KDM5_DROME - dbPTM
KDM5_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KDM5_DROME
UniProt AC Q9VMJ7
Protein Name Lysine-specific demethylase lid
Gene Name lid
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1838
Subcellular Localization Nucleus .
Protein Description Histone demethylase that specifically demethylates 'Lys-4' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-9', H3 'Lys-27', H3 'Lys-36', H3 'Lys-79' or H4 'Lys-20'. Specifically demethylates trimethylated H3 'Lys-4'. Required for the correct regulation of homeotic genes during development. Plays a role in the regulation of the circadian rhythm and in maintaining the normal periodicity of the circadian clock. Regulates the expression of clock-controlled genes including tim, per and cry..
Protein Sequence MSAKTEADNTTAANSGGGGVGSGTSSGGGASANGTATPARRLRTRNSTGNGTNSGSESVKKSNANDEPSTPVTPAGATGSHTHAPPGISPAVMERPMPSVPMNHASSSVSASKKYHNSCPHPTPTPAPTGHKKSVHTQPHSSNKFDQGKNEEFHFDTPPECPVFRPTTEEFKNPLAYISKIRSIAEKCGIAKILPPATWSPPFAVDVDKLRFVPRVQRLNELEAKTRVKLNFLDQIAKFWELQGSSLKIPMVERKALDLYTLHRIVQEEGGMEQTTKDRKWAKVANRMQYPSSKSVGATLKAHYERILHPFEVYTSGKVLGPTPTSSGSGSTPVKLEDGGGTDYKAHEIPTRQQIAPPNETNTRRSKRFGNSNASCGLSGVTPTTKPSAGVFVKTETKEEFKRDLLSSFNAVNSGGSPLATGTTANTRGASQKKGGEPPALIVDPLMKYICHICNRGDVEESMLLCDGCDDSYHTFCLLPPLTSIPKGEWLCPRCVVEEVSKPQEAFGFEQAEREYTLQQFGQMADQFKQEYFRKPVHLVPTEMVEREFWRIVSSIDEDVTVEYGADLHTMDHGSGFPTKSSLYLLPGDQEYAESSWNLNNLPLLEDSILGHINADISGMNAPWMYVGMCFAAFCWHNEDHWSYSINYLHWGEPKTWYGVPGSCAEQFEETMKQAAPELFSSQPDLLHQLVTIMNPNILMNNRVPVFRTDQHAGEFVITFPRAYHAGFNQGYNFAEAVNFAPADWLKMGRECVNHYSMLRRFCVFSHDELVCKMALEPAKLTFGIATACYIDMAEMVDTEKKLRKSLLEWGVTRAERRAFELVNDDERHCQECNTTCFLSAVACECNDKLIVCLRHYTVLCGCAPEKHTLIYRYTLDEMPLMLQKLKVKAHSFERWLSRCRDIVDAHTPTSVTLQELQELCKEAETKKFPSSLLIDRLNAAAVEAEKCVTVIQQLGINKVRTRSDHNQEAAQYKLTMEELELFVQEIDNLCCIIDEGASVRELLVLGKQFVERSESQLQLSLESLEESELETLINEGSSLRIELQQLDLLQKRLKQCKWYKRSQGLRETSSKLTYQDVKNLLHIAAADLDPTDPYVDKEMRKLQQIGADIEAWESQAAKYFRRLTQQHELGEIEQFLKSASDINGQVPSHGLLKDALRKAREWLRAVEQLQQNNHVTYCHTLEAMIERGLNIPIQLEELSRMQGHLNSAHQWKDNTACAFLKKGTFYTLLEVLMPRSDAINIDSDLKPRFQDDFLKEKNPAEIVASFKHAEEQELLDMRELRRQNMNKNPMRDMFCLCKSEFRNLMFNCQLCRDWFHEDCVPPPSATNQNGIVNGGSGPGTNRPKWLCPSCVRSKRPRLETILPLLVQLQQLPIRLPEDEALRCLAERAMNWQDRARKALSSPDVSAAQEAIMAQQQQKRRSEGGAGVGNISSPRKPRRRGSLTKEASGSTESDADDDDDEDECRLRIVEDNFSNDEDEPRTAPATSTVNSDLLKLLSDSEIENLLDLMMEGDLLEVSLDETQELWRILETMPPTLLQAEAMERVVQYMQRQRQQHTNPLPTSGAEDSNDSLMVQNSPNSNSNSGGATGSASNSGRNKKRRSNDTGGNSAVPRKKQSTPKQTPGKKGSAAAARKSDAKASPAASTTPGADADAENKQANGGNTNSSTGSGGGNSATTTPTPGSTHKKRKRTSTTATNNNNNNNNNSTNNSNSSTNLNSNTTSGQGAATGGNNATGGQKKHAQRSQQAAQEDDEEECRAENCHKPTGREVDWVQCDGGCNEWFHMYCVGLNRSQIKPDDDYICIRCTKTVAIGTQGSGHSMSVASTTTPGKQRAVQSAR
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
44PhosphorylationTPARRLRTRNSTGNG
CCCHHCCCCCCCCCC		38.5019429919
47PhosphorylationRRLRTRNSTGNGTNS
HHCCCCCCCCCCCCC		34.1119429919
48PhosphorylationRLRTRNSTGNGTNSG
HCCCCCCCCCCCCCC		37.9119429919
52PhosphorylationRNSTGNGTNSGSESV
CCCCCCCCCCCCCCH		30.1519429919
54PhosphorylationSTGNGTNSGSESVKK
CCCCCCCCCCCCHHC		43.4619429919
56PhosphorylationGNGTNSGSESVKKSN
CCCCCCCCCCHHCCC		26.9019429919
58PhosphorylationGTNSGSESVKKSNAN
CCCCCCCCHHCCCCC		40.7219429919
69PhosphorylationSNANDEPSTPVTPAG
CCCCCCCCCCCCCCC		43.2121082442
70PhosphorylationNANDEPSTPVTPAGA
CCCCCCCCCCCCCCC		32.2821082442
323PhosphorylationSGKVLGPTPTSSGSG
CCCEECCCCCCCCCC		37.0822817900
329PhosphorylationPTPTSSGSGSTPVKL
CCCCCCCCCCCCEEC		31.3629892262
331PhosphorylationPTSSGSGSTPVKLED
CCCCCCCCCCEECCC		31.1022668510
332PhosphorylationTSSGSGSTPVKLEDG
CCCCCCCCCEECCCC		35.3122668510
382PhosphorylationSCGLSGVTPTTKPSA
CCCCCCCCCCCCCCC		20.6021082442
417PhosphorylationNAVNSGGSPLATGTT
CCCCCCCCCCCCCCC		21.9230478224
1422PhosphorylationQQQQKRRSEGGAGVG
HHHHHHHHCCCCCCC		44.6319429919
1432PhosphorylationGAGVGNISSPRKPRR
CCCCCCCCCCCCCCC		37.9919429919
1433PhosphorylationAGVGNISSPRKPRRR
CCCCCCCCCCCCCCC		25.5619429919
1453PhosphorylationEASGSTESDADDDDD
CCCCCCCCCCCCCCC		37.8822668510
1474PhosphorylationRIVEDNFSNDEDEPR
EEEECCCCCCCCCCC		50.0221082442
1571PhosphorylationGAEDSNDSLMVQNSP
CCCCCCCCEEEECCC		23.7122668510
1577PhosphorylationDSLMVQNSPNSNSNS
CCEEEECCCCCCCCC		14.3622668510
1602PhosphorylationGRNKKRRSNDTGGNS
CCCCCCCCCCCCCCC		42.9919429919
1635PhosphorylationSAAAARKSDAKASPA
CHHHHHHHCCCCCCC		36.9322817900
1640PhosphorylationRKSDAKASPAASTTP
HHHCCCCCCCCCCCC		17.8622817900
1644PhosphorylationAKASPAASTTPGADA
CCCCCCCCCCCCCCC		34.6119429919
1645PhosphorylationKASPAASTTPGADAD
CCCCCCCCCCCCCCC		32.0819429919
1646PhosphorylationASPAASTTPGADADA
CCCCCCCCCCCCCCC		19.7519429919
1676PhosphorylationSGGGNSATTTPTPGS
CCCCCCCCCCCCCCC		30.9021082442
1677PhosphorylationGGGNSATTTPTPGST
CCCCCCCCCCCCCCC		30.4121082442
1827PhosphorylationMSVASTTTPGKQRAV
EEEEECCCCCCHHHH		30.0821082442
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 KDM5_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KDM5_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 KDM5_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EAF3_DROMEMRG15physical
19782028
HDAC1_DROMERpd3physical
19782028
CTBP_DROMECtBPphysical
19782028
MCM4_DROMEdpaphysical
19782028
MCM6_DROMEMcm6physical
19782028
MCM7_DROMEMcm7physical
19782028
ASF1_DROMEasf1physical
19782028
MYC_DROMEdmgenetic
17311883
MYC_DROMEdmphysical
17311883
ASH2_DROMEash2physical
17311883
CADE_DROMEshggenetic
26490676
PTP61_DROMEPtp61Fgenetic
26490676
JHD1_DROMEKdm2genetic
21124823
SUV39_DROMESu(var)3-9genetic
21205864
STAT_DROMEStat92Egenetic
26490676
HDAC1_DROMERpd3physical
26848313
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KDM5_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-323; SER-1422; SER-1433;SER-1635 AND SER-1640, 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-1474, AND MASSSPECTROMETRY.

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