ID JADE1_HUMAN Reviewed; 842 AA. AC Q6IE81; D3DNY0; D3DNY1; Q4W5D5; Q6ZSL7; Q8NC41; Q96JL8; Q96SQ1; Q9H692; DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 02-OCT-2024, entry version 164. DE RecName: Full=Protein Jade-1; DE AltName: Full=Jade family PHD finger protein 1; DE AltName: Full=PHD finger protein 17; GN Name=JADE1; Synonyms=KIAA1807, PHF17; 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 [MRNA] (ISOFORM 3), INTERACTION WITH VHL, TISSUE RP SPECIFICITY, AND SUBCELLULAR LOCATION. RX PubMed=12169691; DOI=10.1074/jbc.m205040200; RA Zhou M.I., Wang H., Ross J.J., Kuzmin I., Xu C., Cohen H.T.; RT "The von Hippel-Lindau tumor suppressor stabilizes novel plant homeodomain RT protein Jade-1."; RL J. Biol. Chem. 277:39887-39898(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Hippocampus; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Cervix; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 141-842. RC TISSUE=Brain; RX PubMed=11347906; DOI=10.1093/dnares/8.2.85; RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XX. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 8:85-95(2001). RN [7] RP IDENTIFICATION (ISOFORM 1). RX PubMed=14612400; DOI=10.1128/mcb.23.23.8553-8562.2003; RA Tzouanacou E., Tweedie S., Wilson V.; RT "Identification of Jade1, a gene encoding a PHD zinc finger protein, in a RT gene trap mutagenesis screen for genes involved in anteroposterior axis RT development."; RL Mol. Cell. Biol. 23:8553-8562(2003). RN [8] RP INTERACTION WITH KAT5, SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=15502158; DOI=10.1074/jbc.m410487200; RA Panchenko M.V., Zhou M.I., Cohen H.T.; RT "von Hippel-Lindau partner Jade-1 is a transcriptional co-activator RT associated with histone acetyltransferase activity."; RL J. Biol. Chem. 279:56032-56041(2004). RN [9] RP TISSUE SPECIFICITY, AND FUNCTION. RX PubMed=16046545; DOI=10.1073/pnas.0500757102; RA Zhou M.I., Foy R.L., Chitalia V.C., Zhao J., Panchenko M.V., Wang H., RA Cohen H.T.; RT "Jade-1, a candidate renal tumor suppressor that promotes apoptosis."; RL Proc. Natl. Acad. Sci. U.S.A. 102:11035-11040(2005). RN [10] RP FUNCTION IN HISTONE H4 ACETYLATION, IDENTIFICATION BY MASS SPECTROMETRY, RP AND IDENTIFICATION IN THE HBO1 COMPLEX. RX PubMed=16387653; DOI=10.1016/j.molcel.2005.12.007; RA Doyon Y., Cayrou C., Ullah M., Landry A.-J., Cote V., Selleck W., RA Lane W.S., Tan S., Yang X.-J., Cote J.; RT "ING tumor suppressor proteins are critical regulators of chromatin RT acetylation required for genome expression and perpetuation."; RL Mol. Cell 21:51-64(2006). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89 AND THR-92, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18220336; DOI=10.1021/pr0705441; RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III; RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient RT phosphoproteomic analysis."; RL J. Proteome Res. 7:1346-1351(2008). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [13] RP FUNCTION, AND IDENTIFICATION IN THE HBO1 COMPLEX. RX PubMed=19187766; DOI=10.1016/j.molcel.2009.01.007; RA Saksouk N., Avvakumov N., Champagne K.S., Hung T., Doyon Y., Cayrou C., RA Paquet E., Ullah M., Landry A.J., Cote V., Yang X.J., Gozani O., RA Kutateladze T.G., Cote J.; RT "HBO1 HAT complexes target chromatin throughout gene coding regions via RT multiple PHD finger interactions with histone H3 tail."; RL Mol. Cell 33:257-265(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-92 AND SER-603, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [15] RP FUNCTION, AND IDENTIFICATION IN THE HBO1 COMPLEX. RX PubMed=20129055; DOI=10.1016/j.molcel.2009.12.012; RA Miotto B., Struhl K.; RT "HBO1 histone acetylase activity is essential for DNA replication licensing RT and inhibited by Geminin."; RL Mol. Cell 37:57-66(2010). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-603, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-603 AND SER-743, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [18] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH NPHP4. RX PubMed=22654112; DOI=10.1074/jbc.m112.385658; RA Borgal L., Habbig S., Hatzold J., Liebau M.C., Dafinger C., Sacarea I., RA Hammerschmidt M., Benzing T., Schermer B.; RT "The ciliary protein nephrocystin-4 translocates the canonical Wnt RT regulator Jade-1 to the nucleus to negatively regulate beta-catenin RT signaling."; RL J. Biol. Chem. 287:25370-25380(2012). RN [19] RP FUNCTION, AND IDENTIFICATION IN THE HBO1 COMPLEX. RX PubMed=24065767; DOI=10.1101/gad.223396.113; RA Lalonde M.E., Avvakumov N., Glass K.C., Joncas F.H., Saksouk N., RA Holliday M., Paquet E., Yan K., Tong Q., Klein B.J., Tan S., Yang X.J., RA Kutateladze T.G., Cote J.; RT "Exchange of associated factors directs a switch in HBO1 acetyltransferase RT histone tail specificity."; RL Genes Dev. 27:2009-2024(2013). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89; SER-603; SER-703 AND RP SER-743, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [21] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-114 AND LYS-573, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [22] RP INTERACTION WITH HISTONES AND KAT7. RX PubMed=29382722; DOI=10.1074/jbc.ra117.000677; RA Han J., Lachance C., Ricketts M.D., McCullough C.E., Gerace M., Black B.E., RA Cote J., Marmorstein R.; RT "The scaffolding protein JADE1 physically links the acetyltransferase RT subunit HBO1 with its histone H3-H4 substrate."; RL J. Biol. Chem. 293:4498-4509(2018). CC -!- FUNCTION: Scaffold subunit of some HBO1 complexes, which have a histone CC H4 acetyltransferase activity (PubMed:16387653, PubMed:19187766, CC PubMed:20129055, PubMed:24065767). Plays a key role in HBO1 complex by CC directing KAT7/HBO1 specificity towards histone H4 acetylation (H4K5ac, CC H4K8ac and H4K12ac), regulating DNA replication initiation, regulating CC DNA replication initiation (PubMed:20129055, PubMed:24065767). May also CC promote acetylation of nucleosomal histone H4 by KAT5 CC (PubMed:15502158). Promotes apoptosis (PubMed:16046545). May act as a CC renal tumor suppressor (PubMed:16046545). Negatively regulates CC canonical Wnt signaling; at least in part, cooperates with NPHP4 in CC this function (PubMed:22654112). {ECO:0000269|PubMed:15502158, CC ECO:0000269|PubMed:16046545, ECO:0000269|PubMed:16387653, CC ECO:0000269|PubMed:19187766, ECO:0000269|PubMed:20129055, CC ECO:0000269|PubMed:22654112, ECO:0000269|PubMed:24065767}. CC -!- SUBUNIT: Component of the HBO1 complex composed at least of ING4 or CC ING5, KAT7/HBO1, MEAF6, and one of JADE1, JADE2 and JADE3 CC (PubMed:16387653, PubMed:19187766, PubMed:20129055, PubMed:24065767, CC PubMed:29382722). Interacts with NPHP4 (PubMed:22654112). CC {ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:19187766, CC ECO:0000269|PubMed:20129055, ECO:0000269|PubMed:22654112, CC ECO:0000269|PubMed:24065767, ECO:0000269|PubMed:29382722}. CC -!- SUBUNIT: [Isoform 3]: Interacts with VHL and KAT5 (PubMed:12169691, CC PubMed:15502158). Does not associate with ING4 or ING5, and does not CC act as a component of the HBO1 complex (PubMed:19187766). CC {ECO:0000269|PubMed:12169691, ECO:0000269|PubMed:15502158, CC ECO:0000269|PubMed:19187766}. CC -!- INTERACTION: CC Q6IE81; O95251: KAT7; NbExp=4; IntAct=EBI-954672, EBI-473199; CC Q6IE81; O75161: NPHP4; NbExp=4; IntAct=EBI-954672, EBI-4281852; CC Q6IE81; Q9BW85: YJU2; NbExp=3; IntAct=EBI-954672, EBI-10300345; CC Q6IE81-3; Q96CV9: OPTN; NbExp=3; IntAct=EBI-12120084, EBI-748974; CC Q6IE81-3; Q9BW85: YJU2; NbExp=3; IntAct=EBI-12120084, EBI-10300345; CC Q6IE81-3; Q9UQR1-2: ZNF148; NbExp=3; IntAct=EBI-12120084, EBI-11742222; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15502158, CC ECO:0000269|PubMed:22654112}. Chromosome {ECO:0000269|PubMed:19187766}. CC Cytoplasm {ECO:0000269|PubMed:12169691, ECO:0000269|PubMed:15502158}. CC Cytoplasm, cytoskeleton, cilium basal body CC {ECO:0000269|PubMed:22654112}. Note=Localizes to the ciliary transition CC zone. {ECO:0000269|PubMed:22654112}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=JADE1L; CC IsoId=Q6IE81-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6IE81-2; Sequence=VSP_021045; CC Name=3; Synonyms=JADE1S; CC IsoId=Q6IE81-3; Sequence=VSP_021046, VSP_021047; CC -!- TISSUE SPECIFICITY: Highly expressed in kidney. Also present in CC pancreas, liver and heart (at protein level). Down-regulated in renal CC cancer cells. {ECO:0000269|PubMed:12169691, CC ECO:0000269|PubMed:16046545}. CC -!- DOMAIN: The 2 PHD-type zinc fingers are required for transcriptional CC activity. CC -!- SIMILARITY: Belongs to the JADE family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB15371.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAC11335.1; Type=Erroneous initiation; Note=Truncated 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; AF520952; AAM95612.1; -; mRNA. DR EMBL; AK027620; BAB55239.1; -; mRNA. DR EMBL; AK026132; BAB15371.1; ALT_INIT; mRNA. DR EMBL; AK074986; BAC11335.1; ALT_INIT; mRNA. DR EMBL; AK127326; BAC86931.1; -; mRNA. DR EMBL; AC108024; AAY40997.1; -; Genomic_DNA. DR EMBL; AC093783; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471056; EAX05171.1; -; Genomic_DNA. DR EMBL; CH471056; EAX05173.1; -; Genomic_DNA. DR EMBL; CH471056; EAX05175.1; -; Genomic_DNA. DR EMBL; CH471056; EAX05176.1; -; Genomic_DNA. DR EMBL; BC032376; AAH32376.1; -; mRNA. DR EMBL; AB058710; BAB47436.1; -; mRNA. DR EMBL; BN000287; CAE30500.1; -; mRNA. DR CCDS; CCDS34062.1; -. [Q6IE81-1] DR CCDS; CCDS47134.1; -. [Q6IE81-3] DR CCDS; CCDS75191.1; -. [Q6IE81-2] DR RefSeq; NP_001274366.1; NM_001287437.1. [Q6IE81-2] DR RefSeq; NP_001274368.1; NM_001287439.1. [Q6IE81-1] DR RefSeq; NP_001274369.1; NM_001287440.1. [Q6IE81-1] DR RefSeq; NP_001274370.1; NM_001287441.1. [Q6IE81-3] DR RefSeq; NP_001274371.1; NM_001287442.1. [Q6IE81-1] DR RefSeq; NP_001274372.1; NM_001287443.1. [Q6IE81-1] DR RefSeq; NP_079176.2; NM_024900.4. [Q6IE81-3] DR RefSeq; NP_955352.1; NM_199320.3. [Q6IE81-1] DR RefSeq; XP_005263289.1; XM_005263232.1. DR PDB; 8GDX; X-ray; 2.74 A; A=201-373. DR PDB; 8GE0; X-ray; 2.40 A; A/B/C=201-373. DR PDBsum; 8GDX; -. DR PDBsum; 8GE0; -. DR AlphaFoldDB; Q6IE81; -. DR SMR; Q6IE81; -. DR BioGRID; 123029; 124. DR ComplexPortal; CPX-718; HBO1-4.1 histone acetyltransferase complex. DR ComplexPortal; CPX-721; HBO1-5.1 histone acetyltransferase complex. DR CORUM; Q6IE81; -. DR IntAct; Q6IE81; 47. DR MINT; Q6IE81; -. DR STRING; 9606.ENSP00000226319; -. DR GlyGen; Q6IE81; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q6IE81; -. DR PhosphoSitePlus; Q6IE81; -. DR BioMuta; JADE1; -. DR DMDM; 74748786; -. DR jPOST; Q6IE81; -. DR MassIVE; Q6IE81; -. DR PaxDb; 9606-ENSP00000226319; -. DR PeptideAtlas; Q6IE81; -. DR ProteomicsDB; 66405; -. [Q6IE81-1] DR ProteomicsDB; 66406; -. [Q6IE81-2] DR ProteomicsDB; 66407; -. [Q6IE81-3] DR Pumba; Q6IE81; -. DR Antibodypedia; 16094; 227 antibodies from 28 providers. DR DNASU; 79960; -. DR Ensembl; ENST00000226319.11; ENSP00000226319.6; ENSG00000077684.16. [Q6IE81-1] DR Ensembl; ENST00000413543.6; ENSP00000404211.2; ENSG00000077684.16. [Q6IE81-3] DR Ensembl; ENST00000452328.6; ENSP00000388015.2; ENSG00000077684.16. [Q6IE81-2] DR Ensembl; ENST00000511647.5; ENSP00000423737.1; ENSG00000077684.16. [Q6IE81-3] DR Ensembl; ENST00000512960.5; ENSP00000425730.1; ENSG00000077684.16. [Q6IE81-1] DR Ensembl; ENST00000610919.4; ENSP00000483219.1; ENSG00000077684.16. [Q6IE81-1] DR Ensembl; ENST00000611140.4; ENSP00000482212.1; ENSG00000077684.16. [Q6IE81-1] DR GeneID; 79960; -. DR KEGG; hsa:79960; -. DR MANE-Select; ENST00000226319.11; ENSP00000226319.6; NM_199320.4; NP_955352.1. DR UCSC; uc003igj.5; human. [Q6IE81-1] DR AGR; HGNC:30027; -. DR CTD; 79960; -. DR DisGeNET; 79960; -. DR GeneCards; JADE1; -. DR HGNC; HGNC:30027; JADE1. DR HPA; ENSG00000077684; Low tissue specificity. DR MIM; 610514; gene. DR neXtProt; NX_Q6IE81; -. DR OpenTargets; ENSG00000077684; -. DR PharmGKB; PA134925124; -. DR VEuPathDB; HostDB:ENSG00000077684; -. DR eggNOG; KOG0954; Eukaryota. DR GeneTree; ENSGT00940000158247; -. DR HOGENOM; CLU_033303_0_0_1; -. DR InParanoid; Q6IE81; -. DR OMA; SSTCWSQ; -. DR OrthoDB; 163389at2759; -. DR PhylomeDB; Q6IE81; -. DR TreeFam; TF316118; -. DR PathwayCommons; Q6IE81; -. DR Reactome; R-HSA-3214847; HATs acetylate histones. DR SignaLink; Q6IE81; -. DR SIGNOR; Q6IE81; -. DR BioGRID-ORCS; 79960; 14 hits in 1160 CRISPR screens. DR ChiTaRS; JADE1; human. DR GeneWiki; PHF17; -. DR GenomeRNAi; 79960; -. DR Pharos; Q6IE81; Tbio. DR PRO; PR:Q6IE81; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; Q6IE81; protein. DR Bgee; ENSG00000077684; Expressed in buccal mucosa cell and 199 other cell types or tissues. DR ExpressionAtlas; Q6IE81; baseline and differential. DR GO; GO:0005813; C:centrosome; IDA:HPA. DR GO; GO:0036064; C:ciliary basal body; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:GO_Central. DR GO; GO:0000123; C:histone acetyltransferase complex; IDA:UniProtKB. DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003713; F:transcription coactivator activity; IDA:MGI. DR GO; GO:0006915; P:apoptotic process; NAS:UniProtKB. DR GO; GO:0006338; P:chromatin remodeling; IEA:GOC. DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:UniProtKB. DR GO; GO:0030308; P:negative regulation of cell growth; NAS:UniProtKB. DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IDA:MGI. DR GO; GO:0051726; P:regulation of cell cycle; IDA:ComplexPortal. DR GO; GO:0001558; P:regulation of cell growth; IDA:ComplexPortal. DR GO; GO:2000278; P:regulation of DNA biosynthetic process; IDA:ComplexPortal. DR GO; GO:0006275; P:regulation of DNA replication; IDA:ComplexPortal. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:ComplexPortal. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd15671; ePHD_JADE; 1. DR CDD; cd15679; PHD_JADE1; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2. DR InterPro; IPR019542; Enhancer_polycomb-like_N. DR InterPro; IPR034732; EPHD. DR InterPro; IPR050701; Histone_Mod_Regulator. DR InterPro; IPR039546; Jade-1_PHD. DR InterPro; IPR019786; Zinc_finger_PHD-type_CS. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR019787; Znf_PHD-finger. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR PANTHER; PTHR13793; PHD FINGER PROTEINS; 1. DR PANTHER; PTHR13793:SF79; PROTEIN JADE-1; 1. DR Pfam; PF10513; EPL1; 1. DR Pfam; PF13831; PHD_2; 1. DR Pfam; PF13832; zf-HC5HC2H_2; 1. DR SMART; SM00249; PHD; 2. DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1. DR PROSITE; PS51805; EPHD; 1. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Alternative splicing; Apoptosis; KW Cell projection; Chromosome; Cytoplasm; Cytoskeleton; Isopeptide bond; KW Metal-binding; Nucleus; Phosphoprotein; Proteomics identification; KW Reference proteome; Repeat; Transcription; Transcription regulation; KW Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..842 FT /note="Protein Jade-1" FT /id="PRO_0000253529" FT ZN_FING 203..253 FT /note="PHD-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146" FT ZN_FING 255..289 FT /note="C2HC pre-PHD-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146" FT ZN_FING 313..369 FT /note="PHD-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146" FT REGION 1..43 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 60..80 FT /note="Interaction with KAT7/HBO1 and histones" FT /evidence="ECO:0000269|PubMed:29382722" FT REGION 80..188 FT /note="Interaction with histones" FT /evidence="ECO:0000269|PubMed:29382722" FT REGION 366..398 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 589..613 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 678..715 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 787..825 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 11..31 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 678..693 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 694..709 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 787..802 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 89 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:23186163" FT MOD_RES 92 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18220336, FT ECO:0007744|PubMed:19690332" FT MOD_RES 603 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 609 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q6ZPI0" FT MOD_RES 703 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 743 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT CROSSLNK 114 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 573 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 99..110 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_021045" FT VAR_SEQ 503..509 FT /note="RNLTYMV -> MIDTDTL (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12169691, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334" FT /id="VSP_021046" FT VAR_SEQ 510..842 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12169691, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334" FT /id="VSP_021047" FT VARIANT 662 FT /note="N -> S (in dbSNP:rs6855813)" FT /id="VAR_053777" FT TURN 207..209 FT /evidence="ECO:0007829|PDB:8GE0" FT STRAND 220..222 FT /evidence="ECO:0007829|PDB:8GE0" FT TURN 224..226 FT /evidence="ECO:0007829|PDB:8GE0" FT STRAND 229..231 FT /evidence="ECO:0007829|PDB:8GE0" FT HELIX 232..235 FT /evidence="ECO:0007829|PDB:8GE0" FT HELIX 248..251 FT /evidence="ECO:0007829|PDB:8GE0" FT STRAND 257..260 FT /evidence="ECO:0007829|PDB:8GDX" FT STRAND 264..271 FT /evidence="ECO:0007829|PDB:8GE0" FT STRAND 277..279 FT /evidence="ECO:0007829|PDB:8GE0" FT HELIX 280..285 FT /evidence="ECO:0007829|PDB:8GE0" FT STRAND 290..293 FT /evidence="ECO:0007829|PDB:8GDX" FT TURN 294..296 FT /evidence="ECO:0007829|PDB:8GE0" FT STRAND 298..301 FT /evidence="ECO:0007829|PDB:8GDX" FT HELIX 303..305 FT /evidence="ECO:0007829|PDB:8GE0" FT HELIX 308..312 FT /evidence="ECO:0007829|PDB:8GE0" FT TURN 316..318 FT /evidence="ECO:0007829|PDB:8GE0" FT HELIX 339..344 FT /evidence="ECO:0007829|PDB:8GE0" FT STRAND 348..353 FT /evidence="ECO:0007829|PDB:8GE0" FT STRAND 359..364 FT /evidence="ECO:0007829|PDB:8GE0" FT HELIX 366..368 FT /evidence="ECO:0007829|PDB:8GE0" SQ SEQUENCE 842 AA; 95533 MW; 239FC2229CE25FFD CRC64; MKRGRLPSSS EDSDDNGSLS TTWSQNSRSQ HRRSSCSRHE DRKPSEVFRT DLITAMKLHD SYQLNPDEYY VLADPWRQEW EKGVQVPVSP GTIPQPVARV VSEEKSLMFI RPKKYIVSSG SEPPELGYVD IRTLADSVCR YDLNDMDAAW LELTNEEFKE MGMPELDEYT MERVLEEFEQ RCYDNMNHAI ETEEGLGIEY DEDVVCDVCQ SPDGEDGNEM VFCDKCNICV HQACYGILKV PEGSWLCRTC ALGVQPKCLL CPKKGGAMKP TRSGTKWVHV SCALWIPEVS IGSPEKMEPI TKVSHIPSSR WALVCSLCNE KFGASIQCSV KNCRTAFHVT CAFDRGLEMK TILAENDEVK FKSYCPKHSS HRKPEESLGK GAAQENGAPE CSPRNPLEPF ASLEQNREEA HRVSVRKQKL QQLEDEFYTF VNLLDVARAL RLPEEVVDFL YQYWKLKRKV NFNKPLITPK KDEEDNLAKR EQDVLFRRLQ LFTHLRQDLE RVRNLTYMVT RREKIKRSVC KVQEQIFNLY TKLLEQERVS GVPSSCSSSS LENMLLFNSP SVGPDAPKIE DLKWHSAFFR KQMGTSLVHS LKKPHKRDPL QNSPGSEGKT LLKQPDLCGR REGMVVPESF LGLEKTFAEA RLISAQQKNG VVMPDHGKRR DNRFHCDLIK GDLKDKSFKQ SHKPLRSTDV SQRHLDNTRA ATSPGVGQSA PGTRKEIVPK CNGSLIKVNY NQTAVKVPTT PASPVKNWGG FRIPKKGERQ QQGEAHDGAC HQHSDYPYLG LGRVPAKERA KSKLKSDNEN DGYVPDVEMS DSESEASEKK CIHTSSTISR RTDIIRRSIL AS //