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Protein Page:
LSD1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
LSD1 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. Component of a RCOR/GFI/KDM1A/HDAC complex. Interacts directly with GFI1 and GFI1B. 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. Ubiquitously expressed. Belongs to the flavin monoamine oxidase family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Transcription factor; Demethylase; EC 1.-.-.-; Oxidoreductase
Cellular Component: nucleoplasm; transcription factor complex; nuclear chromatin; nucleolus; nucleus
Molecular Function: FAD binding; p53 binding; oxidoreductase activity; transcription factor binding; histone demethylase activity (H3-K9 specific); histone demethylase activity (H3-K4 specific); protein binding; MRF binding; enzyme binding; histone demethylase activity; ligand-dependent nuclear receptor transcription coactivator activity; androgen receptor binding; chromatin binding; transcription factor activity; demethylase activity
Biological Process: negative regulation of histone H3-K9 methylation; transcription, DNA-dependent; granulocyte differentiation; in utero embryonic development; positive regulation of erythrocyte differentiation; negative regulation of transcription factor activity; muscle cell development; negative regulation of histone H3-K4 methylation; negative regulation of transcription from RNA polymerase II promoter; negative regulation of DNA binding; protein amino acid demethylation; regulation of transcription from RNA polymerase II promoter; cell proliferation; negative regulation of DNA damage response, signal transduction by p53 class mediator; histone H3-K9 demethylation; pituitary gland development; positive regulation of hormone biosynthetic process; positive regulation of transcription from RNA polymerase II promoter; positive regulation of megakaryocyte differentiation; positive regulation of transcription factor activity; negative regulation of protein binding; blood coagulation; negative regulation of transcription, DNA-dependent
Reference #:  O60341 (UniProtKB)
Alt. Names/Synonyms: amine oxidase (flavin containing) domain 2; AOF2; BHC110; BRAF35-HDAC complex protein BHC110; FAD-binding protein BRAF35-HDAC complex, 110 kDa subunit; Flavin-containing amine oxidase domain-containing protein 2; KDM1; KDM1A; KIAA0601; LSD1; lysine (K)-specific demethylase 1; lysine (K)-specific demethylase 1A; lysine-specific histone demethylase 1; Lysine-specific histone demethylase 1A
Gene Symbols: KDM1A
Molecular weight: 92,903 Da
Basal Isoelectric point: 6.11  Predict pI for various phosphorylation states
CST Pathways:  Histone Methylation
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

LSD1

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 3 T59-p PGAVGERtPRKKEPP
0 3 T104-p METGIAEtPEGRRTs
1 10 S111-p tPEGRRTsRRKRAKV
0 7 S126-p EYREMDEsLANLsED
0 285 S131-p DEsLANLsEDEyysE
0 48 Y135-p ANLsEDEyysEEERN
0 40 Y136-p NLsEDEyysEEERNA
0 293 S137-p LsEDEyysEEERNAK
0 22 S166-p PPEEENEsEPEEPsG
0 3 S172-p EsEPEEPsGVEGAAF
0 1 S299-p AAARQLQsFGMDVtL
0 1 T305-p QsFGMDVtLLEARDR
0 1 K322-ub GRVATFRkGNYVADL
0 1 T335-p DLGAMVVtGLGGNPM
0 1 S346-p GNPMAVVskQVNMEL
0 1 K347-ub NPMAVVskQVNMELA
0 1 K355-ub QVNMELAkIKQKCPL
0 10 Y363-p IKQKCPLyEANGQAV
0 1 K374-ub GQAVPKEkDEMVEQE
0 1 K424-ub QLQEKHVkDEQIEHW
0 1 K432-ac DEQIEHWkkIVkTQE
0 1 K432-ub DEQIEHWkkIVkTQE
0 1 K433-ac EQIEHWkkIVkTQEE
0 1 K436-ac EHWkkIVkTQEELkE
0 1 K442-ub VkTQEELkELLNkMV
0 1 K447-ub ELkELLNkMVNLKEK
0 1 K481-ub ITAEFLVkSKHRDLT
0 1 K503-ub ELAETQGkLEEKLQE
0 1 T588-p GLDIKLNtAVRQVRY
0 6 S611-p AVNTRSTsQTFIYKC
0 1 K647-ub VPPLPEWkTSAVQRM
0 1 K744-ub SSAVPQPkETVVSRW
0 1 Y807 GEHTIRNYPATVHGA
0 1 T810 TIRNYPATVHGALLS
0 12 T841-p YTLPRQAtPGVPAQQ
0 15 S849-p PGVPAQQsPsM____
0 4 S851-p VPAQQsPsM______
  LSD1 iso2  
T59 PGAVGERTPRKKEPP
T104 METGIAETPEGRRTS
S111 TPEGRRTSRRKRAKV
S126 EYREMDESLANLSED
S131 DESLANLSEDEYYSE
Y135 ANLSEDEYYSEEERN
Y136 NLSEDEYYSEEERNA
S137 LSEDEYYSEEERNAK
S166-p PPEEENEsEPEEPsG
S172-p EsEPEEPsGQAGGLQ
S319 AAARQLQSFGMDVTL
T325 QSFGMDVTLLEARDR
K342 GRVATFRKGNYVADL
T355 DLGAMVVTGLGGNPM
S366 GNPMAVVSKQVNMEL
K367 NPMAVVSKQVNMELA
K375 QVNMELAKIKQKCPL
Y383 IKQKCPLYEANGQAD
K398 TVKVPKEKDEMVEQE
K448 QLQEKHVKDEQIEHW
K456 DEQIEHWKKIVKTQE
K456 DEQIEHWKKIVKTQE
K457 EQIEHWKKIVKTQEE
K460 EHWKKIVKTQEELKE
K466 VKTQEELKELLNKMV
K471 ELKELLNKMVNLKEK
K505 ITAEFLVKSKHRDLT
K527 ELAETQGKLEEKLQE
T612 GLDIKLNTAVRQVRY
S635 AVNTRSTSQTFIYKC
K671 VPPLPEWKTSAVQRM
K768 SSAVPQPKETVVSRW
Y831 GEHTIRNYPATVHGA
T834 TIRNYPATVHGALLS
T865 YTLPRQATPGVPAQQ
S873 PGVPAQQSPSM____
S875 VPAQQSPSM______
  mouse

► Hide Isoforms
 
T60 TGAAGERTPRKKEPP
T105 METGIAETPEGRRTs
S112-p TPEGRRTsRRKRAKV
S127-p EYREMDEsLANLsED
S132-p DEsLANLsEDEyysE
Y136-p ANLsEDEyysEEERN
Y137-p NLsEDEyysEEERNA
S138-p LsEDEyysEEERNAK
S167-p PPEEENEsEPEEPsG
S173-p EsEPEEPsGVEGAAF
S300 AAARQLQSFGMDVTL
T306 QSFGMDVTLLEARDR
K323 GRVATFRKGNYVADL
T336 DLGAMVVTGLGGNPM
S347 GNPMAVVSKQVNMEL
K348 NPMAVVSKQVNMELA
K356 QVNMELAKIKQKCPL
Y364 IKQKCPLYEANGQAV
K375 GQAVPKEKDEMVEQE
K425 QLQEKHVKDEQIEHW
K433 DEQIEHWKKIVKTQE
K433 DEQIEHWKKIVKTQE
K434 EQIEHWKKIVKTQEE
K437 EHWKKIVKTQEELKE
K443 VKTQEELKELLNKMV
K448 ELKELLNKMVNLKEK
K482 ITAEFLVKSKHRDLT
K504 ELAETQGKLEEKLQE
T589 GLDIKLNTAVRQVRY
S612 AVNTRSTSQTFIYKC
K648 VPPLPEWKTSAVQRM
K745 SSAVPQPKETVVSRW
Y808-p GEHTIRNyPAtVHGA
T811-p TIRNyPAtVHGALLS
T842-p YTLPRQAtPGVPAQQ
S850-p PGVPAQQsPsM____
S852-p VPAQQsPsM______
  LSD1 iso2  
T60 TGAAGERTPRKKEPP
T105 METGIAETPEGRRTS
S112 TPEGRRTSRRKRAKV
S127 EYREMDESLANLSED
S132 DESLANLSEDEYYSE
Y136 ANLSEDEYYSEEERN
Y137 NLSEDEYYSEEERNA
S138 LSEDEYYSEEERNAK
S167-p PPEEENEsEPEEPSG
S173 EsEPEEPSGQAGGLQ
S320 AAARQLQSFGMDVTL
T326 QSFGMDVTLLEARDR
K343 GRVATFRKGNYVADL
T356 DLGAMVVTGLGGNPM
S367 GNPMAVVSKQVNMEL
K368 NPMAVVSKQVNMELA
K376 QVNMELAKIKQKCPL
Y384 IKQKCPLYEANGQAV
K395 GQAVPKEKDEMVEQE
K445 QLQEKHVKDEQIEHW
K453 DEQIEHWKKIVKTQE
K453 DEQIEHWKKIVKTQE
K454 EQIEHWKKIVKTQEE
K457 EHWKKIVKTQEELKE
K463 VKTQEELKELLNKMV
K468 ELKELLNKMVNLKEK
K502 ITAEFLVKSKHRDLT
K524 ELAETQGKLEEKLQE
T609 GLDIKLNTAVRQVRY
S632 AVNTRSTSQTFIYKC
K668 VPPLPEWKTSAVQRM
K765 SSAVPQPKETVVSRW
Y828 GEHTIRNYPATVHGA
T831 TIRNYPATVHGALLS
T862 YTLPRQATPGVPAQQ
S870 PGVPAQQSPSM____
S872 VPAQQSPSM______
  rat

 
T59 TGAAGERTPRKKEPP
T104 METGIAETPEGRRTS
S111 TPEGRRTSRRKRAKV
S126-p EYREMDEsLANLsED
S131-p DEsLANLsEDEYYsE
Y135 ANLsEDEYYsEEERN
Y136 NLsEDEYYsEEERNA
S137-p LsEDEYYsEEERNAK
S166 PPEEENESEPEEPSG
S172 ESEPEEPSGQAGGLQ
S319 AAARQLQSFGMDVTL
T325 QSFGMDVTLLEARDR
K342 GRVATFRKGNYVADL
T355 DLGAMVVTGLGGNPM
S366 GNPMAVVSKQVNMEL
K367 NPMAVVSKQVNMELA
K375 QVNMELAKIKQKCPL
Y383 IKQKCPLYEANGQAV
K394 GQAVPKEKDEMVEQE
K444 QLQEKHVKDEQIEHW
K452 DEQIEHWKKIVKTQE
K452 DEQIEHWKKIVKTQE
K453 EQIEHWKKIVKTQEE
K456 EHWKKIVKTQEELKE
K462 VKTQEELKELLNKMV
K467 ELKELLNKMVNLKEK
K501 ITAEFLVKSKHRDLT
K523 ELAETQGKLEEKLQE
T608 GLDIKLNTAVRQVRY
S631 AVNTRSTSQTFIYKC
K667 VPPLPEWKTSAVQRM
K764 SSAVPQPKETVVSRW
Y827 GEHTIRNYPATVHGA
T830 TIRNYPATVHGALLS
T861 YTLPRQATPGVPAQQ
S869 PGVPAQQSPSM____
S871 VPAQQSPSM______
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