSGNSSTIVLRDGNGALYPLAKDCLGSIKDPQWFDLPPVKSITMSTISLPAMLSGVNLKSKVCMTALLFDTQKLMPHILRCDVKNSFAALGRLEREDQADTALVVEERCDGARNIFHACVIMCAPSSNKDSPPDSPSGGVEKKSLVGLSVARSIPTVSTSAYVSSIAFGASASSSNENSSFATMSSSAAGSASSTSRDNRTNLRDMMNRLINSDQAEQSGSQPMATNNEDHAYIPWPAETPAASNLSASSSQNVSDSIEDDISKIIPSSSQSSMLSNIKLGSPTYTFDLAQRREHALTILQQMCVSPALRPYLCHMLSTKDAQGQTPFMLSVSCRAYEAGIILLNTILMLSEQDPQLKEAMIFPNGSPADQSPLHVICYNDTCSFTWTGADHINQNIFECKTCGLTGSLCCCTECARVCHKGHDCKLKRTAPTAYCDCWEKCKCKALIAGNLTKRFALLCKLVSCTDLVTKFNSKGESILLFLIQTVGRQIVEQRQYRFSVRVRNVSTAATGATGNNSVISNRKTSAAEIDNDMPDHDLEPPKFARKALERLLIDWNAVRSMIMSGAERGDVPNPAGSASENSNSEGFNMFIQTQHGSTLLDKFTHSLIVKCTSDHLDTLLLTLVRELQNASVSNRSKEAEEVVRRFVRSVARVFVIFNLEKQPNPEKRKSHSSCNKYVQSCVKVFQTLHKISIEELCEVSEALIAPVRLGVVRPTAPFTMSSSNLDNSDDLFSVDPLAPSNVESPSEQILVHDAGNDQSANFNIQQNYDVVAMETIRDASESEEVINREANSHNQDDELIENQRNEDGMQDDESDNDFTFNDAETESDSDDNQSNQEVQRSVQAGATVGSENDIGVLFLEDESGDSSAQEEDGSEDGESDDQSDEFNFNEQQLERRSTNSNARSDLAPQTMQWAIRSRDTARSSVRVPTGSNMVFIDPMALRRSTVPASTTVTTPSIEPHTMATTASNLARAFGITIRQISELISILSYNVLNDIETSLKIQNDEAIAVQAFVEKRLKATWDWMFTVMDGTEAQLKFGAYLTNYTDPNHPLHPLNLSAQASSSQTPAPATSSSVNGVNIMGSNSRRDFFTYCLSLMRSHTSEHRDALPVLDITALRHIAYVLDAFVYYMRNDSGFYDKQDTISGRINNLSPMTESYDTDDELANLEEFNADVQMSASSMPSGSQGTRRHAFFARSESTLSLGCSAPEGFELPLDMAMPLADKPHLLQPNSKRQELFANLPLLVTTNANNSGATNDGDGGSIFDYTPTRLGFSNSLKRNERVYETVPIDSSKTGDGNVTNKAEGSTDSNIYVQLKKKQGSDDFKSHKEADGNQSKYEKVVLMETDDSLPSTSKSTEALMATRPEVIIAPNKASVSPATAARSVIVLAGGSCLKTIDSDINNYSASNLSTAEQAKCDTQYQKSTSDHLLLFPARGSQFYQSNFSELPSWNFLLSRWKLTLDLFGRVFMDDVGMEHGSVLPELRGFPVKEMRFRRHMEKLRNGQQRDLVLCKLERNRESLIVQTFKELNTQFGNQSRRIQPPITFNRVKVTFKDEPGEGSGVARSFYTSIAEALLASAKIPNLESVQVGTNHSKYVVPFSSILRSRTVSGSSRDQSTLQRRGSNSKILWRSARERKALNLDARPYTPPNSSDNATPESLNDHLSVHLQQIGERLYPKIHSINQTHAPKITGMLLEIPTPQLLSVISSDETLRQKVNEAIEIITFKQKSETSAQSSQPKKSPSVVVVDPVDDDNEPLFYSPGKRGFYTPRQGFASFERINAFRNIGRLIGLCLLQNELLPLFLQRHVLKYILGRKIKFHDLAFFDPALYESFRQIIQNAQTKEGEETINRMELCFVIDLMKEEGCGNRELIPGGRDVAVTSSNIFEYVRRYTEYRLIKSQEKALEALKDGVFDVLPDNSMINLTAEDLRLLLNGVGDINVSTLISYTTFNDESSEGPDKLLKFKKWFWSIVEKMNIMERQDLVYFWTGSPALPASEEGFQPLPSVTIRPADDSHLPTANTCISRLYIPLYSSKSILRSKMLMAIKSKNFGFV
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
124PhosphorylationRATGRSNSTGQGSGS
HHHCCCCCCCCCCCC		34.8522817900
264PhosphorylationDRIRSERSNANANAA
HHHHHHHHCCCCCCC		35.9221082442
322PhosphorylationYGPRRWISKDDYTWE
CCCCCCCCCCCCCCC		24.0721082442
588PhosphorylationNLNAHGITPDKDLPK
CCCCCCCCCCCCCCC		29.9921082442
628PhosphorylationIDMPPPPSPASSTCS
CCCCCCCCCCCCCCC		38.5822817900
631PhosphorylationPPPPSPASSTCSDTG
CCCCCCCCCCCCCCC		29.5722817900
632PhosphorylationPPPSPASSTCSDTGS
CCCCCCCCCCCCCCC		35.2222817900
633PhosphorylationPPSPASSTCSDTGSV
CCCCCCCCCCCCCCC		17.3422817900
650PhosphorylationHKRTKRATTKEDSNA
CCCCCCCCCCCCCCC		42.2921082442
967PhosphorylationAPSSNKDSPPDSPSG
CCCCCCCCCCCCCCC		39.6822817900
971PhosphorylationNKDSPPDSPSGGVEK
CCCCCCCCCCCCCCC		27.0919429919
973PhosphorylationDSPPDSPSGGVEKKS
CCCCCCCCCCCCCHH		52.7319429919
980PhosphorylationSGGVEKKSLVGLSVA
CCCCCCHHHHCHHHC		39.0821082442
1106PhosphorylationSKIIPSSSQSSMLSN
HHHCCCCCCHHHHHC		38.1221082442
1118PhosphorylationLSNIKLGSPTYTFDL
HHCCCCCCCEEEECH		25.2219429919
1120PhosphorylationNIKLGSPTYTFDLAQ
CCCCCCCEEEECHHH		36.5719429919
1122PhosphorylationKLGSPTYTFDLAQRR
CCCCCEEEECHHHHH		17.1019429919
1343PhosphorylationSVRVRNVSTAATGAT
EEEEEEECCCCCCCC		18.8421082442
1361PhosphorylationSVISNRKTSAAEIDN
CCCCCCCCCHHHCCC		21.9919429919
1362PhosphorylationVISNRKTSAAEIDND
CCCCCCCCHHHCCCC		28.6319429919
1617PhosphorylationMETIRDASESEEVIN
EEEECCHHHCHHHHH		46.0419429919
1629PhosphorylationVINREANSHNQDDEL
HHHHHHHHCCCCHHH		30.7522817900
2032PhosphorylationRHAFFARSESTLSLG
CEEEEEECCCEECCC		32.2519429919
2034PhosphorylationAFFARSESTLSLGCS
EEEEECCCEECCCCC		35.5819429919
2035PhosphorylationFFARSESTLSLGCSA
EEEECCCEECCCCCC		19.1319429919
2037PhosphorylationARSESTLSLGCSAPE
EECCCEECCCCCCCC		23.8619429919
2041PhosphorylationSTLSLGCSAPEGFEL
CEECCCCCCCCCCCC		45.0923607784
2156PhosphorylationQLKKKQGSDDFKSHK
EEEHHCCCCCHHHHH		31.3619429919
2180PhosphorylationEKVVLMETDDSLPST
EEEEEEECCCCCCCC		31.0119429919
2183PhosphorylationVLMETDDSLPSTSKS
EEEECCCCCCCCCCC		45.0119429919
2211PhosphorylationAPNKASVSPATAARS
CCCCCCCCHHHHHCE		13.3119429919
2214PhosphorylationKASVSPATAARSVIV
CCCCCHHHHHCEEEE		25.0025749252
2218PhosphorylationSPATAARSVIVLAGG
CHHHHHCEEEEECCC		16.0921082442
2226PhosphorylationVIVLAGGSCLKTIDS
EEEECCCCHHHHHCC		18.5021082442
2258PhosphorylationCDTQYQKSTSDHLLL
CCCCCCCCCCCEEEE		20.0219429919
2259PhosphorylationDTQYQKSTSDHLLLF
CCCCCCCCCCEEEEE		45.2519429919
2260PhosphorylationTQYQKSTSDHLLLFP
CCCCCCCCCEEEEEE		30.0819429919
2435PhosphorylationKYVVPFSSILRSRTV
CEEEEHHHHHEEECC		26.4821082442
2445PhosphorylationRSRTVSGSSRDQSTL
EEECCCCCCCCHHHH		18.0727626673
2446PhosphorylationSRTVSGSSRDQSTLQ
EECCCCCCCCHHHHH		43.3225749252
2574PhosphorylationQSSQPKKSPSVVVVD
CCCCCCCCCCEEEEC		28.6519429919
2576PhosphorylationSQPKKSPSVVVVDPV
CCCCCCCCEEEECCC		34.3419429919
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 HYD_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HYD_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 HYD_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PABP_DROMEpAbpgenetic
20604743
HH_DROMEhhgenetic
12421709
SGG_DROMEsggphysical
26334301
CI_DROMEciphysical
26334301
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HYD_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-628; SER-631; SER-967;SER-1362; SER-2037 AND SER-2574, AND MASS 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-2183, AND MASSSPECTROMETRY.

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