ZZZ3_HUMAN
ID ZZZ3_HUMAN Reviewed; 903 AA.
AC Q8IYH5; B7WPC6; Q6N004; Q6N070; Q8IYP0; Q8IYR1; Q8TEK4; Q9Y4U0;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=ZZ-type zinc finger-containing protein 3;
GN Name=ZZZ3;
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 [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 84-903 (ISOFORM 2).
RC TISSUE=Adipose tissue, Colon endothelium, and Rectum tumor;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 286-903 (ISOFORM 2).
RC TISSUE=Brain, Lymph, and Placenta;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 161-903 (ISOFORM 4).
RC TISSUE=Spleen;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130; SER-131 AND SER-135, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP FUNCTION, AND IDENTIFICATION IN ATAC COMPLEX.
RX PubMed=19103755; DOI=10.1128/mcb.01599-08;
RA Guelman S., Kozuka K., Mao Y., Pham V., Solloway M.J., Wang J., Wu J.,
RA Lill J.R., Zha J.;
RT "The double-histone-acetyltransferase complex ATAC is essential for
RT mammalian development.";
RL Mol. Cell. Biol. 29:1176-1188(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-701, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82; SER-89; SER-113; SER-135
RP AND SER-606, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-647 AND LYS-708, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-276; LYS-647 AND LYS-708, 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 [14]
RP STRUCTURE BY NMR OF 807-875 IN COMPLEX WITH ZINC IONS.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the ZZ domain of ZZZ3 protein.";
RL Submitted (JUN-2006) to the PDB data bank.
RN [15] {ECO:0007744|PDB:6E83, ECO:0007744|PDB:6E86}
RP STRUCTURE BY NMR OF 816-874, FUNCTION, INTERACTION WITH HISTONE H3, AND
RP MUTAGENESIS OF PHE-821; ASP-824 AND ASP-848.
RX PubMed=30217978; DOI=10.1038/s41467-018-06247-5;
RA Mi W., Zhang Y., Lyu J., Wang X., Tong Q., Peng D., Xue Y., Tencer A.H.,
RA Wen H., Li W., Kutateladze T.G., Shi X.;
RT "The ZZ-type zinc finger of ZZZ3 modulates the ATAC complex-mediated
RT histone acetylation and gene activation.";
RL Nat. Commun. 9:3759-3759(2018).
RN [16]
RP VARIANT [LARGE SCALE ANALYSIS] SER-456.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Histone H3 reader that is required for the ATAC complex-
CC mediated maintenance of histone acetylation and gene activation
CC (PubMed:30217978). Component of the ATAC complex, a complex with
CC histone acetyltransferase activity on histones H3 and H4
CC (PubMed:19103755). {ECO:0000269|PubMed:19103755,
CC ECO:0000269|PubMed:30217978}.
CC -!- SUBUNIT: Component of the ADA2A-containing complex (ATAC), composed of
CC KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1
CC (PubMed:19103755). Interacts via (ZZ-type zinc finger) with histone H3
CC in a methylation-independent manner and acetylation on 'Lys-4' (H3K4ac)
CC moderately enhances the interaction (PubMed:30217978).
CC {ECO:0000269|PubMed:19103755, ECO:0000269|PubMed:30217978}.
CC -!- INTERACTION:
CC Q8IYH5; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-2795524, EBI-11530605;
CC Q8IYH5; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-2795524, EBI-2349927;
CC Q8IYH5; Q86V42: FAM124A; NbExp=3; IntAct=EBI-2795524, EBI-744506;
CC Q8IYH5; Q08379: GOLGA2; NbExp=3; IntAct=EBI-2795524, EBI-618309;
CC Q8IYH5; Q92830: KAT2A; NbExp=2; IntAct=EBI-2795524, EBI-477622;
CC Q8IYH5; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-2795524, EBI-79165;
CC Q8IYH5; Q96KQ4: PPP1R13B; NbExp=3; IntAct=EBI-2795524, EBI-1105153;
CC Q8IYH5; Q12933: TRAF2; NbExp=3; IntAct=EBI-2795524, EBI-355744;
CC Q8IYH5; P61964: WDR5; NbExp=3; IntAct=EBI-2795524, EBI-540834;
CC Q8IYH5; P09022: Hoxa1; Xeno; NbExp=3; IntAct=EBI-2795524, EBI-3957603;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8IYH5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IYH5-2; Sequence=VSP_025511;
CC Name=3;
CC IsoId=Q8IYH5-3; Sequence=VSP_025509, VSP_025510;
CC Name=4;
CC IsoId=Q8IYH5-4; Sequence=VSP_025512, VSP_025513;
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DR EMBL; AL080063; CAB45694.1; -; mRNA.
DR EMBL; BX641001; CAE46004.1; -; mRNA.
DR EMBL; BX640658; CAE45800.1; -; mRNA.
DR EMBL; BX640766; CAE45870.1; -; mRNA.
DR EMBL; AC093575; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX06376.1; -; Genomic_DNA.
DR EMBL; BC035397; AAH35397.1; -; mRNA.
DR EMBL; BC035079; AAH35079.1; -; mRNA.
DR EMBL; BC035818; AAH35818.1; -; mRNA.
DR EMBL; AK074119; BAB84945.1; -; mRNA.
DR CCDS; CCDS677.1; -. [Q8IYH5-1]
DR CCDS; CCDS76172.1; -. [Q8IYH5-3]
DR PIR; T12463; T12463.
DR RefSeq; NP_001295166.1; NM_001308237.1. [Q8IYH5-3]
DR RefSeq; NP_056349.1; NM_015534.5. [Q8IYH5-1]
DR RefSeq; XP_005270782.1; XM_005270725.3.
DR RefSeq; XP_005270783.1; XM_005270726.3.
DR RefSeq; XP_005270784.1; XM_005270727.3.
DR RefSeq; XP_005270786.1; XM_005270729.4. [Q8IYH5-3]
DR RefSeq; XP_016856459.1; XM_017000970.1.
DR PDB; 2FC7; NMR; -; A=807-886.
DR PDB; 2YUM; NMR; -; A=652-713.
DR PDB; 6E83; NMR; -; B=816-874.
DR PDB; 6E86; NMR; -; B=816-874.
DR PDBsum; 2FC7; -.
DR PDBsum; 2YUM; -.
DR PDBsum; 6E83; -.
DR PDBsum; 6E86; -.
DR AlphaFoldDB; Q8IYH5; -.
DR SMR; Q8IYH5; -.
DR BioGRID; 117482; 121.
DR ComplexPortal; CPX-1004; PCAF-containing ATAC complex.
DR ComplexPortal; CPX-997; GCN5-containing ATAC complex.
DR CORUM; Q8IYH5; -.
DR DIP; DIP-47289N; -.
DR IntAct; Q8IYH5; 62.
DR MINT; Q8IYH5; -.
DR STRING; 9606.ENSP00000359837; -.
DR MEROPS; A22.007; -.
DR GlyGen; Q8IYH5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8IYH5; -.
DR PhosphoSitePlus; Q8IYH5; -.
DR BioMuta; ZZZ3; -.
DR DMDM; 74762495; -.
DR EPD; Q8IYH5; -.
DR jPOST; Q8IYH5; -.
DR MassIVE; Q8IYH5; -.
DR MaxQB; Q8IYH5; -.
DR PaxDb; Q8IYH5; -.
DR PeptideAtlas; Q8IYH5; -.
DR PRIDE; Q8IYH5; -.
DR ProteomicsDB; 71174; -. [Q8IYH5-1]
DR ProteomicsDB; 71175; -. [Q8IYH5-2]
DR ProteomicsDB; 71176; -. [Q8IYH5-3]
DR ProteomicsDB; 71177; -. [Q8IYH5-4]
DR Antibodypedia; 33487; 93 antibodies from 24 providers.
DR DNASU; 26009; -.
DR Ensembl; ENST00000370798.5; ENSP00000359834.1; ENSG00000036549.13. [Q8IYH5-3]
DR Ensembl; ENST00000370801.8; ENSP00000359837.3; ENSG00000036549.13. [Q8IYH5-1]
DR GeneID; 26009; -.
DR KEGG; hsa:26009; -.
DR MANE-Select; ENST00000370801.8; ENSP00000359837.3; NM_015534.6; NP_056349.1.
DR UCSC; uc001dhq.4; human. [Q8IYH5-1]
DR CTD; 26009; -.
DR DisGeNET; 26009; -.
DR GeneCards; ZZZ3; -.
DR HGNC; HGNC:24523; ZZZ3.
DR HPA; ENSG00000036549; Low tissue specificity.
DR neXtProt; NX_Q8IYH5; -.
DR OpenTargets; ENSG00000036549; -.
DR PharmGKB; PA134873184; -.
DR VEuPathDB; HostDB:ENSG00000036549; -.
DR eggNOG; ENOG502QS4F; Eukaryota.
DR GeneTree; ENSGT00390000005307; -.
DR HOGENOM; CLU_319257_0_0_1; -.
DR InParanoid; Q8IYH5; -.
DR OMA; NCDDCQL; -.
DR OrthoDB; 139813at2759; -.
DR PhylomeDB; Q8IYH5; -.
DR TreeFam; TF106396; -.
DR PathwayCommons; Q8IYH5; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; Q8IYH5; -.
DR BioGRID-ORCS; 26009; 189 hits in 1114 CRISPR screens.
DR ChiTaRS; ZZZ3; human.
DR EvolutionaryTrace; Q8IYH5; -.
DR GeneWiki; ZZZ3; -.
DR GenomeRNAi; 26009; -.
DR Pharos; Q8IYH5; Tdark.
DR PRO; PR:Q8IYH5; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8IYH5; protein.
DR Bgee; ENSG00000036549; Expressed in calcaneal tendon and 204 other tissues.
DR ExpressionAtlas; Q8IYH5; baseline and differential.
DR Genevisible; Q8IYH5; HS.
DR GO; GO:0140672; C:ATAC complex; IDA:ComplexPortal.
DR GO; GO:0072686; C:mitotic spindle; IC:ComplexPortal.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IDA:UniProtKB.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0043966; P:histone H3 acetylation; IMP:UniProtKB.
DR GO; GO:0044154; P:histone H3-K14 acetylation; IDA:ComplexPortal.
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; IC:ComplexPortal.
DR GO; GO:0031063; P:regulation of histone deacetylation; IMP:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:ComplexPortal.
DR GO; GO:0090043; P:regulation of tubulin deacetylation; IMP:ComplexPortal.
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 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 3D-structure; Acetylation; Alternative splicing; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..903
FT /note="ZZ-type zinc finger-containing protein 3"
FT /id="PRO_0000287495"
FT DOMAIN 647..707
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 680..703
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT ZN_FING 818..877
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 1..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 823
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 826
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 838
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 841
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 850
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 853
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 863
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 867
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 394
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6KAQ7"
FT MOD_RES 606
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 701
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 276
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 647
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 708
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..494
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025509"
FT VAR_SEQ 495..502
FT /note="VALKHNKD -> MIDLWLYS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025510"
FT VAR_SEQ 598
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_025511"
FT VAR_SEQ 661..683
FT /note="KKLEQLLIKYPPEEVESRRWQKI -> VINISKSCRLKKTSKQLTSESVL
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025512"
FT VAR_SEQ 684..903
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025513"
FT VARIANT 456
FT /note="P -> S (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035718"
FT MUTAGEN 821
FT /note="F->A: Reduced histone H3 binding. Significant
FT reduction in the acetyltransferase activity of the ATAC
FT complex on histone H3 but no effect on the complex
FT integrity."
FT /evidence="ECO:0000269|PubMed:30217978"
FT MUTAGEN 824
FT /note="D->A: Loss of histone H3 binding. Significant
FT reduction in the acetyltransferase activity of the ATAC
FT complex on histone H3 but no effect on the complex
FT integrity."
FT /evidence="ECO:0000269|PubMed:30217978"
FT MUTAGEN 848
FT /note="D->A: Loss of histone H3 binding."
FT /evidence="ECO:0000269|PubMed:30217978"
FT CONFLICT 596
FT /note="D -> G (in Ref. 4; AAH35079)"
FT /evidence="ECO:0000305"
FT CONFLICT 655
FT /note="W -> G (in Ref. 1; CAB45694)"
FT /evidence="ECO:0000305"
FT CONFLICT 698
FT /note="R -> Q (in Ref. 4; AAH35079)"
FT /evidence="ECO:0000305"
FT CONFLICT 721
FT /note="Y -> C (in Ref. 4; AAH35079)"
FT /evidence="ECO:0000305"
FT CONFLICT 807
FT /note="Q -> R (in Ref. 1; CAE45800)"
FT /evidence="ECO:0000305"
FT CONFLICT 877
FT /note="T -> A (in Ref. 1; CAE45870)"
FT /evidence="ECO:0000305"
FT HELIX 657..669
FT /evidence="ECO:0007829|PDB:2YUM"
FT HELIX 676..687
FT /evidence="ECO:0007829|PDB:2YUM"
FT STRAND 688..690
FT /evidence="ECO:0007829|PDB:2YUM"
FT HELIX 692..703
FT /evidence="ECO:0007829|PDB:2YUM"
FT HELIX 704..706
FT /evidence="ECO:0007829|PDB:2YUM"
FT STRAND 807..809
FT /evidence="ECO:0007829|PDB:2FC7"
FT STRAND 817..820
FT /evidence="ECO:0007829|PDB:2FC7"
FT STRAND 824..826
FT /evidence="ECO:0007829|PDB:2FC7"
FT STRAND 829..833
FT /evidence="ECO:0007829|PDB:2FC7"
FT STRAND 835..841
FT /evidence="ECO:0007829|PDB:2FC7"
FT STRAND 843..845
FT /evidence="ECO:0007829|PDB:2FC7"
FT STRAND 848..850
FT /evidence="ECO:0007829|PDB:2FC7"
FT HELIX 851..853
FT /evidence="ECO:0007829|PDB:2FC7"
FT STRAND 865..867
FT /evidence="ECO:0007829|PDB:2FC7"
FT STRAND 869..872
FT /evidence="ECO:0007829|PDB:2FC7"
SQ SEQUENCE 903 AA; 102023 MW; 16ED137C0A8202EA CRC64;
MAASRSTRVT RSTVGLNGLD ESFCGRTLRN RSIAHPEEIS SNSQVRSRSP KKRPEPVPIQ
KGNNNGRTTD LKQQSTRESW VSPRKRGLSS SEKDNIERQA IENCERRQTE PVSPVLKRIK
RCLRSEAPNS SEEDSPIKSD KESVEQRSTV VDNDADFQGT KRACRCLILD DCEKREIKKV
NVSEEGPLNS AVVEEITGYL AVNGVDDSDS AVINCDDCQP DGNTKQNSIG SYVLQEKSVA
ENGDTDTQTS MFLDSRKEDS YIDHKVPCTD SQVQVKLEDH KIVTACLPVE HVNQLTTEPA
TGPFSETQSS LRDSEEEVDV VGDSSASKEQ CKENTNNELD TSLESMPASG EPEPSPVLDC
VSAQMMSLSE PQEHRYTLRT SPRRAAPTRG SPTKNSSPYR ENGQFEENNL SPNETNATVS
DNVSQSPTNP GEISQNEKGI CCDSQNNGSE GVSKPPSEAR LNIGHLPSAK ESASQHITEE
EDDDPDVYYF ESDHVALKHN KDYQRLLQTI AVLEAQRSQA VQDLESLGRH QREALKNPIG
FVEKLQKKAD IGLPYPQRVV QLPEIVWDQY THSLGNFERE FKNRKRHTRR VKLVFDKVGL
PARPKSPLDP KKDGESLSYS MLPLSDGPEG SSSRPQMIRG RLCDDTKPET FNQLWTVEEQ
KKLEQLLIKY PPEEVESRRW QKIADELGNR TAKQVASRVQ KYFIKLTKAG IPVPGRTPNL
YIYSKKSSTS RRQHPLNKHL FKPSTFMTSH EPPVYMDEDD DRSCFHSHMN TAVEDASDDE
SIPIMYRNLP EYKELLQFKK LKKQKLQQMQ AESGFVQHVG FKCDNCGIEP IQGVRWHCQD
CPPEMSLDFC DSCSDCLHET DIHKEDHQLE PIYRSETFLD RDYCVSQGTS YNYLDPNYFP
ANR
