KDM2B_MOUSE
ID KDM2B_MOUSE Reviewed; 1309 AA.
AC Q6P1G2; Q3V396; Q6PFD0; Q6ZPE8; Q9CSF7; Q9QZN6;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Lysine-specific demethylase 2B;
DE EC=1.14.11.27 {ECO:0000250|UniProtKB:Q8NHM5};
DE AltName: Full=F-box and leucine-rich repeat protein 10;
DE AltName: Full=F-box protein FBL10;
DE AltName: Full=F-box/LRR-repeat protein 10;
DE AltName: Full=JmjC domain-containing histone demethylation protein 1B;
DE AltName: Full=[Histone-H3]-lysine-36 demethylase 1B;
GN Name=Kdm2b; Synonyms=Fbl10, Fbxl10, Jhdm1b, Kiaa3014;
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 [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Embryo;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 6-1309 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1011-1309 (ISOFORMS 1/2).
RX PubMed=10531037; DOI=10.1016/s0960-9822(00)80021-4;
RA Winston J.T., Koepp D.M., Zhu C., Elledge S.J., Harper J.W.;
RT "A family of mammalian F-box proteins.";
RL Curr. Biol. 9:1180-1182(1999).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Histone demethylase that demethylates 'Lys-4' and 'Lys-36' of
CC histone H3, thereby playing a central role in histone code.
CC Preferentially demethylates trimethylated H3 'Lys-4' and dimethylated
CC H3 'Lys-36' residue while it has weak or no activity for mono- and tri-
CC methylated H3 'Lys-36'. Preferentially binds the transcribed region of
CC ribosomal RNA and represses the transcription of ribosomal RNA genes
CC which inhibits cell growth and proliferation (By similarity). May also
CC serve as a substrate-recognition component of the SCF (SKP1-CUL1-F-box
CC protein)-type E3 ubiquitin ligase complex (By similarity).
CC {ECO:0000250|UniProtKB:Q8NHM5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3]
CC + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2
CC succinate; Xref=Rhea:RHEA:42032, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC COMP:9787, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031,
CC ChEBI:CHEBI:61976; EC=1.14.11.27;
CC Evidence={ECO:0000250|UniProtKB:Q8NHM5};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000250|UniProtKB:Q8NHM5};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9Y2K7};
CC -!- ACTIVITY REGULATION: Histone demethylase activity is inhibited by
CC fumarate. {ECO:0000250|UniProtKB:Q8NHM5}.
CC -!- SUBUNIT: Interacts with SKP1, forming heterodimers (By similarity). The
CC KDM2B-SKP1 heterodimeric complex interacts with the PCGF1-BCORL
CC heterodimeric complex to form a homotetrameric polycomb repression
CC complex 1 (PRC1.1) (By similarity). Directly interacts with CUL1. The
CC SKP1-KDM2B interacts with UBB (By similarity).
CC {ECO:0000250|UniProtKB:Q8NHM5, ECO:0000305}.
CC -!- INTERACTION:
CC Q6P1G2; Q9CQJ4: Rnf2; NbExp=4; IntAct=EBI-1216214, EBI-927321;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q8NHM5}. Nucleus {ECO:0000250|UniProtKB:Q8NHM5}.
CC Chromosome {ECO:0000250|UniProtKB:Q8NHM5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6P1G2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6P1G2-2; Sequence=VSP_011342, VSP_011343;
CC Name=3;
CC IsoId=Q6P1G2-3; Sequence=VSP_017477, VSP_017478;
CC Name=4;
CC IsoId=Q6P1G2-4; Sequence=VSP_019003;
CC -!- DOMAIN: The LRR repeats are required for the interaction with the
CC PCGF1-BCORL1 heterodimeric complex. {ECO:0000250|UniProtKB:Q8NHM5}.
CC -!- DOMAIN: The JmjC domain mediates demethylation activity (By
CC similarity). It is also required for repression of ribosomal RNA genes
CC (By similarity). {ECO:0000250|UniProtKB:Q8NHM5}.
CC -!- DOMAIN: The CXXC zinc finger mediates binding to DNA containing
CC unmethylated cytidine-phosphate-guanosine (CpG) dinucleotides.
CC {ECO:0000250|UniProtKB:Q8NHM5}.
CC -!- DOMAIN: The F-box domain mediates interaction with UBB.
CC {ECO:0000250|UniProtKB:Q8NHM5}.
CC -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family.
CC {ECO:0000305}.
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DR EMBL; AK012952; BAB28568.2; -; mRNA.
DR EMBL; AK043352; BAE20639.1; -; mRNA.
DR EMBL; BC057622; AAH57622.1; -; mRNA.
DR EMBL; BC065090; AAH65090.1; -; mRNA.
DR EMBL; AK129479; BAC98289.1; -; mRNA.
DR EMBL; AF176524; AAF09133.1; -; mRNA.
DR CCDS; CCDS19657.1; -. [Q6P1G2-2]
DR CCDS; CCDS39259.1; -. [Q6P1G2-1]
DR RefSeq; NP_001003953.1; NM_001003953.2. [Q6P1G2-1]
DR RefSeq; NP_038938.1; NM_013910.2. [Q6P1G2-2]
DR AlphaFoldDB; Q6P1G2; -.
DR SMR; Q6P1G2; -.
DR BioGRID; 205978; 21.
DR DIP; DIP-46351N; -.
DR IntAct; Q6P1G2; 11.
DR STRING; 10090.ENSMUSP00000038229; -.
DR iPTMnet; Q6P1G2; -.
DR PhosphoSitePlus; Q6P1G2; -.
DR EPD; Q6P1G2; -.
DR jPOST; Q6P1G2; -.
DR MaxQB; Q6P1G2; -.
DR PaxDb; Q6P1G2; -.
DR PeptideAtlas; Q6P1G2; -.
DR PRIDE; Q6P1G2; -.
DR ProteomicsDB; 263518; -. [Q6P1G2-1]
DR ProteomicsDB; 263519; -. [Q6P1G2-2]
DR ProteomicsDB; 263520; -. [Q6P1G2-3]
DR ProteomicsDB; 263521; -. [Q6P1G2-4]
DR Antibodypedia; 31579; 321 antibodies from 30 providers.
DR DNASU; 30841; -.
DR Ensembl; ENSMUST00000031435; ENSMUSP00000031435; ENSMUSG00000029475. [Q6P1G2-2]
DR Ensembl; ENSMUST00000046073; ENSMUSP00000038229; ENSMUSG00000029475. [Q6P1G2-1]
DR GeneID; 30841; -.
DR KEGG; mmu:30841; -.
DR UCSC; uc008zmq.2; mouse. [Q6P1G2-2]
DR UCSC; uc008zms.3; mouse. [Q6P1G2-1]
DR UCSC; uc008zmu.2; mouse. [Q6P1G2-3]
DR CTD; 84678; -.
DR MGI; MGI:1354737; Kdm2b.
DR VEuPathDB; HostDB:ENSMUSG00000029475; -.
DR eggNOG; KOG1633; Eukaryota.
DR eggNOG; KOG1947; Eukaryota.
DR GeneTree; ENSGT00940000154717; -.
DR HOGENOM; CLU_003540_0_2_1; -.
DR InParanoid; Q6P1G2; -.
DR OMA; LWKRMNC; -.
DR OrthoDB; 324938at2759; -.
DR PhylomeDB; Q6P1G2; -.
DR TreeFam; TF106480; -.
DR BRENDA; 1.14.11.27; 3474.
DR Reactome; R-MMU-3214842; HDMs demethylate histones.
DR BioGRID-ORCS; 30841; 2 hits in 80 CRISPR screens.
DR ChiTaRS; Kdm2b; mouse.
DR PRO; PR:Q6P1G2; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q6P1G2; protein.
DR Bgee; ENSMUSG00000029475; Expressed in animal zygote and 67 other tissues.
DR ExpressionAtlas; Q6P1G2; baseline and differential.
DR Genevisible; Q6P1G2; MM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0031519; C:PcG protein complex; ISO:MGI.
DR GO; GO:0032452; F:histone demethylase activity; IBA:GO_Central.
DR GO; GO:0140680; F:histone H3-di/monomethyl-lysine-36 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0051864; F:histone H3-methyl-lysine-36 demethylase activity; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0045322; F:unmethylated CpG binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IMP:BHF-UCL.
DR GO; GO:0030900; P:forebrain development; IMP:BHF-UCL.
DR GO; GO:0021592; P:fourth ventricle development; IMP:BHF-UCL.
DR GO; GO:0030902; P:hindbrain development; IMP:BHF-UCL.
DR GO; GO:0035518; P:histone H2A monoubiquitination; ISO:MGI.
DR GO; GO:0070544; P:histone H3-K36 demethylation; IDA:MGI.
DR GO; GO:0021993; P:initiation of neural tube closure; IMP:BHF-UCL.
DR GO; GO:0021670; P:lateral ventricle development; IMP:BHF-UCL.
DR GO; GO:0030901; P:midbrain development; IMP:BHF-UCL.
DR GO; GO:0021555; P:midbrain-hindbrain boundary morphogenesis; IMP:BHF-UCL.
DR GO; GO:2000178; P:negative regulation of neural precursor cell proliferation; IMP:BHF-UCL.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0030307; P:positive regulation of cell growth; IDA:MGI.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IDA:MGI.
DR GO; GO:0006482; P:protein demethylation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IMP:BHF-UCL.
DR GO; GO:0021678; P:third ventricle development; IMP:BHF-UCL.
DR Gene3D; 3.30.40.10; -; 1.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR041070; JHD.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR006553; Leu-rich_rpt_Cys-con_subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR002857; Znf_CXXC.
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; PF00646; F-box; 1.
DR Pfam; PF17811; JHD; 1.
DR Pfam; PF16866; PHD_4; 1.
DR Pfam; PF02008; zf-CXXC; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00367; LRR_CC; 5.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51058; ZF_CXXC; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Chromosome; Coiled coil;
KW Dioxygenase; DNA-binding; Iron; Isopeptide bond; Leucine-rich repeat;
KW Metal-binding; Nucleus; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; RNA-binding; rRNA-binding; Transcription;
KW Transcription regulation; Ubl conjugation; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..1309
FT /note="Lysine-specific demethylase 2B"
FT /id="PRO_0000119854"
FT DOMAIN 147..315
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT DOMAIN 1032..1078
FT /note="F-box"
FT REPEAT 1106..1127
FT /note="LRR 1"
FT REPEAT 1129..1155
FT /note="LRR 2"
FT REPEAT 1195..1220
FT /note="LRR 3"
FT REPEAT 1221..1250
FT /note="LRR 4"
FT REPEAT 1251..1275
FT /note="LRR 5"
FT REPEAT 1276..1309
FT /note="LRR 6"
FT ZN_FING 579..625
FT /note="CXXC-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT ZN_FING 632..698
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 378..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..1005
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 916..944
FT /evidence="ECO:0000255"
FT COMPBIAS 378..402
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 724..787
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 841..879
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..936
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..976
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 208
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 213
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 586
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 589
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 592
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 597
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 600
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 603
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 619
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 624
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00509"
FT BINDING 635
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8NHM5"
FT BINDING 638
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8NHM5"
FT BINDING 661
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8NHM5"
FT BINDING 664
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8NHM5"
FT BINDING 669
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8NHM5"
FT BINDING 672
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8NHM5"
FT BINDING 692
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8NHM5"
FT BINDING 695
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8NHM5"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NHM5"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NHM5"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NHM5"
FT MOD_RES 466
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NHM5"
FT MOD_RES 470
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NHM5"
FT MOD_RES 924
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NHM5"
FT MOD_RES 948
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NHM5"
FT MOD_RES 952
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NHM5"
FT MOD_RES 991
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NHM5"
FT MOD_RES 1004
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NHM5"
FT CROSSLNK 830
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NHM5"
FT CROSSLNK 863
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8NHM5"
FT VAR_SEQ 1..533
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011342"
FT VAR_SEQ 2..1196
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_019003"
FT VAR_SEQ 534..551
FT /note="TLAITGVPVVSWPKKTAK -> MAMSVSAEDDDYESEPDQ (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011343"
FT VAR_SEQ 627..656
FT /note="PVLPHTAVCLVCGEAGKEDTVEEEEGKFNL -> VSAQKAQAGLMQGLPAIC
FT PALGLLCGMGEV (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017477"
FT VAR_SEQ 657..1309
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_017478"
FT CONFLICT 461
FT /note="T -> M (in Ref. 3; BAC98289)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1309 AA; 149733 MW; 5BD203C3535C4D88 CRC64;
MEAEKDSGRR LRAIDRQRYD ENEDLSDVEE IVSVRGFSLE EKLRSQLYQG DFVHAMEGKD
FNYEYVQREA LRVPLVFRDK DGLGIKMPDP DFTVRDVKLL VGSRRLVDVM DVNTQKGTEM
SMSQFVRYYE TPEAQRDKLY NVISLEFSHT KLEHLVKRPT VVDLVDWVDN MWPQHLKEKQ
TEATNALAEM KYPKVKKYCL MSVKGCFTDF HIDFGGTSVW YHVFRGGKIF WLIPPTLHNL
ALYEEWVLSG KQSDIFLGDR VERCQRIELK QGYTFFIPSG WIHAVYTPVD SLVFGGNILH
SFNVPMQLRI YEIEDRTRVQ PKFRYPFYYE MCWYVLERYV YCVTQRSYLT QEYQRELMLI
DAPRKTSVDG FSSDSWLDME EESCEQQPQE EEEEEEDKEE EGDGADKTPK PPTDDPTSPT
STPPEDQDST GKKPKAPAIR FLKRTLSNES EESVKSTSMP TDDPKTPTGS PATEVSTKWT
HLTEFELKGL KALVEKLESL PENKKCVPEG IEDPQALLEG VKNVLKEHVD DDPTLAITGV
PVVSWPKKTA KNRVVGRPKG KLGPASAVKL AANRTTAGAR RRRTRCRKCE ACLRTECGEC
HFCKDMKKFG GPGRMKQSCI MRQCIAPVLP HTAVCLVCGE AGKEDTVEEE EGKFNLMLME
CSICNEIIHP GCLKIKESEG VVNDELPNCW ECPKCNHAGK TGKQKRGPGF KYASNLPGSL
LKEQKMNRDN KEGQEPAKRR SECEEAPRRR SDEHPKKVPA DGILRRKSDD VHLRRKRKYE
KPQELSGRKR ASSLQTSPGS SSHLSPRPPL GSSLSPWWRS SLTYFQQQLK PGKEDKLFRK
KRRSWKNAED RLSLANKPLR RFKQEPEDDL PEAPPKTRES DQSRSSSPTA GPSTEGAEGP
EEKKKVKMRR KRRLVNKELS KELSKELNHE IQKTESTLAH ESQQPIKSEP ESENDEPKRP
LSHCERPHRF SKGLNGTPRE LRHSLGPGLR SPPRVMSRPP PSASPPKCIQ MERHVIRPPP
ISPPPDSLPL DDGAAHVMHR EVWMAVFSYL SHRDLCVCMR VCRTWNRWCC DKRLWTRIDL
NRCKSITPLM LSGIIRRQPV SLDLSWTNIS KKQLSWLINR LPGLRDLVLS GCSWIAVSAL
CSSSCPLLRT LDVQWVEGLK DAQMRDLLSP PTDNRPGQMD NRSKLRNIVE LRLAGLDITD
VSLRLIIRHM PLLSKLQLSY CNHINDQSIN LLTAVGTTTR DSLTEVNLSD CNKVTDLCLS
FFKRCGNICH IDLRYCKQVT KEGCEQFIAE MSVSVQFGQV EEKLLQKLS
