JADE2_MOUSE
ID JADE2_MOUSE Reviewed; 829 AA.
AC Q6ZQF7; Q3UHD5; Q6IE83;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=E3 ubiquitin-protein ligase Jade-2 {ECO:0000303|PubMed:25018020};
DE EC=2.3.2.27 {ECO:0000269|PubMed:25018020};
DE AltName: Full=Jade family PHD finger protein 2;
DE AltName: Full=PHD finger protein 15;
GN Name=Jade2; Synonyms=Kiaa0239, Phf15;
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; TISSUE=Brain;
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).
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 (ISOFORM 2).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-32; LYS-38 AND LYS-298, AND
RP IDENTIFICATION BY MASS 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).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH KDM1A, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=25018020; DOI=10.1016/j.molcel.2014.06.006;
RA Han X., Gui B., Xiong C., Zhao L., Liang J., Sun L., Yang X., Yu W., Si W.,
RA Yan R., Yi X., Zhang D., Li W., Li L., Yang J., Wang Y., Sun Y.E.,
RA Zhang D., Meng A., Shang Y.;
RT "Destabilizing LSD1 by Jade-2 promotes neurogenesis: an antibraking system
RT in neural development.";
RL Mol. Cell 55:482-494(2014).
CC -!- FUNCTION: Scaffold subunit of some HBO1 complexes, which have a histone
CC H4 acetyltransferase activity (By similarity). Acts as a E3 ubiquitin-
CC protein ligase mediating the ubiquitination and subsequent proteasomal
CC degradation of target protein histone demethylase KDM1A
CC (PubMed:25018020). Also acts as a ubiquitin ligase E3 toward itself
CC (PubMed:25018020). Positive regulator of neurogenesis
CC (PubMed:25018020). {ECO:0000250|UniProtKB:Q9NQC1,
CC ECO:0000269|PubMed:25018020}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:25018020};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000305|PubMed:25018020}.
CC -!- SUBUNIT: Component of the HBO1 complex composed at least of ING4 or
CC ING5, MYST2/HBO1, MEAF6, and one of JADE1, JADE2 and JADE3 (By
CC similarity). Interacts (via C-terminus) with KDM1A (via AOD/Tower
CC domain) (PubMed:25018020). {ECO:0000250|UniProtKB:Q9NQC1,
CC ECO:0000269|PubMed:25018020}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ZQF7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZQF7-2; Sequence=VSP_021052, VSP_021053;
CC -!- DOMAIN: The first PHD domain is essential for its E3 ubiquitin ligase
CC activity. {ECO:0000250|UniProtKB:Q9NQC1}.
CC -!- DISRUPTION PHENOTYPE: Strongly decreased level of KDM1A
CC polyubiquitination resulting in increased level of KDM1A protein.
CC Decelerated emergence of neural progenitors and mature neurons.
CC Embryonic stem cells grow in aggregates with smoother-edged, rounder-
CC shaped cell clones and fail to organize in rosettes with surrounding
CC cells exhibiting neuronal morphology with extensive arborization.
CC Decreased expression of neural markers. {ECO:0000269|PubMed:25018020}.
CC -!- SIMILARITY: Belongs to the JADE family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC97907.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK129097; BAC97907.1; ALT_INIT; mRNA.
DR EMBL; AK147453; BAE27922.1; -; mRNA.
DR EMBL; BC117856; AAI17857.1; -; mRNA.
DR EMBL; BC117857; AAI17858.1; -; mRNA.
DR EMBL; BN000285; CAE30498.1; -; mRNA.
DR CCDS; CCDS24662.1; -. [Q6ZQF7-1]
DR RefSeq; NP_955003.2; NM_199299.3. [Q6ZQF7-1]
DR RefSeq; XP_006534532.1; XM_006534469.3. [Q6ZQF7-1]
DR RefSeq; XP_006534533.1; XM_006534470.3. [Q6ZQF7-1]
DR RefSeq; XP_011247611.1; XM_011249309.2. [Q6ZQF7-1]
DR RefSeq; XP_017170321.1; XM_017314832.1. [Q6ZQF7-1]
DR AlphaFoldDB; Q6ZQF7; -.
DR SMR; Q6ZQF7; -.
DR BioGRID; 218388; 3.
DR ComplexPortal; CPX-795; HBO1-4.2 histone acetyltransferase complex.
DR ComplexPortal; CPX-798; HBO1-5.2 histone acetyltransferase complex.
DR STRING; 10090.ENSMUSP00000020655; -.
DR iPTMnet; Q6ZQF7; -.
DR PhosphoSitePlus; Q6ZQF7; -.
DR EPD; Q6ZQF7; -.
DR jPOST; Q6ZQF7; -.
DR MaxQB; Q6ZQF7; -.
DR PaxDb; Q6ZQF7; -.
DR PRIDE; Q6ZQF7; -.
DR ProteomicsDB; 269024; -. [Q6ZQF7-1]
DR ProteomicsDB; 269025; -. [Q6ZQF7-2]
DR Antibodypedia; 14678; 48 antibodies from 12 providers.
DR DNASU; 76901; -.
DR Ensembl; ENSMUST00000020655; ENSMUSP00000020655; ENSMUSG00000020387. [Q6ZQF7-1]
DR Ensembl; ENSMUST00000109091; ENSMUSP00000104719; ENSMUSG00000020387. [Q6ZQF7-1]
DR GeneID; 76901; -.
DR KEGG; mmu:76901; -.
DR UCSC; uc007iuq.1; mouse. [Q6ZQF7-1]
DR CTD; 23338; -.
DR MGI; MGI:1924151; Jade2.
DR VEuPathDB; HostDB:ENSMUSG00000020387; -.
DR eggNOG; KOG0954; Eukaryota.
DR GeneTree; ENSGT00940000158570; -.
DR HOGENOM; CLU_016215_2_0_1; -.
DR InParanoid; Q6ZQF7; -.
DR OMA; RKANGNQ; -.
DR OrthoDB; 1235709at2759; -.
DR PhylomeDB; Q6ZQF7; -.
DR TreeFam; TF316118; -.
DR Reactome; R-MMU-3214847; HATs acetylate histones.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 76901; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Jade2; mouse.
DR PRO; PR:Q6ZQF7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q6ZQF7; protein.
DR Bgee; ENSMUSG00000020387; Expressed in primary oocyte and 195 other tissues.
DR ExpressionAtlas; Q6ZQF7; baseline and differential.
DR Genevisible; Q6ZQF7; MM.
DR GO; GO:0000123; C:histone acetyltransferase complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
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:1990138; P:neuron projection extension; IGI:MGI.
DR GO; GO:0050769; P:positive regulation of neurogenesis; IDA:MGI.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:0001558; P:regulation of cell growth; IC:ComplexPortal.
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:0050767; P:regulation of neurogenesis; IGI: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; IC:ComplexPortal.
DR GO; GO:0060395; P:SMAD protein signal transduction; IDA:MGI.
DR CDD; cd15705; ePHD_JADE2; 1.
DR CDD; cd15680; PHD_JADE2; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR039549; JADE2_ePHD.
DR InterPro; IPR039548; JADE2_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 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; Alternative splicing; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..829
FT /note="E3 ubiquitin-protein ligase Jade-2"
FT /id="PRO_0000253533"
FT ZN_FING 199..249
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 251..285
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 309..365
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..553
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQC1"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NQC1"
FT MOD_RES 32
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 38
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 298
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT VAR_SEQ 103
FT /note="V -> VSWAARGGQAKASLFITTILFP (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_021052"
FT VAR_SEQ 518..561
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_021053"
SQ SEQUENCE 829 AA; 92174 MW; 0B5B6275F7BD6769 CRC64;
MEEKRRKYSI SSDNSDTTDG HVTSTSASRC SKLPSSTKSG WPRQNEKKPS EVFRTDLITA
MKIPDSYQLS PDDYYILADP WRQEWEKGVQ VPAGAEAIPE PVVRLLPPLK GPPTQMSPDS
PTLGEGAHPD WPGGSRYDLD EIDAYWLELL NSELKEMEKP ELDELTLERV LEELETLCHQ
NMAQAIETQE GLGIEYDEDV VCDVCRSPEG EDGNEMVFCD KCNVCVHQAC YGILKVPTGS
WLCRTCALGV QPKCLLCPKR GGALKPTRSG TKWVHVSCAL WIPEVSIGCP EKMEPITKIS
HIPASRWALS CSLCKECTGT CIQCSMPSCI TAFHVTCAFD RGLEMRTILA DNDEVKFKSL
CQEHSDGGPR SEPTSEPVEP SQAVEDLEKV TLRKQRLQQL EENFYELVEP AEVAERLDLA
EALVDFIYQY WKLKRRANAN QPLLTPKTDE VDNLAQQEQD VLYRRLKLFT HLRQDLERVR
NLCYMVTRRE RTKHTICKLQ EQIFHLQMKL IEQDLCREPS GRRSKGKKND SKRKGREGPK
GSSPEKKEKV KAGPESVLGQ LGLSTSFPID GTFFNSWLAQ SVQITAEDMA MSEWSLNSGH
REDPAPGLLS EELLQDEETL LSFMRDPSLR PGDPARKARG RTRLPAKKKP SPLQDGPSAR
TTPDKQPKKA WAQDGKGTQG PPMRKPPRRT SSHLPSSPAA GDCPVPATLE SPPPLASEIL
DKTAPMASDL NVQVPGPTVS PKPLGRLRPP REMKVSRKSP GARSDAGTGL PSAVAERPKV
SLHFDTEADG YFSDEEMSDS EVEAEDSGVQ RASREAGAEE VVRMGVLAS
