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Database: UniProt
Entry: F4MHI3_HUMAN
LinkDB: F4MHI3_HUMAN
Original site: F4MHI3_HUMAN 
ID   F4MHI3_HUMAN            Unreviewed;      1014 AA.
AC   F4MHI3;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 2.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=[histone H3]-trimethyl-L-lysine(27) demethylase {ECO:0000256|ARBA:ARBA00034525};
DE            EC=1.14.11.68 {ECO:0000256|ARBA:ARBA00034525};
GN   Name=UTY {ECO:0000313|EMBL:ABS19060.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:ABS19060.1};
RN   [1] {ECO:0000313|EMBL:ABS19060.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=21329462; DOI=10.1089/omi.2010.0107;
RA   Laaser I., Theis F.J., de Angelis M.H., Kolb H.J., Adamski J.;
RT   "Huge splicing frequency in human Y chromosomal UTY gene.";
RL   OMICS 15:141-154(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 2-oxoglutarate + N(6),N(6),N(6)-trimethyl-L-lysyl(27)-
CC         [histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + N(6)-methyl-L-
CC         lysyl(27)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:60224,
CC         Rhea:RHEA-COMP:15535, Rhea:RHEA-COMP:15544, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842,
CC         ChEBI:CHEBI:30031, ChEBI:CHEBI:61929, ChEBI:CHEBI:61961;
CC         EC=1.14.11.68; Evidence={ECO:0000256|ARBA:ARBA00034421};
CC   -!- COFACTOR:
CC       Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC         Evidence={ECO:0000256|ARBA:ARBA00001961};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the UTX family. {ECO:0000256|ARBA:ARBA00034483}.
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DR   EMBL; EF685339; ABS19060.1; -; mRNA.
DR   PeptideAtlas; F4MHI3; -.
DR   ChiTaRS; UTY; human.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   Gene3D; 1.20.58.1370; -; 1.
DR   Gene3D; 2.60.120.650; Cupin; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 3.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR14017:SF25; HISTONE DEMETHYLASE UTY; 1.
DR   PANTHER; PTHR14017; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR   Pfam; PF13181; TPR_8; 1.
DR   SMART; SM00028; TPR; 6.
DR   SUPFAM; SSF48452; TPR-like; 2.
DR   PROSITE; PS50005; TPR; 2.
PE   2: Evidence at transcript level;
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT   REPEAT          90..123
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REPEAT          127..160
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REGION          519..660
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          722..786
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          830..857
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          957..1000
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        831..851
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        960..990
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   UNSURE          177
FT                   /note="D or N"
FT                   /evidence="ECO:0000313|EMBL:ABS19060.1"
SQ   SEQUENCE   1014 AA;  111327 MW;  FBF89EFC131D687E CRC64;
     MKSCAVSLTT AAVAFGDEAK KMAEGKASRE SEEESVSLTV EEREALGGMD SRLFGFVRLH
     EDGARTKTLL GKAVRCYESL ILKAEGKVES DFFCQLGHFN LLLEDYSKAL SAYQRYYSLQ
     ADYWKNAAFL YGLGLVYFYY NAFHWAIKAF QDVLYVDPSF CRAKEXHLRL GLMFKVDTDY
     KSSLKHFQLA LIDCNPCTLS NAEIQFHIAH LYETQRKYHS AKEAYEQLLQ TENLPAQVKA
     TVLQQLGWMH HNMDLVGDKA TKESYAIQYL QKSLEADPNS GQSWYFLGSV LYQQQNQPMD
     ALQAYICAVQ LDHGHAAAWM DLGTLYESCN QPQDAIKCYL NAARSKRCSN TSXLAARIKF
     LQNGSDNWNG GQSLSHHPVQ QVYSLCLTPQ KLQHLEQLRA NRDNLNPAQK HQLEQLESQF
     VLMQQMRHKE XAQVRTTGIH NGAITDSSLP TNSVSNRQPH GALTRVSSVS QPGVRPACVE
     KLLSSGAFSA GCIPCGTSKI LGSTDTILLG SNCIAGSESN GNVPYLQQNT HTLPHNHTDL
     NSSTEEPWRK QLSNSAQGLH KSQSSCLSGP NEEQPLFSTG SAQYHQATST GIKKANEHLT
     LPSNSVPQGD ADSHLSCHTA TSGGQQGIMX TKESKPSKNR SLVPETSRHT GDTSNGCADV
     KGLSNHVHQL IADAVSSPNH GDSPNLLIAD NPQLSALLIG KANGNVGTGT CDKVNNIHPA
     VHTKTDHSVA SSPXSAISTA TPSPKSTEQR SINSVTSLNS PHSGLHTVNG EGLGKSQSST
     KVDLPLASHR STSQILPSMS VSICPSSTEV LKACRNPGKN GLSNSXILLD KCPPPRPPTS
     PYPPLPKDKL NPPTPSIYLE NKRDAFFPPL HQFCTNPKNP VTVIRGLAGA LKLDLGLFST
     KTLVEANNEH MVEVRTQLLQ PADENWDPTG TKKIWRCESN RSHTTIAKYA QYQASSFQES
     LREENEKRTQ HKDHSDNEST SSENSGRRRK GPFKTIKFGT NIDLSDNKNN LCLS
//
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