UniProt ID | JHD1_DROME | |
---|---|---|
UniProt AC | Q9VHH9 | |
Protein Name | JmjC domain-containing histone demethylation protein 1 | |
Gene Name | Kdm2 | |
Organism | Drosophila melanogaster (Fruit fly). | |
Sequence Length | 1345 | |
Subcellular Localization | Nucleus. | |
Protein Description | Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code.. | |
Protein Sequence | MSTAVETGSSPAKSNSNNSSSGGNNNNGNGNLSPNAKGVQRRQLRERKQRKLYLEEWSLGDEDGEGTRGFSVAEKLESSKFAQAGMVREMRGCDLTVAFLQQHGFNIPLLFRDKAGLGLRMPDPQEFTVNDVRLCVGSRRLLDVMDVNTQKNLQMTMKEWQQYYDSPQKDRLLNVISLEFSHTRLDRFVQSPEIVRQIDWVDVVWPKQLKDAQREGTNLLGGMMYPKVQKYCLMSVKNCYTDFHIDFGGTSVWYHILRGSKVFWLIPPTDRNLQLYEKWVLSGKQADIFFGDTVEKCARVYLTAGNTFFIPTGWIHAVYTPTQSLVFGGNFLHSFGIVKQLKTASVEDSTKVPQKFRYPFFTEMLWYVLARYVHTLLGHSHLEGEASLSEDEMAARPHTHLTHHELFGLKEIVMYLYDLPPQKKNVPSLVLDPVALIKDVRSLVERHCKDQQDLAITGVSVLKSPPGSQPPFLLYDRTRVKQEIKQEIARKNAEVIREQQQLEAGRAREAESDTSQSTGVGSVIGMGAGVEYSNGVMKKEQLENGSGVTVGGHGSQPEATFALPTDTLKYRPPKKMHLATALVAAAASSSSGGGGPVAGVGGSAVVGSSHSPTGGGVGPVTGAGGAISVIATSSSYIEGGQVGGILNMDNCHSPEGGGAKLSPNLTGTGQPRRRRTRCKNCAACQRSDCGTCPFCMDMVKFGGPGRAKQTCMMRQCLSPMLPVTAQCVYCHLDGWRQTPVSPQTKQLASADGPSALMECSVCYEIAHPDCALSQLDGTEDAADAKGIVNEDLPNSWECPSCCRSGKNYDYKPRHFRARQKSSEVRRVSVSHGQGGAEGHADGNTLLPPPVGQYNDFVFTSESEMESGTVSGHMTHWKHGMKRHHQLEVKTERNNSCDTPSPGISPNAIGGDSKVGKRRKSDDGTSVSSSMHESNDAPCGSSAEGAGGAGNANVSTNQWSGSGGGGGSRKKNSIRSQLAQQMLNSSTRVLKKPQYVVRPASGTGSSSSSGNGGSASATNGISNGSNQSGANSCGAGNGERGTNNGGLSGSNGLGNQHYSSSQNLALDPTVLKIIFRYLPQDTLVTCCSVCKVWSNAAVDPDLWKKMNCSEHKMSASLLTAIVRRQPEHLILDWTQIAKRQLAWLVARLPALKNLSLQNCPIQAVLALHTCLCPPLQTLDLSFVRGLNDAAIRDILSPPKDSRPGLSDSKTRLRDLKVMKLAGTDISDVAVRYITQSLPYLRHLDLSSCQRITDAGVAQIGTSTTATARLTELNLSACRLVSENALEHLAKCEGLIWLDLRHVPQVSTQSVIRFASNSKHDLCVRDIKLVERRRRNSTTANRSWHHD | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
10 | Phosphorylation | TAVETGSSPAKSNSN CCCCCCCCCCCCCCC | 30.16 | 19429919 | |
33 | Phosphorylation | NNGNGNLSPNAKGVQ CCCCCCCCCCHHHHH | 21.80 | 29892262 | |
53 | Phosphorylation | ERKQRKLYLEEWSLG HHHHHHHHHEECCCC | 18.33 | 22817900 | |
58 | Phosphorylation | KLYLEEWSLGDEDGE HHHHEECCCCCCCCC | 26.25 | 18327897 | |
78 | Phosphorylation | SVAEKLESSKFAQAG CHHHHHHCCHHHHHC | 49.63 | 22817900 | |
79 | Phosphorylation | VAEKLESSKFAQAGM HHHHHHCCHHHHHCC | 23.55 | 22817900 | |
662 | Phosphorylation | EGGGAKLSPNLTGTG CCCCCCCCCCCCCCC | 15.84 | 29892262 |
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 JHD1_DROME !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of JHD1_DROME !! |
* 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 JHD1_DROME !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
MOX12_DROME | olf413 | physical | 14605208 | |
KDM5_DROME | lid | genetic | 21124823 | |
PSC_DROME | Psc | physical | 18923078 | |
PSC_DROME | Psc | physical | 25415640 | |
RING1_DROME | Sce | physical | 18923078 | |
RING1_DROME | Sce | physical | 25415640 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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 TYR-53; SER-58 AND SER-79,AND MASS SPECTROMETRY. |