JADE1_HUMAN
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 03-AUG-2022, entry version 152.
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=2; 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};
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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. [Q6IE81-1]
DR AlphaFoldDB; Q6IE81; -.
DR SMR; Q6IE81; -.
DR BioGRID; 123029; 116.
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; 41.
DR MINT; Q6IE81; -.
DR STRING; 9606.ENSP00000226319; -.
DR iPTMnet; Q6IE81; -.
DR PhosphoSitePlus; Q6IE81; -.
DR BioMuta; JADE1; -.
DR DMDM; 74748786; -.
DR EPD; Q6IE81; -.
DR jPOST; Q6IE81; -.
DR MassIVE; Q6IE81; -.
DR MaxQB; Q6IE81; -.
DR PaxDb; Q6IE81; -.
DR PeptideAtlas; Q6IE81; -.
DR PRIDE; Q6IE81; -.
DR ProteomicsDB; 66405; -. [Q6IE81-1]
DR ProteomicsDB; 66406; -. [Q6IE81-2]
DR ProteomicsDB; 66407; -. [Q6IE81-3]
DR Antibodypedia; 16094; 190 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 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; 1235709at2759; -.
DR PhylomeDB; Q6IE81; -.
DR TreeFam; TF316118; -.
DR PathwayCommons; Q6IE81; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; Q6IE81; -.
DR BioGRID-ORCS; 79960; 14 hits in 1081 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 197 other tissues.
DR ExpressionAtlas; Q6IE81; baseline and differential.
DR Genevisible; Q6IE81; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
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:ComplexPortal.
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:0043966; P:histone H3 acetylation; IDA:UniProtKB.
DR GO; GO:0043983; P:histone H4-K12 acetylation; IDA:UniProtKB.
DR GO; GO:0043981; P:histone H4-K5 acetylation; IDA:UniProtKB.
DR GO; GO:0043982; P:histone H4-K8 acetylation; IDA:UniProtKB.
DR GO; GO:0016570; P:histone modification; IDA:ComplexPortal.
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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:ComplexPortal.
DR CDD; cd15679; PHD_JADE1; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
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 Pfam; PF10513; EPL1; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF57903; SSF57903; 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 Acetylation; Activator; Alternative splicing; Apoptosis; Cell projection;
KW Chromosome; Cytoplasm; Cytoskeleton; Isopeptide bond; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; 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"
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
