JMJD4_HUMAN
ID JMJD4_HUMAN Reviewed; 463 AA.
AC Q9H9V9; Q5TBZ1; Q5TBZ6; Q9H970;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=2-oxoglutarate and iron-dependent oxygenase JMJD4 {ECO:0000303|PubMed:24486019};
DE EC=1.14.11.- {ECO:0000269|PubMed:24486019};
DE AltName: Full=JmjC domain-containing protein 4;
DE AltName: Full=Jumonji domain-containing protein 4;
DE AltName: Full=Lysyl-hydroxylase JMJD4 {ECO:0000303|PubMed:24486019};
GN Name=JMJD4;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP VAL-11.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH ETF1 AND ETF1-GSPT1 COMPLEX,
RP COFACTOR, SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-235.
RX PubMed=24486019; DOI=10.1016/j.molcel.2013.12.028;
RA Feng T., Yamamoto A., Wilkins S.E., Sokolova E., Yates L.A., Muenzel M.,
RA Singh P., Hopkinson R.J., Fischer R., Cockman M.E., Shelley J.,
RA Trudgian D.C., Schoedel J., McCullagh J.S., Ge W., Kessler B.M.,
RA Gilbert R.J., Frolova L.Y., Alkalaeva E., Ratcliffe P.J., Schofield C.J.,
RA Coleman M.L.;
RT "Optimal translational termination requires C4 lysyl hydroxylation of
RT eRF1.";
RL Mol. Cell 53:645-654(2014).
CC -!- FUNCTION: Catalyzes the 2-oxoglutarate and iron-dependent C4-lysyl
CC hydroxylation of ETF1 at 'Lys-63' thereby promoting the translational
CC termination efficiency of ETF1. {ECO:0000269|PubMed:24486019}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-lysyl-[protein] + O2 = 4-hydroxy-L-lysyl-
CC [protein] + CO2 + succinate; Xref=Rhea:RHEA:57156, Rhea:RHEA-
CC COMP:9752, Rhea:RHEA-COMP:15084, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:141495;
CC Evidence={ECO:0000269|PubMed:24486019};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:24486019};
CC -!- SUBUNIT: Interacts with ETF1 (PubMed:24486019). Interacts with the
CC ETF1-GSPT1 complex (PubMed:24486019). {ECO:0000269|PubMed:24486019}.
CC -!- INTERACTION:
CC Q9H9V9; P62805: H4C9; NbExp=3; IntAct=EBI-2866290, EBI-302023;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24486019}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H9V9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H9V9-2; Sequence=VSP_026324;
CC -!- CAUTION: It is uncertain whether Met-1 or Met-47 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB14366.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK022579; BAB14109.1; -; mRNA.
DR EMBL; AK023030; BAB14366.1; ALT_INIT; mRNA.
DR EMBL; AL136378; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001154937.1; NM_001161465.1.
DR RefSeq; NP_075383.2; NM_023007.2.
DR AlphaFoldDB; Q9H9V9; -.
DR SMR; Q9H9V9; -.
DR BioGRID; 122393; 61.
DR IntAct; Q9H9V9; 43.
DR MINT; Q9H9V9; -.
DR STRING; 9606.ENSP00000355720; -.
DR iPTMnet; Q9H9V9; -.
DR PhosphoSitePlus; Q9H9V9; -.
DR BioMuta; JMJD4; -.
DR DMDM; 150383500; -.
DR EPD; Q9H9V9; -.
DR jPOST; Q9H9V9; -.
DR MassIVE; Q9H9V9; -.
DR MaxQB; Q9H9V9; -.
DR PaxDb; Q9H9V9; -.
DR PeptideAtlas; Q9H9V9; -.
DR PRIDE; Q9H9V9; -.
DR ProteomicsDB; 81365; -. [Q9H9V9-1]
DR ProteomicsDB; 81366; -. [Q9H9V9-2]
DR Antibodypedia; 20772; 295 antibodies from 30 providers.
DR DNASU; 65094; -.
DR Ensembl; ENST00000438896.3; ENSP00000387830.3; ENSG00000081692.13.
DR GeneID; 65094; -.
DR KEGG; hsa:65094; -.
DR UCSC; uc001hrb.3; human. [Q9H9V9-1]
DR CTD; 65094; -.
DR DisGeNET; 65094; -.
DR GeneCards; JMJD4; -.
DR HGNC; HGNC:25724; JMJD4.
DR HPA; ENSG00000081692; Low tissue specificity.
DR neXtProt; NX_Q9H9V9; -.
DR PharmGKB; PA142671643; -.
DR VEuPathDB; HostDB:ENSG00000081692; -.
DR eggNOG; KOG2131; Eukaryota.
DR InParanoid; Q9H9V9; -.
DR OMA; MFSRRFT; -.
DR PhylomeDB; Q9H9V9; -.
DR TreeFam; TF105936; -.
DR PathwayCommons; Q9H9V9; -.
DR SignaLink; Q9H9V9; -.
DR BioGRID-ORCS; 65094; 12 hits in 1080 CRISPR screens.
DR ChiTaRS; JMJD4; human.
DR GenomeRNAi; 65094; -.
DR Pharos; Q9H9V9; Tbio.
DR PRO; PR:Q9H9V9; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9H9V9; protein.
DR Bgee; ENSG00000081692; Expressed in left adrenal gland cortex and 104 other tissues.
DR ExpressionAtlas; Q9H9V9; baseline and differential.
DR Genevisible; Q9H9V9; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IMP:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106156; F:peptidyl-lysine 4-dioxygenase activity; IEA:RHEA.
DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0010629; P:negative regulation of gene expression; IBA:GO_Central.
DR GO; GO:0045905; P:positive regulation of translational termination; IMP:UniProtKB.
DR GO; GO:0018126; P:protein hydroxylation; IMP:UniProtKB.
DR InterPro; IPR003347; JmjC_dom.
DR Pfam; PF02373; JmjC; 1.
DR SMART; SM00558; JmjC; 1.
DR PROSITE; PS51184; JMJC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Dioxygenase; Iron; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..463
FT /note="2-oxoglutarate and iron-dependent oxygenase JMJD4"
FT /id="PRO_0000291959"
FT DOMAIN 188..347
FT /note="JmjC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538"
FT BINDING 235
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC1"
FT BINDING 237
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC1"
FT BINDING 315
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q6NYC1"
FT VAR_SEQ 354..369
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_026324"
FT VARIANT 11
FT /note="A -> V (in dbSNP:rs7419238)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_032898"
FT VARIANT 16
FT /note="G -> C (in dbSNP:rs34560898)"
FT /id="VAR_032899"
FT VARIANT 65
FT /note="D -> E (in dbSNP:rs2295994)"
FT /id="VAR_032900"
FT VARIANT 461
FT /note="A -> V (in dbSNP:rs3087908)"
FT /id="VAR_032901"
FT MUTAGEN 235
FT /note="H->A: Loss of interaction with ETF1 and its ability
FT to hydroxylate ETF1."
FT /evidence="ECO:0000269|PubMed:24486019"
FT CONFLICT 244
FT /note="W -> R (in Ref. 1; BAB14366)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="Q -> R (in Ref. 1; BAB14366)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 463 AA; 52493 MW; CD79490AB06E8652 CRC64;
MRAGPEPQAL AGQKRGALRL LVPRLVLTVS APAEVRRRVL RPVLSWMDRE TRALADSHFR
GLGVDVPGVG QAPGRVAFVS EPGAFSYADF VRGFLLPNLP CVFSSAFTQG WGSRRRWVTP
AGRPDFDHLL RTYGDVVVPV ANCGVQEYNS NPKEHMTLRD YITYWKEYIQ AGYSSPRGCL
YLKDWHLCRD FPVEDVFTLP VYFSSDWLNE FWDALDVDDY RFVYAGPAGS WSPFHADIFR
SFSWSVNVCG RKKWLLFPPG QEEALRDRHG NLPYDVTSPA LCDTHLHPRN QLAGPPLEIT
QEAGEMVFVP SGWHHQVHNL DDTISINHNW VNGFNLANMW RFLQQELCAV QEEVSEWRDS
MPDWHHHCQV IMRSCSGINF EEFYHFLKVI AEKRLLVLRE AAAEDGAGLG FEQAAFDVGR
ITEVLASLVA HPDFQRVDTS AFSPQPKELL QQLREAVDAA AAP
