KDM4A_HUMAN
ID KDM4A_HUMAN Reviewed; 1064 AA.
AC O75164; Q5VVB1;
DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Lysine-specific demethylase 4A;
DE EC=1.14.11.66 {ECO:0000269|PubMed:16603238};
DE EC=1.14.11.69 {ECO:0000269|PubMed:16603238};
DE AltName: Full=JmjC domain-containing histone demethylation protein 3A;
DE AltName: Full=Jumonji domain-containing protein 2A;
DE AltName: Full=[histone H3]-trimethyl-L-lysine(36) demethylase 4A {ECO:0000305};
DE AltName: Full=[histone H3]-trimethyl-L-lysine(9) demethylase 4A {ECO:0000305};
GN Name=KDM4A; Synonyms=JHDM3A, JMJD2, JMJD2A, KIAA0677;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-482.
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-482.
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH HDAC1;
RP HDAC2; HDAC3; RB1 AND HTLV-1 TAX.
RX PubMed=15927959; DOI=10.1074/jbc.m413687200;
RA Gray S.G., Iglesias A.H., Lizcano F., Villanueva R., Camelo S., Jingu H.,
RA Teh B.T., Koibuchi N., Chin W.W., Kokkotou E., Dangond F.;
RT "Functional characterization of JMJD2A, a histone deacetylase- and
RT retinoblastoma-binding protein.";
RL J. Biol. Chem. 280:28507-28518(2005).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NCOR1.
RX PubMed=16024779; DOI=10.1128/mcb.25.15.6404-6414.2005;
RA Zhang D., Yoon H.-G., Wong J.;
RT "JMJD2A is a novel N-CoR-interacting protein and is involved in repression
RT of the human transcription factor achaete scute-like homologue 2
RT (ASCL2/Hash2).";
RL Mol. Cell. Biol. 25:6404-6414(2005).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, DOMAIN, AND MUTAGENESIS OF HIS-188.
RX PubMed=16603238; DOI=10.1016/j.cell.2006.03.028;
RA Whetstine J.R., Nottke A., Lan F., Huarte M., Smolikov S., Chen Z.,
RA Spooner E., Li E., Zhang G., Colaiacovo M., Shi Y.;
RT "Reversal of histone lysine trimethylation by the JMJD2 family of histone
RT demethylases.";
RL Cell 125:467-481(2006).
RN [7]
RP DOMAIN.
RX PubMed=16415788; DOI=10.1038/sj.embor.7400625;
RA Kim J., Daniel J., Espejo A., Lake A., Krishna M., Xia L., Zhang Y.,
RA Bedford M.T.;
RT "Tudor, MBT and chromo domains gauge the degree of lysine methylation.";
RL EMBO Rep. 7:397-403(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP UBIQUITINATION, DOMAIN, AND MUTAGENESIS OF HIS-188 AND ASP-939.
RX PubMed=22373579; DOI=10.1038/emboj.2012.47;
RA Mallette F.A., Mattiroli F., Cui G., Young L.C., Hendzel M.J., Mer G.,
RA Sixma T.K., Richard S.;
RT "RNF8- and RNF168-dependent degradation of KDM4A/JMJD2A triggers 53BP1
RT recruitment to DNA damage sites.";
RL EMBO J. 31:1865-1878(2012).
RN [12]
RP ALTERNATIVE SPLICING (ISOFORM 2), AND FUNCTION (ISOFORM 2).
RX PubMed=21694756; DOI=10.1371/journal.pgen.1001390;
RA Verrier L., Escaffit F., Chailleux C., Trouche D., Vandromme M.;
RT "A new isoform of the histone demethylase JMJD2A/KDM4A is required for
RT skeletal muscle differentiation.";
RL PLoS Genet. 7:E1001390-E1001390(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-523, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 1-350 IN COMPLEX WITH IRON AND
RP 2-OXOGLUTARATE, ZINC-BINDING, AND MUTAGENESIS OF GLY-133; GLY-138; GLY-165;
RP GLY-170; 279-SER-THR-280 AND TYR-973.
RX PubMed=16677698; DOI=10.1016/j.cell.2006.04.024;
RA Chen Z., Zang J., Whetstine J., Hong X., Davrazou F., Kutateladze T.G.,
RA Simpson M., Mao Q., Pan C.-H., Dai S., Hagman J., Hansen K., Shi Y.,
RA Zhang G.;
RT "Structural insights into histone demethylation by JMJD2 family members.";
RL Cell 125:691-702(2006).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 895-1011 IN COMPLEX WITH
RP TRIMETHYLATED H3 'LYS-4', DOMAIN, AND MUTAGENESIS OF ASP-945; TRP-967 AND
RP TYR-973.
RX PubMed=16601153; DOI=10.1126/science.1125162;
RA Huang Y., Fang J., Bedford M.T., Zhang Y., Xu R.-M.;
RT "Recognition of histone H3 lysine-4 methylation by the double Tudor domain
RT of JMJD2A.";
RL Science 312:748-751(2006).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 4-355 IN COMPLEX WITH ZINC AND
RP SEVERAL INHIBITORS, FUNCTION, ACTIVITY REGULATION, AND COFACTOR.
RX PubMed=26741168; DOI=10.1021/acs.jmedchem.5b01635;
RA Bavetsias V., Lanigan R.M., Ruda G.F., Atrash B., McLaughlin M.G.,
RA Tumber A., Mok N.Y., Le Bihan Y.V., Dempster S., Boxall K.J.,
RA Jeganathan F., Hatch S.B., Savitsky P., Velupillai S., Krojer T.,
RA England K.S., Sejberg J., Thai C., Donovan A., Pal A., Scozzafava G.,
RA Bennett J.M., Kawamura A., Johansson C., Szykowska A., Gileadi C.,
RA Burgess-Brown N.A., von Delft F., Oppermann U., Walters Z., Shipley J.,
RA Raynaud F.I., Westaway S.M., Prinjha R.K., Fedorov O., Burke R.,
RA Schofield C.J., Westwood I.M., Bountra C., Muller S., van Montfort R.L.,
RA Brennan P.E., Blagg J.;
RT "8-Substituted Pyrido[3,4-d]pyrimidin-4(3H)-one Derivatives As Potent, Cell
RT Permeable, KDM4 (JMJD2) and KDM5 (JARID1) Histone Lysine Demethylase
RT Inhibitors.";
RL J. Med. Chem. 59:1388-1409(2016).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 11-161 AND 170-354.
RX PubMed=27214403; DOI=10.1038/nchembio.2087;
RA Johansson C., Velupillai S., Tumber A., Szykowska A., Hookway E.S.,
RA Nowak R.P., Strain-Damerell C., Gileadi C., Philpott M., Burgess-Brown N.,
RA Wu N., Kopec J., Nuzzi A., Steuber H., Egner U., Badock V., Munro S.,
RA LaThangue N.B., Westaway S., Brown J., Athanasou N., Prinjha R.,
RA Brennan P.E., Oppermann U.;
RT "Structural analysis of human KDM5B guides histone demethylase inhibitor
RT development.";
RL Nat. Chem. Biol. 12:539-545(2016).
CC -!- FUNCTION: Histone demethylase that specifically demethylates 'Lys-9'
CC and 'Lys-36' residues of histone H3, thereby playing a central role in
CC histone code (PubMed:26741168). Does not demethylate histone H3 'Lys-
CC 4', H3 'Lys-27' nor H4 'Lys-20'. Demethylates trimethylated H3 'Lys-9'
CC and H3 'Lys-36' residue, while it has no activity on mono- and
CC dimethylated residues. Demethylation of Lys residue generates
CC formaldehyde and succinate. Participates in transcriptional repression
CC of ASCL2 and E2F-responsive promoters via the recruitment of histone
CC deacetylases and NCOR1, respectively. {ECO:0000269|PubMed:16024779,
CC ECO:0000269|PubMed:16603238, ECO:0000269|PubMed:26741168}.
CC -!- FUNCTION: [Isoform 2]: Crucial for muscle differentiation, promotes
CC transcriptional activation of the Myog gene by directing the removal of
CC repressive chromatin marks at its promoter. Lacks the N-terminal
CC demethylase domain. {ECO:0000269|PubMed:21694756}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(9)-
CC [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC lysyl(9)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60200, Rhea:RHEA-
CC COMP:15538, Rhea:RHEA-COMP:15542, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961;
CC EC=1.14.11.66; Evidence={ECO:0000269|PubMed:16603238};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-
CC [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC lysyl(36)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60236,
CC Rhea:RHEA-COMP:9786, Rhea:RHEA-COMP:15536, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961;
CC EC=1.14.11.69; Evidence={ECO:0000269|PubMed:16603238};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:16603238};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:16603238};
CC -!- ACTIVITY REGULATION: Several specific inhibitors are being developed
CC and tested. {ECO:0000269|PubMed:26741168}.
CC -!- SUBUNIT: Interacts with histone deacetylase proteins HDAC1, HDAC2 and
CC HDAC3. Interacts with RB and NCOR1. {ECO:0000269|PubMed:15927959,
CC ECO:0000269|PubMed:16024779, ECO:0000269|PubMed:16601153,
CC ECO:0000269|PubMed:16677698}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HTLV-1 Tax protein.
CC {ECO:0000269|PubMed:15927959}.
CC -!- INTERACTION:
CC O75164; P11308: ERG; NbExp=2; IntAct=EBI-936709, EBI-79704;
CC O75164; Q16695: H3-4; NbExp=6; IntAct=EBI-936709, EBI-358900;
CC O75164; P68431: H3C12; NbExp=7; IntAct=EBI-936709, EBI-79722;
CC O75164; P62805: H4C9; NbExp=7; IntAct=EBI-936709, EBI-302023;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537,
CC ECO:0000269|PubMed:15927959, ECO:0000269|PubMed:16024779}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75164-1; Sequence=Displayed;
CC Name=2; Synonyms=deltaN-JMJD2A;
CC IsoId=O75164-2; Sequence=VSP_044239;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:15927959}.
CC -!- DOMAIN: The 2 Tudor domains recognize and bind methylated histone H3
CC 'Lys-4' residue (H3K4me). Double Tudor domain has an interdigitated
CC structure and the unusual fold is required for its ability to bind
CC methylated histone tails. Trimethylated H3 'Lys-4' (H3K4me3) is bound
CC in a cage of 3 aromatic residues, 2 of which are from the Tudor domain
CC 2, while the binding specificity is determined by side-chain
CC interactions involving residues from the Tudor domain 1. The Tudor
CC domains are also able to bind trimethylated histone H3 'Lys-9'
CC (H3K9me3), di- and trimethylated H4 'Lys-20' (H4K20me2 and H4K20me3).
CC Has high affinity for H4K20me2, blocking recruitment of proteins such
CC as TP53BP1. {ECO:0000269|PubMed:16415788, ECO:0000269|PubMed:16601153,
CC ECO:0000269|PubMed:16603238, ECO:0000269|PubMed:22373579}.
CC -!- PTM: Ubiquitinated by RNF8 and RNF168 following DNA damage, leading to
CC its degradation. Degradation promotes accessibility of H4K20me2 mark
CC for DNA repair protein TP53BP1, which is then recruited.
CC {ECO:0000269|PubMed:22373579}.
CC -!- SIMILARITY: Belongs to the JHDM3 histone demethylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31652.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB014577; BAA31652.2; ALT_INIT; mRNA.
DR EMBL; AC092815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL451062; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002558; AAH02558.1; -; mRNA.
DR CCDS; CCDS491.1; -. [O75164-1]
DR RefSeq; NP_055478.2; NM_014663.2. [O75164-1]
DR RefSeq; XP_005271411.1; XM_005271354.3. [O75164-1]
DR RefSeq; XP_005271412.1; XM_005271355.3. [O75164-1]
DR PDB; 2GF7; X-ray; 2.20 A; A/B/C/D=895-1011.
DR PDB; 2GFA; X-ray; 2.10 A; A/B=895-1011.
DR PDB; 2GP3; X-ray; 2.35 A; A/B=2-350.
DR PDB; 2GP5; X-ray; 2.28 A; A/B=2-350.
DR PDB; 2OQ6; X-ray; 2.00 A; A/B=1-359.
DR PDB; 2OQ7; X-ray; 2.15 A; A/B=1-359.
DR PDB; 2OS2; X-ray; 2.30 A; A/B=1-359.
DR PDB; 2OT7; X-ray; 2.13 A; A/B=1-359.
DR PDB; 2OX0; X-ray; 1.95 A; A/B=1-359.
DR PDB; 2P5B; X-ray; 1.99 A; A/B=2-350.
DR PDB; 2PXJ; X-ray; 2.00 A; A/B=2-348.
DR PDB; 2Q8C; X-ray; 2.05 A; A/B=1-350.
DR PDB; 2Q8D; X-ray; 2.29 A; A/B=1-350.
DR PDB; 2Q8E; X-ray; 2.05 A; A/B=1-350.
DR PDB; 2QQR; X-ray; 1.80 A; A/B=897-1011.
DR PDB; 2QQS; X-ray; 2.82 A; A/B=897-1011.
DR PDB; 2VD7; X-ray; 2.25 A; A/B=1-359.
DR PDB; 2WWJ; X-ray; 2.60 A; A/B=7-353.
DR PDB; 2YBK; X-ray; 2.40 A; A/B=1-359.
DR PDB; 2YBP; X-ray; 2.02 A; A/B=1-359.
DR PDB; 2YBS; X-ray; 2.32 A; A/B=1-359.
DR PDB; 3NJY; X-ray; 2.60 A; A/B=1-359.
DR PDB; 3PDQ; X-ray; 1.99 A; A/B=1-359.
DR PDB; 3RVH; X-ray; 2.25 A; A/B=1-359.
DR PDB; 3U4S; X-ray; 2.15 A; A/B=1-359.
DR PDB; 4AI9; X-ray; 2.25 A; A/B=1-359.
DR PDB; 4BIS; X-ray; 2.49 A; A/B=1-359.
DR PDB; 4GD4; X-ray; 2.33 A; A/B=1-359.
DR PDB; 4URA; X-ray; 2.23 A; A/B=1-359.
DR PDB; 4V2V; X-ray; 2.00 A; A/B=1-359.
DR PDB; 4V2W; X-ray; 1.81 A; A/B=1-359.
DR PDB; 5A7N; X-ray; 2.39 A; A/B=1-359.
DR PDB; 5A7O; X-ray; 2.15 A; A/B=1-359.
DR PDB; 5A7P; X-ray; 2.28 A; A/B=1-359.
DR PDB; 5A7Q; X-ray; 2.00 A; A/B=1-359.
DR PDB; 5A7S; X-ray; 2.20 A; A/B=1-359.
DR PDB; 5A7W; X-ray; 2.27 A; A/B=1-359.
DR PDB; 5A80; X-ray; 2.28 A; A/B=1-359.
DR PDB; 5ANQ; X-ray; 2.00 A; A/B=1-359.
DR PDB; 5D6W; X-ray; 1.99 A; A/B/C/D=895-1011.
DR PDB; 5D6X; X-ray; 2.15 A; A/B=895-1011.
DR PDB; 5D6Y; X-ray; 2.29 A; A/B/C/D/E/F=895-1011.
DR PDB; 5F2S; X-ray; 2.08 A; A/B/C/D=1-359.
DR PDB; 5F2W; X-ray; 2.60 A; A/B/C/D=1-359.
DR PDB; 5F32; X-ray; 2.05 A; A/B/C/D=1-359.
DR PDB; 5F37; X-ray; 2.22 A; A/B/C/D=1-359.
DR PDB; 5F39; X-ray; 2.65 A; A/B/C/D=1-359.
DR PDB; 5F3C; X-ray; 2.06 A; A/B/C/D=1-359.
DR PDB; 5F3E; X-ray; 2.16 A; A/B/C/D=1-359.
DR PDB; 5F3G; X-ray; 2.50 A; A/B/C/D=1-359.
DR PDB; 5F3I; X-ray; 2.24 A; A/B/C/D=1-359.
DR PDB; 5F5I; X-ray; 2.63 A; A/B=1-359.
DR PDB; 5FPV; X-ray; 2.44 A; A/B/C/D/E/F/G/H=1-359.
DR PDB; 5FWE; X-ray; 2.05 A; A/B=1-359.
DR PDB; 5FY8; X-ray; 2.34 A; A/B=1-359.
DR PDB; 5FYC; X-ray; 2.26 A; A/B=1-359.
DR PDB; 5FYH; X-ray; 2.35 A; A/B=1-359.
DR PDB; 5FYI; X-ray; 2.10 A; A/B=1-359.
DR PDB; 5LY1; X-ray; 2.50 A; A/B/C/D=1-359.
DR PDB; 5LY2; X-ray; 2.43 A; A/B/C/D=1-359.
DR PDB; 5TVR; X-ray; 2.09 A; A/B=1-359.
DR PDB; 5TVS; X-ray; 2.75 A; A/B=1-359.
DR PDB; 5VAR; X-ray; 1.83 A; A=897-1011.
DR PDB; 5VGI; X-ray; 2.07 A; A/B/C/D=5-354.
DR PDB; 5VMP; X-ray; 2.48 A; A/B/C/D=5-354.
DR PDB; 6CG1; X-ray; 2.16 A; A/B/C/D=5-354.
DR PDB; 6CG2; X-ray; 2.34 A; A/B/C/D=5-354.
DR PDB; 6G5W; X-ray; 1.83 A; A/B=1-359.
DR PDB; 6G5X; X-ray; 1.78 A; A/B=1-359.
DR PDB; 6H4O; X-ray; 2.25 A; A/B/C/D=1-359.
DR PDB; 6H4P; X-ray; 2.19 A; A/B/C/D=1-359.
DR PDB; 6H4Q; X-ray; 2.31 A; A/B/C/D=1-359.
DR PDB; 6H4R; X-ray; 2.14 A; A/B/C/D=1-359.
DR PDB; 6H4S; X-ray; 2.45 A; A/B/C/D=1-359.
DR PDB; 6H4T; X-ray; 2.38 A; A/B/C/D=1-359.
DR PDB; 6H4U; X-ray; 2.21 A; A/B/C/D=1-359.
DR PDB; 6H4V; X-ray; 2.15 A; A/B/C/D=1-359.
DR PDB; 6H4W; X-ray; 2.81 A; A/B/C/D=1-359.
DR PDB; 6H4X; X-ray; 2.34 A; A/B/C/D=1-359.
DR PDB; 6H4Y; X-ray; 2.38 A; A/B/C/D=1-359.
DR PDB; 6H8P; X-ray; 1.98 A; A/B=1-359.
DR PDB; 6HGT; X-ray; 2.33 A; A/B/C/D=1-359.
DR PDB; 7D4A; X-ray; 2.20 A; A=898-1011.
DR PDBsum; 2GF7; -.
DR PDBsum; 2GFA; -.
DR PDBsum; 2GP3; -.
DR PDBsum; 2GP5; -.
DR PDBsum; 2OQ6; -.
DR PDBsum; 2OQ7; -.
DR PDBsum; 2OS2; -.
DR PDBsum; 2OT7; -.
DR PDBsum; 2OX0; -.
DR PDBsum; 2P5B; -.
DR PDBsum; 2PXJ; -.
DR PDBsum; 2Q8C; -.
DR PDBsum; 2Q8D; -.
DR PDBsum; 2Q8E; -.
DR PDBsum; 2QQR; -.
DR PDBsum; 2QQS; -.
DR PDBsum; 2VD7; -.
DR PDBsum; 2WWJ; -.
DR PDBsum; 2YBK; -.
DR PDBsum; 2YBP; -.
DR PDBsum; 2YBS; -.
DR PDBsum; 3NJY; -.
DR PDBsum; 3PDQ; -.
DR PDBsum; 3RVH; -.
DR PDBsum; 3U4S; -.
DR PDBsum; 4AI9; -.
DR PDBsum; 4BIS; -.
DR PDBsum; 4GD4; -.
DR PDBsum; 4URA; -.
DR PDBsum; 4V2V; -.
DR PDBsum; 4V2W; -.
DR PDBsum; 5A7N; -.
DR PDBsum; 5A7O; -.
DR PDBsum; 5A7P; -.
DR PDBsum; 5A7Q; -.
DR PDBsum; 5A7S; -.
DR PDBsum; 5A7W; -.
DR PDBsum; 5A80; -.
DR PDBsum; 5ANQ; -.
DR PDBsum; 5D6W; -.
DR PDBsum; 5D6X; -.
DR PDBsum; 5D6Y; -.
DR PDBsum; 5F2S; -.
DR PDBsum; 5F2W; -.
DR PDBsum; 5F32; -.
DR PDBsum; 5F37; -.
DR PDBsum; 5F39; -.
DR PDBsum; 5F3C; -.
DR PDBsum; 5F3E; -.
DR PDBsum; 5F3G; -.
DR PDBsum; 5F3I; -.
DR PDBsum; 5F5I; -.
DR PDBsum; 5FPV; -.
DR PDBsum; 5FWE; -.
DR PDBsum; 5FY8; -.
DR PDBsum; 5FYC; -.
DR PDBsum; 5FYH; -.
DR PDBsum; 5FYI; -.
DR PDBsum; 5LY1; -.
DR PDBsum; 5LY2; -.
DR PDBsum; 5TVR; -.
DR PDBsum; 5TVS; -.
DR PDBsum; 5VAR; -.
DR PDBsum; 5VGI; -.
DR PDBsum; 5VMP; -.
DR PDBsum; 6CG1; -.
DR PDBsum; 6CG2; -.
DR PDBsum; 6G5W; -.
DR PDBsum; 6G5X; -.
DR PDBsum; 6H4O; -.
DR PDBsum; 6H4P; -.
DR PDBsum; 6H4Q; -.
DR PDBsum; 6H4R; -.
DR PDBsum; 6H4S; -.
DR PDBsum; 6H4T; -.
DR PDBsum; 6H4U; -.
DR PDBsum; 6H4V; -.
DR PDBsum; 6H4W; -.
DR PDBsum; 6H4X; -.
DR PDBsum; 6H4Y; -.
DR PDBsum; 6H8P; -.
DR PDBsum; 6HGT; -.
DR PDBsum; 7D4A; -.
DR AlphaFoldDB; O75164; -.
DR PCDDB; O75164; -.
DR SMR; O75164; -.
DR BioGRID; 115035; 56.
DR CORUM; O75164; -.
DR DIP; DIP-29372N; -.
DR IntAct; O75164; 54.
DR MINT; O75164; -.
DR STRING; 9606.ENSP00000361473; -.
DR BindingDB; O75164; -.
DR ChEMBL; CHEMBL5896; -.
DR GuidetoPHARMACOLOGY; 2675; -.
DR iPTMnet; O75164; -.
DR PhosphoSitePlus; O75164; -.
DR BioMuta; KDM4A; -.
DR EPD; O75164; -.
DR jPOST; O75164; -.
DR MassIVE; O75164; -.
DR MaxQB; O75164; -.
DR PaxDb; O75164; -.
DR PeptideAtlas; O75164; -.
DR PRIDE; O75164; -.
DR ProteomicsDB; 49829; -. [O75164-1]
DR ABCD; O75164; 10 sequenced antibodies.
DR Antibodypedia; 1997; 460 antibodies from 43 providers.
DR DNASU; 9682; -.
DR Ensembl; ENST00000372396.4; ENSP00000361473.3; ENSG00000066135.13. [O75164-1]
DR GeneID; 9682; -.
DR KEGG; hsa:9682; -.
DR MANE-Select; ENST00000372396.4; ENSP00000361473.3; NM_014663.3; NP_055478.2.
DR UCSC; uc001cjx.4; human. [O75164-1]
DR CTD; 9682; -.
DR DisGeNET; 9682; -.
DR GeneCards; KDM4A; -.
DR HGNC; HGNC:22978; KDM4A.
DR HPA; ENSG00000066135; Low tissue specificity.
DR MIM; 609764; gene.
DR neXtProt; NX_O75164; -.
DR OpenTargets; ENSG00000066135; -.
DR PharmGKB; PA164721403; -.
DR VEuPathDB; HostDB:ENSG00000066135; -.
DR eggNOG; KOG0958; Eukaryota.
DR GeneTree; ENSGT00940000159643; -.
DR HOGENOM; CLU_001442_0_1_1; -.
DR InParanoid; O75164; -.
DR OMA; AQQPPYC; -.
DR OrthoDB; 1186832at2759; -.
DR PhylomeDB; O75164; -.
DR TreeFam; TF106449; -.
DR BioCyc; MetaCyc:ENSG00000066135-MON; -.
DR BRENDA; 1.14.11.27; 2681.
DR BRENDA; 1.14.11.66; 2681.
DR BRENDA; 1.14.11.67; 2681.
DR BRENDA; 1.14.11.69; 2681.
DR BRENDA; 1.14.99.66; 2681.
DR PathwayCommons; O75164; -.
DR Reactome; R-HSA-3214842; HDMs demethylate histones.
DR Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-HSA-9029569; NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux.
DR SignaLink; O75164; -.
DR BioGRID-ORCS; 9682; 49 hits in 1100 CRISPR screens.
DR ChiTaRS; KDM4A; human.
DR EvolutionaryTrace; O75164; -.
DR GeneWiki; JMJD2A; -.
DR GenomeRNAi; 9682; -.
DR Pharos; O75164; Tchem.
DR PRO; PR:O75164; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O75164; protein.
DR Bgee; ENSG00000066135; Expressed in cortical plate and 182 other tissues.
DR ExpressionAtlas; O75164; baseline and differential.
DR Genevisible; O75164; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005721; C:pericentric heterochromatin; IEA:Ensembl.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0051864; F:histone H3-methyl-lysine-36 demethylase activity; IDA:UniProtKB.
DR GO; GO:0032454; F:histone H3-methyl-lysine-9 demethylase activity; IMP:UniProtKB.
DR GO; GO:0140681; F:histone H3-tri/dimethyl-lysine-36 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0140684; F:histone H3-tri/dimethyl-lysine-9 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; IEA:Ensembl.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0016577; P:histone demethylation; IDA:UniProtKB.
DR GO; GO:0070544; P:histone H3-K36 demethylation; IDA:UniProtKB.
DR GO; GO:0033169; P:histone H3-K9 demethylation; IMP:UniProtKB.
DR GO; GO:0048712; P:negative regulation of astrocyte differentiation; IEA:Ensembl.
DR GO; GO:0010507; P:negative regulation of autophagy; IMP:ParkinsonsUK-UCL.
DR GO; GO:0060548; P:negative regulation of cell death; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IMP:ParkinsonsUK-UCL.
DR GO; GO:1900113; P:negative regulation of histone H3-K9 trimethylation; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
DR CDD; cd04508; TUDOR; 2.
DR Gene3D; 3.30.40.10; -; 2.
DR IDEAL; IID00360; -.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR040477; KDM4_Tudor_2.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF18104; Tudor_2; 2.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00333; TUDOR; 2.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chromatin regulator;
KW Dioxygenase; Host-virus interaction; Iron; Metal-binding; Nucleus;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..1064
FT /note="Lysine-specific demethylase 4A"
FT /id="PRO_0000183172"
FT DOMAIN 14..56
FT /note="JmjN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00537"
FT DOMAIN 142..308
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT DOMAIN 897..954
FT /note="Tudor 1"
FT DOMAIN 955..1011
FT /note="Tudor 2"
FT ZN_FING 709..767
FT /note="PHD-type 1"
FT ZN_FING 772..805
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 828..885
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 358..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 597..638
FT /note="Interaction with NCOR1"
FT /evidence="ECO:0000269|PubMed:16024779"
FT REGION 616..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 132
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000269|PubMed:16677698"
FT BINDING 188
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538,
FT ECO:0000269|PubMed:16677698, ECO:0000305|PubMed:26741168"
FT BINDING 190
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16677698,
FT ECO:0000305|PubMed:26741168"
FT BINDING 198
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000269|PubMed:16677698"
FT BINDING 206
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000269|PubMed:16677698"
FT BINDING 234
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:5F2W, ECO:0007744|PDB:5F32,
FT ECO:0007744|PDB:5F37, ECO:0007744|PDB:5F39,
FT ECO:0007744|PDB:5F3E, ECO:0007744|PDB:5F3G,
FT ECO:0007744|PDB:5F5I"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:5F2W, ECO:0007744|PDB:5F32,
FT ECO:0007744|PDB:5F37, ECO:0007744|PDB:5F39,
FT ECO:0007744|PDB:5F3E, ECO:0007744|PDB:5F3G,
FT ECO:0007744|PDB:5F5I"
FT BINDING 241
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:B2RXH2"
FT BINDING 276
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538,
FT ECO:0000269|PubMed:16677698, ECO:0000305|PubMed:26741168"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:5F2W, ECO:0007744|PDB:5F32,
FT ECO:0007744|PDB:5F37, ECO:0007744|PDB:5F39,
FT ECO:0007744|PDB:5F3E, ECO:0007744|PDB:5F3G,
FT ECO:0007744|PDB:5F5I"
FT BINDING 308
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0007744|PDB:5F2W, ECO:0007744|PDB:5F32,
FT ECO:0007744|PDB:5F37, ECO:0007744|PDB:5F39,
FT ECO:0007744|PDB:5F3E, ECO:0007744|PDB:5F3G,
FT ECO:0007744|PDB:5F5I"
FT SITE 945
FT /note="Histone H3K4me3 binding"
FT SITE 967
FT /note="Histone H3K4me3 binding"
FT SITE 973
FT /note="Histone H3K4me3 binding"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..583
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_044239"
FT VARIANT 482
FT /note="A -> E (in dbSNP:rs586339)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9734811"
FT /id="VAR_023775"
FT VARIANT 877
FT /note="V -> G (in dbSNP:rs12759032)"
FT /id="VAR_031217"
FT MUTAGEN 133
FT /note="G->A: Abolishes histone demethylase activity; when
FT associated with A-138."
FT /evidence="ECO:0000269|PubMed:16677698"
FT MUTAGEN 138
FT /note="G->A: Abolishes histone demethylase activity; when
FT associated with A-138."
FT /evidence="ECO:0000269|PubMed:16677698"
FT MUTAGEN 165
FT /note="G->A: Abolishes histone demethylase activity; when
FT associated with A-165."
FT /evidence="ECO:0000269|PubMed:16677698"
FT MUTAGEN 170
FT /note="G->A: Abolishes histone demethylase activity; when
FT associated with A-165."
FT /evidence="ECO:0000269|PubMed:16677698"
FT MUTAGEN 188
FT /note="H->A: Abolishes histone demethylase activity without
FT affecting ability to bind H4K20me2."
FT /evidence="ECO:0000269|PubMed:16603238,
FT ECO:0000269|PubMed:22373579"
FT MUTAGEN 288..289
FT /note="ST->AI: Displays histone demethylase activity for
FT both dimethylated and H3-K9Me3."
FT MUTAGEN 288..289
FT /note="ST->TV,NV,GG: Abolishes histone demethylase
FT activity."
FT MUTAGEN 939
FT /note="D->R: Impairs binding to H4K20me2, promoting partial
FT recruitment of TP53BP1."
FT /evidence="ECO:0000269|PubMed:22373579"
FT MUTAGEN 945
FT /note="D->A: Impairs binding to H3K4me3."
FT /evidence="ECO:0000269|PubMed:16601153"
FT MUTAGEN 945
FT /note="D->R: Abolishes binding to H3K4me3."
FT /evidence="ECO:0000269|PubMed:16601153"
FT MUTAGEN 967
FT /note="W->H: Abolishes binding to H3K4me3."
FT /evidence="ECO:0000269|PubMed:16601153"
FT MUTAGEN 973
FT /note="Y->A: Abolishes binding to H3K4me3."
FT /evidence="ECO:0000269|PubMed:16601153,
FT ECO:0000269|PubMed:16677698"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:6G5X"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:6H8P"
FT STRAND 15..17
FT /evidence="ECO:0007829|PDB:4V2W"
FT HELIX 21..24
FT /evidence="ECO:0007829|PDB:6G5X"
FT HELIX 27..36
FT /evidence="ECO:0007829|PDB:6G5X"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:6G5X"
FT STRAND 43..47
FT /evidence="ECO:0007829|PDB:6G5X"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:6G5W"
FT TURN 61..64
FT /evidence="ECO:0007829|PDB:6H8P"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:6G5X"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:6G5X"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:6G5X"
FT HELIX 94..102
FT /evidence="ECO:0007829|PDB:6G5X"
FT TURN 104..106
FT /evidence="ECO:0007829|PDB:6G5X"
FT HELIX 114..124
FT /evidence="ECO:0007829|PDB:6G5X"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:6G5X"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:5F32"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:6G5X"
FT HELIX 159..164
FT /evidence="ECO:0007829|PDB:6G5X"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:6G5X"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:6G5X"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:6G5X"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:6G5X"
FT STRAND 195..204
FT /evidence="ECO:0007829|PDB:6G5X"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:6G5X"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:6G5X"
FT HELIX 216..226
FT /evidence="ECO:0007829|PDB:6G5X"
FT HELIX 228..233
FT /evidence="ECO:0007829|PDB:6G5X"
FT HELIX 237..240
FT /evidence="ECO:0007829|PDB:6G5X"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:6G5X"
FT HELIX 247..252
FT /evidence="ECO:0007829|PDB:6G5X"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:6G5X"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:6G5X"
FT STRAND 275..280
FT /evidence="ECO:0007829|PDB:6G5X"
FT STRAND 282..291
FT /evidence="ECO:0007829|PDB:6G5X"
FT HELIX 296..302
FT /evidence="ECO:0007829|PDB:6G5X"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:6G5X"
FT HELIX 318..324
FT /evidence="ECO:0007829|PDB:6G5X"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:6G5X"
FT HELIX 329..333
FT /evidence="ECO:0007829|PDB:6G5X"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:5F3I"
FT HELIX 348..352
FT /evidence="ECO:0007829|PDB:6G5X"
FT STRAND 904..908
FT /evidence="ECO:0007829|PDB:2QQR"
FT STRAND 912..932
FT /evidence="ECO:0007829|PDB:2QQR"
FT STRAND 937..941
FT /evidence="ECO:0007829|PDB:2QQR"
FT HELIX 943..945
FT /evidence="ECO:0007829|PDB:2QQR"
FT HELIX 951..954
FT /evidence="ECO:0007829|PDB:2QQR"
FT STRAND 962..966
FT /evidence="ECO:0007829|PDB:2QQR"
FT STRAND 972..990
FT /evidence="ECO:0007829|PDB:2QQR"
FT STRAND 995..998
FT /evidence="ECO:0007829|PDB:2QQR"
FT HELIX 1000..1002
FT /evidence="ECO:0007829|PDB:2QQR"
FT STRAND 1003..1005
FT /evidence="ECO:0007829|PDB:2QQR"
SQ SEQUENCE 1064 AA; 120662 MW; 4A811BEECFEDC6B3 CRC64;
MASESETLNP SARIMTFYPT MEEFRNFSRY IAYIESQGAH RAGLAKVVPP KEWKPRASYD
DIDDLVIPAP IQQLVTGQSG LFTQYNIQKK AMTVREFRKI ANSDKYCTPR YSEFEELERK
YWKNLTFNPP IYGADVNGTL YEKHVDEWNI GRLRTILDLV EKESGITIEG VNTPYLYFGM
WKTSFAWHTE DMDLYSINYL HFGEPKSWYS VPPEHGKRLE RLAKGFFPGS AQSCEAFLRH
KMTLISPLML KKYGIPFDKV TQEAGEFMIT FPYGYHAGFN HGFNCAESTN FATRRWIEYG
KQAVLCSCRK DMVKISMDVF VRKFQPERYK LWKAGKDNTV IDHTLPTPEA AEFLKESELP
PRAGNEEECP EEDMEGVEDG EEGDLKTSLA KHRIGTKRHR VCLEIPQEVS QSELFPKEDL
SSEQYEMTEC PAALAPVRPT HSSVRQVEDG LTFPDYSDST EVKFEELKNV KLEEEDEEEE
QAAAALDLSV NPASVGGRLV FSGSKKKSSS SLGSGSSRDS ISSDSETSEP LSCRAQGQTG
VLTVHSYAKG DGRVTVGEPC TRKKGSAARS FSERELAEVA DEYMFSLEEN KKSKGRRQPL
SKLPRHHPLV LQECVSDDET SEQLTPEEEA EETEAWAKPL SQLWQNRPPN FEAEKEFNET
MAQQAPHCAV CMIFQTYHQV EFGGFNQNCG NASDLAPQKQ RTKPLIPEMC FTSTGCSTDI
NLSTPYLEED GTSILVSCKK CSVRVHASCY GVPPAKASED WMCSRCSANA LEEDCCLCSL
RGGALQRAND DRWVHVSCAV AILEARFVNI AERSPVDVSK IPLPRFKLKC IFCKKRRKRT
AGCCVQCSHG RCPTAFHVSC AQAAGVMMQP DDWPFVVFIT CFRHKIPNLE RAKGALQSIT
AGQKVISKHK NGRFYQCEVV RLTTETFYEV NFDDGSFSDN LYPEDIVSQD CLQFGPPAEG
EVVQVRWTDG QVYGAKFVAS HPIQMYQVEF EDGSQLVVKR DDVYTLDEEL PKRVKSRLSV
ASDMRFNEIF TEKEVKQEKK RQRVINSRYR EDYIEPALYR AIME
