ID H2QSC6_PANTR Unreviewed; 922 AA.
AC H2QSC6;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Lysine demethylase 1B {ECO:0000313|Ensembl:ENSPTRP00000030324.7};
GN Name=KDM1B {ECO:0000313|Ensembl:ENSPTRP00000030324.7,
GN ECO:0000313|VGNC:VGNC:7900};
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:ENSPTRP00000030324.7, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000030324.7, 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:ENSPTRP00000030324.7}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; AACZ04065890; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_009448848.1; XM_009450573.2.
DR AlphaFoldDB; H2QSC6; -.
DR Ensembl; ENSPTRT00000032824.7; ENSPTRP00000030324.7; ENSPTRG00000017757.7.
DR GeneID; 462459; -.
DR CTD; 221656; -.
DR VGNC; VGNC:7900; KDM1B.
DR eggNOG; KOG0029; Eukaryota.
DR GeneTree; ENSGT00940000157751; -.
DR HOGENOM; CLU_007885_0_0_1; -.
DR InParanoid; H2QSC6; -.
DR OMA; AVYYDMD; -.
DR OrthoDB; 5402444at2759; -.
DR TreeFam; TF352593; -.
DR Proteomes; UP000002277; Chromosome 6.
DR Bgee; ENSPTRG00000017757; Expressed in bone marrow and 22 other cell types or tissues.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0000786; C:nucleosome; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0071949; F:FAD binding; IEA:Ensembl.
DR GO; GO:0140682; F:FAD-dependent H3K4me/H3K4me3 demethylase activity; IEA:Ensembl.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IEA:Ensembl.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0044726; P:epigenetic programing of female pronucleus; IEA:Ensembl.
DR GO; GO:0071514; P:genomic imprinting; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.40.100; -; 1.
DR Gene3D; 3.90.660.10; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR007526; SWIRM.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR011124; Znf_CW.
DR PANTHER; PTHR10742; FLAVIN MONOAMINE OXIDASE; 1.
DR PANTHER; PTHR10742:SF413; LYSINE-SPECIFIC HISTONE DEMETHYLASE 1B; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR Pfam; PF04433; SWIRM; 1.
DR Pfam; PF07496; zf-CW; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS50934; SWIRM; 1.
DR PROSITE; PS51050; ZF_CW; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00454}.
FT DOMAIN 233..293
FT /note="CW-type"
FT /evidence="ECO:0000259|PROSITE:PS51050"
FT DOMAIN 375..473
FT /note="SWIRM"
FT /evidence="ECO:0000259|PROSITE:PS50934"
FT REGION 60..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 922 AA; 102971 MW; 5552A1251216C6CB CRC64;
MGRAERALRL RRRRGPYPSL VLWAPPTPGH AVTGAEAAAA AAAEKRLGLA ARLQPSCARG
ARLRRGARSP GRRAPPRWRS ERCLFPETPG TSSAQRLFNV MATPRGRTKK KASFDHSPDS
LPLRSSGRQA KKKATETTDE DEDGGSEKKY RKCEKAGCTA TCPVCFASAS ERCAKNGYTS
RWYHLSCGEH FCNECFDHYY RSHKDGYDKY TTWKKIWTSN GKTEPSPKAF MADQQLPYWV
QCTKPECRKW RQLTKEIQLT PQIAKTYRCG MKPNTAIKPE TSDHCSLPED LRVLEVSNHW
WYSMLILPPL LKDSVAAPLL SAYYPDCVGM SPSCTSTNRA AATGNASPGK LEHSKAALSV
HVPGMNRYFQ PFYQPNECGK ALCVRPDVME LDELYEFPEY SRDPTMYLAL RNLILALWYT
NCKEALTPQK CIPHIIVRGL VRIRCVQEVE RILYFMTRKG LINTGVLSVG ADQYLLPKDY
HNKSVIIIGA GPAGLAAARQ LHNFGIKVTV LEAKDRIGGR VWDDKSFKGV TVGRGAQIVN
GCINNPVALM CEQLGISMHK FGERCDLIQE GGRITDPTID KRMDFHFNAL LDVVSEWRKD
KTQLQDVPLG EKIEEIYKAF IKESGIQFSE LEGQVLQFHL SNLEYACGSN LHQVSARSWD
HNEFFAQFAG DHTLLTPGYS VIIEKLAEGL DIQLKSPVQC IDYSGDEVQV TTTDGTGYSA
QKVLVTVPLA LLQKGAIQFN PPLSEKKMKA INSLGAGIIE KIALQFPYRF WDSKVQGADF
FGHVPPSASK RGLFAVFYDM DPQKKHSVLM SVIAGEAVAS VRTLDDKQVL QQCMATLREL
FKEQEVPDPI KYFVTRWSTD PWIQMAYSFV KTGGSGEAYD IIAEDIQGTV FFAGEATNRH
FPQTVTGAYL SGVREASKIA AF
//
