ID G1SQ17_RABIT Unreviewed; 1341 AA.
AC G1SQ17;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 2.
DT 27-MAR-2024, entry version 75.
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:ENSOCUP00000005165.3};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000005165.3, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000005165.3, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000005165.3,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000005165.3}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000005165.3};
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}.
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DR EMBL; AAGW02061430; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02061431; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02061432; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02061433; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_017205019.1; XM_017349530.1.
DR SMR; G1SQ17; -.
DR STRING; 9986.ENSOCUP00000005165; -.
DR PaxDb; 9986-ENSOCUP00000005165; -.
DR Ensembl; ENSOCUT00000005967.4; ENSOCUP00000005165.3; ENSOCUG00000005961.4.
DR GeneID; 100349603; -.
DR eggNOG; KOG1633; Eukaryota.
DR eggNOG; KOG1947; Eukaryota.
DR GeneTree; ENSGT00940000154717; -.
DR HOGENOM; CLU_003540_0_1_1; -.
DR InParanoid; G1SQ17; -.
DR OMA; HTHLTHY; -.
DR OrthoDB; 2784357at2759; -.
DR Proteomes; UP000001811; Chromosome 21.
DR Bgee; ENSOCUG00000005961; Expressed in uterus and 17 other cell types or tissues.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0031519; C:PcG protein complex; IEA:Ensembl.
DR GO; GO:0140680; F:histone H3K36me/H3K36me2 demethylase activity; IEA:UniProtKB-EC.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0045322; F:unmethylated CpG binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IEA:Ensembl.
DR GO; GO:0021592; P:fourth ventricle development; IEA:Ensembl.
DR GO; GO:0021993; P:initiation of neural tube closure; IEA:Ensembl.
DR GO; GO:0021670; P:lateral ventricle development; IEA:Ensembl.
DR GO; GO:0030901; P:midbrain development; IEA:Ensembl.
DR GO; GO:0021555; P:midbrain-hindbrain boundary morphogenesis; IEA:Ensembl.
DR GO; GO:2000178; P:negative regulation of neural precursor cell proliferation; IEA:Ensembl.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0021678; P:third ventricle development; IEA:Ensembl.
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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
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:UP000001811};
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 183..351
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT DOMAIN 613..659
FT /note="CXXC-type"
FT /evidence="ECO:0000259|PROSITE:PS51058"
FT DOMAIN 666..732
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 734..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..437
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..821
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..850
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 875..915
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..1008
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1341 AA; 152966 MW; 20218F984BB2064F CRC64;
MEKLRPQRES TLPKDTKPAS GESGLEPRLP ISAVPLSTTC GSPDSQERPI DRQRYDENED
LSDVEEIVSV RGFSLEEKLR SQLYQGDFVH AMEGKDFNYE YVQREALRVP LVFREKDGLG
IKMPDPDFTV RDVKLLVGSR RLVDVMDVNT QKGTEMSMSQ FVRYYETPEA QRDKLYNVIS
LEFSHTKLEH LVKRPTVVDL VDWVDNMWPQ HLKEKQTEAT NAIAEMKYPK VKKYCLMSVK
GCFTDFHIDF GGTSVWYHVF RGGKIFWLIP PTLHNLALYE EWVLSGKQSD IFLGDRVERC
QRIELKQGYT FFIPSGWIHA VYTPVDSLVF GGNILHSFNV PMQLRIYEIE DRTRVQPKFR
YPFYYEMCWY VLERYVYCVT QRSHLTQEYQ RESMLIDAPR KPSIDGFSSD SWLEMEEESC
EQQPQEEEKE EEEEEGEGSD KAPRPPTEGP ASPTSNPSED QEAPGKKPKA PAMRFLKRTL
SNESEESVKS TAMATDYPKT PTGSPSTEVS AKWTHLTEFE LKGLKALVEK LESLPENKKC
VPEGIEDPQA LLEGVKNVLK EHADDDPSLA ITGVPVVTWP KKTPKNRAVG RPKGKLGPAS
AVKLAANRTT AGARRRRTRC RKCEACLRTE CGECHFCKDM KKFGGPGRMK QSCIMRQCIA
PVLPHTAVCL VCGEAGKEDT VEEEEGKFNL MLMECSICNE IIHPGCLKIK ESEGVVNDEL
PNCWECPKCN HAGKTGKQKR GPGFKYASNL PGSLLKEQKM NRDNKEGQEP AKRRSECEEA
PRRRSDEHPK KVPPDGILRR KSDDVHLRRK RKYEKPQELS ARKRASTLQT SPGSSSHLSP
RPPLGSSLSP WWRSSLTYFQ QQLKPGKEDK LFRKKRRSWK NTEDRMASKP LRRFKQEPED
DLPEAPPKTR ESDHSRSSSP TAGPSTEAAE GPEEKKKVKM RRKRRLPNKE LSKELSKELN
HEIQKTESSL AHENHQPIKS EPESEHEEPK RPLGLCERPH RFSKGLNGAP RELRHPLGSG
LRSPPRVISR PPPSVSPPKC IQMERHVIRP PPISPPPDSL PLDDGAAHVM HREVWMAVFS
YLSHQDLCVC MRVCRTWNRW CCDKRLWTRI DLNHCKSITP LMLSGIIRRQ PVSLDLSWTN
ISKKQLSWLI NRLPGLRDLV LSGCSWVAVS ALCSSSCPLL RTLDVQWVEG LKDAQMRDLL
SPPTDNRPGQ MDNRSKLRNI VELRLAGLDI TDASLRLIIR HMPLLSKLHL SYCNHVTDQS
INLLTAVGTT TRDSLTEINL SDCNKVTDQC LSFFKRCGNI CHIDLRYCKQ VTKEGCEQFI
AEMSVSVQFG QVEEKLLQKL S
//
