Q75AL5 (JHD1_ASHGO) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 61.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: JmjC domain-containing histone demethylation protein 1 EC=1.14.11.27 Alternative name(s): [Histone-H3]-lysine-36 demethylase 1 | ||||
| Gene names |
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| Organism | Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) (Yeast) (Eremothecium gossypii) [Complete proteome] | ||||
| Taxonomic identifier | 284811 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Eremothecium |
Protein attributes
| Sequence length | 486 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code By similarity. |
| Catalytic activity | Protein N6,N(6)-dimethyl-L-lysine + 2-oxoglutarate + O2 = protein N(6)-methyl-L-lysine + succinate + formaldehyde + CO2. Protein N(6)-methyl-L-lysine + 2-oxoglutarate + O2 = protein L-lysine + succinate + formaldehyde + CO2. |
| Cofactor | Binds 1 Fe2+ ion per subunit By similarity. |
| Subcellular location | Nucleus By similarity. |
| Domain | The JmjC domain mediates the demethylation activity By similarity. |
| Sequence similarities | Belongs to the JHDM1 histone demethylase family. Contains 1 JmjC domain. Contains 1 PHD-type zinc finger. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transcription Transcription regulation |
| Cellular component | Nucleus |
| Domain | Zinc-finger |
| Ligand | Iron Metal-binding Zinc |
| Molecular function | Chromatin regulator Dioxygenase Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependentInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | histone demethylase activity (H3-K36 specific) Inferred from electronic annotation. Source: EC oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygenInferred from electronic annotation. Source: UniProtKB-KW zinc ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 486 | 486 | JmjC domain-containing histone demethylation protein 1 | PRO_0000226791 | |||||
Regions | |||||||||
| Domain | 245 – 404 | 160 | JmjC | ||||||
| Zinc finger | 28 – 83 | 56 | PHD-type; degenerate | ||||||
Sites | |||||||||
| Metal binding | 300 | 1 | Iron; catalytic By similarity | ||||||
| Metal binding | 302 | 1 | Iron; catalytic By similarity | ||||||
| Metal binding | 372 | 1 | Iron; catalytic By similarity | ||||||
| Binding site | 297 | 1 | Substrate By similarity | ||||||
| Binding site | 317 | 1 | Substrate By similarity | ||||||
Sequences
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References
| [1] | "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces cerevisiae genome." Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S., Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A., Gaffney T.D., Philippsen P. Science 304:304-307(2004) [PubMed: 15001715] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE016817 Genomic DNA. Translation: AAS51832.1. |
| RefSeq | NP_984008.2. NM_209361.2. |
3D structure databases | |
| ProteinModelPortal | Q75AL5. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q75AL5. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 4620150. |
| GenomeReviews | Gene locus ADL088W in contig AE016817_GR. |
| KEGG | ago:AGOS_ADL088W. |
| NMPDR | fig|33169.1.peg.1653. |
Organism-specific databases | |
| AGD | ADL088W. |
Phylogenomic databases | |
| eggNOG | fuNOG04730. |
| HOGENOM | HBG398146. |
| OMA | ISLEVSH. |
| OrthoDB | EOG4SXRNC. |
| PhylomeDB | Q75AL5. |
Family and domain databases | |
| InterPro | IPR003347. TF_JmjC_AAH. IPR011011. Znf_FYVE_PHD. IPR001965. Znf_PHD. IPR013083. Znf_RING/FYVE/PHD. [Graphical view] |
| Gene3D | G3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 1 hit. |
| KO | K10276. |
| SMART | SM00558. JmjC. 1 hit. SM00249. PHD. 1 hit. [Graphical view] |
| SUPFAM | SSF57903. FYVE_PHD_ZnF. 1 hit. |
| PROSITE | PS51184. JMJC. 1 hit. PS01359. ZF_PHD_1. False negative. PS50016. ZF_PHD_2. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | JHD1_ASHGO | ||||||||
| Accession | Primary (citable) accession number: Q75AL5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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