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Database: UniProt
Entry: Q8IYH5
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Original site: Q8IYH5 
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   07-APR-2021, entry version 174.
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]
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: Component of the ATAC complex, a complex with histone
CC       acetyltransferase activity on histones H3 and H4.
CC       {ECO:0000269|PubMed:19103755}.
CC   -!- SUBUNIT: Component of the ADA2A-containing complex (ATAC), composed of
CC       KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1.
CC       {ECO:0000269|PubMed:19103755, ECO:0000269|Ref.14}.
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   SMR; Q8IYH5; -.
DR   BioGRID; 117482; 66.
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; 38.
DR   MINT; Q8IYH5; -.
DR   STRING; 9606.ENSP00000359837; -.
DR   MEROPS; A22.007; -.
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; 87 antibodies.
DR   DNASU; 26009; -.
DR   Ensembl; ENST00000370798; ENSP00000359834; ENSG00000036549. [Q8IYH5-3]
DR   Ensembl; ENST00000370801; ENSP00000359837; ENSG00000036549. [Q8IYH5-1]
DR   GeneID; 26009; -.
DR   KEGG; hsa:26009; -.
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:ENSG00000036549.12; -.
DR   eggNOG; ENOG502QS4F; Eukaryota.
DR   GeneTree; ENSGT00390000005307; -.
DR   HOGENOM; CLU_319257_0_0_1; -.
DR   InParanoid; Q8IYH5; -.
DR   OMA; TELYEHR; -.
DR   OrthoDB; 139813at2759; -.
DR   PhylomeDB; Q8IYH5; -.
DR   TreeFam; TF106396; -.
DR   PathwayCommons; Q8IYH5; -.
DR   Reactome; R-HSA-3214847; HATs acetylate histones.
DR   BioGRID-ORCS; 26009; 176 hits in 1025 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 corpus callosum and 237 other tissues.
DR   ExpressionAtlas; Q8IYH5; baseline and differential.
DR   Genevisible; Q8IYH5; HS.
DR   GO; GO:0005671; C:Ada2/Gcn5/Ada3 transcription activator complex; IBA:GO_Central.
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:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0043967; P:histone H4 acetylation; IBA:GO_Central.
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         817..867
FT                   /note="ZZ-type"
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   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:0007744|PDB:2YUM"
FT   HELIX           676..687
FT                   /evidence="ECO:0007744|PDB:2YUM"
FT   STRAND          688..690
FT                   /evidence="ECO:0007744|PDB:2YUM"
FT   HELIX           692..703
FT                   /evidence="ECO:0007744|PDB:2YUM"
FT   HELIX           704..706
FT                   /evidence="ECO:0007744|PDB:2YUM"
FT   STRAND          807..809
FT                   /evidence="ECO:0007744|PDB:2FC7"
FT   STRAND          817..820
FT                   /evidence="ECO:0007744|PDB:2FC7"
FT   STRAND          824..826
FT                   /evidence="ECO:0007744|PDB:2FC7"
FT   STRAND          829..833
FT                   /evidence="ECO:0007744|PDB:2FC7"
FT   STRAND          835..841
FT                   /evidence="ECO:0007744|PDB:2FC7"
FT   STRAND          843..845
FT                   /evidence="ECO:0007744|PDB:2FC7"
FT   STRAND          848..850
FT                   /evidence="ECO:0007744|PDB:2FC7"
FT   HELIX           851..853
FT                   /evidence="ECO:0007744|PDB:2FC7"
FT   STRAND          865..867
FT                   /evidence="ECO:0007744|PDB:2FC7"
FT   STRAND          869..872
FT                   /evidence="ECO:0007744|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
//
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