LSDA_DROME - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LSDA_DROME
• UniProt AC: Q9VW97
• Protein Name: Possible lysine-specific histone demethylase 1
• Gene Name: Su(var)3-3
• Organism: Drosophila melanogaster (Fruit fly).
• Sequence Length: 890
• Subcellular Localization: Nucleus . Chromosome . In early cleavage, protein displays a uniform nuclear distribution. At metaphase, protein is detected at the chromosome periphery, and between the chromosomes during anaphase. A rather uniform interphase chromatin association i
• Protein Description: Probable histone demethylase that specifically demethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. Required for heterochromatic gene silencing. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Demethylates both mono- and tri-methylated 'Lys-4' of histone H3. May also demethylate 'Lys-9' of histone H3, Plays a role in the repression of neuronal genes..
• Protein Sequence: MKPTQFGGSSSKMTEPIEYVTLISDDSDGEPTPKRNVNHPPSALSAPNPGQKQKHPDEDSNDAPATSDERRTSRRNRPKVDYSNRPSGSGDTASNDKSGSASMGPNNQQAERRSQSQTRKSEANATSSSVSGPSAGNSRPSQNGDSKDRDAGTPTVLSGQEGAVFQSRLPFNKMTPNEEACFPDISRSGILGHRVFLNIRNSLLHMWVDNPKIQLSFEIALKNLPPPFDSEPSLVRRVHSFLERHGFINFGIFKRLKPIPAKKLGKVIVIGAGISGLAVAHQLQQFGMDVIVLEARDRVGGRISTFRKNSYIADVGAMVVTGVYGNPMTILSKQIGMDLVPIQQTCPLYGPDGKPVPKEKDDVIEREFNRLLESASYLSHRLDFNYAGDCPVSLGDALEWIISMQEMQVMHKRGQHMQEIIATQTKIIEQRRRLKTLRDTIGKLKNEHLAMINQRKPKGTDGDLKYCYQEFNIRNTQIKMEETISTFHDLHAEEKQMLAKLHELEQNRPSDVYLSSRDRLILDWHFANLEFANATRLNNLSLKHWDQDDDFEFIGHHTTVRNGYSCVPVALTENLDIRVNSAVKEIKYGTKGVEVVAENLKTSNSQMTYKADLVVCTLTLGVLKVAVAHKESQQSNTVKFDPPLPDWKQQAIKRLGFGNLNKVVLCFDRIFWDPNANLFGHVGSTTASRGEMFLFWSISSSPVLLALVAGMAANLVESVTDDIIIGRCMSVLKNIFGNTSVPQPKETVVTRWRSDPWARGSYSYVSVGSSGSDYDLLAAPVIPPSSKDAEGLPRLFFAGEHTIRNYPATVHGAYLSGLREAGRIADYYLGYPEGTPPDIGYSVAEAANLVSVGNVVKLRDLSPNLSDSSPSSKKSEENSNSNTADSTELQ

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
19	Phosphorylation	KMTEPIEYVTLISDD CCCCCEEEEEEEECC	10.23	25749252
21	Phosphorylation	TEPIEYVTLISDDSD CCCEEEEEEEECCCC	19.92	19429919
24	Phosphorylation	IEYVTLISDDSDGEP EEEEEEEECCCCCCC	38.18	19429919
27	Phosphorylation	VTLISDDSDGEPTPK EEEEECCCCCCCCCC	53.13	19429919
32	Phosphorylation	DDSDGEPTPKRNVNH CCCCCCCCCCCCCCC	36.82	19429919
60	Phosphorylation	QKHPDEDSNDAPATS CCCCCCCCCCCCCCH	34.26	25749252
862	Phosphorylation	VVKLRDLSPNLSDSS EEEHHHCCCCCCCCC	18.94	22817900
866	Phosphorylation	RDLSPNLSDSSPSSK HHCCCCCCCCCCCCC	41.93	18327897

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of LSDA_DROME !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of LSDA_DROME !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of LSDA_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DECA_DROME	dpp	genetic	21482791
KDM5_DROME	lid	genetic	21205864
SUH_DROME	Su(H)	genetic	21205864
HP1_DROME	Su(var)205	physical	17434130
HDAC1_DROME	Rpd3	physical	17434130
SUV39_DROME	Su(var)3-9	physical	17434130

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-24; SER-27 AND SER-866,AND MASS SPECTROMETRY.
PubMed: 18327897