ID KDM5B_HUMAN Reviewed; 1544 AA.
AC Q9UGL1; O95811; Q15752; Q9Y3Q5;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 27-MAR-2024, entry version 185.
DE RecName: Full=Lysine-specific demethylase 5B;
DE EC=1.14.11.67 {ECO:0000250|UniProtKB:Q80Y84};
DE AltName: Full=Cancer/testis antigen 31;
DE Short=CT31;
DE AltName: Full=Histone demethylase JARID1B;
DE AltName: Full=Jumonji/ARID domain-containing protein 1B;
DE AltName: Full=PLU-1;
DE AltName: Full=Retinoblastoma-binding protein 2 homolog 1;
DE Short=RBP2-H1;
DE AltName: Full=[histone H3]-trimethyl-L-lysine(4) demethylase 5B {ECO:0000305};
GN Name=KDM5B; Synonyms=JARID1B, PLU1, RBBP2H1;
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 [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Mammary cancer;
RX PubMed=10336460; DOI=10.1074/jbc.274.22.15633;
RA Lu P.J., Sundquist K., Baeckstrom D., Poulsom R., Hanby A., Meier-Ewert S.,
RA Jones T., Mitchell M., Pitha-Rowe P., Freemont P., Taylor-Papadimitriou J.;
RT "A novel gene (PLU-1) containing highly conserved putative DNA/chromatin
RT binding motifs is specifically up-regulated in breast cancer.";
RL J. Biol. Chem. 274:15633-15645(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Teratocarcinoma;
RX PubMed=10616211;
RA Vogt T., Kroiss M., McClelland M., Gruss C., Becker B., Bosserhoff A.K.,
RA Rumpler G., Bogenrieder T., Landthaler M., Stolz W.;
RT "Deficiency of a novel retinoblastoma binding protein 2-homolog is a
RT consistent feature of sporadic human melanoma skin cancer.";
RL Lab. Invest. 79:1615-1627(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=10878660; DOI=10.1038/sj.ejhg.5200474;
RA Kashuba V., Protopopov A., Podowski R., Gizatullin R., Li J., Klein G.,
RA Wahlestedt C., Zabarovsky E.;
RT "Isolation and chromosomal localization of a new human retinoblastoma
RT binding protein 2 homologue 1a (RBBP2H1A).";
RL Eur. J. Hum. Genet. 8:407-413(2000).
RN [4]
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 [5]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=12237901; DOI=10.1002/ijc.10644;
RA Barrett A., Madsen B., Copier J., Lu P.J., Cooper L., Scibetta A.G.,
RA Burchell J., Taylor-Papadimitriou J.;
RT "PLU-1 nuclear protein, which is upregulated in breast cancer, shows
RT restricted expression in normal human adult tissues: a new cancer/testis
RT antigen?";
RL Int. J. Cancer 101:581-588(2002).
RN [6]
RP FUNCTION, AND INTERACTION WITH FOXG1B AND PAX9.
RX PubMed=12657635; DOI=10.1074/jbc.m301994200;
RA Tan K., Shaw A.L., Madsen B., Jensen K., Taylor-Papadimitriou J.,
RA Freemont P.S.;
RT "Human PLU-1 has transcriptional repression properties and interacts with
RT the developmental transcription factors BF-1 and PAX9.";
RL J. Biol. Chem. 278:20507-20513(2003).
RN [7]
RP TISSUE SPECIFICITY, AND INTERACTION WITH RB1.
RX PubMed=15803180; DOI=10.1038/modpathol.3800413;
RA Roesch A., Becker B., Meyer S., Wild P., Hafner C., Landthaler M., Vogt T.;
RT "Retinoblastoma-binding protein 2-homolog 1: a retinoblastoma-binding
RT protein downregulated in malignant melanomas.";
RL Mod. Pathol. 18:1249-1257(2005).
RN [8]
RP FUNCTION, AND INTERACTION WITH RB1.
RX PubMed=16645588; DOI=10.1038/sj.jid.5700324;
RA Roesch A., Becker B., Schneider-Brachert W., Hagen I., Landthaler M.,
RA Vogt T.;
RT "Re-expression of the retinoblastoma-binding protein 2-homolog 1 reveals
RT tumor-suppressive functions in highly metastatic melanoma cells.";
RL J. Invest. Dermatol. 126:1850-1859(2006).
RN [9]
RP FUNCTION.
RX PubMed=17320161; DOI=10.1016/j.cell.2007.02.003;
RA Christensen J., Agger K., Cloos P.A.C., Pasini D., Rose S., Sennels L.,
RA Rappsilber J., Hansen K.H., Salcini A.E., Helin K.;
RT "RBP2 belongs to a family of demethylases, specific for tri-and
RT dimethylated lysine 4 on histone 3.";
RL Cell 128:1063-1076(2007).
RN [10]
RP INTERACTION WITH MYC AND MYCN.
RX PubMed=17311883; DOI=10.1101/gad.1523007;
RA Secombe J., Li L., Carlos L., Eisenman R.N.;
RT "The Trithorax group protein Lid is a trimethyl histone H3K4 demethylase
RT required for dMyc-induced cell growth.";
RL Genes Dev. 21:537-551(2007).
RN [11]
RP INTERACTION WITH HDAC1; HDAC4; HDAC5 AND HDAC7, AND MUTAGENESIS OF HIS-335
RP AND HIS-1200.
RX PubMed=17373667; DOI=10.1002/ijc.22673;
RA Barrett A., Santangelo S., Tan K., Catchpole S., Roberts K.,
RA Spencer-Dene B., Hall D., Scibetta A., Burchell J., Verdin E., Freemont P.,
RA Taylor-Papadimitriou J.;
RT "Breast cancer associated transcriptional repressor PLU-1/JARID1B interacts
RT directly with histone deacetylases.";
RL Int. J. Cancer 121:265-275(2007).
RN [12]
RP FUNCTION, AND MUTAGENESIS OF HIS-499.
RX PubMed=17363312; DOI=10.1016/j.molcel.2007.03.001;
RA Yamane K., Tateishi K., Klose R.J., Fang J., Fabrizio L.A.,
RA Erdjument-Bromage H., Taylor-Papadimitriou J., Tempst P., Zhang Y.;
RT "PLU-1 is an H3K4 demethylase involved in transcriptional repression and
RT breast cancer cell proliferation.";
RL Mol. Cell 25:801-812(2007).
RN [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-986; SER-1328 AND SER-1456,
RP AND IDENTIFICATION BY 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 [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-242 AND LYS-278, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-242; LYS-278 AND LYS-769, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [17]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=26645689; DOI=10.1074/jbc.m115.698449;
RA Horton J.R., Engstrom A., Zoeller E.L., Liu X., Shanks J.R., Zhang X.,
RA Johns M.A., Vertino P.M., Fu H., Cheng X.;
RT "Characterization of a Linked Jumonji Domain of the KDM5/JARID1 Family of
RT Histone H3 Lysine 4 Demethylases.";
RL J. Biol. Chem. 291:2631-2646(2016).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-148; LYS-204; LYS-209; LYS-242;
RP LYS-274; LYS-278; LYS-769 AND LYS-1450, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [19]
RP INVOLVEMENT IN MRT65, AND VARIANTS MRT65 299-ARG--LYS-1544 DEL AND
RP 1370-LEU--LYS-1544 DEL.
RX PubMed=29276005; DOI=10.1016/j.ajhg.2017.11.013;
RG Clinical Assessment of the Utility of Sequencing and Evaluation as a Service (CAUSES) Study;
RG Deciphering Developmental Disorders (DDD) Study;
RA Faundes V., Newman W.G., Bernardini L., Canham N., Clayton-Smith J.,
RA Dallapiccola B., Davies S.J., Demos M.K., Goldman A., Gill H., Horton R.,
RA Kerr B., Kumar D., Lehman A., McKee S., Morton J., Parker M.J., Rankin J.,
RA Robertson L., Temple I.K., Banka S.;
RT "Histone lysine methylases and demethylases in the landscape of human
RT developmental disorders.";
RL Am. J. Hum. Genet. 102:175-187(2018).
RN [20]
RP INVOLVEMENT IN MRT65.
RX PubMed=30409806; DOI=10.1126/science.aar6731;
RG Deciphering Developmental Disorders Study;
RA Martin H.C., Jones W.D., McIntyre R., Sanchez-Andrade G., Sanderson M.,
RA Stephenson J.D., Jones C.P., Handsaker J., Gallone G., Bruntraeger M.,
RA McRae J.F., Prigmore E., Short P., Niemi M., Kaplanis J., Radford E.J.,
RA Akawi N., Balasubramanian M., Dean J., Horton R., Hulbert A., Johnson D.S.,
RA Johnson K., Kumar D., Lynch S.A., Mehta S.G., Morton J., Parker M.J.,
RA Splitt M., Turnpenny P.D., Vasudevan P.C., Wright M., Bassett A.,
RA Gerety S.S., Wright C.F., FitzPatrick D.R., Firth H.V., Hurles M.E.,
RA Barrett J.C.;
RT "Quantifying the contribution of recessive coding variation to
RT developmental disorders.";
RL Science 362:1161-1164(2018).
RN [21]
RP STRUCTURE BY NMR OF 306-360 IN COMPLEX WITH ZINC AND HISTONE H3, FUNCTION,
RP INTERACTION WITH HISTONE H3, AND MUTAGENESIS OF ASP-308; LEU-309; TYR-310;
RP VAL-311; GLU-321; ASP-322; LEU-324; LEU-325; LEU-326; ASP-328; ASP-332;
RP SER-333; TYR-334; ASP-345 AND TRP-351.
RX PubMed=24952722; DOI=10.1007/s13238-014-0078-4;
RA Zhang Y., Yang H., Guo X., Rong N., Song Y., Xu Y., Lan W., Zhang X.,
RA Liu M., Xu Y., Cao C.;
RT "The PHD1 finger of KDM5B recognizes unmodified H3K4 during the
RT demethylation of histone H3K4me2/3 by KDM5B.";
RL Protein Cell 5:837-850(2014).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 26-101 AND 374-772 IN COMPLEX
RP WITH ZINC; MANGANESE AND AN INHIBITOR, FUNCTION, AND ACTIVITY REGULATION.
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 [23]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 26-101 AND 374-772 IN COMPLEX
RP WITH SEVERAL INHIBITORS; ZINC AND MANGANESE, DOMAIN, FUNCTION, AND ACTIVITY
RP REGULATION.
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).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 26-100 AND 374-772 IN COMPLEX
RP WITH INHIBITOR KDOAM-25; ZINC AND MANGANESE, FUNCTION, ACTIVITY REGULATION,
RP AND MUTAGENESIS OF 499-HIS--GLU-501.
RX PubMed=28262558; DOI=10.1016/j.chembiol.2017.02.006;
RA Tumber A., Nuzzi A., Hookway E.S., Hatch S.B., Velupillai S., Johansson C.,
RA Kawamura A., Savitsky P., Yapp C., Szykowska A., Wu N., Bountra C.,
RA Strain-Damerell C., Burgess-Brown N.A., Ruda G.F., Fedorov O., Munro S.,
RA England K.S., Nowak R.P., Schofield C.J., La Thangue N.B., Pawlyn C.,
RA Davies F., Morgan G., Athanasou N., Muller S., Oppermann U., Brennan P.E.;
RT "Potent and Selective KDM5 Inhibitor Stops Cellular Demethylation of
RT H3K4me3 at Transcription Start Sites and Proliferation of MM1S Myeloma
RT Cells.";
RL Cell Chem. Biol. 24:371-380(2017).
CC -!- FUNCTION: Histone demethylase that demethylates 'Lys-4' of histone H3,
CC thereby playing a central role in histone code (PubMed:24952722,
CC PubMed:27214403, PubMed:28262558). Does not demethylate histone H3
CC 'Lys-9' or H3 'Lys-27'. Demethylates trimethylated, dimethylated and
CC monomethylated H3 'Lys-4'. Acts as a transcriptional corepressor for
CC FOXG1B and PAX9. Favors the proliferation of breast cancer cells by
CC repressing tumor suppressor genes such as BRCA1 and HOXA5
CC (PubMed:24952722). In contrast, may act as a tumor suppressor for
CC melanoma. Represses the CLOCK-BMAL1 heterodimer-mediated
CC transcriptional activation of the core clock component PER2 (By
CC similarity). {ECO:0000250|UniProtKB:Q80Y84,
CC ECO:0000269|PubMed:12657635, ECO:0000269|PubMed:16645588,
CC ECO:0000269|PubMed:17320161, ECO:0000269|PubMed:17363312,
CC ECO:0000269|PubMed:24952722, ECO:0000269|PubMed:26645689,
CC ECO:0000269|PubMed:26741168, ECO:0000269|PubMed:27214403,
CC ECO:0000269|PubMed:28262558}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(4)-
CC [histone H3] + 3 O2 = 3 CO2 + 3 formaldehyde + L-lysyl(4)-[histone
CC H3] + 3 succinate; Xref=Rhea:RHEA:60208, Rhea:RHEA-COMP:15537,
CC Rhea:RHEA-COMP:15547, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:61961; EC=1.14.11.67;
CC Evidence={ECO:0000250|UniProtKB:Q80Y84};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Several specific inhibitors are being developed
CC and tested (PubMed:27214403, PubMed:26741168). The inhibitor KDOAM-25
CC inhibits its demethylase activity, resulting to cell cycle arrest in
CC myeloma cells (PubMed:28262558). {ECO:0000269|PubMed:26741168,
CC ECO:0000269|PubMed:27214403, ECO:0000269|PubMed:28262558}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9 uM for 2-oxoglutarate {ECO:0000269|PubMed:26645689};
CC KM=4 uM for histone H3K4me3 {ECO:0000269|PubMed:26645689};
CC Note=kcat is 1.9 min(-1) and 2.0 min(-1) for 2-oxoglutarate and
CC histone H3K4me3, respectively. {ECO:0000269|PubMed:26645689};
CC -!- SUBUNIT: Interacts with FOXG1B, PAX9, MYC, MYCN and RB1. Interacts with
CC HDAC1, HDAC4, HDAC5 and HDAC7. Interacts (via PHD-type 1 zinc finger)
CC with histone H3 unmodified at 'Lys-4'; the interaction is inhibited
CC when histone H3 is methylated at 'Arg-2' or 'Lys-4' (PubMed:24952722).
CC {ECO:0000269|PubMed:12657635, ECO:0000269|PubMed:15803180,
CC ECO:0000269|PubMed:16645588, ECO:0000269|PubMed:17311883,
CC ECO:0000269|PubMed:17373667, ECO:0000269|PubMed:24952722}.
CC -!- INTERACTION:
CC Q9UGL1; P49711: CTCF; NbExp=8; IntAct=EBI-2514978, EBI-932887;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355,
CC ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000269|PubMed:10336460,
CC ECO:0000269|PubMed:12237901}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UGL1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UGL1-2; Sequence=VSP_026408;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC testis. Down-regulated in melanoma and glioblastoma. Up-regulated in
CC breast cancer (at protein level). {ECO:0000269|PubMed:10336460,
CC ECO:0000269|PubMed:10616211, ECO:0000269|PubMed:10878660,
CC ECO:0000269|PubMed:12237901, ECO:0000269|PubMed:15803180}.
CC -!- DOMAIN: Both the JmjC domain and the JmjN domain are required for
CC enzymatic activity. However ARID and PHD-type 1 domain are not required
CC for activity per se but contributed to recognition of the H3(1-21)K4me2
CC substrate peptide. {ECO:0000269|PubMed:27214403}.
CC -!- DOMAIN: The 2 first PHD-type zinc finger domains are required for
CC transcription repression activity.
CC -!- DISEASE: Intellectual developmental disorder, autosomal recessive 65
CC (MRT65) [MIM:618109]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period. MRT65
CC patients have moderate to severe intellectual disability, developmental
CC delay, and facial dysmorphism. Camptodactyly is present in some
CC patients. {ECO:0000269|PubMed:29276005, ECO:0000269|PubMed:30409806}.
CC Note=The disease may be caused by variants affecting the gene
CC represented in this entry.
CC -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB63108.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ132440; CAB43532.1; -; mRNA.
DR EMBL; AF087481; AAD16061.1; -; mRNA.
DR EMBL; AJ243706; CAB63108.1; ALT_INIT; mRNA.
DR EMBL; AC098934; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104463; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS30974.1; -. [Q9UGL1-1]
DR CCDS; CCDS81417.1; -. [Q9UGL1-2]
DR RefSeq; NP_001300971.1; NM_001314042.1. [Q9UGL1-2]
DR RefSeq; NP_006609.3; NM_006618.4. [Q9UGL1-1]
DR PDB; 2MA5; NMR; -; A=1487-1544.
DR PDB; 2MNY; NMR; -; A=306-360.
DR PDB; 2MNZ; NMR; -; A=306-360.
DR PDB; 5A1F; X-ray; 2.10 A; A=26-770.
DR PDB; 5A3N; X-ray; 2.00 A; A=26-101, A=374-772.
DR PDB; 5A3P; X-ray; 2.01 A; A=26-101, A=374-770.
DR PDB; 5A3T; X-ray; 1.90 A; A=26-101, A=374-772.
DR PDB; 5A3W; X-ray; 2.00 A; A=26-101, A=374-772.
DR PDB; 5FPL; X-ray; 2.35 A; A=26-101, A=374-772.
DR PDB; 5FPU; X-ray; 2.24 A; A=26-101, A=374-772.
DR PDB; 5FUN; X-ray; 2.30 A; A=26-101, A=374-772.
DR PDB; 5FUP; X-ray; 2.15 A; A=26-101, A=374-770.
DR PDB; 5FV3; X-ray; 2.37 A; A=26-101, A=374-770.
DR PDB; 5FY4; X-ray; 2.10 A; A=26-101, A=374-770.
DR PDB; 5FY5; X-ray; 2.47 A; A=26-101, A=374-770.
DR PDB; 5FY9; X-ray; 2.03 A; A=26-101, A=374-770.
DR PDB; 5FYB; X-ray; 1.87 A; A=26-101, A=374-770.
DR PDB; 5FYS; X-ray; 1.89 A; A=26-101, A=374-770.
DR PDB; 5FYT; X-ray; 1.87 A; A=26-101, A=374-770.
DR PDB; 5FYU; X-ray; 2.06 A; A=26-101, A=374-770.
DR PDB; 5FYV; X-ray; 1.87 A; A=26-101, A=374-770.
DR PDB; 5FYY; X-ray; 2.18 A; A=26-101, A=374-770.
DR PDB; 5FYZ; X-ray; 1.75 A; A=26-101, A=374-770.
DR PDB; 5FZ0; X-ray; 2.42 A; A=26-101, A=374-770.
DR PDB; 5FZ1; X-ray; 2.39 A; A=26-101, A=374-770.
DR PDB; 5FZ3; X-ray; 2.50 A; A=26-101, A=374-770.
DR PDB; 5FZ4; X-ray; 2.07 A; A=26-101, A=374-770.
DR PDB; 5FZ6; X-ray; 2.33 A; A=26-101, A=374-770.
DR PDB; 5FZ7; X-ray; 2.30 A; A=26-101, A=374-770.
DR PDB; 5FZ8; X-ray; 1.86 A; A=26-101, A=374-770.
DR PDB; 5FZ9; X-ray; 2.06 A; A=26-101, A=374-770.
DR PDB; 5FZA; X-ray; 2.10 A; A=26-101, A=374-770.
DR PDB; 5FZB; X-ray; 2.18 A; A=26-101, A=374-770.
DR PDB; 5FZC; X-ray; 2.05 A; A=26-101, A=374-770.
DR PDB; 5FZD; X-ray; 2.05 A; A=26-101, A=374-770.
DR PDB; 5FZE; X-ray; 2.02 A; A=26-101, A=374-770.
DR PDB; 5FZF; X-ray; 1.97 A; A=26-101, A=374-770.
DR PDB; 5FZG; X-ray; 1.96 A; A=26-101, A=374-770.
DR PDB; 5FZH; X-ray; 2.09 A; A=26-101, A=374-442, A=444-770.
DR PDB; 5FZI; X-ray; 1.95 A; A=26-101, A=374-770.
DR PDB; 5FZK; X-ray; 2.05 A; A=26-101, A=374-770.
DR PDB; 5FZL; X-ray; 2.55 A; A=26-101, A=374-770.
DR PDB; 5FZM; X-ray; 2.49 A; A=26-101, A=376-770.
DR PDB; 5LW9; X-ray; 2.30 A; A=26-99, A=374-772.
DR PDB; 5LWB; X-ray; 2.39 A; A=26-101, A=374-772.
DR PDB; 6EIN; X-ray; 2.11 A; A=26-101, A=374-772.
DR PDB; 6EIU; X-ray; 1.88 A; A=26-100, A=374-754.
DR PDB; 6EIY; X-ray; 2.15 A; A=26-100, A=374-754.
DR PDB; 6EJ0; X-ray; 2.06 A; A=26-98, A=375-754.
DR PDB; 6EJ1; X-ray; 2.07 A; A=26-98, A=375-754.
DR PDB; 6EK6; X-ray; 2.05 A; A=347-754.
DR PDB; 6H4Z; X-ray; 2.30 A; A=26-101, A=374-772.
DR PDB; 6H50; X-ray; 2.19 A; A=26-101, A=374-772.
DR PDB; 6H51; X-ray; 2.21 A; A=26-101, A=374-772.
DR PDB; 6H52; X-ray; 2.14 A; A=26-101, A=374-772.
DR PDB; 6RBI; X-ray; 2.21 A; A=26-101, A=374-772.
DR PDBsum; 2MA5; -.
DR PDBsum; 2MNY; -.
DR PDBsum; 2MNZ; -.
DR PDBsum; 5A1F; -.
DR PDBsum; 5A3N; -.
DR PDBsum; 5A3P; -.
DR PDBsum; 5A3T; -.
DR PDBsum; 5A3W; -.
DR PDBsum; 5FPL; -.
DR PDBsum; 5FPU; -.
DR PDBsum; 5FUN; -.
DR PDBsum; 5FUP; -.
DR PDBsum; 5FV3; -.
DR PDBsum; 5FY4; -.
DR PDBsum; 5FY5; -.
DR PDBsum; 5FY9; -.
DR PDBsum; 5FYB; -.
DR PDBsum; 5FYS; -.
DR PDBsum; 5FYT; -.
DR PDBsum; 5FYU; -.
DR PDBsum; 5FYV; -.
DR PDBsum; 5FYY; -.
DR PDBsum; 5FYZ; -.
DR PDBsum; 5FZ0; -.
DR PDBsum; 5FZ1; -.
DR PDBsum; 5FZ3; -.
DR PDBsum; 5FZ4; -.
DR PDBsum; 5FZ6; -.
DR PDBsum; 5FZ7; -.
DR PDBsum; 5FZ8; -.
DR PDBsum; 5FZ9; -.
DR PDBsum; 5FZA; -.
DR PDBsum; 5FZB; -.
DR PDBsum; 5FZC; -.
DR PDBsum; 5FZD; -.
DR PDBsum; 5FZE; -.
DR PDBsum; 5FZF; -.
DR PDBsum; 5FZG; -.
DR PDBsum; 5FZH; -.
DR PDBsum; 5FZI; -.
DR PDBsum; 5FZK; -.
DR PDBsum; 5FZL; -.
DR PDBsum; 5FZM; -.
DR PDBsum; 5LW9; -.
DR PDBsum; 5LWB; -.
DR PDBsum; 6EIN; -.
DR PDBsum; 6EIU; -.
DR PDBsum; 6EIY; -.
DR PDBsum; 6EJ0; -.
DR PDBsum; 6EJ1; -.
DR PDBsum; 6EK6; -.
DR PDBsum; 6H4Z; -.
DR PDBsum; 6H50; -.
DR PDBsum; 6H51; -.
DR PDBsum; 6H52; -.
DR PDBsum; 6RBI; -.
DR AlphaFoldDB; Q9UGL1; -.
DR BMRB; Q9UGL1; -.
DR SASBDB; Q9UGL1; -.
DR SMR; Q9UGL1; -.
DR BioGRID; 115984; 92.
DR CORUM; Q9UGL1; -.
DR DIP; DIP-53652N; -.
DR IntAct; Q9UGL1; 19.
DR MINT; Q9UGL1; -.
DR STRING; 9606.ENSP00000356233; -.
DR BindingDB; Q9UGL1; -.
DR ChEMBL; CHEMBL3774295; -.
DR GuidetoPHARMACOLOGY; 2681; -.
DR GlyGen; Q9UGL1; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q9UGL1; -.
DR PhosphoSitePlus; Q9UGL1; -.
DR SwissPalm; Q9UGL1; -.
DR BioMuta; KDM5B; -.
DR DMDM; 296439317; -.
DR EPD; Q9UGL1; -.
DR jPOST; Q9UGL1; -.
DR MassIVE; Q9UGL1; -.
DR MaxQB; Q9UGL1; -.
DR PaxDb; 9606-ENSP00000356234; -.
DR PeptideAtlas; Q9UGL1; -.
DR ProteomicsDB; 84231; -. [Q9UGL1-1]
DR ProteomicsDB; 84232; -. [Q9UGL1-2]
DR Pumba; Q9UGL1; -.
DR ABCD; Q9UGL1; 1 sequenced antibody.
DR Antibodypedia; 20655; 446 antibodies from 33 providers.
DR DNASU; 10765; -.
DR Ensembl; ENST00000367264.7; ENSP00000356233.2; ENSG00000117139.18. [Q9UGL1-2]
DR Ensembl; ENST00000367265.9; ENSP00000356234.3; ENSG00000117139.18. [Q9UGL1-1]
DR GeneID; 10765; -.
DR KEGG; hsa:10765; -.
DR MANE-Select; ENST00000367265.9; ENSP00000356234.3; NM_006618.5; NP_006609.3.
DR UCSC; uc001gyf.4; human. [Q9UGL1-1]
DR AGR; HGNC:18039; -.
DR CTD; 10765; -.
DR DisGeNET; 10765; -.
DR GeneCards; KDM5B; -.
DR HGNC; HGNC:18039; KDM5B.
DR HPA; ENSG00000117139; Tissue enhanced (testis).
DR MalaCards; KDM5B; -.
DR MIM; 605393; gene.
DR MIM; 618109; phenotype.
DR neXtProt; NX_Q9UGL1; -.
DR OpenTargets; ENSG00000117139; -.
DR Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability.
DR Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability.
DR PharmGKB; PA164721626; -.
DR VEuPathDB; HostDB:ENSG00000117139; -.
DR eggNOG; KOG1246; Eukaryota.
DR GeneTree; ENSGT00940000157076; -.
DR HOGENOM; CLU_000991_2_2_1; -.
DR InParanoid; Q9UGL1; -.
DR OMA; TMMNPGR; -.
DR OrthoDB; 48111at2759; -.
DR PhylomeDB; Q9UGL1; -.
DR TreeFam; TF106476; -.
DR BioCyc; MetaCyc:ENSG00000117139-MONOMER; -.
DR BRENDA; 1.14.11.67; 2681.
DR PathwayCommons; Q9UGL1; -.
DR Reactome; R-HSA-3214842; HDMs demethylate histones.
DR Reactome; R-HSA-8866911; TFAP2 (AP-2) family regulates transcription of cell cycle factors.
DR Reactome; R-HSA-9821002; Chromatin modifications during the maternal to zygotic transition (MZT).
DR SignaLink; Q9UGL1; -.
DR SIGNOR; Q9UGL1; -.
DR BioGRID-ORCS; 10765; 32 hits in 1200 CRISPR screens.
DR ChiTaRS; KDM5B; human.
DR GeneWiki; JARID1B; -.
DR GenomeRNAi; 10765; -.
DR Pharos; Q9UGL1; Tchem.
DR PRO; PR:Q9UGL1; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9UGL1; Protein.
DR Bgee; ENSG00000117139; Expressed in sperm and 186 other cell types or tissues.
DR ExpressionAtlas; Q9UGL1; baseline and differential.
DR Genevisible; Q9UGL1; HS.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:CAFA.
DR GO; GO:0003677; F:DNA binding; IDA:GDB.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0032452; F:histone demethylase activity; TAS:Reactome.
DR GO; GO:0032453; F:histone H3K4 demethylase activity; IDA:CACAO.
DR GO; GO:0034647; F:histone H3K4me/H3K4me2/H3K4me3 demethylase activity; IDA:UniProtKB.
DR GO; GO:0003676; F:nucleic acid binding; IMP:DisProt.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IMP:CAFA.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; IEA:Ensembl.
DR GO; GO:0044344; P:cellular response to fibroblast growth factor stimulus; IEA:Ensembl.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0070306; P:lens fiber cell differentiation; IEA:Ensembl.
DR GO; GO:0060763; P:mammary duct terminal end bud growth; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:GDB.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0033601; P:positive regulation of mammary gland epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR GO; GO:2000864; P:regulation of estradiol secretion; IEA:Ensembl.
DR GO; GO:0060992; P:response to fungicide; IEA:Ensembl.
DR GO; GO:0048511; P:rhythmic process; IEA:UniProtKB-KW.
DR GO; GO:0007338; P:single fertilization; IEA:Ensembl.
DR GO; GO:0061038; P:uterus morphogenesis; IEA:Ensembl.
DR CDD; cd16874; ARID_KDM5B; 1.
DR CDD; cd15603; PHD1_KDM5B; 1.
DR CDD; cd15607; PHD2_KDM5B; 1.
DR CDD; cd15687; PHD3_KDM5B; 1.
DR DisProt; DP00712; -.
DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR048615; KDM5_C-hel.
DR InterPro; IPR047981; KDM5B_ARID.
DR InterPro; IPR047978; KDM5B_PHD1.
DR InterPro; IPR047979; KDM5B_PHD3.
DR InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR004198; Znf_C5HC2.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF3; LYSINE-SPECIFIC DEMETHYLASE 5B; 1.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF21323; KDM5_C-hel; 1.
DR Pfam; PF00628; PHD; 3.
DR Pfam; PF08429; PLU-1; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM01014; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 3.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 3.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Biological rhythms;
KW Chromatin regulator; Dioxygenase; Disease variant; Intellectual disability;
KW Iron; Isopeptide bond; Metal-binding; Nucleus; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1544
FT /note="Lysine-specific demethylase 5B"
FT /id="PRO_0000292412"
FT DOMAIN 32..73
FT /note="JmjN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00537"
FT DOMAIN 97..187
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT DOMAIN 453..619
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT ZN_FING 309..359
FT /note="PHD-type 1"
FT /evidence="ECO:0000269|PubMed:24952722,
FT ECO:0007744|PDB:2MNY"
FT ZN_FING 692..744
FT /note="C5HC2"
FT /evidence="ECO:0000269|PubMed:26741168,
FT ECO:0000269|PubMed:27214403, ECO:0000269|PubMed:28262558"
FT ZN_FING 1176..1224
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 1484..1538
FT /note="PHD-type 3"
FT /evidence="ECO:0007744|PDB:2MA5"
FT REGION 201..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1374..1400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1374..1390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 425
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P29375"
FT BINDING 499
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:26741168,
FT ECO:0000305|PubMed:27214403, ECO:0000305|PubMed:28262558"
FT BINDING 501
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:26741168,
FT ECO:0000305|PubMed:27214403, ECO:0000305|PubMed:28262558"
FT BINDING 507
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P29375"
FT BINDING 509
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P29375"
FT BINDING 517
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000250|UniProtKB:P29375"
FT BINDING 587
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000305|PubMed:26741168,
FT ECO:0000305|PubMed:27214403, ECO:0000305|PubMed:28262558"
FT MOD_RES 832
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q80Y84"
FT MOD_RES 986
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 148
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 204
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 209
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 242
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 274
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 278
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 769
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 1450
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 237
FT /note="E -> ERQSLAVLPRLECSGAILAHCNLRLLDSSNSSASASQ (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:10616211"
FT /id="VSP_026408"
FT VARIANT 299..1544
FT /note="Missing (in MRT65)"
FT /evidence="ECO:0000269|PubMed:29276005"
FT /id="VAR_081276"
FT VARIANT 1370..1544
FT /note="Missing (in MRT65)"
FT /evidence="ECO:0000269|PubMed:29276005"
FT /id="VAR_081277"
FT MUTAGEN 308
FT /note="D->A: Slightly decreases interaction with histone
FT H3. Decreases by 21% demethylase activity and repression of
FT tumor suppressor genes expression."
FT /evidence="ECO:0000269|PubMed:24952722"
FT MUTAGEN 309
FT /note="L->A: No effect on interaction with histone H3."
FT /evidence="ECO:0000269|PubMed:24952722"
FT MUTAGEN 310
FT /note="Y->A: Slightly decreases interaction with histone
FT H3."
FT /evidence="ECO:0000269|PubMed:24952722"
FT MUTAGEN 310
FT /note="Y->F: No effect on interaction with histone H3."
FT /evidence="ECO:0000269|PubMed:24952722"
FT MUTAGEN 311
FT /note="V->A: No effect on interaction with histone H3."
FT /evidence="ECO:0000269|PubMed:24952722"
FT MUTAGEN 321
FT /note="E->A: Decreases interaction with histone H3."
FT /evidence="ECO:0000269|PubMed:24952722"
FT MUTAGEN 322
FT /note="D->A: No effect on interaction with histone H3."
FT /evidence="ECO:0000269|PubMed:24952722"
FT MUTAGEN 324
FT /note="L->A: No effect on interaction with histone H3."
FT /evidence="ECO:0000269|PubMed:24952722"
FT MUTAGEN 325
FT /note="L->A: Abolishes interaction with histone H3.
FT Decreases by 44% demethylase activity and repression of
FT tumor suppressor genes expression; when associated with A-
FT 328."
FT /evidence="ECO:0000269|PubMed:24952722"
FT MUTAGEN 326
FT /note="L->A: No effect on interaction with histone H3."
FT /evidence="ECO:0000269|PubMed:24952722"
FT MUTAGEN 328
FT /note="D->A: Almost abolishes interaction with histone H3.
FT Decreases by 44% demethylase activity and repression of
FT tumor suppressor genes expression; when associated with A-
FT 325."
FT /evidence="ECO:0000269|PubMed:24952722"
FT MUTAGEN 332
FT /note="D->A: No effect on interaction with histone H3."
FT /evidence="ECO:0000269|PubMed:24952722"
FT MUTAGEN 333
FT /note="S->A: No effect on interaction with histone H3."
FT /evidence="ECO:0000269|PubMed:24952722"
FT MUTAGEN 334
FT /note="Y->A: No effect on interaction with histone H3."
FT /evidence="ECO:0000269|PubMed:24952722"
FT MUTAGEN 335
FT /note="H->A: Slightly impairs transcription repression
FT ability."
FT /evidence="ECO:0000269|PubMed:17373667"
FT MUTAGEN 345
FT /note="D->A: No effect on interaction with histone H3."
FT /evidence="ECO:0000269|PubMed:24952722"
FT MUTAGEN 351
FT /note="W->A: Abolishes interaction with histone H3.
FT Decreases by 28% demethylase activity and repression of
FT tumor suppressor genes expression."
FT /evidence="ECO:0000269|PubMed:24952722"
FT MUTAGEN 499..501
FT /note="HIE->AIA: Abolishes lysine-specific histone
FT demethylase activity."
FT /evidence="ECO:0000269|PubMed:28262558"
FT MUTAGEN 499
FT /note="H->Y: Abolishes lysine-specific histone demethylase
FT activity."
FT /evidence="ECO:0000269|PubMed:17363312"
FT MUTAGEN 1200
FT /note="H->A: Impairs transcription repression ability and
FT interaction with HDAC4."
FT /evidence="ECO:0000269|PubMed:17373667"
FT CONFLICT 78
FT /note="V -> G (in Ref. 3; CAB63108)"
FT /evidence="ECO:0000305"
FT CONFLICT 585..589
FT /note="AYHSG -> VPQW (in Ref. 2; AAD16061)"
FT /evidence="ECO:0000305"
FT CONFLICT 708
FT /note="C -> W (in Ref. 2; AAD16061)"
FT /evidence="ECO:0000305"
FT CONFLICT 759
FT /note="A -> P (in Ref. 2; AAD16061)"
FT /evidence="ECO:0000305"
FT CONFLICT 771
FT /note="N -> T (in Ref. 2; AAD16061 and 3; CAB63108)"
FT /evidence="ECO:0000305"
FT CONFLICT 1182
FT /note="Q -> R (in Ref. 2; AAD16061)"
FT /evidence="ECO:0000305"
FT CONFLICT 1293
FT /note="A -> P (in Ref. 2; AAD16061)"
FT /evidence="ECO:0000305"
FT CONFLICT 1307
FT /note="P -> L (in Ref. 2; AAD16061)"
FT /evidence="ECO:0000305"
FT CONFLICT 1331
FT /note="S -> ST (in Ref. 2; AAD16061)"
FT /evidence="ECO:0000305"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:5FYZ"
FT HELIX 45..56
FT /evidence="ECO:0007829|PDB:5FYZ"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:5FYZ"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:5FYZ"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:5FYZ"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:5FYZ"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:6EIU"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:2MNY"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:2MNZ"
FT HELIX 319..323
FT /evidence="ECO:0007829|PDB:2MNY"
FT STRAND 324..326
FT /evidence="ECO:0007829|PDB:2MNY"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:2MNY"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:2MNY"
FT TURN 336..339
FT /evidence="ECO:0007829|PDB:2MNY"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:6EK6"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:6EK6"
FT HELIX 379..394
FT /evidence="ECO:0007829|PDB:5FYZ"
FT HELIX 398..400
FT /evidence="ECO:0007829|PDB:5FYZ"
FT HELIX 403..415
FT /evidence="ECO:0007829|PDB:5FYZ"
FT STRAND 422..429
FT /evidence="ECO:0007829|PDB:5FYZ"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:5FYT"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:5A3N"
FT HELIX 449..454
FT /evidence="ECO:0007829|PDB:5FYZ"
FT STRAND 458..460
FT /evidence="ECO:0007829|PDB:5FZ7"
FT TURN 461..466
FT /evidence="ECO:0007829|PDB:5FYZ"
FT STRAND 467..469
FT /evidence="ECO:0007829|PDB:5A3P"
FT HELIX 472..474
FT /evidence="ECO:0007829|PDB:5FYZ"
FT HELIX 480..483
FT /evidence="ECO:0007829|PDB:5FYZ"
FT STRAND 486..490
FT /evidence="ECO:0007829|PDB:5FYZ"
FT STRAND 495..499
FT /evidence="ECO:0007829|PDB:5FYZ"
FT HELIX 502..504
FT /evidence="ECO:0007829|PDB:5FYZ"
FT STRAND 506..515
FT /evidence="ECO:0007829|PDB:5FYZ"
FT STRAND 517..521
FT /evidence="ECO:0007829|PDB:5FYZ"
FT HELIX 524..526
FT /evidence="ECO:0007829|PDB:5FYZ"
FT HELIX 527..537
FT /evidence="ECO:0007829|PDB:5FYZ"
FT HELIX 539..542
FT /evidence="ECO:0007829|PDB:5FYZ"
FT HELIX 548..550
FT /evidence="ECO:0007829|PDB:5FYZ"
FT STRAND 552..554
FT /evidence="ECO:0007829|PDB:5FZG"
FT HELIX 558..563
FT /evidence="ECO:0007829|PDB:5FYZ"
FT STRAND 569..573
FT /evidence="ECO:0007829|PDB:5FYZ"
FT STRAND 578..581
FT /evidence="ECO:0007829|PDB:5FYZ"
FT STRAND 587..602
FT /evidence="ECO:0007829|PDB:5FYZ"
FT HELIX 605..607
FT /evidence="ECO:0007829|PDB:5FYZ"
FT HELIX 608..621
FT /evidence="ECO:0007829|PDB:5FYZ"
FT HELIX 629..637
FT /evidence="ECO:0007829|PDB:5FYZ"
FT HELIX 638..642
FT /evidence="ECO:0007829|PDB:5FYZ"
FT HELIX 645..671
FT /evidence="ECO:0007829|PDB:5FYZ"
FT STRAND 676..679
FT /evidence="ECO:0007829|PDB:5FYZ"
FT HELIX 682..684
FT /evidence="ECO:0007829|PDB:5FYZ"
FT HELIX 687..689
FT /evidence="ECO:0007829|PDB:5FYZ"
FT STRAND 690..692
FT /evidence="ECO:0007829|PDB:5FYZ"
FT TURN 693..695
FT /evidence="ECO:0007829|PDB:5FYZ"
FT STRAND 701..706
FT /evidence="ECO:0007829|PDB:5FYZ"
FT HELIX 719..721
FT /evidence="ECO:0007829|PDB:5FYZ"
FT HELIX 727..729
FT /evidence="ECO:0007829|PDB:5FYZ"
FT STRAND 730..735
FT /evidence="ECO:0007829|PDB:5FYZ"
FT HELIX 738..752
FT /evidence="ECO:0007829|PDB:5FYZ"
FT STRAND 1495..1500
FT /evidence="ECO:0007829|PDB:2MA5"
FT STRAND 1502..1505
FT /evidence="ECO:0007829|PDB:2MA5"
FT TURN 1506..1509
FT /evidence="ECO:0007829|PDB:2MA5"
FT STRAND 1511..1514
FT /evidence="ECO:0007829|PDB:2MA5"
FT HELIX 1515..1518
FT /evidence="ECO:0007829|PDB:2MA5"
FT HELIX 1522..1526
FT /evidence="ECO:0007829|PDB:2MA5"
FT HELIX 1533..1537
FT /evidence="ECO:0007829|PDB:2MA5"
SQ SEQUENCE 1544 AA; 175658 MW; 70A0738D9A709F61 CRC64;
MEAATTLHPG PRPALPLGGP GPLGEFLPPP ECPVFEPSWE EFADPFAFIH KIRPIAEQTG
ICKVRPPPDW QPPFACDVDK LHFTPRIQRL NELEAQTRVK LNFLDQIAKY WELQGSTLKI
PHVERKILDL FQLNKLVAEE GGFAVVCKDR KWTKIATKMG FAPGKAVGSH IRGHYERILN
PYNLFLSGDS LRCLQKPNLT TDTKDKEYKP HDIPQRQSVQ PSETCPPARR AKRMRAEAMN
IKIEPEETTE ARTHNLRRRM GCPTPKCENE KEMKSSIKQE PIERKDYIVE NEKEKPKSRS
KKATNAVDLY VCLLCGSGND EDRLLLCDGC DDSYHTFCLI PPLHDVPKGD WRCPKCLAQE
CSKPQEAFGF EQAARDYTLR TFGEMADAFK SDYFNMPVHM VPTELVEKEF WRLVSTIEED
VTVEYGADIA SKEFGSGFPV RDGKIKLSPE EEEYLDSGWN LNNMPVMEQS VLAHITADIC
GMKLPWLYVG MCFSSFCWHI EDHWSYSINY LHWGEPKTWY GVPGYAAEQL ENVMKKLAPE
LFVSQPDLLH QLVTIMNPNT LMTHEVPVYR TNQCAGEFVI TFPRAYHSGF NQGFNFAEAV
NFCTVDWLPL GRQCVEHYRL LHRYCVFSHD EMICKMASKA DVLDVVVAST VQKDMAIMIE
DEKALRETVR KLGVIDSERM DFELLPDDER QCVKCKTTCF MSAISCSCKP GLLVCLHHVK
ELCSCPPYKY KLRYRYTLDD LYPMMNALKL RAESYNEWAL NVNEALEAKI NKKKSLVSFK
ALIEESEMKK FPDNDLLRHL RLVTQDAEKC ASVAQQLLNG KRQTRYRSGG GKSQNQLTVN
ELRQFVTQLY ALPCVLSQTP LLKDLLNRVE DFQQHSQKLL SEETPSAAEL QDLLDVSFEF
DVELPQLAEM RIRLEQARWL EEVQQACLDP SSLTLDDMRR LIDLGVGLAP YSAVEKAMAR
LQELLTVSEH WDDKAKSLLK ARPRHSLNSL ATAVKEIEEI PAYLPNGAAL KDSVQRARDW
LQDVEGLQAG GRVPVLDTLI ELVTRGRSIP VHLNSLPRLE TLVAEVQAWK ECAVNTFLTE
NSPYSLLEVL CPRCDIGLLG LKRKQRKLKE PLPNGKKKST KLESLSDLER ALTESKETAS
AMATLGEARL REMEALQSLR LANEGKLLSP LQDVDIKICL CQKAPAAPMI QCELCRDAFH
TSCVAVPSIS QGLRIWLCPH CRRSEKPPLE KILPLLASLQ RIRVRLPEGD ALRYMIERTV
NWQHRAQQLL SSGNLKFVQD RVGSGLLYSR WQASAGQVSD TNKVSQPPGT TSFSLPDDWD
NRTSYLHSPF STGRSCIPLH GVSPEVNELL MEAQLLQVSL PEIQELYQTL LAKPSPAQQT
DRSSPVRPSS EKNDCCRGKR DGINSLERKL KRRLEREGLS SERWERVKKM RTPKKKKIKL
SHPKDMNNFK LERERSYELV RSAETHSLPS DTSYSEQEDS EDEDAICPAV SCLQPEGDEV
DWVQCDGSCN QWFHQVCVGV SPEMAEKEDY ICVRCTVKDA PSRK
//
