GENTAUR Molecular Products.

 ZN217_HUMAN             Reviewed;        1048 AA.
 O75362; E1P5Y6; Q14DB8;
 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
 01-NOV-1998, sequence version 1.
 12-SEP-2018, entry version 170.
 RecName: Full=Zinc finger protein 217;
 Name=ZNF217; Synonyms=ZABC1;
 Homo sapiens (Human).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
 Catarrhini; Hominidae; Homo.
 NCBI_TaxID=9606;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA].
 PubMed=9671742; DOI=10.1073/pnas.95.15.8703;
 Collins C., Rommens J.M., Kowbel D., Godfrey T., Tanner M.,
 Hwang S.-I., Polikoff D., Nonet G., Cochran J., Myambo K., Jay K.E.,
 Froula J., Cloutier T., Kuo W.-L., Yaswen P., Dairkee S.,
 Giovanola J., Hutchinson G.B., Isola J., Kallioniemi O.-P.,
 Palazzolo M., Martin C., Ericsson C., Pinkel D., Albertson D.,
 Li W.-B., Gray J.W.;
 "Positional cloning of ZNF217 and NABC1: genes amplified at 20q13.2
 and overexpressed in breast carcinoma.";
 Proc. Natl. Acad. Sci. U.S.A. 95:8703-8708(1998).
 [2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 PubMed=11780052; DOI=10.1038/414865a;
 Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
 Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
 Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
 Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
 Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
 Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
 Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
 Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
 Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
 Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
 Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
 Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
 Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
 Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
 Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
 Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
 Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
 Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
 Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
 Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
 Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
 Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
 Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
 Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
 Rogers J.;
 "The DNA sequence and comparative analysis of human chromosome 20.";
 Nature 414:865-871(2001).
 [3]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
 Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
 Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
 Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
 Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
 Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
 Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
 Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
 Venter J.C.;
 Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
 [4]
 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
 TISSUE=Colon;
 PubMed=15489334; DOI=10.1101/gr.2596504;
 The MGC Project Team;
 "The status, quality, and expansion of the NIH full-length cDNA
 project: the Mammalian Gene Collection (MGC).";
 Genome Res. 14:2121-2127(2004).
 [5]
 IDENTIFICATION IN THE BHC COMPLEX WITH GSE1; GTF2I; HDAC1; HDAC2;
 HMG20B; KDM1A; PHF21A; RCOR1; ZMYM2 AND ZMYM3.
 PubMed=12493763; DOI=10.1074/jbc.M208992200;
 Hakimi M.-A., Dong Y., Lane W.S., Speicher D.W., Shiekhattar R.;
 "A candidate X-linked mental retardation gene is a component of a new
 family of histone deacetylase-containing complexes.";
 J. Biol. Chem. 278:7234-7239(2003).
 [6]
 FUNCTION.
 PubMed=16203743; DOI=10.1093/hmg/ddi352;
 Huang G., Krig S., Kowbel D., Xu H., Hyun B., Volik S., Feuerstein B.,
 Mills G.B., Stokoe D., Yaswen P., Collins C.;
 "ZNF217 suppresses cell death associated with chemotherapy and
 telomere dysfunction.";
 Hum. Mol. Genet. 14:3219-3225(2005).
 [7]
 FUNCTION.
 PubMed=17259635; DOI=10.1074/jbc.M611752200;
 Krig S.R., Jin V.X., Bieda M.C., O'Geen H., Yaswen P., Green R.,
 Farnham P.J.;
 "Identification of genes directly regulated by the oncogene ZNF217
 using chromatin immunoprecipitation (ChIP)-chip assays.";
 J. Biol. Chem. 282:9703-9712(2007).
 [8]
 SUBUNIT, IDENTIFICATION IN A COMPLEX WITH HDAC2; KDM1A AND CTBP1, AND
 FUNCTION.
 PubMed=18625718; DOI=10.1128/MCB.00246-08;
 Thillainadesan G., Isovic M., Loney E., Andrews J., Tini M.,
 Torchia J.;
 "Genome analysis identifies the p15ink4b tumor suppressor as a direct
 target of the ZNF217/CoREST complex.";
 Mol. Cell. Biol. 28:6066-6077(2008).
 [9]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321; THR-322; THR-648
 AND SER-662, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
 ANALYSIS].
 TISSUE=Cervix carcinoma;
 PubMed=18669648; DOI=10.1073/pnas.0805139105;
 Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
 Elledge S.J., Gygi S.P.;
 "A quantitative atlas of mitotic phosphorylation.";
 Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
 [10]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407 AND SER-795, AND
 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 PubMed=21406692; DOI=10.1126/scisignal.2001570;
 Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
 Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
 Blagoev B.;
 "System-wide temporal characterization of the proteome and
 phosphoproteome of human embryonic stem cell differentiation.";
 Sci. Signal. 4:RS3-RS3(2011).
 [11]
 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; SER-407; SER-593
 AND SER-662, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
 ANALYSIS].
 TISSUE=Cervix carcinoma, and Erythroleukemia;
 PubMed=23186163; DOI=10.1021/pr300630k;
 Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
 Mohammed S.;
 "Toward a comprehensive characterization of a human cancer cell
 phosphoproteome.";
 J. Proteome Res. 12:260-271(2013).
 [12]
 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-819, AND IDENTIFICATION BY
 MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
 PubMed=28112733; DOI=10.1038/nsmb.3366;
 Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
 Nielsen M.L.;
 "Site-specific mapping of the human SUMO proteome reveals co-
 modification with phosphorylation.";
 Nat. Struct. Mol. Biol. 24:325-336(2017).
 [13]
 X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 752-760 IN COMPLEX WITH
 CTBP1, INTERACTION WITH CTBP1 AND CTBP2, AND FUNCTION.
 PubMed=16940172; DOI=10.1128/MCB.00680-06;
 Quinlan K.G.R., Nardini M., Verger A., Francescato P., Yaswen P.,
 Corda D., Bolognesi M., Crossley M.;
 "Specific recognition of ZNF217 and other zinc finger proteins at a
 surface groove of C-terminal binding proteins.";
 Mol. Cell. Biol. 26:8159-8172(2006).
 [14]
 VARIANT [LARGE SCALE ANALYSIS] ASN-323.
 PubMed=16959974; DOI=10.1126/science.1133427;
 Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
 Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
 Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
 Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
 Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
 Vogelstein B., Kinzler K.W., Velculescu V.E.;
 "The consensus coding sequences of human breast and colorectal
 cancers.";
 Science 314:268-274(2006).
 -!- FUNCTION: Binds to the promoters of target genes and functions as
     repressor. Promotes cell proliferation and antagonizes cell death.
     Promotes phosphorylation of AKT1 at 'Ser-473'.
     {ECO:0000269|PubMed:16203743, ECO:0000269|PubMed:16940172,
     ECO:0000269|PubMed:17259635, ECO:0000269|PubMed:18625718}.
 -!- SUBUNIT: Component of a histone deacetylase complex that contains
     HDAC2, KDM1A, CTBP1 and ZNF217. May be a component of a BHC
     histone deacetylase complex that contains HDAC1, HDAC2,
     HMG20B/BRAF35, KDM1A, RCOR1/CoREST, PHF21A/BHC80, ZMYM2, ZNF217,
     ZMYM3, GSE1 and GTF2I. Interacts with CTBP1 and CTBP2.
     {ECO:0000269|PubMed:12493763, ECO:0000269|PubMed:16940172,
     ECO:0000269|PubMed:18625718}.
 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
 -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
     family. {ECO:0000305}.
 -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
     and Haematology;
     URL="http://atlasgeneticsoncology.org/Genes/ZNF217ID42875ch20q13.html";
 -----------------------------------------------------------------------
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 EMBL; AF041259; AAC39895.1; -; mRNA.
 EMBL; AL157838; -; NOT_ANNOTATED_CDS; Genomic_DNA.
 EMBL; CH471077; EAW75580.1; -; Genomic_DNA.
 EMBL; BC113427; AAI13428.1; -; mRNA.
 CCDS; CCDS13443.1; -.
 RefSeq; NP_006517.1; NM_006526.2.
 RefSeq; XP_016883548.1; XM_017028059.1.
 UniGene; Hs.155040; -.
 UniGene; Hs.711564; -.
 PDB; 2HU2; X-ray; 2.85 A; B=752-760.
 PDB; 3UK3; X-ray; 2.10 A; C/D=469-523.
 PDB; 4F2J; X-ray; 2.64 A; C=469-523.
 PDB; 4IS1; X-ray; 2.10 A; C/D=469-523.
 PDBsum; 2HU2; -.
 PDBsum; 3UK3; -.
 PDBsum; 4F2J; -.
 PDBsum; 4IS1; -.
 ProteinModelPortal; O75362; -.
 SMR; O75362; -.
 BioGrid; 113547; 12.
 CORUM; O75362; -.
 IntAct; O75362; 6.
 MINT; O75362; -.
 STRING; 9606.ENSP00000304308; -.
 iPTMnet; O75362; -.
 PhosphoSitePlus; O75362; -.
 BioMuta; ZNF217; -.
 EPD; O75362; -.
 MaxQB; O75362; -.
 PaxDb; O75362; -.
 PeptideAtlas; O75362; -.
 PRIDE; O75362; -.
 ProteomicsDB; 49925; -.
 Ensembl; ENST00000302342; ENSP00000304308; ENSG00000171940.
 Ensembl; ENST00000371471; ENSP00000360526; ENSG00000171940.
 GeneID; 7764; -.
 KEGG; hsa:7764; -.
 UCSC; uc002xwq.5; human.
 CTD; 7764; -.
 DisGeNET; 7764; -.
 EuPathDB; HostDB:ENSG00000171940.13; -.
 GeneCards; ZNF217; -.
 HGNC; HGNC:13009; ZNF217.
 HPA; HPA051857; -.
 MIM; 602967; gene.
 neXtProt; NX_O75362; -.
 OpenTargets; ENSG00000171940; -.
 PharmGKB; PA37588; -.
 eggNOG; KOG1721; Eukaryota.
 eggNOG; COG5048; LUCA.
 GeneTree; ENSGT00530000063100; -.
 HOGENOM; HOG000276541; -.
 HOVERGEN; HBG061769; -.
 InParanoid; O75362; -.
 OMA; PSITCPF; -.
 OrthoDB; EOG091G010T; -.
 PhylomeDB; O75362; -.
 TreeFam; TF332241; -.
 Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
 SIGNOR; O75362; -.
 ChiTaRS; ZNF217; human.
 EvolutionaryTrace; O75362; -.
 GeneWiki; ZNF217; -.
 GenomeRNAi; 7764; -.
 PRO; PR:O75362; -.
 Proteomes; UP000005640; Chromosome 20.
 Bgee; ENSG00000171940; Expressed in 206 organ(s), highest expression level in endometrium epithelium.
 CleanEx; HS_ZNF217; -.
 ExpressionAtlas; O75362; baseline and differential.
 Genevisible; O75362; HS.
 GO; GO:0000118; C:histone deacetylase complex; IDA:UniProtKB.
 GO; GO:0005739; C:mitochondrion; IDA:HPA.
 GO; GO:0016607; C:nuclear speck; IDA:HPA.
 GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
 GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
 GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
 GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
 GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
 GO; GO:0007275; P:multicellular organism development; IBA:GO_Central.
 GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
 GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
 GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
 GO; GO:0007165; P:signal transduction; IBA:GO_Central.
 GO; GO:0006351; P:transcription, DNA-templated; TAS:ProtInc.
 InterPro; IPR036236; Znf_C2H2_sf.
 InterPro; IPR013087; Znf_C2H2_type.
 SMART; SM00355; ZnF_C2H2; 8.
 SUPFAM; SSF57667; SSF57667; 4.
 PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
 PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
 1: Evidence at protein level;
 3D-structure; Complete proteome; DNA-binding; Isopeptide bond;
 Metal-binding; Nucleus; Phosphoprotein; Polymorphism;
 Reference proteome; Repeat; Repressor; Transcription;
 Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
 CHAIN         1   1048       Zinc finger protein 217.
                              /FTId=PRO_0000047460.
 ZN_FING      65     88       C2H2-type 1. {ECO:0000255|PROSITE-
                              ProRule:PRU00042}.
 ZN_FING     128    150       C2H2-type 2. {ECO:0000255|PROSITE-
                              ProRule:PRU00042}.
 ZN_FING     156    178       C2H2-type 3. {ECO:0000255|PROSITE-
                              ProRule:PRU00042}.
 ZN_FING     216    238       C2H2-type 4. {ECO:0000255|PROSITE-
                              ProRule:PRU00042}.
 ZN_FING     375    397       C2H2-type 5. {ECO:0000255|PROSITE-
                              ProRule:PRU00042}.
 ZN_FING     471    493       C2H2-type 6. {ECO:0000255|PROSITE-
                              ProRule:PRU00042}.
 ZN_FING     499    521       C2H2-type 7. {ECO:0000255|PROSITE-
                              ProRule:PRU00042}.
 MOD_RES     106    106       Phosphoserine.
                              {ECO:0000244|PubMed:23186163}.
 MOD_RES     321    321       Phosphoserine.
                              {ECO:0000244|PubMed:18669648}.
 MOD_RES     322    322       Phosphothreonine.
                              {ECO:0000244|PubMed:18669648}.
 MOD_RES     407    407       Phosphoserine.
                              {ECO:0000244|PubMed:21406692,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES     593    593       Phosphoserine.
                              {ECO:0000244|PubMed:23186163}.
 MOD_RES     648    648       Phosphothreonine.
                              {ECO:0000244|PubMed:18669648}.
 MOD_RES     662    662       Phosphoserine.
                              {ECO:0000244|PubMed:18669648,
                              ECO:0000244|PubMed:23186163}.
 MOD_RES     795    795       Phosphoserine.
                              {ECO:0000244|PubMed:21406692}.
 CROSSLNK    819    819       Glycyl lysine isopeptide (Lys-Gly)
                              (interchain with G-Cter in SUMO2).
                              {ECO:0000244|PubMed:28112733}.
 VARIANT     323    323       D -> N (in a colorectal cancer sample;
                              somatic mutation; dbSNP:rs767530299).
                              {ECO:0000269|PubMed:16959974}.
                              /FTId=VAR_035572.
 VARIANT     739    739       V -> I (in dbSNP:rs6063966).
                              /FTId=VAR_052795.
 VARIANT     889    889       D -> G (in dbSNP:rs34323943).
                              /FTId=VAR_061939.
 TURN        474    476       {ECO:0000244|PDB:3UK3}.
 HELIX       483    494       {ECO:0000244|PDB:3UK3}.
 STRAND      502    505       {ECO:0000244|PDB:3UK3}.
 STRAND      507    510       {ECO:0000244|PDB:3UK3}.
 HELIX       511    521       {ECO:0000244|PDB:3UK3}.
 SEQUENCE   1048 AA;  115272 MW;  797FC620817D1E1F CRC64;
 MQSKVTGNMP TQSLLMYMDG PEVIGSSLGS PMEMEDALSM KGTAVVPFRA TQEKNVIQIE
 GYMPLDCMFC SQTFTHSEDL NKHVLMQHRP TLCEPAVLRV EAEYLSPLDK SQVRTEPPKE
 KNCKENEFSC EVCGQTFRVA FDVEIHMRTH KDSFTYGCNM CGRRFKEPWF LKNHMRTHNG
 KSGARSKLQQ GLESSPATIN EVVQVHAAES ISSPYKICMV CGFLFPNKES LIEHRKVHTK
 KTAFGTSSAQ TDSPQGGMPS SREDFLQLFN LRPKSHPETG KKPVRCIPQL DPFTTFQAWQ
 LATKGKVAIC QEVKESGQEG STDNDDSSSE KELGETNKGS CAGLSQEKEK CKHSHGEAPS
 VDADPKLPSS KEKPTHCSEC GKAFRTYHQL VLHSRVHKKD RRAGAESPTM SVDGRQPGTC
 SPDLAAPLDE NGAVDRGEGG SEDGSEDGLP EGIHLDKNDD GGKIKHLTSS RECSYCGKFF
 RSNYYLNIHL RTHTGEKPYK CEFCEYAAAQ KTSLRYHLER HHKEKQTDVA AEVKNDGKNQ
 DTEDALLTAD SAQTKNLKRF FDGAKDVTGS PPAKQLKEMP SVFQNVLGSA VLSPAHKDTQ
 DFHKNAADDS ADKVNKNPTP AYLDLLKKRS AVETQANNLI CRTKADVTPP PDGSTTHNLE
 VSPKEKQTET AADCRYRPSV DCHEKPLNLS VGALHNCPAI SLSKSLIPSI TCPFCTFKTF
 YPEVLMMHQR LEHKYNPDVH KNCRNKSLLR SRRTGCPPAL LGKDVPPLSS FCKPKPKSAF
 PAQSKSLPSA KGKQSPPGPG KAPLTSGIDS STLAPSNLKS HRPQQNVGVQ GAATRQQQSE
 MFPKTSVSPA PDKTKRPETK LKPLPVAPSQ PTLGSSNING SIDYPAKNDS PWAPPGRDYF
 CNRSASNTAA EFGEPLPKRL KSSVVALDVD QPGANYRRGY DLPKYHMVRG ITSLLPQDCV
 YPSQALPPKP RFLSSSEVDS PNVLTVQKPY GGSGPLYTCV PAGSPASSST LEGKRPVSYQ
 HLSNSMAQKR NYENFIGNAH YRPNDKKT

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