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Database: UniProt
Entry: A0A2K6BQ23_MACNE
LinkDB: A0A2K6BQ23_MACNE
Original site: A0A2K6BQ23_MACNE 
ID   A0A2K6BQ23_MACNE        Unreviewed;      1267 AA.
AC   A0A2K6BQ23;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=[histone H3]-dimethyl-L-lysine(36) demethylase {ECO:0000256|ARBA:ARBA00013246};
DE            EC=1.14.11.27 {ECO:0000256|ARBA:ARBA00013246};
GN   Name=KDM2B {ECO:0000313|Ensembl:ENSMNEP00000013475.1};
OS   Macaca nemestrina (Pig-tailed macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000013475.1, ECO:0000313|Proteomes:UP000233120};
RN   [1] {ECO:0000313|Ensembl:ENSMNEP00000013475.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001574};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the JHDM1 histone demethylase family.
CC       {ECO:0000256|ARBA:ARBA00008037}.
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DR   AlphaFoldDB; A0A2K6BQ23; -.
DR   Ensembl; ENSMNET00000037675.1; ENSMNEP00000013475.1; ENSMNEG00000030664.1.
DR   GeneTree; ENSGT00940000154717; -.
DR   Proteomes; UP000233120; Unplaced.
DR   Bgee; ENSMNEG00000030664; Expressed in lymph node and 12 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0140680; F:histone H3K36me/H3K36me2 demethylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0045322; F:unmethylated CpG binding; IEA:UniProt.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd21785; CTD_KDM2B; 1.
DR   CDD; cd22180; F-box_FBXL10; 1.
DR   CDD; cd15644; PHD_KDM2B; 1.
DR   Gene3D; 1.20.58.1360; -; 1.
DR   Gene3D; 2.60.120.650; Cupin; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR041667; Cupin_8.
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   PANTHER; PTHR23123:SF10; LYSINE-SPECIFIC DEMETHYLASE 2B; 1.
DR   PANTHER; PTHR23123; PHD/F-BOX CONTAINING PROTEIN; 1.
DR   Pfam; PF13621; Cupin_8; 1.
DR   Pfam; PF12937; F-box-like; 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; 6.
DR   SMART; SM00249; PHD; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF52047; RNI-like; 1.
DR   PROSITE; PS51184; JMJC; 1.
DR   PROSITE; PS51058; ZF_CXXC; 1.
DR   PROSITE; PS50016; ZF_PHD_2; 1.
PE   3: Inferred from homology;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW   Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233120};
KW   Repressor {ECO:0000256|ARBA:ARBA00022491};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00509}.
FT   DOMAIN          147..315
FT                   /note="JmjC"
FT                   /evidence="ECO:0000259|PROSITE:PS51184"
FT   DOMAIN          575..621
FT                   /note="CXXC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51058"
FT   DOMAIN          628..694
FT                   /note="PHD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50016"
FT   REGION          379..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          696..962
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..397
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        447..470
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        720..790
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        799..841
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        873..890
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        891..905
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        906..934
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1267 AA;  145038 MW;  3A40044C4B7FBD51 CRC64;
     MEAEKDSGRR LRPIDRQRYD ENEDLSDVEE IVSVRGFSLE EKLRSQLYQG DFVHAMEGKD
     FNYEYVQREA LRVPLIFREK DGLGIKMPDP DFTVRDVKLL VGSRRLVDVM DVNTQKGTEM
     SMSQFVRYYE TPEAQRDKLY NVISLEFSHT KLEHLVKRPT VVDLVDWVDN MWPQHLKEKQ
     TEATNAIAEM KYPKVKKYCL MSVKGCFTDF HIDFGGTSVW YHVFRGGKIF WLIPPTLHNL
     ALYEEWVLSG KQSDIFLGDR VERCQRIELK QGYTFFIPSG WIHAVYTPVD SLVFGGNILH
     SFNVPMQLRI YEIEDRTRVQ PKFRYPFYYE MCWYVLERYV YCVTQRSHLT QEYQRESMLI
     DAPRKPSIDG FSSDSWLEME EEACDQQPQE EEEKDEEGEG RDRAPKPPTD GSASPTSMPS
     EDQEALGKKP KAPALRFLKR TLSNESEESV KSTTLPVDYP KTPTGSPATE VSAKWTHLTE
     FELKGLKALV EKLESLPENK KCVPEGIEDP QALLEGVKNV LKEHADDDPS LAITGVPVVT
     WPKKTPKNRA VGRPKGKLGP ASAVKLAANR TTAGARRRRT RCRKCEACLR TECGECHFCK
     DMKKFGGPGR MKQSCIMRQC IAPVLPHTAV CLVCGEAGKE DTVEEEEGKF NLMLMECSIC
     NEIIHPGCLK IKESEGVVND ELPNCWECPK CNHAGKTGKQ KRGPGFKYAS NLPGSLLKEQ
     KMNRDNKEGQ EPAKRRSECE EAPRRRSDEH PKKVPPDGLL RRKSDDVHLR KKRKYEKPQE
     LSGRKRLKPG KEDKLFRKKR RSWKNAEDRM ALANKPLRRF KQEPEDDLPE APPKTRESDH
     SRSSSPTAGP STEGTEGPEE KKKVKMRRKR RLPNKELSRE LSKELNHEIQ RTESSLANEN
     QQPIKSEPES EGEEPKRPPG VCERPHRFSK GLNGTPRELR HQLGPGLRSP PRVISRPPPS
     VSPPKCIQME RHVIRPPPIS PPPDSLPLDD GAAHVMHREV WMAVFSYLSH QDLCVCMRVC
     RTWNRWCCDK RLWTRIDLNH CKSITPLMLS GIIRRQPVSL DLSWTNISKK QLSWLINRLP
     GLRDLVLSGC SWIAVSALCS SSCPLLRTLD VQWVEGLKDA QMRDLLSPPT DNRPGQMDNR
     SKLRNIVELR LAGLDITDAS LRLIIRHMPL LSKLHLSYCN HVTDQSINLL TAVGTTTRDS
     LTEINLSDCN KVTDQCLSFF KRCGNICHID LRYCKQVTKE GCEQFIAEMS VSVQFGQVEE
     KLLQKLS
//
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