ID JMJD8_HUMAN Reviewed; 264 AA. AC Q96S16; B2RNS7; D3DU58; Q4PKE3; Q4VBY1; Q6GMW5; Q71RB8; DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot. DT 10-OCT-2018, sequence version 2. DT 24-JAN-2024, entry version 131. DE RecName: Full=JmjC domain-containing protein 8 {ECO:0000305}; DE AltName: Full=Jumonji domain-containing protein 8; DE Flags: Precursor; GN Name=JMJD8 {ECO:0000312|HGNC:HGNC:14148}; GN Synonyms=C16orf20 {ECO:0000312|HGNC:HGNC:14148}; ORFNames=PP14397; 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] (ISOFORM 1). RX PubMed=15498874; DOI=10.1073/pnas.0404089101; RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X., RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.; RT "Large-scale cDNA transfection screening for genes related to cancer RT development and progression."; RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Li H., Nong W., Zhou G., Ke R., Shen C., Zhong G., Zheng Z., Liang M., RA Wen S., Lin L., Yang S.; RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11157797; DOI=10.1093/hmg/10.4.339; RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.; RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of RT the short arm of human chromosome 16."; RL Hum. Mol. Genet. 10:339-352(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Kidney, and Uterus; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP INTERACTION WITH PKM, SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=27199445; DOI=10.1161/atvbaha.116.307695; RA Boeckel J.N., Derlet A., Glaser S.F., Luczak A., Lucas T., Heumueller A.W., RA Krueger M., Zehendner C.M., Kaluza D., Doddaballapur A., Ohtani K., RA Treguer K., Dimmeler S.; RT "JMJD8 Regulates Angiogenic Sprouting and Cellular Metabolism by RT Interacting With Pyruvate Kinase M2 in Endothelial Cells."; RL Arterioscler. Thromb. Vasc. Biol. 36:1425-1433(2016). RN [8] RP FUNCTION. RX PubMed=27671354; DOI=10.1038/srep34125; RA Yeo K.S., Tan M.C., Wong W.Y., Loh S.W., Lam Y.L., Tan C.L., Lim Y.Y., RA Ea C.K.; RT "JMJD8 is a positive regulator of TNF-induced NF-kappaB signaling."; RL Sci. Rep. 6:34125-34125(2016). RN [9] RP GLYCOSYLATION, SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=29133832; DOI=10.1038/s41598-017-15676-z; RA Yeo K.S., Tan M.C., Lim Y.Y., Ea C.K.; RT "JMJD8 is a novel endoplasmic reticulum protein with a JmjC domain."; RL Sci. Rep. 7:15407-15407(2017). CC -!- FUNCTION: Functions as a positive regulator of TNF-induced NF-kappa-B CC signaling (PubMed:27671354). Regulates angiogenesis and cellular CC metabolism through interaction with PKM (PubMed:27199445). CC {ECO:0000269|PubMed:27199445, ECO:0000269|PubMed:27671354}. CC -!- SUBUNIT: Oligomer (PubMed:29133832). Dimer (PubMed:29133832). Interacts CC with PKM; regulates angiogenesis and metabolism (PubMed:27199445). CC {ECO:0000269|PubMed:27199445, ECO:0000269|PubMed:29133832}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen CC {ECO:0000269|PubMed:29133832}. Cytoplasm {ECO:0000269|PubMed:27199445}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q96S16-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96S16-2; Sequence=VSP_034849; CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:29133832}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH73785.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAI37101.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAI37102.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAK61243.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=EAW85754.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=EAW85755.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; 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; AF370420; AAQ15256.1; -; mRNA. DR EMBL; DQ074695; AAY82251.1; -; mRNA. DR EMBL; AE006464; AAK61243.1; ALT_INIT; Genomic_DNA. DR EMBL; Z92544; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471112; EAW85754.1; ALT_INIT; Genomic_DNA. DR EMBL; CH471112; EAW85755.1; ALT_INIT; Genomic_DNA. DR EMBL; BC073785; AAH73785.1; ALT_INIT; mRNA. DR EMBL; BC094850; AAH94850.1; -; mRNA. DR EMBL; BC137100; AAI37101.1; ALT_INIT; mRNA. DR EMBL; BC137101; AAI37102.1; ALT_INIT; mRNA. DR CCDS; CCDS45369.2; -. [Q96S16-1] DR CCDS; CCDS92074.1; -. [Q96S16-2] DR RefSeq; NP_001005920.2; NM_001005920.2. [Q96S16-1] DR RefSeq; NP_001310847.1; NM_001323918.1. DR RefSeq; NP_001310848.1; NM_001323919.1. DR RefSeq; NP_001310851.1; NM_001323922.1. DR AlphaFoldDB; Q96S16; -. DR SMR; Q96S16; -. DR BioGRID; 130831; 53. DR IntAct; Q96S16; 11. DR STRING; 9606.ENSP00000399475; -. DR GlyCosmos; Q96S16; 3 sites, No reported glycans. DR GlyGen; Q96S16; 5 sites, 1 O-linked glycan (2 sites). DR iPTMnet; Q96S16; -. DR PhosphoSitePlus; Q96S16; -. DR BioMuta; JMJD8; -. DR DMDM; 74717267; -. DR EPD; Q96S16; -. DR MassIVE; Q96S16; -. DR PaxDb; 9606-ENSP00000399475; -. DR PeptideAtlas; Q96S16; -. DR ProteomicsDB; 78054; -. [Q96S16-1] DR ProteomicsDB; 78055; -. [Q96S16-2] DR Pumba; Q96S16; -. DR Antibodypedia; 22813; 109 antibodies from 22 providers. DR DNASU; 339123; -. DR Ensembl; ENST00000562824.5; ENSP00000454358.1; ENSG00000161999.13. [Q96S16-2] DR Ensembl; ENST00000609261.6; ENSP00000477481.1; ENSG00000161999.13. [Q96S16-1] DR GeneID; 339123; -. DR KEGG; hsa:339123; -. DR MANE-Select; ENST00000609261.6; ENSP00000477481.1; NM_001005920.4; NP_001005920.3. DR UCSC; uc002ciw.2; human. [Q96S16-1] DR AGR; HGNC:14148; -. DR CTD; 339123; -. DR DisGeNET; 339123; -. DR GeneCards; JMJD8; -. DR HGNC; HGNC:14148; JMJD8. DR HPA; ENSG00000161999; Low tissue specificity. DR MalaCards; JMJD8; -. DR neXtProt; NX_Q96S16; -. DR OpenTargets; ENSG00000161999; -. DR PharmGKB; PA162392531; -. DR VEuPathDB; HostDB:ENSG00000161999; -. DR eggNOG; KOG2131; Eukaryota. DR GeneTree; ENSGT00390000015438; -. DR InParanoid; Q96S16; -. DR OMA; KEPHFHP; -. DR OrthoDB; 120564at2759; -. DR PhylomeDB; Q96S16; -. DR TreeFam; TF313408; -. DR PathwayCommons; Q96S16; -. DR SignaLink; Q96S16; -. DR BioGRID-ORCS; 339123; 31 hits in 1158 CRISPR screens. DR ChiTaRS; JMJD8; human. DR GenomeRNAi; 339123; -. DR Pharos; Q96S16; Tbio. DR PRO; PR:Q96S16; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; Q96S16; Protein. DR Bgee; ENSG00000161999; Expressed in apex of heart and 161 other cell types or tissues. DR ExpressionAtlas; Q96S16; baseline and differential. DR Genevisible; Q96S16; HS. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0005788; C:endoplasmic reticulum lumen; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IMP:UniProtKB. DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IMP:UniProtKB. DR GO; GO:0006110; P:regulation of glycolytic process; IMP:UniProtKB. DR GO; GO:1903302; P:regulation of pyruvate kinase activity; IMP:UniProtKB. DR Gene3D; 2.60.120.650; Cupin; 1. DR InterPro; IPR041667; Cupin_8. DR InterPro; IPR003347; JmjC_dom. DR PANTHER; PTHR12480; ARGININE DEMETHYLASE AND LYSYL-HYDROXYLASE JMJD; 1. DR PANTHER; PTHR12480:SF35; JMJC DOMAIN-CONTAINING PROTEIN 8; 1. DR Pfam; PF13621; Cupin_8; 1. DR SUPFAM; SSF51197; Clavaminate synthase-like; 1. DR PROSITE; PS51184; JMJC; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cytoplasm; Endoplasmic reticulum; Glycoprotein; KW Reference proteome; Signal. FT SIGNAL 1..23 FT /evidence="ECO:0000255" FT CHAIN 24..264 FT /note="JmjC domain-containing protein 8" FT /evidence="ECO:0000255" FT /id="PRO_0000344531" FT DOMAIN 131..264 FT /note="JmjC" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00538" FT CARBOHYD 130 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 140 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT CARBOHYD 209 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498" FT VAR_SEQ 30..59 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.2" FT /id="VSP_034849" FT CONFLICT 158 FT /note="L -> P (in Ref. 2; AAY82251)" FT /evidence="ECO:0000305" FT CONFLICT 207 FT /note="H -> R (in Ref. 2; AAY82251)" FT /evidence="ECO:0000305" SQ SEQUENCE 264 AA; 29509 MW; 764DAF7EE2977FBC CRC64; MAPASRLLAL WALAAVALPG SGAEGDGGWR PGGPGAVAEE ERCTVERRAD LTYAEFVQQY AFVRPVILQG LTDNSRFRAL CSRDRLLASF GDRVVRLSTA NTYSYHKVDL PFQEYVEQLL HPQDPTSLGN DTLYFFGDNN FTEWASLFRH YSPPPFGLLG TAPAYSFGIA GAGSGVPFHW HGPGYSEVIY GRKRWFLYPP EKTPEFHPNK TTLAWLRDTY PALPPSARPL ECTIRAGEVL YFPDRWWHAT LNLDTSVFIS TFLG //