ID   KDM5B_MOUSE             Reviewed;        1544 AA.
AC   Q80Y84; Q5DTR9; Q8BLU1; Q8JZL8;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   24-JAN-2024, entry version 159.
DE   RecName: Full=Lysine-specific demethylase 5B;
DE            EC=1.14.11.67 {ECO:0000269|PubMed:17310255};
DE   AltName: Full=Histone demethylase JARID1B;
DE   AltName: Full=Jumonji/ARID domain-containing protein 1B;
DE   AltName: Full=PLU-1;
DE   AltName: Full=[histone H3]-trimethyl-L-lysine(4) demethylase 5B {ECO:0000305};
GN   Name=Kdm5b; Synonyms=Jarid1b, Kiaa4034, Plu1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RC   STRAIN=BALB/cJ; TISSUE=Testis;
RX   PubMed=14516692; DOI=10.1016/s0925-4773(03)00123-0;
RA   Madsen B., Spencer-Dene B., Poulsom R., Hall D., Lu P.J., Scott K.,
RA   Shaw A.T., Burchell J.M., Freemont P., Taylor-Papadimitriou J.;
RT   "Characterisation and developmental expression of mouse Plu-1, a homologue
RT   of a human nuclear protein (PLU-1) which is specifically up-regulated in
RT   breast cancer.";
RL   Mech. Dev. 119:S239-S246(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT   complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT   screening of terminal sequences of cDNA clones randomly sampled from size-
RT   fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1433.
RC   STRAIN=C57BL/6J; TISSUE=Aorta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   TISSUE SPECIFICITY.
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   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=14579128; DOI=10.1007/s00412-003-0252-6;
RA   Madsen B., Tarsounas M., Burchell J.M., Hall D., Poulsom R.,
RA   Taylor-Papadimitriou J.;
RT   "PLU-1, a transcriptional repressor and putative testis-cancer antigen, has
RT   a specific expression and localisation pattern during meiosis.";
RL   Chromosoma 112:124-132(2003).
RN   [7]
RP   FUNCTION.
RX   PubMed=17320160; DOI=10.1016/j.cell.2007.02.017;
RA   Iwase S., Lan F., Bayliss P., de la Torre-Ubieta L., Huarte M., Qi H.H.,
RA   Whetstine J.R., Bonni A., Roberts T.M., Shi Y.;
RT   "The X-linked mental retardation gene SMCX/JARID1C defines a family of
RT   histone H3 lysine 4 demethylases.";
RL   Cell 128:1077-1088(2007).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF HIS-499.
RX   PubMed=17310255; DOI=10.1038/nsmb1200;
RA   Seward D.J., Cubberley G., Kim S., Schonewald M., Zhang L., Tripet B.,
RA   Bentley D.L.;
RT   "Demethylation of trimethylated histone H3 Lys4 in vivo by JARID1 JmjC
RT   proteins.";
RL   Nat. Struct. Mol. Biol. 14:240-242(2007).
RN   [9]
RP   FUNCTION.
RX   PubMed=21960634; DOI=10.1126/science.1206022;
RA   DiTacchio L., Le H.D., Vollmers C., Hatori M., Witcher M., Secombe J.,
RA   Panda S.;
RT   "Histone lysine demethylase JARID1a activates CLOCK-BMAL1 and influences
RT   the circadian clock.";
RL   Science 333:1881-1885(2011).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-832, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [11]
RP   DISRUPTION PHENOTYPE.
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).
CC   -!- FUNCTION: Histone demethylase that demethylates 'Lys-4' of histone H3,
CC       thereby playing a central role in histone code. Does not demethylate
CC       histone H3 'Lys-9' or H3 'Lys-27'. Demethylates trimethylated,
CC       dimethylated and monomethylated H3 'Lys-4'. Acts as a transcriptional
CC       corepressor for FOXG1B and PAX9. Represses the CLOCK-BMAL1 heterodimer-
CC       mediated transcriptional activation of the core clock component PER2.
CC       {ECO:0000269|PubMed:17310255, ECO:0000269|PubMed:17320160,
CC       ECO:0000269|PubMed:21960634}.
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:0000269|PubMed:17310255};
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   -!- 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' (By similarity).
CC       {ECO:0000250|UniProtKB:Q9UGL1}.
CC   -!- INTERACTION:
CC       Q80Y84; P60762: Morf4l1; NbExp=4; IntAct=EBI-1249551, EBI-2943018;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355,
CC       ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000269|PubMed:14579128}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q80Y84-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q80Y84-2; Sequence=VSP_026409;
CC   -!- TISSUE SPECIFICITY: Present at highest levels in testis, where it is
CC       enriched in spermatogonia and pachytene cells (at protein level).
CC       {ECO:0000269|PubMed:12237901, ECO:0000269|PubMed:14516692,
CC       ECO:0000269|PubMed:14579128}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in developing brain, mammary bud,
CC       thymus, teeth, whisker follicle, intervertebral disks, olfactory
CC       epithelium, eye, stomach and limbs. {ECO:0000269|PubMed:14516692}.
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:0000250|UniProtKB:Q9UGL1}.
CC   -!- DOMAIN: The 2 first PHD-type zinc finger domains are required for
CC       transcription repression activity. {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: Homozygous KDM5B-null mice are subviable, exhibit
CC       vertebral patterning defects, and manifest numerous behavioral
CC       abnormalities including increased anxiety, less sociability, and
CC       reduced long-term memory compared with that of wild-types. Heterozygous
CC       mice appear normal. {ECO:0000269|PubMed:30409806}.
CC   -!- SIMILARITY: Belongs to the JARID1 histone demethylase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90482.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY082429; AAL92848.1; -; mRNA.
DR   EMBL; AY082430; AAL92849.1; -; mRNA.
DR   EMBL; AK220451; BAD90482.1; ALT_INIT; mRNA.
DR   EMBL; BC048180; AAH48180.1; -; mRNA.
DR   EMBL; BC057318; AAH57318.1; -; mRNA.
DR   EMBL; AK041304; BAC30898.1; -; mRNA.
DR   CCDS; CCDS35716.1; -. [Q80Y84-1]
DR   RefSeq; NP_690855.2; NM_152895.2. [Q80Y84-1]
DR   PDB; 2EQY; NMR; -; A=94-208.
DR   PDBsum; 2EQY; -.
DR   AlphaFoldDB; Q80Y84; -.
DR   BMRB; Q80Y84; -.
DR   SMR; Q80Y84; -.
DR   BioGRID; 217610; 11.
DR   IntAct; Q80Y84; 4.
DR   MINT; Q80Y84; -.
DR   STRING; 10090.ENSMUSP00000038138; -.
DR   iPTMnet; Q80Y84; -.
DR   PhosphoSitePlus; Q80Y84; -.
DR   EPD; Q80Y84; -.
DR   MaxQB; Q80Y84; -.
DR   PaxDb; 10090-ENSMUSP00000038138; -.
DR   PeptideAtlas; Q80Y84; -.
DR   ProteomicsDB; 263427; -. [Q80Y84-1]
DR   ProteomicsDB; 263428; -. [Q80Y84-2]
DR   Pumba; Q80Y84; -.
DR   Antibodypedia; 20655; 446 antibodies from 33 providers.
DR   DNASU; 75605; -.
DR   Ensembl; ENSMUST00000047714.14; ENSMUSP00000038138.8; ENSMUSG00000042207.18. [Q80Y84-1]
DR   Ensembl; ENSMUST00000112198.3; ENSMUSP00000107817.2; ENSMUSG00000042207.18. [Q80Y84-2]
DR   GeneID; 75605; -.
DR   KEGG; mmu:75605; -.
DR   UCSC; uc007csg.2; mouse. [Q80Y84-2]
DR   UCSC; uc011wsg.1; mouse. [Q80Y84-1]
DR   AGR; MGI:1922855; -.
DR   CTD; 10765; -.
DR   MGI; MGI:1922855; Kdm5b.
DR   VEuPathDB; HostDB:ENSMUSG00000042207; -.
DR   eggNOG; KOG1246; Eukaryota.
DR   GeneTree; ENSGT00940000157076; -.
DR   HOGENOM; CLU_000991_2_2_1; -.
DR   InParanoid; Q80Y84; -.
DR   OMA; PRCDIGM; -.
DR   OrthoDB; 48111at2759; -.
DR   PhylomeDB; Q80Y84; -.
DR   TreeFam; TF106476; -.
DR   Reactome; R-MMU-3214842; HDMs demethylate histones.
DR   Reactome; R-MMU-8866911; TFAP2 (AP-2) family regulates transcription of cell cycle factors.
DR   BioGRID-ORCS; 75605; 4 hits in 84 CRISPR screens.
DR   ChiTaRS; Kdm5b; mouse.
DR   EvolutionaryTrace; Q80Y84; -.
DR   PRO; PR:Q80Y84; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q80Y84; Protein.
DR   Bgee; ENSMUSG00000042207; Expressed in rostral migratory stream and 280 other cell types or tissues.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0003677; F:DNA binding; ISO:MGI.
DR   GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR   GO; GO:0032453; F:histone H3K4 demethylase activity; IDA:MGI.
DR   GO; GO:0034647; F:histone H3K4me/H3K4me2/H3K4me3 demethylase activity; ISS:UniProtKB.
DR   GO; GO:0003676; F:nucleic acid binding; ISO:MGI.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0003714; F:transcription corepressor activity; ISO:MGI.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; IMP:MGI.
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; IEP:MGI.
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; IMP:MGI.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; IGI:MGI.
DR   GO; GO:0033601; P:positive regulation of mammary gland epithelial cell proliferation; IMP:MGI.
DR   GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR   GO; GO:0042752; P:regulation of circadian rhythm; NAS:UniProtKB.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR   GO; GO:2000864; P:regulation of estradiol secretion; IMP:MGI.
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; IMP:MGI.
DR   GO; GO:0061038; P:uterus morphogenesis; IMP:MGI.
DR   CDD; cd16874; ARID_KDM5B; 1.
DR   CDD; cd15603; PHD1_KDM5B; 1.
DR   CDD; cd15687; PHD3_KDM5B; 1.
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); 3.
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.
DR   Genevisible; Q80Y84; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; Biological rhythms;
KW   Chromatin regulator; Dioxygenase; Iron; Isopeptide bond; Metal-binding;
KW   Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome; Repeat;
KW   Repressor; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..1544
FT                   /note="Lysine-specific demethylase 5B"
FT                   /id="PRO_0000292413"
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:0000255|PROSITE-ProRule:PRU00146"
FT   ZN_FING         692..744
FT                   /note="C5HC2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGL1"
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:0000255|PROSITE-ProRule:PRU00146"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          200..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          269..297
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1297..1318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1374..1447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1374..1391
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1392..1429
FT                   /note="Basic and acidic 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:0000255|PROSITE-ProRule:PRU00538"
FT   BINDING         501
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P29375"
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:0000255|PROSITE-ProRule:PRU00538"
FT   MOD_RES         832
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         986
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGL1"
FT   MOD_RES         1328
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGL1"
FT   MOD_RES         1456
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGL1"
FT   CROSSLNK        148
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGL1"
FT   CROSSLNK        204
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGL1"
FT   CROSSLNK        209
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGL1"
FT   CROSSLNK        242
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGL1"
FT   CROSSLNK        274
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGL1"
FT   CROSSLNK        278
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGL1"
FT   CROSSLNK        769
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGL1"
FT   CROSSLNK        1450
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UGL1"
FT   VAR_SEQ         1501..1544
FT                   /note="DWVQCDGSCNQWFHQVCVGVSPEMAEKEDYICVRCTGKDAPSRK -> SEVW
FT                   AIEDALSPNSETL (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_026409"
FT   MUTAGEN         499
FT                   /note="H->A: Abolishes enzymatic activity."
FT                   /evidence="ECO:0000269|PubMed:17310255"
FT   CONFLICT        28
FT                   /note="P -> S (in Ref. 2; BAD90482)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        139
FT                   /note="E -> Q (in Ref. 4; BAC30898)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        761
FT                   /note="N -> Y (in Ref. 1; AAL92848/AAL92849)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1428
FT                   /note="K -> R (in Ref. 1; AAL92848/AAL92849)"
FT                   /evidence="ECO:0000305"
FT   HELIX           97..114
FT                   /evidence="ECO:0007829|PDB:2EQY"
FT   STRAND          122..127
FT                   /evidence="ECO:0007829|PDB:2EQY"
FT   HELIX           130..140
FT                   /evidence="ECO:0007829|PDB:2EQY"
FT   HELIX           143..148
FT                   /evidence="ECO:0007829|PDB:2EQY"
FT   TURN            149..151
FT                   /evidence="ECO:0007829|PDB:2EQY"
FT   HELIX           152..158
FT                   /evidence="ECO:0007829|PDB:2EQY"
FT   STRAND          163..165
FT                   /evidence="ECO:0007829|PDB:2EQY"
FT   HELIX           166..177
FT                   /evidence="ECO:0007829|PDB:2EQY"
FT   HELIX           179..187
FT                   /evidence="ECO:0007829|PDB:2EQY"
SQ   SEQUENCE   1544 AA;  175555 MW;  D83E2691C65DCB31 CRC64;
     MEPATTLPPG PRPALPLGGP GPLGEFLPPP ECPVFEPSWE EFADPFAFIH KIRPIAEQTG
     ICKVRPPPDW QPPFACDVDK LHFTPRIQRL NELEAQTRVK LNFLDQIAKY WELQGSTLKI
     PHVERKILDL FQLNKLVAEE GGFAVVCKDR KWTKIATKMG FAPGKAVGSH IRGHYERILN
     PYNLFLSGDS LRCLQKPNLT SDTKDKEYKP HDIPQRQSVQ PAETCPPARR AKRMRAEAMN
     IKIEPEEATE ARTHNLRRRM GCTTPKWENE KEMKSTIKQE PTEKKDCELE SEKEKPKSRA
     KKTATAVDLY VCLLCGSGND EDRLLLCDGC DDSYHTFCLV PPLHDVPKGD WRCPKCLAQE
     CNKPQEAFGF EQAARDYTLR TFGEMADAFK SDYFNMPVHM VPTELVEKEF WRLVSTIEED
     VTVEYGADIA SKEFGSGFPV RDGKIKISPE EEEYLDSGWN LNNMPVMEQS VLAHITADIC
     GMKLPWLYVG MCFSSFCWHI EDHWSYSINY LHWGEPKTWY GVPGYAAEQL ENVMKKLAPE
     LFVSQPDLLH QLVTIMNPNT LMTHEVPVYR TNQCAGEFVI TFPRAYHSGF NQGFNFAEAV
     NFCTVDWLPL GRQCVEHYRL LHRYCVFSHD EMICKMASKA DVLDVVVAST VQKDMAIMIE
     DEKALRETVR KLGVIDSERM DFELLPDDER QCIKCKTTCF MSAISCSCKP GLLVCLHHVK
     ELCSCPPYKY NLRYRYTLDD LYPMMNALKL RAESYNEWAL NVNEALEAKI NKKKSLVSFK
     ALIEESEMKK FPDNDLLRHL RLVTQDAEKC ASVAQQLLNG KRQTRYRSGG GKSQNQLTVN
     ELRQFVTQLY ALPCVLSQTP LLKDLLNRVE DFQQQSQKLL SEEMPSAAEL QELLDVSFEF
     DVELPQLTEM RIRLEQARWL EEVQQACLDS SSLSLDDMRR LIDLGVGLAP YSAVEKAMAR
     LQELLTVSEH WDDKAKSLLR ARPRHSLSSL ATAVKEMEEI PAYLPNGTVL KDSVQRARDW
     VQDVDALQAG GRVPVLETLI ELVARGRSIP VHLNSLPRLE MLVAEVHAWK ECAAKTFLPE
     NSTYSLLEVL CPRCDIGLLG LKRKQRKLKE PLPSGKKRST KLESLSDLER ALMESKETAA
     AMATLGEARL REMEALQSLR FANEEKLLSP VQDLEMKVCL CQKTPATPMI QCELCRDAFH
     TSCVAAPSIS QSSRIWLCPH CRRSEKPPLE KILPLLASLQ RIRVRLPEGD ALRYMIERTV
     NWQHRAQQLL SSGNLKLVQD QVGSGLLSSR WPASAGQASA TDKVSQPPGT TSFSLPDDWD
     NRTSYLHSPF STGQSCLPLH GLSPEVNELL MEAQLLQVSL PEIQELYQTL LTKPSSVQQA
     DRSSPVRSSS EKNDCLRGKR DAINSPERKL KRRPEREGLP SERWDRVKHM RTPQKKKIKL
     SHPKDMDSFK LERERSYDLV RNAETHSLPS DTSYSEQEDS EDEDAICPAV SCLQPEGDEV
     DWVQCDGSCN QWFHQVCVGV SPEMAEKEDY ICVRCTGKDA PSRK
//