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O60341 (KDM1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysine-specific histone demethylase 1A

EC=1.-.-.-
Alternative name(s):
BRAF35-HDAC complex protein BHC110
Flavin-containing amine oxidase domain-containing protein 2
Gene names
Name:KDM1A
Synonyms:AOF2, KDM1, KIAA0601, LSD1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length852 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Histone demethylase that demethylates both 'Lys-4' (H3K4me) and 'Lys-9' (H3K9me) of histone H3, thereby acting as a coactivator or a corepressor, depending on the context. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. 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. 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. Also acts as a coactivator of androgen receptor (ANDR)-dependent transcription, by being recruited to ANDR target genes and mediating demethylation of H3K9me, a specific tag for epigenetic transcriptional repression. The presence of PRKCB in ANDR-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. 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. 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. Effector of SNAI1-mediated transcription repression of E-cadherin/CDH1, CDN7 and KRT8. Required for the maintenance of the silenced state of the SNAI1 target genes E-cadherin/CDH1 and CDN7. Ref.5 Ref.8 Ref.12 Ref.15 Ref.23 Ref.24

Cofactor

FAD. Ref.8 Ref.9

Subunit structure

Component of a RCOR/GFI/KDM1A/HDAC complex. Interacts directly with GFI1 and GFI1B. Interacts with INSM1 By similarity. Component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B, KDM1A, RCOR1 and PHF21A. The BHC complex may also contain ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. In the complex, RCOR1/CoREST strongly enhances the demethylase activity and protects it from the proteasome while PHF21A/BHC80 inhibits the demethylase activity. Interacts with the androgen receptor (AR). Interacts with ASXL1. Interacts with SNAI1 (via SNAG domain). Ref.5 Ref.6 Ref.7 Ref.10 Ref.11 Ref.12 Ref.22 Ref.24

Subcellular location

Nucleus Ref.6 Ref.12.

Tissue specificity

Ubiquitously expressed. Ref.12

Domain

The SWIRM domain may act as an anchor site for a histone tail. Ref.31

Sequence similarities

Belongs to the flavin monoamine oxidase family.

Contains 1 SWIRM domain.

Biophysicochemical properties

Kinetic parameters:

KM=3.0 µM for H3 monomethyl-K4 Ref.13

KM=4.2 µM for H3 dimethyl-K4

KM=3.9 µM for H3 monomethyl-K4-monomethyl-K9

KM=17.5 µM for monomethyl-K4-acetyl-K9

Sequence caution

The sequence BAA25527.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
   LigandFAD
Flavoprotein
   Molecular functionChromatin regulator
Developmental protein
Oxidoreductase
Repressor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement. Source: Reactome

cell proliferation

Inferred from electronic annotation. Source: Ensembl

granulocyte differentiation

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

muscle cell development

Inferred from sequence or structural similarity PubMed 20833138. Source: BHF-UCL

negative regulation of DNA binding

Inferred by curator Ref.15. Source: BHF-UCL

negative regulation of DNA damage response, signal transduction by p53 class mediator

Inferred from mutant phenotype Ref.15. Source: BHF-UCL

negative regulation of histone H3-K4 methylation

Inferred from electronic annotation. Source: Ensembl

negative regulation of histone H3-K9 methylation

Inferred from electronic annotation. Source: Ensembl

negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator

Inferred from mutant phenotype Ref.15. Source: BHF-UCL

negative regulation of protein binding

Inferred from mutant phenotype Ref.15. Source: BHF-UCL

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 19497860. Source: BHF-UCL

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.15. Source: BHF-UCL

pituitary gland development

Inferred from electronic annotation. Source: Ensembl

positive regulation of erythrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of hormone biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of megakaryocyte differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of neural precursor cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 20833138. Source: BHF-UCL

positive regulation of stem cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 20833138. Source: BHF-UCL

regulation of primitive erythrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentnuclear chromatin

Inferred from direct assay PubMed 17277772. Source: BHF-UCL

nucleoplasm

Traceable author statement. Source: Reactome

transcription factor complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionMRF binding

Inferred from direct assay PubMed 20833138. Source: BHF-UCL

androgen receptor binding

Inferred from direct assay Ref.12. Source: UniProtKB

chromatin binding

Inferred from direct assay Ref.12Ref.23. Source: UniProtKB

flavin adenine dinucleotide binding

Inferred from direct assay Ref.8. Source: UniProtKB

histone demethylase activity (H3-K9 specific)

Inferred from direct assay Ref.12Ref.23. Source: UniProtKB

histone demethylase activity (H3-dimethyl-K4 specific)

Inferred from direct assay Ref.23. Source: UniProtKB

ligand-dependent nuclear receptor transcription coactivator activity

Inferred from mutant phenotype Ref.12. Source: UniProtKB

oxidoreductase activity

Inferred from direct assay Ref.8. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

transcription regulatory region DNA binding

Inferred from sequence or structural similarity. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O60341-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O60341-2)

The sequence of this isoform differs from the canonical sequence as follows:
     173-173: G → GQAGGLQDDSSGGYGDGQASG
     369-369: A → ADTVK
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 852852Lysine-specific histone demethylase 1A
PRO_0000099881

Regions

Domain174 – 273100SWIRM
Nucleotide binding281 – 30929FAD Potential
Nucleotide binding332 – 3332FAD
Nucleotide binding810 – 8112FAD
Region300 – 852553Demethylase activity
Coiled coil110 – 15142 Potential
Coiled coil428 – 51487 Potential
Compositional bias7 – 4236Ala-rich
Compositional bias152 – 1565Poly-Pro

Sites

Binding site2891FAD
Binding site3081FAD
Binding site3101FAD
Binding site3161FAD
Binding site8011FAD

Amino acid modifications

Modified residue1041Phosphothreonine Ref.18 Ref.21
Modified residue1261Phosphoserine Ref.18
Modified residue1311Phosphoserine Ref.14 Ref.17 Ref.18 Ref.20 Ref.21 Ref.25 Ref.27
Modified residue1371Phosphoserine Ref.21 Ref.25 Ref.27
Modified residue1661Phosphoserine Ref.16 Ref.18 Ref.25 Ref.27
Modified residue8491Phosphoserine Ref.18 Ref.25

Natural variations

Alternative sequence1731G → GQAGGLQDDSSGGYGDGQAS G in isoform 2.
VSP_011198
Alternative sequence3691A → ADTVK in isoform 2.
VSP_011199

Experimental info

Mutagenesis5351N → A: Strongly reduces demethylase activity. Ref.30
Mutagenesis5641H → A: Strongly reduces demethylase activity. Ref.30
Mutagenesis6611K → A: Abolishes histone demethylase activity. Ref.11
Mutagenesis7611Y → A: Strongly reduces demethylase activity. Ref.30
Sequence conflict781P → Q in AAH40194. Ref.3
Sequence conflict4051P → H in AAH48134. Ref.3
Sequence conflict6691V → A in CAD38675. Ref.4
Sequence conflict8141A → V in AAH16639. Ref.3

Secondary structure

......................................................................................................................... 852
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 16, 2004. Version 2.
Checksum: A61CEDE51E4E0C1D

FASTA85292,903
        10         20         30         40         50         60 
MLSGKKAAAA AAAAAAAATG TEAGPGTAGG SENGSEVAAQ PAGLSGPAEV GPGAVGERTP 

        70         80         90        100        110        120 
RKKEPPRASP PGGLAEPPGS AGPQAGPTVV PGSATPMETG IAETPEGRRT SRRKRAKVEY 

       130        140        150        160        170        180 
REMDESLANL SEDEYYSEEE RNAKAEKEKK LPPPPPQAPP EEENESEPEE PSGVEGAAFQ 

       190        200        210        220        230        240 
SRLPHDRMTS QEAACFPDII SGPQQTQKVF LFIRNRTLQL WLDNPKIQLT FEATLQQLEA 

       250        260        270        280        290        300 
PYNSDTVLVH RVHSYLERHG LINFGIYKRI KPLPTKKTGK VIIIGSGVSG LAAARQLQSF 

       310        320        330        340        350        360 
GMDVTLLEAR DRVGGRVATF RKGNYVADLG AMVVTGLGGN PMAVVSKQVN MELAKIKQKC 

       370        380        390        400        410        420 
PLYEANGQAV PKEKDEMVEQ EFNRLLEATS YLSHQLDFNV LNNKPVSLGQ ALEVVIQLQE 

       430        440        450        460        470        480 
KHVKDEQIEH WKKIVKTQEE LKELLNKMVN LKEKIKELHQ QYKEASEVKP PRDITAEFLV 

       490        500        510        520        530        540 
KSKHRDLTAL CKEYDELAET QGKLEEKLQE LEANPPSDVY LSSRDRQILD WHFANLEFAN 

       550        560        570        580        590        600 
ATPLSTLSLK HWDQDDDFEF TGSHLTVRNG YSCVPVALAE GLDIKLNTAV RQVRYTASGC 

       610        620        630        640        650        660 
EVIAVNTRST SQTFIYKCDA VLCTLPLGVL KQQPPAVQFV PPLPEWKTSA VQRMGFGNLN 

       670        680        690        700        710        720 
KVVLCFDRVF WDPSVNLFGH VGSTTASRGE LFLFWNLYKA PILLALVAGE AAGIMENISD 

       730        740        750        760        770        780 
DVIVGRCLAI LKGIFGSSAV PQPKETVVSR WRADPWARGS YSYVAAGSSG NDYDLMAQPI 

       790        800        810        820        830        840 
TPGPSIPGAP QPIPRLFFAG EHTIRNYPAT VHGALLSGLR EAGRIADQFL GAMYTLPRQA 

       850 
TPGVPAQQSP SM 

« Hide

Isoform 2 [UniParc].

Checksum: 966CA72A70F68111
Show »

FASTA87695,155

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain, Skin and Testis.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 245-852 (ISOFORM 1).
Tissue: Brain.
[5]"A core-BRAF35 complex containing histone deacetylase mediates repression of neuronal-specific genes."
Hakimi M.-A., Bochar D.A., Chenoweth J., Lane W.S., Mandel G., Shiekhattar R.
Proc. Natl. Acad. Sci. U.S.A. 99:7420-7425(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE, INTERACTION WITH A HISTONE DEACETYLASE-CONTAINING COMPLEX, FUNCTION.
[6]"Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1."
Humphrey G.W., Wang Y., Russanova V.R., Hirai T., Qin J., Nakatani Y., Howard B.H.
J. Biol. Chem. 276:6817-6824(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH THE HDAC1 COMPLEX, MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[7]"A candidate X-linked mental retardation gene is a component of a new family of histone deacetylase-containing complexes."
Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R.
J. Biol. Chem. 278:7234-7239(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH A HISTONE DEACETYLASE-CONTAINING COMPLEX, MASS SPECTROMETRY.
[8]"Histone demethylation mediated by the nuclear amine oxidase homolog LSD1."
Shi Y.-J., Lan F., Matson C., Mulligan P., Whetstine J.R., Cole P.A., Casero R.A., Shi Y.
Cell 119:941-953(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME ACTIVITY, FUNCTION, COFACTOR.
[9]"Histone demethylation catalysed by LSD1 is a flavin-dependent oxidative process."
Forneris F., Binda C., Vanoni M.A., Mattevi A., Battaglioli E.
FEBS Lett. 579:2203-2207(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME ACTIVITY, COFACTOR.
[10]"Regulation of LSD1 histone demethylase activity by its associated factors."
Shi Y.-J., Matson C., Lan F., Iwase S., Baba T., Shi Y.
Mol. Cell 19:857-864(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RCOR1 AND PHF21A.
[11]"An essential role for CoREST in nucleosomal histone 3 lysine 4 demethylation."
Lee M.G., Wynder C., Cooch N., Shiekhattar R.
Nature 437:432-435(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RCOR1, MUTAGENESIS OF LYS-661.
[12]"LSD1 demethylates repressive histone marks to promote androgen-receptor-dependent transcription."
Metzger E., Wissmann M., Yin N., Mueller J.M., Schneider R., Peters A.H.F.M., Guenther T., Buettner R., Schuele R.
Nature 437:436-439(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH ANDR.
[13]"Human histone demethylase LSD1 reads the histone code."
Forneris F., Binda C., Vanoni M.A., Battaglioli E., Mattevi A.
J. Biol. Chem. 280:41360-41365(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[14]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"p53 is regulated by the lysine demethylase LSD1."
Huang J., Sengupta R., Espejo A.B., Lee M.G., Dorsey J.A., Richter M., Opravil S., Shiekhattar R., Bedford M.T., Jenuwein T., Berger S.L.
Nature 449:105-108(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-104; SER-126; SER-131; SER-166 AND SER-849, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-104; SER-131 AND SER-137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[22]"ASXL1 represses retinoic acid receptor-mediated transcription through associating with HP1 and LSD1."
Lee S.W., Cho Y.S., Na J.M., Park U.H., Kang M., Kim E.J., Um S.J.
J. Biol. Chem. 285:18-29(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ASXL1.
[23]"Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at histone H3K4."
Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N., Muller J.M., Greschik H., Kirfel J., Ji S., Kunowska N., Beisenherz-Huss C., Gunther T., Buettner R., Schule R.
Nature 464:792-796(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[24]"Requirement of the histone demethylase LSD1 in Snai1-mediated transcriptional repression during epithelial-mesenchymal transition."
Lin T., Ponn A., Hu X., Law B.K., Lu J.
Oncogene 29:4896-4904(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SNAI.
[25]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131; SER-137; SER-166 AND SER-849, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[26]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131; SER-137 AND SER-166, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"Structural basis for CoREST-dependent demethylation of nucleosomes by the human LSD1 histone demethylase."
Yang M., Gocke C.B., Luo X., Borek D., Tomchick D.R., Machius M., Otwinowski Z., Yu H.
Mol. Cell 23:377-387(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 171-836 IN COMPLEX WITH FAD AND RCOR1.
[30]"Crystal structure of human histone lysine-specific demethylase 1 (LSD1)."
Chen Y., Yang Y., Wang F., Wan K., Yamane K., Zhang Y., Lei M.
Proc. Natl. Acad. Sci. U.S.A. 103:13956-13961(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 172-835 IN COMPLEX WITH FAD, MUTAGENESIS OF ASN-535; HIS-564 AND TYR-761.
[31]"Solution structure of the SWIRM domain of human histone demethylase LSD1."
Tochio N., Umehara T., Koshiba S., Inoue M., Yabuki T., Aoki M., Seki E., Watanabe S., Tomo Y., Hanada M., Ikari M., Sato M., Terada T., Nagase T., Ohara O., Shirouzu M., Tanaka A., Kigawa T., Yokoyama S.
Structure 14:457-468(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 166-285, DOMAIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB011173 mRNA. Translation: BAA25527.1. Different initiation.
AL031428 Genomic DNA. Translation: CAI19707.2.
AL031428 Genomic DNA. Translation: CAI19708.2.
BC016639 mRNA. Translation: AAH16639.1.
BC025362 mRNA. Translation: AAH25362.1.
BC040194 mRNA. Translation: AAH40194.3.
BC048134 mRNA. Translation: AAH48134.2.
AL833812 mRNA. Translation: CAD38675.2.
RefSeqNP_001009999.1. NM_001009999.2.
NP_055828.2. NM_015013.3.
UniGeneHs.591518.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2COMNMR-A169-279[»]
2DW4X-ray2.30A172-831[»]
2EJRX-ray2.70A172-833[»]
2H94X-ray2.90A172-835[»]
2HKOX-ray2.80A172-835[»]
2IW5X-ray2.57A171-836[»]
2L3DNMR-A174-273[»]
2UXNX-ray2.72A171-836[»]
2UXXX-ray2.74A171-836[»]
2V1DX-ray3.10A123-852[»]
2X0LX-ray3.00A123-852[»]
2XAFX-ray3.25A1-852[»]
2XAGX-ray3.10A1-852[»]
2XAHX-ray3.10A1-852[»]
2XAJX-ray3.30A1-852[»]
2XAQX-ray3.20A1-852[»]
2XASX-ray3.20A1-852[»]
2Y48X-ray3.00A123-852[»]
2Z3YX-ray2.25A172-833[»]
2Z5UX-ray2.25A172-833[»]
3ABTX-ray3.20A172-833[»]
3ABUX-ray3.10A172-833[»]
3ZMSX-ray2.96A1-852[»]
3ZMTX-ray3.10A1-852[»]
3ZMUX-ray3.20A1-852[»]
3ZMVX-ray3.00A1-852[»]
3ZMZX-ray3.00A1-852[»]
3ZN0X-ray2.80A1-852[»]
3ZN1X-ray3.10A1-852[»]
4BAYX-ray3.10A172-852[»]
ProteinModelPortalO60341.
SMRO60341. Positions 171-836.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116667. 276 interactions.
DIPDIP-34641N.
IntActO60341. 216 interactions.
MINTMINT-1372817.

Chemistry

BindingDBO60341.
ChEMBLCHEMBL6136.

PTM databases

PhosphoSiteO60341.

Proteomic databases

PaxDbO60341.
PRIDEO60341.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356634; ENSP00000349049; ENSG00000004487. [O60341-1]
ENST00000400181; ENSP00000383042; ENSG00000004487. [O60341-2]
GeneID23028.
KEGGhsa:23028.
UCSCuc001bgi.2. human. [O60341-1]
uc001bgj.2. human. [O60341-2]

Organism-specific databases

CTD23028.
GeneCardsGC01P023347.
HGNCHGNC:29079. KDM1A.
HPACAB005884.
HPA053660.
MIM609132. gene.
neXtProtNX_O60341.
PharmGKBPA165751392.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1231.
KOK11450.
OMAHRIHSYL.
OrthoDBEOG7X9G66.
TreeFamTF312972.

Enzyme and pathway databases

ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressO60341.
BgeeO60341.
CleanExHS_AOF2.
GenevestigatorO60341.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR002937. Amino_oxidase.
IPR017366. Hist_Lys-spec_deMease.
IPR009057. Homeodomain-like.
IPR007526. SWIRM.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF01593. Amino_oxidase. 1 hit.
PF04433. SWIRM. 1 hit.
[Graphical view]
PIRSFPIRSF038051. Histone_Lys-demethylase. 1 hit.
SUPFAMSSF46689. SSF46689. 1 hit.
PROSITEPS50934. SWIRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKDM1A. human.
EvolutionaryTraceO60341.
GenomeRNAi23028.
NextBio43998.
PROO60341.
SOURCESearch...

Entry information

Entry nameKDM1A_HUMAN
AccessionPrimary (citable) accession number: O60341
Secondary accession number(s): A8MWP9 expand/collapse secondary AC list , Q5TH94, Q5TH95, Q86VT7, Q8IXK4, Q8NDP6, Q8TAZ3, Q96AW4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: March 19, 2014
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM