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Lysine-specific histone demethylase 1A (human)

Protein
Encoding Gene
Dates
  • Create:
    2017-04-15
  • Modify:
    2025-01-28
Description
A lysine-specific histone demethylase 1A that is encoded in the genome of human.
Histone demethylase that can demethylate both 'Lys-4' (H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a coactivator or a corepressor, depending on the context (PMID: 15620353, PMID: 15811342, PMID: 16079794, PMID: 16079795, PMID: 16140033, PMID: 16223729, PMID: 27292636). Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed (PMID: 15620353, PMID: 15811342, PMID: 16079794, PMID: 21300290). Acts as a corepressor by mediating demethylation of H3K4me, a specific tag for epigenetic transcriptional activation. Demethylates both mono- (H3K4me1) and di-methylated (H3K4me2) H3K4me (PMID: 15620353, PMID: 20389281, PMID: 21300290, PMID: 23721412). May play a role in the repression of neuronal genes. Alone, it is unable to demethylate H3K4me on nucleosomes and requires the presence of RCOR1/CoREST to achieve such activity (PMID: 16079794, PMID: 16140033, PMID: 16885027, PMID: 21300290, PMID: 23721412). Also acts as a coactivator of androgen receptor (AR)-dependent transcription, by being recruited to AR target genes and mediating demethylation of H3K9me, a specific tag for epigenetic transcriptional repression. The presence of PRKCB in AR-containing complexes, which mediates phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag that prevents demethylation H3K4me, prevents H3K4me demethylase activity of KDM1A (PMID: 16079795). Demethylates di-methylated 'Lys-370' of p53/TP53 which prevents interaction of p53/TP53 with TP53BP1 and represses p53/TP53-mediated transcriptional activation. Demethylates and stabilizes the DNA methylase DNMT1 (PMID: 29691401). Demethylates methylated 'Lys-42' and methylated 'Lys-117' of SOX2 (PMID: 29358331). Required for gastrulation during embryogenesis. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development (PMID: 16079794, PMID: 16140033). Facilitates epithelial-to-mesenchymal transition by acting as an effector of SNAI1-mediated transcription repression of epithelial markers E-cadherin/CDH1, CDN7 and KRT8 (PMID: 20562920, PMID: 27292636). Required for the maintenance of the silenced state of the SNAI1 target genes E-cadherin/CDH1 and CDN7 (PMID: 20389281).

1 Names and Identifiers

1.1 Synonyms

  • Lysine-specific histone demethylase 1A
  • EC 1.14.99.66
  • BRAF35-HDAC complex protein BHC110
  • Flavin-containing amine oxidase domain-containing protein 2
  • [histone H3]-dimethyl-L-lysine(4) FAD-dependent demethylase 1A

1.2 Other Identifiers

1.2.1 RefSeq Accession

1.2.2 UniProt ID

1.2.3 NCI Thesaurus Code

1.2.4 Enzyme Commission (EC) Number

1.2.5 PRO ID

1.2.6 ChEMBL Target ID

1.2.7 DrugBank Target ID

1.2.8 Guide to PHARMACOLOGY Target ID

1.2.9 NCBI Proteins

1.2.10 GlyCosmos Protein

1.2.11 GlyGen Protein

1.2.12 Pharos Target

1.2.13 Open Targets ID

1.2.14 STRING Protein ID

1.2.15 Wikidata

1.2.16 neXtProt Accession

1.2.17 HPA ID

1.2.18 BRENDA EC Number

1.2.19 IntAct Protein

1.2.20 InterPro Protein

3 Chemicals and Bioactivities

3.1 Tested Compounds

4 BioAssays

5 Sequence

>sp|O60341|KDM1A_HUMAN Lysine-specific histone demethylase 1A (Run BLAST)

MLSGKKAAAAAAAAAAAATGTEAGPGTAGGSENGSEVAAQPAGLSGPAEVGPGAVGERTPRKKEPPRASPPGGLAEPPGSAGPQAGPTVVPGSATPMETGIAETPEGRRTSRRKRAKVEYREMDESLANLSEDEYYSEEERNAKAEKEKKLPPPPPQAPPEEENESEPEEPSGVEGAAFQSRLPHDRMTSQEAACFPDIISGPQQTQKVFLFIRNRTLQLWLDNPKIQLTFEATLQQLEAPYNSDTVLVHRVHSYLERHGLINFGIYKRIKPLPTKKTGKVIIIGSGVSGLAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVNMELAKIKQKCPLYEANGQAVPKEKDEMVEQEFNRLLEATSYLSHQLDFNVLNNKPVSLGQALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKPPRDITAEFLVKSKHRDLTALCKEYDELAETQGKLEEKLQELEANPPSDVYLSSRDRQILDWHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAVRQVRYTASGCEVIAVNTRSTSQTFIYKCDAVLCTLPLGVLKQQPPAVQFVPPLPEWKTSAVQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWNLYKAPILLALVAGEAAGIMENISDDVIVGRCLAILKGIFGSSAVPQPKETVVSRWRADPWARGSYSYVAAGSSGNDYDLMAQPITPGPSIPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRIADQFLGAMYTLPRQATPGVPAQQSPSM

6 3D Structures

6.1 PDB Structures

6.2 NCBI Protein Structures

6.3 AlphaFold Structures

Highly accurate protein structure prediction with AlphaFold. Nature. 2021 Aug;596(7873):583-589. DOI:10.1038/s41586-021-03819-2. PMID:34265844; PMCID:PMC8371605

7 Domains

7.1 CDD Domains

7.2 InterPro Domains

8 Diseases and Phenotypes

8.1 Protein-Disease Associations

9 Interactions and Pathways

9.1 Chemical-Protein Interactions

9.2 Interactions

9.3 Pathways

10 Biochemical Reactions

11 Glycobiology

11.1 Glycosylation

2 sites, 1 O-linked glycan (2 sites)

12 Target Development Level

13 Literature

13.1 Consolidated References

14 Patents

15 Classification

15.1 NCI Thesaurus Tree

15.2 IUPHAR / BPS Guide to PHARMACOLOGY Target Classification

15.3 ChEMBL Target Tree

15.4 Enzyme Classification

16 Information Sources

  1. NCBI Protein
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    https://www.ncbi.nlm.nih.gov/home/about/policies/
  2. PubChem
  3. BindingDB
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    https://www.bindingdb.org/rwd/bind/info.jsp
  4. ChEMBL
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    http://www.ebi.ac.uk/Information/termsofuse.html
  5. Chemical Probes Portal
  6. DrugBank
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    Creative Common's Attribution-NonCommercial 4.0 International License (http://creativecommons.org/licenses/by-nc/4.0/legalcode)
    https://www.drugbank.ca/legal/terms_of_use
  7. IUPHAR/BPS Guide to PHARMACOLOGY
    LICENSE
    The Guide to PHARMACOLOGY database is licensed under the Open Data Commons Open Database License (ODbL) https://opendatacommons.org/licenses/odbl/. Its contents are licensed under a Creative Commons Attribution-ShareAlike 4.0 International License (http://creativecommons.org/licenses/by-sa/4.0/)
    https://www.guidetopharmacology.org/about.jsp#license
    Guide to Pharmacology Target Classification
    https://www.guidetopharmacology.org/targets.jsp
  8. Therapeutic Target Database (TTD)
  9. Toxin and Toxin Target Database (T3DB)
    LICENSE
    T3DB is offered to the public as a freely available resource. Use and re-distribution of the data, in whole or in part, for commercial purposes requires explicit permission of the authors and explicit acknowledgment of the source material (T3DB) and the original publication.
    http://www.t3db.ca/downloads
  10. BioGRID
    LICENSE
    The MIT License (MIT); Copyright Mike Tyers Lab
    https://wiki.thebiogrid.org/doku.php/terms_and_conditions
  11. Database of Interacting Proteins (DIP)
    LICENSE
    All DIP database records available under the terms set by the Creative Commons Attribution-NoDerivs License.
    https://dip.doe-mbi.ucla.edu/dip/termsofuse.html
  12. STRING: functional protein association networks
  13. BRENDA: Enzyme Functional Data
    LICENSE
    The usage of the BRENDA data is licensed under Creative Commons Attribution License CC BY 4.0.
    https://www.brenda-enzymes.org/license.php
  14. GlyCosmos Glycoscience Portal
    LICENSE
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    https://glycosmos.org/license
  15. GlyGen
  16. Human Protein Atlas (HPA)
    LICENSE
    The Human Protein Atlas is licensed under the Creative Commons Attribution-ShareAlike 3.0 International License for all copyrightable parts of our database.
    https://www.proteinatlas.org/about/licence
  17. IntAct Molecular Interaction Database
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    https://www.ebi.ac.uk/intact/about#license_privacy
  18. InterPro
    LICENSE
    All of the InterPro, Pfam, PRINTS and SFLD downloadable data provided on the InterPro website is freely available under CC0 1.0 Universal (CC0 1.0) Public Domain Dedication.
    https://www.ebi.ac.uk/interpro/about/license/
  19. NCBI Conserved Domains (CDD)
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    https://www.ncbi.nlm.nih.gov/home/about/policies/
  20. NCBI Structure
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  21. NCI Thesaurus (NCIt)
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    https://www.cancer.gov/policies/copyright-reuse
  22. Open Targets
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    Datasets generated by the Open Targets Platform are freely available for download.
    https://platform-docs.opentargets.org/licence
  23. Pharos
    LICENSE
    Data accessed from Pharos and TCRD is publicly available from the primary sources listed above. Please respect their individual licenses regarding proper use and redistribution.
    https://pharos.nih.gov/about
    Lysine-specific histone demethylase 1A
    https://pharos.nih.gov/targets/O60341
  24. Protein Ontology
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    PRO is distributed under the Creative Commons CC-BY 4.0 license (https://creativecommons.org/licenses/by/4.0/).
  25. UniProt
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    https://www.uniprot.org/help/license
  26. RCSB Protein Data Bank (RCSB PDB)
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    Data files contained in the PDB archive (ftp://ftp.wwpdb.org) are free of all copyright restrictions and made fully and freely available for both non-commercial and commercial use. Users of the data should attribute the original authors of that structural data.
    https://www.rcsb.org/pages/policies
  27. Swiss Institute of Bioinformatics neXtProt
    LICENSE
    Creative Commons Attribution 4.0 International (CC BY 4.0)
    https://www.nextprot.org/help/faq
  28. Wikidata
  29. Swiss Institute of Bioinformatics ENZYME
    LICENSE
    Copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution (CC BY 4.0) License (https://creativecommons.org/licenses/by/4.0/).
    https://enzyme.expasy.org/enzyme.get
    Enzyme Classification
    https://enzyme.expasy.org/
  30. AlphaFold DB
    LICENSE
    All of the data provided is freely available for both academic and commercial use under Creative Commons Attribution 4.0 (CC-BY 4.0) licence terms.
    https://alphafold.ebi.ac.uk/faq
  31. Rhea - annotated reactions database
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    https://www.rhea-db.org/help/license-disclaimer
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