KDM5B_MOUSE
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 03-AUG-2022, entry version 151.
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-ARNTL/BMAL1
CC heterodimer-mediated transcriptional activation of the core clock
CC component PER2. {ECO:0000269|PubMed:17310255,
CC ECO:0000269|PubMed:17320160, 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; 10.
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; Q80Y84; -.
DR PeptideAtlas; Q80Y84; -.
DR PRIDE; Q80Y84; -.
DR ProteomicsDB; 263427; -. [Q80Y84-1]
DR ProteomicsDB; 263428; -. [Q80Y84-2]
DR Antibodypedia; 20655; 392 antibodies from 33 providers.
DR DNASU; 75605; -.
DR Ensembl; ENSMUST00000047714; ENSMUSP00000038138; ENSMUSG00000042207. [Q80Y84-1]
DR Ensembl; ENSMUST00000112198; ENSMUSP00000107817; ENSMUSG00000042207. [Q80Y84-2]
DR GeneID; 75605; -.
DR KEGG; mmu:75605; -.
DR UCSC; uc007csg.2; mouse. [Q80Y84-2]
DR UCSC; uc011wsg.1; mouse. [Q80Y84-1]
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; DGISYME; -.
DR OrthoDB; 664180at2759; -.
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; 2 hits in 78 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 277 other tissues.
DR Genevisible; Q80Y84; MM.
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:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0032453; F:histone H3-methyl-lysine-4 demethylase activity; IDA:MGI.
DR GO; GO:0034647; F:histone H3-tri/di/monomethyl-lysine-4 demethylase activity; ISS:UniProtKB.
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:0034720; P:histone H3-K4 demethylation; IDA:MGI.
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 transcription, DNA-templated; 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: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 Gene3D; 1.10.150.60; -; 1.
DR Gene3D; 3.30.40.10; -; 3.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
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 Pfam; PF01388; ARID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF00628; PHD; 3.
DR Pfam; PF08429; PLU-1; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 3.
DR SUPFAM; SSF46774; SSF46774; 1.
DR SUPFAM; SSF57903; SSF57903; 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; 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
