Reviewed, UniProtKB/Swiss-Prot O60341 (KDM1_HUMAN)

Names and origin

Protein names

Recommended name:
    Lysine-specific histone demethylase 1
    EC=1.-.-.-
Alternative name(s):
    Flavin-containing amine oxidase domain-containing protein 2
    BRAF35-HDAC complex protein BHC110

Gene names

Name:	KDM1
Synonyms:	AOF2, KIAA0601, LSD1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	852 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Histone demethylase that demethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Demethylates both mono- and di-methylated 'Lys-4' of histone H3. May play a role in the repression of neuronal genes. Alone, it is unable to demethylate H3 'Lys-4' on nucleosomes and requires the presence of RCOR1/CoREST to achieve such activity. May also demethylate 'Lys-9' of histone H3, a specific tag for epigenetic transcriptional repression, thereby leading to derepression of androgen receptor target genes. 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.
Cofactor	FAD. Ref.8 Ref.9
Subunit structure	Component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1, RCOR1/CoREST and PHF21A/BHC80. 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). Ref.5 Ref.12 Ref.6 Ref.7 Ref.10 Ref.11
Subcellular location	Nucleus. Ref.12 Ref.6
Tissue specificity	Ubiquitously expressed. Ref.12
Domain	The SWIRN domain may act as an anchor site for a histone tail. Ref.22
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 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

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Ligand	FAD
Molecular function	Chromatin regulator Developmental protein Oxidoreductase Repressor
PTM	Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	histone demethylation Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro electron carrier activity Inferred from electronic annotation. Source: InterPro oxidoreductase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HIST3H3	Q16695	1	EBI-710124,EBI-358900
IMMT	Q16891	1	EBI-710124,EBI-473801

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 852

852

Lysine-specific histone demethylase 1

PRO_0000099881

Regions

Domain

174 – 273

100

SWIRM

Nucleotide binding

281 – 309

29

FAD Potential

Nucleotide binding

332 – 333

2

FAD

Nucleotide binding

810 – 811

2

FAD

Region

300 – 852

553

Demethylase activity

Coiled coil

110 – 151

42

Potential

Coiled coil

428 – 514

87

Potential

Compositional bias

7 – 42

36

Ala-rich

Compositional bias

152 – 156

5

Poly-Pro

Sites

Binding site

289

1

FAD

Binding site

308

1

FAD

Binding site

310

1

FAD

Binding site

316

1

FAD

Binding site

801

1

FAD

Amino acid modifications

Modified residue

80

1

Phosphoserine Ref.18

Modified residue

104

1

Phosphothreonine Ref.18

Modified residue

126

1

Phosphoserine Ref.18

Modified residue

131

1

Phosphoserine Ref.18 Ref.17

Modified residue

137

1

Phosphoserine Ref.18 Ref.17

Modified residue

166

1

Phosphoserine Ref.18 Ref.14 Ref.16

Modified residue

849

1

Phosphoserine Ref.18

Natural variations

Alternative sequence

173

1

G → GQAGGLQDDSSGGYGDGQAS G in isoform 2.

VSP_011198

Alternative sequence

369

1

A → ADTVK in isoform 2.

VSP_011199

Experimental info

Mutagenesis

535

1

N → A: Strongly reduces demethylase activity. Ref.21

Mutagenesis

564

1

H → A: Strongly reduces demethylase activity. Ref.21

Mutagenesis

661

1

K → A: Abolishes histone demethylase activity. Ref.11

Mutagenesis

761

1

Y → A: Strongly reduces demethylase activity. Ref.21

Sequence conflict

78

1

P → Q in AAH40194. Ref.3

Sequence conflict

405

1

P → H in AAH48134. Ref.3

Sequence conflict

669

1

V → A in CAD38675. Ref.4

Sequence conflict

814

1

A → V in AAH16639. Ref.3

Secondary structure

1

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852

Helix Strand Turn

Details...

Helix

173 – 180

8

Helix

190 – 195

6

Helix

197 – 200

4

Helix

204 – 223

20

Helix

231 – 237

7

Helix

242 – 244

3

Helix

246 – 258

13

Beta strand

261 – 263

3

Beta strand

280 – 284

5

Helix

288 – 299

12

Beta strand

303 – 307

5

Beta strand

309 – 314

6

Beta strand

319 – 322

4

Beta strand

325 – 330

6

Helix

341 – 349

9

Beta strand

353 – 355

3

Helix

372 – 394

23

Helix

408 – 457

50

Helix

476 – 511

36

Helix

523 – 540

18

Helix

544 – 546

3

Turn

549 – 555

7

Helix

556 – 558

3

Beta strand

565 – 567

3

Helix

573 – 579

7

Beta strand

583 – 585

3

Beta strand

587 – 596

10

Beta strand

599 – 609

11

Beta strand

613 – 623

11

Helix

627 – 631

5

Beta strand

636 – 641

6

Helix

645 – 653

9

Beta strand

654 – 656

3

Beta strand

660 – 665

6

Beta strand

676 – 680

5

Beta strand

683 – 685

3

Turn

686 – 691

6

Beta strand

693 – 695

3

Beta strand

702 – 707

6

Helix

709 – 715

7

Helix

720 – 735

16

Turn

737 – 739

3

Beta strand

744 – 748

5

Turn

751 – 753

3

Turn

755 – 757

3

Beta strand

758 – 760

3

Helix

770 – 777

8

Beta strand

796 – 798

3

Helix

801 – 803

3

Helix

811 – 829

19

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 16, 2004. Version 2. Checksum: A61CEDE51E4E0C1D	FASTA	852	92,903
	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
	Isoform 2. Checksum: 966CA72A70F68111	FASTA	876	95,155
	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 PSGQAGGLQD 190 200 210 220 230 240 DSSGGYGDGQ ASGVEGAAFQ SRLPHDRMTS QEAACFPDII SGPQQTQKVF LFIRNRTLQL 250 260 270 280 290 300 WLDNPKIQLT FEATLQQLEA PYNSDTVLVH RVHSYLERHG LINFGIYKRI KPLPTKKTGK 310 320 330 340 350 360 VIIIGSGVSG LAAARQLQSF GMDVTLLEAR DRVGGRVATF RKGNYVADLG AMVVTGLGGN 370 380 390 400 410 420 PMAVVSKQVN MELAKIKQKC PLYEANGQAD TVKVPKEKDE MVEQEFNRLL EATSYLSHQL 430 440 450 460 470 480 DFNVLNNKPV SLGQALEVVI QLQEKHVKDE QIEHWKKIVK TQEELKELLN KMVNLKEKIK 490 500 510 520 530 540 ELHQQYKEAS EVKPPRDITA EFLVKSKHRD LTALCKEYDE LAETQGKLEE KLQELEANPP 550 560 570 580 590 600 SDVYLSSRDR QILDWHFANL EFANATPLST LSLKHWDQDD DFEFTGSHLT VRNGYSCVPV 610 620 630 640 650 660 ALAEGLDIKL NTAVRQVRYT ASGCEVIAVN TRSTSQTFIY KCDAVLCTLP LGVLKQQPPA 670 680 690 700 710 720 VQFVPPLPEW KTSAVQRMGF GNLNKVVLCF DRVFWDPSVN LFGHVGSTTA SRGELFLFWN 730 740 750 760 770 780 LYKAPILLAL VAGEAAGIME NISDDVIVGR CLAILKGIFG SSAVPQPKET VVSRWRADPW 790 800 810 820 830 840 ARGSYSYVAA GSSGNDYDLM AQPITPGPSI PGAPQPIPRL FFAGEHTIRN YPATVHGALL 850 860 870 SGLREAGRIA DQFLGAMYTL PRQATPGVPA QQSPSM

References

	« Hide 'large scale' referencesShow '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: 9628581] [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. , 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: 16710414] [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: 15489334] [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., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [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: 12032298] [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: 11102443] [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: 12493763] [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: 15620353] [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: 15811342] [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: 16140033] [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: 16079794] [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: 16079795] [Abstract] Cited for: POSSIBLE FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH AR.
[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: 16223729] [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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, MASS SPECTROMETRY. Tissue: Epithelium.
[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: 17805299] [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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166, MASS SPECTROMETRY.
[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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131 AND SER-137, MASS SPECTROMETRY.
[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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; THR-104; SER-126; SER-131; SER-137; SER-166 AND SER-849, MASS SPECTROMETRY.
[19]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[20]	"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: 16885027] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 171-836 IN COMPLEX WITH FAD AND RCOR1.
[21]	"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: 16956976] [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.
[22]	"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: 16531230] [Abstract] Cited for: STRUCTURE BY NMR OF 166-285, DOMAIN.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

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.

IPI

IPI00217540.
IPI00456631.

RefSeq

NP_055828.2.

UniGene

Hs.591518
Hs.656420

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2COM	NMR	-	A	169-279	[»]
2DW4	X-ray	2.30	A	172-831	[»]
2EJR	X-ray	2.70	A	172-833	[»]
2H94	X-ray	2.90	A	172-835	[»]
2HKO	X-ray	2.80	A	172-835	[»]
2IW5	X-ray	2.57	A	171-836	[»]
2UXN	X-ray	2.72	A	171-836	[»]
2UXX	X-ray	2.74	A	171-836	[»]
2V1D	X-ray	3.10	A	123-852	[»]
2Z3Y	X-ray	2.25	A	172-833	[»]
2Z5U	X-ray	2.25	A	172-833	[»]

ModBase

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Protein-protein interaction databases

IntAct

O60341. 10 interactions.

PTM databases

PhosphoSite

O60341.

Proteomic databases

PRIDE

O60341.

Genome annotation databases

Ensembl

ENSG00000004487. Homo sapiens. [Contig view]

GeneID

23028.

KEGG

hsa:23028.

Organism-specific databases

GeneCards

GC01P023218.

H-InvDB

HIX0000238.

HGNC

HGNC:29079. KDM1.

HPA

CAB005884.

MIM

609132. gene.

PharmGKB

PA134972783.

HUGE

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GenAtlas

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Phylogenomic databases

HOVERGEN

O60341.

OMA

O60341. VFLYIRN.

Enzyme and pathway databases

Pathway_Interaction_DB

ar_pathway. Coregulation of Androgen receptor activity.

Gene expression databases

Bgee

O60341.

CleanEx

HS_AOF2.

GermOnline

ENSG00000004487. Homo sapiens.

Family and domain databases

InterPro

IPR002937. Amino_oxidase.
IPR017366. Hist_Lys-spec_deMease.
IPR007526. SWIRM.
[Graphical view]

Pfam

PF01593. Amino_oxidase. 1 hit.
PF04433. SWIRM. 1 hit.
[Graphical view]

PIRSF

PIRSF038051. Histone_Lys-demethylase. 1 hit.

PROSITE

PS50934. SWIRM. 1 hit.
[Graphical view]

ProtoNet

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Other Resources

NextBio

43998.

SOURCE

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Entry information

Entry name

KDM1_HUMAN

Accession

Primary (citable) accession number: O60341
Secondary accession number(s): 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:	June 16, 2009
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)