ID A0A2I3T5P5_PANTR Unreviewed; 1265 AA.
AC A0A2I3T5P5; A0A2J8MDE4;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 33.
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:ENSPTRP00000084542.1,
GN ECO:0000313|VGNC:VGNC:8429};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000084542.1, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000084542.1, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000084542.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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}.
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; AACZ04070268; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04070269; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04070270; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AACZ04070271; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_016779908.1; XM_016924419.1.
DR AlphaFoldDB; A0A2I3T5P5; -.
DR Ensembl; ENSPTRT00000108269.1; ENSPTRP00000084542.1; ENSPTRG00000005560.6.
DR VGNC; VGNC:8429; KDM2B.
DR GeneTree; ENSGT00940000154717; -.
DR OMA; HTHLTHY; -.
DR OrthoDB; 2784357at2759; -.
DR Proteomes; UP000002277; Chromosome 12.
DR Bgee; ENSPTRG00000005560; Expressed in lymph node and 21 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:UP000002277};
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..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..964
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 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 1265 AA; 144749 MW; 145BA5F1C9C50A2D 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 RDRAPKPPAD GSTSPTSTPS
EDQEALGKKP KAPALRFLKR TLSNESEESV KSTTLAVDYP 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 KQEPEDELPE APPKTRESDH
SRSSSPTAGP STEGAEGPEE KKKVKMRRKR RLPNKELSRE LSKELNHEIQ RTENSLANEN
QQPIKSEPES EGEEPKRPPG ICERPHRFSK GLNGTPRELR HQLGPSLRSP 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 SFQGRSCSTT
RLGDE
//
