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Database: UniProt
Entry: F4MHF0_HUMAN
LinkDB: F4MHF0_HUMAN
Original site: F4MHF0_HUMAN 
ID   F4MHF0_HUMAN            Unreviewed;       605 AA.
AC   F4MHF0;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 41.
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:ABS19027.1};
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:ABS19027.1};
RN   [1] {ECO:0000313|EMBL:ABS19027.1}
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; EF685306; ABS19027.1; -; mRNA.
DR   PeptideAtlas; F4MHF0; -.
DR   ChiTaRS; UTY; human.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 4.
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; 2.
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          398..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          565..605
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   605 AA;  67529 MW;  FF19FBD401F656A0 CRC64;
     MKSCAVSLTT AAVAFGDEAK KMAEGKASRE SEEESVSLTV EEREALGGMD SRLFGFVRLH
     EDGARTKTLL GKAVRCYESL ILKAEGKVES DFFCQLGHFN LLLEDYSKAL SAYQRYYSLQ
     ADYWKNAAFL YGLGLVYFYY NAFHWAIKAF QDVLYVDPSF CRAKEIHLRL GLMFKVNTDY
     KSSLKHFQLA LIDCNPCTLS NAEIQFHIAH LYETQRKYHS AKEAYEQLLQ TENLPAQVKA
     TVLQQLGWMH HNMDLVGDKA TKESYAIQYL QKSLEADPNS GQSWYFLGSV LYQQQNQPMD
     ALQAYICAVQ LDHGHAAAWM DLGTLYESCN QPQDAIKCYL NAARSKRCSN TSTLAARIKF
     LQAQLCNLXQ SSLXNKTKLL PSIEEAWSLP IPAELTSRQG AMNTAQQNGS DNWNGGQSLS
     HHPVQQVYSL CLTPQKLQHL EQLRANRDNL NPAQKHQLEQ LESQFVLMQQ MRHKEVAQVR
     TTGIHNGAIT DSSLPTNSVS NRQPHGALTR VSSVSQPGVR PACVEKLLSS GAFSAGCIPC
     GTSKILGSTD TILLGSNCIA GSESNGNVPY LQQNTHTLPH NHTDLNSSTE EPWRKQLSNS
     AQESR
//
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