JADE1_MOUSE
ID JADE1_MOUSE Reviewed; 834 AA.
AC Q6ZPI0; Q6IE84; Q8C7S6; Q8CFM2; Q8R362;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 139.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [4]
RP IDENTIFICATION, ALTERNATIVE SPLICING, DEVELOPMENTAL STAGE, SUBCELLULAR
RP LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=C57BL/6J;
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 [5]
RP TISSUE SPECIFICITY.
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-609, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Scaffold subunit of some HBO1 complexes, which have a histone
CC H4 acetyltransferase activity. 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. May also promote acetylation of nucleosomal
CC histone H4 by KAT5. Promotes apoptosis. May act as a renal tumor
CC suppressor. Negatively regulates canonical Wnt signaling; at least in
CC part, cooperates with NPHP4 in this function.
CC {ECO:0000250|UniProtKB:Q6IE81}.
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. Interacts
CC with NPHP4. {ECO:0000250|UniProtKB:Q6IE81}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q6IE81}.
CC Chromosome {ECO:0000250|UniProtKB:Q6IE81}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q6IE81}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:Q6IE81}. Note=Localizes to the ciliary
CC transition zone. {ECO:0000250|UniProtKB:Q6IE81}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Jade1L;
CC IsoId=Q6ZPI0-1; Sequence=Displayed;
CC Name=2; Synonyms=Jade1S;
CC IsoId=Q6ZPI0-2; Sequence=VSP_021048, VSP_021049;
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney. Also present in liver
CC (at protein level). {ECO:0000269|PubMed:12169691}.
CC -!- DEVELOPMENTAL STAGE: Expressed from 6.5 dpc. From 12.5 to 15.5 dpc,
CC expressed in the nervous system and developing muscles.
CC {ECO:0000269|PubMed:14612400}.
CC -!- DOMAIN: The 2 PHD-type zinc fingers are required for transcriptional
CC activity. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable and fertile, and show no visible
CC phenotype. {ECO:0000269|PubMed:14612400}.
CC -!- SIMILARITY: Belongs to the JADE family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH26471.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC98255.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK129445; BAC98255.1; ALT_INIT; mRNA.
DR EMBL; AK049332; BAC33688.1; -; mRNA.
DR EMBL; AK147466; BAE27932.1; -; mRNA.
DR EMBL; BC020316; AAH20316.1; -; mRNA.
DR EMBL; BC026471; AAH26471.1; ALT_INIT; mRNA.
DR EMBL; BN000282; CAE30497.1; -; mRNA.
DR EMBL; BN000281; CAE30496.1; -; mRNA.
DR CCDS; CCDS17331.1; -. [Q6ZPI0-1]
DR RefSeq; NP_001123656.1; NM_001130184.1. [Q6ZPI0-1]
DR RefSeq; NP_001123657.1; NM_001130185.1. [Q6ZPI0-1]
DR RefSeq; NP_001123658.1; NM_001130186.1. [Q6ZPI0-1]
DR RefSeq; NP_758507.3; NM_172303.4. [Q6ZPI0-1]
DR AlphaFoldDB; Q6ZPI0; -.
DR SMR; Q6ZPI0; -.
DR BioGRID; 234652; 10.
DR ComplexPortal; CPX-794; HBO1-4.1 histone acetyltransferase complex.
DR ComplexPortal; CPX-797; HBO1-5.1 histone acetyltransferase complex.
DR IntAct; Q6ZPI0; 6.
DR STRING; 10090.ENSMUSP00000128152; -.
DR iPTMnet; Q6ZPI0; -.
DR PhosphoSitePlus; Q6ZPI0; -.
DR EPD; Q6ZPI0; -.
DR jPOST; Q6ZPI0; -.
DR MaxQB; Q6ZPI0; -.
DR PaxDb; Q6ZPI0; -.
DR PeptideAtlas; Q6ZPI0; -.
DR PRIDE; Q6ZPI0; -.
DR ProteomicsDB; 269356; -. [Q6ZPI0-1]
DR ProteomicsDB; 269357; -. [Q6ZPI0-2]
DR Antibodypedia; 16094; 190 antibodies from 28 providers.
DR DNASU; 269424; -.
DR Ensembl; ENSMUST00000026865; ENSMUSP00000026865; ENSMUSG00000025764. [Q6ZPI0-1]
DR Ensembl; ENSMUST00000163764; ENSMUSP00000128152; ENSMUSG00000025764. [Q6ZPI0-1]
DR Ensembl; ENSMUST00000168086; ENSMUSP00000131441; ENSMUSG00000025764. [Q6ZPI0-1]
DR Ensembl; ENSMUST00000170711; ENSMUSP00000127113; ENSMUSG00000025764. [Q6ZPI0-1]
DR Ensembl; ENSMUST00000191952; ENSMUSP00000141499; ENSMUSG00000025764. [Q6ZPI0-2]
DR GeneID; 269424; -.
DR KEGG; mmu:269424; -.
DR UCSC; uc008pcj.2; mouse. [Q6ZPI0-1]
DR CTD; 79960; -.
DR MGI; MGI:1925835; Jade1.
DR VEuPathDB; HostDB:ENSMUSG00000025764; -.
DR eggNOG; KOG0954; Eukaryota.
DR GeneTree; ENSGT00940000158247; -.
DR HOGENOM; CLU_016215_0_0_1; -.
DR InParanoid; Q6ZPI0; -.
DR OMA; SSTCWSQ; -.
DR PhylomeDB; Q6ZPI0; -.
DR TreeFam; TF316118; -.
DR Reactome; R-MMU-3214847; HATs acetylate histones.
DR BioGRID-ORCS; 269424; 4 hits in 78 CRISPR screens.
DR ChiTaRS; Jade1; mouse.
DR PRO; PR:Q6ZPI0; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q6ZPI0; protein.
DR Bgee; ENSMUSG00000025764; Expressed in lacrimal gland and 240 other tissues.
DR ExpressionAtlas; Q6ZPI0; baseline and differential.
DR Genevisible; Q6ZPI0; MM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0036064; C:ciliary basal body; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0043966; P:histone H3 acetylation; ISS:UniProtKB.
DR GO; GO:0043983; P:histone H4-K12 acetylation; ISS:UniProtKB.
DR GO; GO:0043981; P:histone H4-K5 acetylation; ISS:UniProtKB.
DR GO; GO:0043982; P:histone H4-K8 acetylation; ISS:UniProtKB.
DR GO; GO:0016570; P:histone modification; ISO:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:0001558; P:regulation of cell growth; ISO:MGI.
DR GO; GO:2000278; P:regulation of DNA biosynthetic process; ISO:MGI.
DR GO; GO:0006275; P:regulation of DNA replication; ISO:MGI.
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; ISO:MGI.
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..834
FT /note="Protein Jade-1"
FT /id="PRO_0000253530"
FT ZN_FING 204..254
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 256..290
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 314..370
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 61..81
FT /note="Interaction with KAT7/HBO1 and histones"
FT /evidence="ECO:0000250|UniProtKB:Q6IE81"
FT REGION 81..189
FT /note="Interaction with histones"
FT /evidence="ECO:0000250|UniProtKB:Q6IE81"
FT REGION 367..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 676..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..819
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..694
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 695..710
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..765
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..794
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..818
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IE81"
FT MOD_RES 93
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6IE81"
FT MOD_RES 603
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IE81"
FT MOD_RES 609
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 704
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IE81"
FT MOD_RES 735
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IE81"
FT CROSSLNK 115
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6IE81"
FT CROSSLNK 573
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6IE81"
FT VAR_SEQ 504..510
FT /note="RNLTYMV -> MIDTDTL (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_021048"
FT VAR_SEQ 511..834
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_021049"
FT CONFLICT 190
FT /note="A -> D (in Ref. 2; BAC33688)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 834 AA; 93897 MW; 43388FC7103D97D6 CRC64;
MKRGRLPSSS EDSDDNGSLS TTWSQHSRSQ HGRSSTCSRP EDRKPSEVFR TDLITAMKLH
DSYQLNPDDY YVLADPWRQE WEKGVQVPVS PGTIPQPVAR VVSEEKSLMF IRPKKYIASS
GSEPPALGYV DIRTLADSVC RYDLNDMDAA WLEVTNEEFK EMGMPELDEY TMERVLEEFE
QRCYDNMNHA IETEEGLGIE YDEDVVCDVC QSPDGEDGNE MVFCDKCNIC VHQACYGILK
VPEGSWLCRT CALGVQPKCL LCPKKGGAMK PTRSGTKWVH VSCALWIPEV SIGSPEKMEP
ITKVSHIPSS RWALVCSLCN EKFGASIQCS VKNCRTAFHV TCAFDRGLEM KTILAENDEV
KFKSYCPKHS SHRKPEEGLG EGAAQENGAP ESSPQSPLEP YGSLEPNREE AHRVSVRKQK
LQQLEDEFYT FVNLLDVARA LRLPEEVVDF LYQYWKLKRK INFNKPLITP KKDEEDNLAK
REQDVLFRRL QLFTHLRQDL ERVRNLTYMV TRREKIKRSV CKVQEQIFTQ YTKLLEQEKV
SGVPSSCSSA LENMLFFNSP SVGPNAPKIE DLKWHSAFFR KQMGTSLVHP LKKSHKRDAV
QNSSGTEGKT SHKQPGLCGR REGLEVSESL LSLEKTFAEA RLLSSAQQKN GVVTPDHGKR
RDNRFHCDLV KGDLKDKSFK QSHKPLRSTD TSQRHLDNTR AATSPGVGQS APGTRKEIVP
KCNGSLVKVP ITPASPVKSW GGFRIPKKGE RQQQGEAHDG ACHQHSDCSH LGVSRAPAKE
RAKSRLRADS ENDGYAPDGE MSDSESEASE KKCIHASSTI SRRTDIIRRS ILAS
