ID F4MHR1_HUMAN Unreviewed; 606 AA.
AC F4MHR1;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
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:ABV82680.1};
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:ABV82680.1};
RN [1] {ECO:0000313|EMBL:ABV82680.1}
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}.
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; EU026349; ABV82680.1; -; mRNA.
DR PeptideAtlas; F4MHR1; -.
DR ChiTaRS; UTY; human.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
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; PF13432; TPR_16; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 7.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50005; TPR; 3.
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 REPEAT 315..348
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 563..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 563..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 606 AA; 67775 MW; 260CCBB970A79992 CRC64;
MKSCAVSLTT AAVAFGDEAK KMXEGKASRE 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 GQSWYFLGRC YSSIGKVQDA
FISYRQSIDK SEASADTWCS IGVLYQQQNQ PMDALQAYIC AVQLDHGHAA AWMDLGTLYE
SCNQPQDAIK CXLNAARSKR CSNTSTLAAR IKFLQNGSDN WNGGQSLSHH PVQQVYSLCL
TPQKLQHLEQ LRANRDNLNP AQKHQLEQLE SQFVLMQQMR HKEVAQVRTT GIHNGAITDS
SLPTNSVSNR QPHGALTRVS SVSQPGVRPA CVEKLLSSGA FSAGCIPCGT SKILGSTDTI
LLGSNCIAGS EXNGNVPYLX QNTHTLPHNH TDLNSSTEEP WRKQLSNSAQ PFPQQHLLLN
PLSREA
//
