ZZZ3_MOUSE
ID ZZZ3_MOUSE Reviewed; 910 AA.
AC Q6KAQ7; Q3TMK6; Q3V189;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=ZZ-type zinc finger-containing protein 3;
GN Name=Zzz3;
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).
RC TISSUE=Embryonic tail;
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Head, and Lung;
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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-401, 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: Histone H3 reader that is required for the ATAC complex-
CC mediated maintenance of histone acetylation and gene activation (By
CC similarity). Component of the ATAC complex, a complex with histone
CC acetyltransferase activity on histones H3 and H4 (By similarity).
CC {ECO:0000250|UniProtKB:Q8IYH5}.
CC -!- SUBUNIT: Component of the ADA2A-containing complex (ATAC), composed of
CC KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1
CC (By similarity). Interacts via (ZZ-type zinc finger) with histone H3 in
CC a methylation-independent manner and acetylation on 'Lys-4' (H3K4ac)
CC moderately enhances the interaction (By similarity).
CC {ECO:0000250|UniProtKB:Q8IYH5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6KAQ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6KAQ7-2; Sequence=VSP_025514, VSP_025517;
CC Name=3;
CC IsoId=Q6KAQ7-3; Sequence=VSP_025515, VSP_025516, VSP_025518;
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DR EMBL; AK131150; BAD21400.1; -; mRNA.
DR EMBL; AK132612; BAE21262.1; -; mRNA.
DR EMBL; AK165882; BAE38435.1; -; mRNA.
DR CCDS; CCDS38674.1; -. [Q6KAQ7-1]
DR CCDS; CCDS84698.1; -. [Q6KAQ7-2]
DR RefSeq; NP_001074224.1; NM_001080755.2. [Q6KAQ7-1]
DR RefSeq; NP_001333584.1; NM_001346655.1. [Q6KAQ7-2]
DR RefSeq; XP_006500911.1; XM_006500848.3. [Q6KAQ7-1]
DR RefSeq; XP_006500913.1; XM_006500850.3. [Q6KAQ7-1]
DR RefSeq; XP_006500914.1; XM_006500851.3.
DR RefSeq; XP_006500919.1; XM_006500856.3. [Q6KAQ7-3]
DR RefSeq; XP_006500920.1; XM_006500857.3. [Q6KAQ7-2]
DR RefSeq; XP_017174912.1; XM_017319423.1. [Q6KAQ7-1]
DR AlphaFoldDB; Q6KAQ7; -.
DR SMR; Q6KAQ7; -.
DR BioGRID; 224485; 2.
DR ComplexPortal; CPX-1025; GCN5-containing ATAC complex.
DR ComplexPortal; CPX-1029; PCAF-containing ATAC complex.
DR IntAct; Q6KAQ7; 3.
DR MINT; Q6KAQ7; -.
DR STRING; 10090.ENSMUSP00000101706; -.
DR iPTMnet; Q6KAQ7; -.
DR PhosphoSitePlus; Q6KAQ7; -.
DR EPD; Q6KAQ7; -.
DR MaxQB; Q6KAQ7; -.
DR PaxDb; Q6KAQ7; -.
DR PeptideAtlas; Q6KAQ7; -.
DR PRIDE; Q6KAQ7; -.
DR ProteomicsDB; 275327; -. [Q6KAQ7-1]
DR ProteomicsDB; 275328; -. [Q6KAQ7-2]
DR ProteomicsDB; 275329; -. [Q6KAQ7-3]
DR Antibodypedia; 33487; 93 antibodies from 24 providers.
DR DNASU; 108946; -.
DR Ensembl; ENSMUST00000106100; ENSMUSP00000101706; ENSMUSG00000039068. [Q6KAQ7-1]
DR Ensembl; ENSMUST00000106101; ENSMUSP00000101707; ENSMUSG00000039068. [Q6KAQ7-1]
DR Ensembl; ENSMUST00000106103; ENSMUSP00000101709; ENSMUSG00000039068. [Q6KAQ7-2]
DR Ensembl; ENSMUST00000200570; ENSMUSP00000143693; ENSMUSG00000039068. [Q6KAQ7-3]
DR GeneID; 108946; -.
DR KEGG; mmu:108946; -.
DR UCSC; uc008rtm.1; mouse. [Q6KAQ7-2]
DR UCSC; uc008rtn.2; mouse. [Q6KAQ7-1]
DR UCSC; uc012czm.1; mouse. [Q6KAQ7-3]
DR CTD; 26009; -.
DR MGI; MGI:1920453; Zzz3.
DR VEuPathDB; HostDB:ENSMUSG00000039068; -.
DR eggNOG; ENOG502QS4F; Eukaryota.
DR GeneTree; ENSGT00390000005307; -.
DR HOGENOM; CLU_034414_0_0_1; -.
DR InParanoid; Q6KAQ7; -.
DR OMA; NCDDCQL; -.
DR OrthoDB; 139813at2759; -.
DR PhylomeDB; Q6KAQ7; -.
DR TreeFam; TF106396; -.
DR BioGRID-ORCS; 108946; 23 hits in 75 CRISPR screens.
DR ChiTaRS; Zzz3; mouse.
DR PRO; PR:Q6KAQ7; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q6KAQ7; protein.
DR Bgee; ENSMUSG00000039068; Expressed in cleaving embryo and 255 other tissues.
DR ExpressionAtlas; Q6KAQ7; baseline and differential.
DR Genevisible; Q6KAQ7; MM.
DR GO; GO:0140672; C:ATAC complex; IDA:ComplexPortal.
DR GO; GO:0072686; C:mitotic spindle; IC:ComplexPortal.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0070577; F:lysine-acetylated histone binding; ISS:UniProtKB.
DR GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043966; P:histone H3 acetylation; ISS:UniProtKB.
DR GO; GO:0044154; P:histone H3-K14 acetylation; ISO:MGI.
DR GO; GO:0043967; P:histone H4 acetylation; IBA:GO_Central.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:0051302; P:regulation of cell division; IDA:ComplexPortal.
DR GO; GO:0045995; P:regulation of embryonic development; IDA:ComplexPortal.
DR GO; GO:0031063; P:regulation of histone deacetylation; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0090043; P:regulation of tubulin deacetylation; ISO:MGI.
DR CDD; cd00167; SANT; 1.
DR CDD; cd02341; ZZ_ZZZ3; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR InterPro; IPR037830; ZZZ3.
DR InterPro; IPR041981; ZZZ3_ZZ.
DR PANTHER; PTHR22705; PTHR22705; 2.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF00569; ZZ; 1.
DR SMART; SM00717; SANT; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
DR PROSITE; PS01357; ZF_ZZ_1; 1.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..910
FT /note="ZZ-type zinc finger-containing protein 3"
FT /id="PRO_0000287496"
FT DOMAIN 654..714
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 687..710
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT ZN_FING 825..884
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 41..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 133..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..641
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 830
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 833
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 845
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 848
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 857
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 860
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 870
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 874
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYH5"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYH5"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYH5"
FT MOD_RES 138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYH5"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYH5"
FT MOD_RES 401
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYH5"
FT MOD_RES 708
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8IYH5"
FT CROSSLNK 283
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IYH5"
FT CROSSLNK 654
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IYH5"
FT CROSSLNK 715
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8IYH5"
FT VAR_SEQ 1..501
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025514"
FT VAR_SEQ 1..496
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025515"
FT VAR_SEQ 497..509
FT /note="FESDHVALKHNKD -> MLGSEVLVQHFNS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025516"
FT VAR_SEQ 502..509
FT /note="VALKHNKD -> MIDLWLYS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025517"
FT VAR_SEQ 605
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025518"
SQ SEQUENCE 910 AA; 102307 MW; 2E67A6E0043CC79B CRC64;
MVGTCHSMAA SRSTRVTRST VGLNGLDESF CGRTLRNRSI AHPEEISSHS QVRSRSPKKR
AEPVPTQKGT NNGRTSDVRQ QSARDSWVSP RKRRLSSSEK DDLERQALES CERRQAEPAP
PVFKNIKRCL RAEATNSSEE DSPVKPDKEP GEHRRIVVDH DADFQGAKRA CRCLILDDCE
KREVKKVNVS EEGPLNAAVV EEITGYLTVN GVDDSDSAVI NCDDCQPDGN TKQNNPGSCV
LQEESVAGDG DSETQTSVFC GSRKEDSCID HFVPCTKSDV QVKLEDHKLV TACLPVERRN
QLTAESASGP VSEIQSSLRD SEEEVDVVGD SSASKEQCNE NSSNPLDTGS ERMPVSGEPE
LSSILDCVSA QMTSLSEPQE HRYTLRTSPR RAALARSSPT KTTSPYRENG QLEETNLSPQ
ETNTTVSDHV SESPTDPAEV PQDGKVLCCD SENYGSEGLS KPPSEARVNI GHLPSAKESA
SQHTAEEEDD DPDVYYFESD HVALKHNKDY QRLLQTIAVL EAQRSQAVQD LESLGKHQRE
ALKNPIGFVE KLQKKADIGL PYPQRVVQLP EIMWDQYTNS LGNFEREFKH RKRHTRRVKL
VFDKVGLPAR PKSPLDPKKD GESLSYSMLP LSDGPEGSHN RPQMIRGRLC DDSKPETFNQ
LWTVEEQKKL EQLLLKYPPE EVESRRWQKI ADELGNRTAK QVASRVQKYF IKLTKAGIPV
PGRTPNLYIY SRKSSTSRRQ HPLNKHLFKP STFMTSHEPP VYMDEDDDRS CLHSHMSTAA
EEASDEESIP IIYRSLPEYK ELLQFKKLKK QKLQQMQAES GFVQHVGFKC DNCGVEPIQG
VRWHCQDCPP EMSLDFCDSC SDCPHETDIH KEDHQLEPVY KSETFLDRDY CVSQGTSYSY
LDPNYFPANR
