JADE3_MOUSE
ID JADE3_MOUSE Reviewed; 823 AA.
AC Q6IE82; A1L3T5; Q6ZQG2;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein Jade-3;
DE AltName: Full=Jade family PHD finger protein 3;
DE AltName: Full=PHD finger protein 16;
GN Name=Jade3; Synonyms=Kiaa0215, Phf16;
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].
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].
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 [3]
RP IDENTIFICATION.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-578; SER-774 AND SER-776, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Spleen, and Testis;
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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-32; LYS-35; LYS-601 AND LYS-735,
RP AND 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).
CC -!- FUNCTION: Scaffold subunit of some HBO1 complexes, which have a histone
CC H4 acetyltransferase activity. {ECO:0000250|UniProtKB:Q92613}.
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.
CC {ECO:0000250|UniProtKB:Q92613}.
CC -!- SIMILARITY: Belongs to the JADE family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC97901.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK129091; BAC97901.1; ALT_FRAME; mRNA.
DR EMBL; BC130270; AAI30271.1; -; mRNA.
DR EMBL; BN000286; CAE30499.1; -; mRNA.
DR RefSeq; NP_955021.2; NM_199317.2.
DR AlphaFoldDB; Q6IE82; -.
DR SMR; Q6IE82; -.
DR BioGRID; 238277; 2.
DR ComplexPortal; CPX-796; HBO1-4.3 histone acetyltransferase complex.
DR ComplexPortal; CPX-799; HBO1-5.3 histone acetyltransferase complex.
DR IntAct; Q6IE82; 1.
DR MINT; Q6IE82; -.
DR STRING; 10090.ENSMUSP00000111042; -.
DR iPTMnet; Q6IE82; -.
DR PhosphoSitePlus; Q6IE82; -.
DR MaxQB; Q6IE82; -.
DR PaxDb; Q6IE82; -.
DR PeptideAtlas; Q6IE82; -.
DR PRIDE; Q6IE82; -.
DR ProteomicsDB; 269112; -.
DR Antibodypedia; 416; 108 antibodies from 20 providers.
DR DNASU; 382207; -.
DR Ensembl; ENSMUST00000043693; ENSMUSP00000048529; ENSMUSG00000037315.
DR GeneID; 382207; -.
DR KEGG; mmu:382207; -.
DR UCSC; uc009ssz.2; mouse.
DR CTD; 9767; -.
DR MGI; MGI:2148019; Jade3.
DR VEuPathDB; HostDB:ENSMUSG00000037315; -.
DR eggNOG; KOG0954; Eukaryota.
DR GeneTree; ENSGT00940000158722; -.
DR HOGENOM; CLU_016215_1_0_1; -.
DR InParanoid; Q6IE82; -.
DR OMA; EFHRGQP; -.
DR OrthoDB; 1235709at2759; -.
DR PhylomeDB; Q6IE82; -.
DR Reactome; R-MMU-3214847; HATs acetylate histones.
DR BioGRID-ORCS; 382207; 3 hits in 77 CRISPR screens.
DR PRO; PR:Q6IE82; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q6IE82; protein.
DR Bgee; ENSMUSG00000037315; Expressed in placenta labyrinth and 194 other tissues.
DR ExpressionAtlas; Q6IE82; baseline and differential.
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: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: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: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 CDD; cd15681; PHD_JADE3; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR019542; Enhancer_polycomb-like_N.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR039550; JADE3_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; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW Zinc; Zinc-finger.
FT CHAIN 1..823
FT /note="Protein Jade-3"
FT /id="PRO_0000253534"
FT ZN_FING 200..250
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 252..286
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 310..366
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..585
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 756..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..577
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..625
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..810
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 30
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92613"
FT MOD_RES 32
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 35
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92613"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 601
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92613"
FT MOD_RES 638
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92613"
FT MOD_RES 735
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 774
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 776
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 823 AA; 93455 MW; E3841F26478D703A CRC64;
MKRHRPVSSS ESSDECPSTS FTSSSMYRKK SKNPKEQKKS AEVFRKDLIS AMKIPDSHHV
NPDSYYLFTD TWKEEWEKGV QVPANPDSVP TPSLRIISEK VKEMLFVRPR KYIRCSSPES
AEPGYINTLE QAASTCRYDL DDMDIFWLQE LNEDLGEMGY GPIDETLMEK TIEVLERHCH
ENMNHAIETV EGLGIEYDED VICDVCRSPD SEEGNDMVFC DKCNVCVHQA CYGILKIPEG
SWLCRSCVLG IYPQCVLCPK KGGAMKTTRT GTKWAHVSCA LWIPEVSIAC PERMEPVTKI
SHIPPSRWAL VCNLCKLKTG ACIQCSVKSC ITAFHVTCAF EHGLEMKTIL DEGDEVKFKS
FCLKHSQNKP KLGDAEYHHH RVAEQSQAKS EKTSLRAQKL RELEEEFYTL VQVEDVAKEM
ELSAFTVDFI YNYWKLKRKS NFNKPLIPPK EEEENGLVQP KEESIHTRMR MFMHLRQDLE
RVRNLCYMIS RREKLKLSHT KVQEQIFGLQ VQLINEEITE GLSLTNALEN SLFYPPPRIT
LKLKMPKSTS EDCKDSSTET EHQLSSPGSS SPGHSKRSPQ MPEEPLDMNV KIYPRYPLES
KSNCLQTSRS HSRCETKSSS PTPRAPSAEF YHGQSLGKPL ALQAALHGQV SIGNGKNQPN
SRVSSSNGLE GNWSGNITQK VNSSEVCYDQ ESMLSSHLPS PGNIRKSSME HFSRSFKEAT
NTWVKPTEDL QYCVKPTKNV SSKEQLWGRQ LLRRPTGRAS YQETDGYCPD LEPSDSEAEG
EGSKETPRVK RESSDRENPS HDSARECHGK TKTHPHSHSS MQR
