ID ZN268_HUMAN Reviewed; 947 AA. AC Q14587; Q8TDG8; Q96RH4; Q9BZJ9; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 29-AUG-2001, sequence version 2. DT 27-MAR-2024, entry version 215. DE RecName: Full=Zinc finger protein 268; DE AltName: Full=Zinc finger protein HZF3; GN Name=ZNF268; 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 [MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Embryo; RX PubMed=11311945; DOI=10.1016/s0167-4781(01)00194-4; RA Gou D.M., Sun Y., Gao L., Chow L.M.C., Huang J., Feng Y.D., Jiang D.H., RA Li W.X.; RT "Cloning and characterization of a novel Kruppel-like zinc finger gene, RT ZNF268, expressed in early human embryo."; RL Biochim. Biophys. Acta 1518:306-310(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY. RX PubMed=12200376; DOI=10.1182/blood-2002-02-0513; RA Krackhardt A.M., Witzens M., Harig S., Hodi F.S., Zauls A.J., Chessia M., RA Barrett P., Gribben J.G.; RT "Identification of tumor-associated antigens in chronic lymphocytic RT leukemia by SEREX."; RL Blood 100:2123-2131(2002). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5; 6 AND 7), AND TISSUE RP SPECIFICITY. RX PubMed=16865230; RA Shao H., Zhu C., Zhao Z., Guo M., Qiu H., Liu H., Wang D., Xue L., Gao L., RA Sun C., Li W.; RT "KRAB-containing zinc finger gene ZNF268 encodes multiple alternatively RT spliced isoforms that contain transcription regulatory domains."; RL Int. J. Mol. Med. 18:457-463(2006). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 4; 5; 6 AND 7), AND TISSUE RP SPECIFICITY. RX PubMed=18949428; RA Zhao Z., Wang D., Zhu C., Shao H., Sun C., Qiu H., Xue L., Xu J., Guo M., RA Li W.; RT "Aberrant alternative splicing of human zinc finger gene ZNF268 in human RT hematological malignancy."; RL Oncol. Rep. 20:1243-1248(2008). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 549-947. RX PubMed=7865130; DOI=10.1089/dna.1995.14.125; RA Abrink M., Aveskogh M., Hellman L.; RT "Isolation of cDNA clones for 42 different Kruppel-related zinc finger RT proteins expressed in the human monoblast cell line U-937."; RL DNA Cell Biol. 14:125-136(1995). RN [7] RP FUNCTION (ISOFORM 1), AND SUBCELLULAR LOCATION. RX PubMed=12822888; DOI=10.1080/1521654031000110208; RA Sun Y., Gou D.M., Liu H., Peng X., Li W.X.; RT "The KRAB domain of zinc finger gene ZNF268: a potential transcriptional RT repressor."; RL IUBMB Life 55:127-131(2003). RN [8] RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE. RX PubMed=15547661; RA Sun Y., Shao H., Li Z., Liu J., Gao L., Peng X., Meng Y., Li W.; RT "ZNF268, a novel kruppel-like zinc finger protein, is implicated in early RT human liver development."; RL Int. J. Mol. Med. 14:971-975(2004). RN [9] RP INDUCTION BY ATF4. RX PubMed=16787922; DOI=10.1074/jbc.m602753200; RA Guo M.X., Wang D., Shao H.J., Qiu H.L., Xue L., Zhao Z.Z., Zhu C.G., RA Shi Y.B., Li W.X.; RT "Transcription of human zinc finger ZNF268 gene requires an intragenic RT promoter element."; RL J. Biol. Chem. 281:24623-24636(2006). RN [10] RP ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=16735226; RA Sun C., Zhao Z.Z., Gao L., Sun Y., Shao H.J., Li W.X.; RT "Cloning and characterization of two novel alternatively spliced RT transcripts of ZNF268."; RL Yi Chuan 28:513-517(2006). RN [11] RP INDUCTION BY UPF1. RX PubMed=18774934; DOI=10.1134/s0006297908080051; RA Zhu C., Zhao Z., Guo M., Shao H., Qiu H., Wang D., Xu J., Xue L., Li W.; RT "The mammalian gene ZNF268 is regulated by hUpf1."; RL Biochemistry (Mosc.) 73:881-885(2008). RN [12] RP INDUCTION BY HTLV-1 TAX. RX PubMed=18375384; DOI=10.1074/jbc.m706426200; RA Wang D., Guo M.X., Hu H.M., Zhao Z.Z., Qiu H.L., Shao H.J., Zhu C.G., RA Xue L., Shi Y.B., Li W.X.; RT "Human T-cell leukemia virus type 1 oncoprotein tax represses ZNF268 RT expression through the cAMP-responsive element-binding protein/activating RT transcription factor pathway."; RL J. Biol. Chem. 283:16299-16308(2008). RN [13] RP FUNCTION, ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, RP AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=18677094; RA Chun J.N., Song I.S., Kang D.H., Song H.J., Kim H.I., Seo J., Suh J.W., RA Lee K.J., Lee K.J., Kim J., Kang S.W.; RT "A splice variant of the C(2)H(2)-type zinc finger protein, ZNF268s, RT regulates NF-kappaB activation by TNF-alpha."; RL Mol. Cells 26:175-180(2008). RN [14] RP FUNCTION (ISOFORMS 1 AND 2), INTERACTION WITH CHUK AND IKBKB, AND TISSUE RP SPECIFICITY. RX PubMed=23091055; DOI=10.1074/jbc.m112.399923; RA Wang W., Guo M., Hu L., Cai J., Zeng Y., Luo J., Shu Z., Li W., Huang Z.; RT "The zinc finger protein ZNF268 is overexpressed in human cervical cancer RT and contributes to tumorigenesis via enhancing NF-kappaB signaling."; RL J. Biol. Chem. 287:42856-42866(2012). RN [15] RP FUNCTION, AND INDUCTION. RX PubMed=22235304; DOI=10.1371/journal.pone.0029518; RA Zeng Y., Wang W., Ma J., Wang X., Guo M., Li W.; RT "Knockdown of ZNF268, which is transcriptionally downregulated by GATA-1, RT promotes proliferation of K562 cells."; RL PLoS ONE 7:E29518-E29518(2012). RN [16] RP INTERACTION WITH TRIM28, SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), AND RP MUTAGENESIS OF ASP-85; VAL-86; VAL-88; PHE-90; GLU-93; GLU-94 AND TRP-95. RX PubMed=23665872; DOI=10.1007/s00018-013-1359-4; RA Wang W., Cai J., Wu Y., Hu L., Chen Z., Hu J., Chen Z., Li W., Guo M., RA Huang Z.; RT "Novel activity of KRAB domain that functions to reinforce nuclear RT localization of KRAB-containing zinc finger proteins by interacting with RT KAP1."; RL Cell. Mol. Life Sci. 70:3947-3958(2013). RN [17] RP FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=23946776; DOI=10.3892/ol.2013.1318; RA Hu L., Wang W., Cai J., Luo J., Huang Y., Xiong S., Li W., Guo M.; RT "Aberrant expression of ZNF268 alters the growth and migration of ovarian RT cancer cells."; RL Oncol. Lett. 6:49-54(2013). RN [18] RP STRUCTURE BY NMR OF 272-947. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the C2H2 type zinc finger region of human zinc RT finger protein 268."; RL Submitted (OCT-2007) to the PDB data bank. CC -!- FUNCTION: [Isoform 1]: Acts as a transcriptional repressor. Inhibits CC erythroid differentiation and tumor cell proliferation. Plays a role CC during ovarian cancer development and progression. CC -!- FUNCTION: [Isoform 2]: Contributes to cervical carcinogenesis in part CC through the TNF-alpha-induced NF-kappa-B signaling pathway by CC interacting with the I-kappa-B-kinase (IKK) core complex. CC -!- SUBUNIT: Interacts (via the KRAB domain) with TRIM28 (via the RBCC CC domain); the interaction increases ZNF268 nuclear localization CC activity. Isoform 2 interacts with CHUK and IKBKB; the interaction is CC further increased in a TNF-alpha-dependent manner. CC {ECO:0000269|PubMed:23091055, ECO:0000269|PubMed:23665872}. CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus CC {ECO:0000269|PubMed:23665872}. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus CC {ECO:0000269|PubMed:23665872}. Cytoplasm {ECO:0000269|PubMed:23665872}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=7; CC Name=1; Synonyms=ZNF268a, KW-4 variant-1; CC IsoId=Q14587-1; Sequence=Displayed; CC Name=2; Synonyms=ZNF268s, KW-4 variant-2; CC IsoId=Q14587-2; Sequence=VSP_006909; CC Name=3; Synonyms=ZNF268c; CC IsoId=Q14587-3; Sequence=VSP_053461, VSP_053471; CC Name=4; Synonyms=ZNF268d; CC IsoId=Q14587-4; Sequence=VSP_053462, VSP_053467; CC Name=5; Synonyms=ZNF268e; CC IsoId=Q14587-6; Sequence=VSP_053466, VSP_053468; CC Name=6; Synonyms=ZNF268f; CC IsoId=Q14587-7; Sequence=VSP_053464, VSP_053465; CC Name=7; Synonyms=ZNF268g; CC IsoId=Q14587-8; Sequence=VSP_053463, VSP_053469, VSP_053470; CC -!- TISSUE SPECIFICITY: Overexpressed in ovarian cancer tissues compared to CC normal ovarian tissues. Isoform 1 and isoform 2 are expressed in CC squamous epithelium tissues. Isoform 2 is overexpressed in squamous CC cervical cancer (at protein level). Expressed in blood cells. Isoform 1 CC is expressed in pancreas, lung, skeletal muscle, heart, placenta, CC liver, kidney and brain. Isoform 2 expressed in chronic lymphocytic CC leukemia (CLL) and several tumor cell lines. Isoform 3 is expressed in CC several tumor cells. Isoform 5 is expressed in fetal liver and several CC tumor cells. Isoform 6 is weakly expressed in brain, lung amd small CC intestin and in several tumor cells. Isoform 7 is expressed in fetal CC liver and several tumor cells. {ECO:0000269|PubMed:12200376, CC ECO:0000269|PubMed:16735226, ECO:0000269|PubMed:16865230, CC ECO:0000269|PubMed:18949428, ECO:0000269|PubMed:23091055, CC ECO:0000269|PubMed:23946776}. CC -!- DEVELOPMENTAL STAGE: Expressed in fetal liver from 5 weeks until 4 CC months but drastically reduced by 6 months and became non-detectable by CC 7 months. Expressed in hematopoietic stem cells in 3 weeks and 5 weeks CC (at protein level). Expressed in fetal liver. CC {ECO:0000269|PubMed:15547661, ECO:0000269|PubMed:16735226}. CC -!- INDUCTION: Down-regulated during erythroid differentiation by GATA1. CC Down-regulated by HTLV-1 Tax through the CREB/ATF pathway. Up-regulated CC by the regulator of nonsense transcript UPF1. Up-regulated by the CC cyclic AMP-dependent transcription factor ATF4. CC {ECO:0000269|PubMed:16787922, ECO:0000269|PubMed:18375384, CC ECO:0000269|PubMed:18774934, ECO:0000269|PubMed:22235304}. CC -!- DOMAIN: The KRAB domain functions to reinforce the nuclear localization CC of isoform 1 in addition to its transcription repression activity. CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF317549; AAG59817.1; -; mRNA. DR EMBL; AF385187; AAK69307.1; -; mRNA. DR EMBL; AF432217; AAL99923.1; -; mRNA. DR EMBL; AC026785; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; DQ057356; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; DQ057357; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; DQ057358; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; DQ057359; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; DQ057360; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; X78926; CAA55526.1; -; mRNA. DR CCDS; CCDS45012.1; -. [Q14587-1] DR CCDS; CCDS53853.1; -. [Q14587-4] DR CCDS; CCDS59240.1; -. [Q14587-6] DR PIR; S47071; S47071. DR RefSeq; NP_001159353.1; NM_001165881.2. [Q14587-1] DR RefSeq; NP_001159355.1; NM_001165883.1. [Q14587-6] DR RefSeq; NP_001159356.2; NM_001165884.2. DR RefSeq; NP_001159357.1; NM_001165885.1. DR RefSeq; NP_001159358.1; NM_001165886.1. DR RefSeq; NP_001159359.1; NM_001165887.1. DR RefSeq; NP_003406.1; NM_003415.2. [Q14587-1] DR RefSeq; NP_694422.2; NM_152943.2. DR PDB; 2EL4; NMR; -; A=663-695. DR PDB; 2EL5; NMR; -; A=749-777. DR PDB; 2EL6; NMR; -; A=831-863. DR PDB; 2EM1; NMR; -; A=637-667. DR PDB; 2EMV; NMR; -; A=859-889. DR PDB; 2EMW; NMR; -; A=301-331. DR PDB; 2EMX; NMR; -; A=273-303. DR PDB; 2EMY; NMR; -; A=551-583. DR PDB; 2EN0; NMR; -; A=385-413. DR PDB; 2EN6; NMR; -; A=887-919. DR PDB; 2EN7; NMR; -; A=495-525. DR PDB; 2EOF; NMR; -; A=411-441. DR PDB; 2EOG; NMR; -; A=693-723. DR PDB; 2EOI; NMR; -; A=329-359. DR PDB; 2EOJ; NMR; -; A=355-385. DR PDB; 2EOK; NMR; -; A=441-469. DR PDB; 2EOL; NMR; -; A=581-609. DR PDB; 2EOP; NMR; -; A=719-751. DR PDB; 2EPV; NMR; -; A=803-833. DR PDB; 2EPW; NMR; -; A=915-947. DR PDB; 2EPY; NMR; -; A=525-553. DR PDB; 2YTF; NMR; -; A=607-639. DR PDB; 2YTQ; NMR; -; A=775-807. DR PDBsum; 2EL4; -. DR PDBsum; 2EL5; -. DR PDBsum; 2EL6; -. DR PDBsum; 2EM1; -. DR PDBsum; 2EMV; -. DR PDBsum; 2EMW; -. DR PDBsum; 2EMX; -. DR PDBsum; 2EMY; -. DR PDBsum; 2EN0; -. DR PDBsum; 2EN6; -. DR PDBsum; 2EN7; -. DR PDBsum; 2EOF; -. DR PDBsum; 2EOG; -. DR PDBsum; 2EOI; -. DR PDBsum; 2EOJ; -. DR PDBsum; 2EOK; -. DR PDBsum; 2EOL; -. DR PDBsum; 2EOP; -. DR PDBsum; 2EPV; -. DR PDBsum; 2EPW; -. DR PDBsum; 2EPY; -. DR PDBsum; 2YTF; -. DR PDBsum; 2YTQ; -. DR AlphaFoldDB; Q14587; -. DR SMR; Q14587; -. DR BioGRID; 116010; 13. DR IntAct; Q14587; 1. DR STRING; 9606.ENSP00000444412; -. DR iPTMnet; Q14587; -. DR PhosphoSitePlus; Q14587; -. DR BioMuta; ZNF268; -. DR DMDM; 19863363; -. DR EPD; Q14587; -. DR jPOST; Q14587; -. DR MassIVE; Q14587; -. DR MaxQB; Q14587; -. DR PaxDb; 9606-ENSP00000444412; -. DR PeptideAtlas; Q14587; -. DR ProteomicsDB; 60060; -. [Q14587-1] DR ProteomicsDB; 60061; -. [Q14587-2] DR Antibodypedia; 834; 186 antibodies from 19 providers. DR DNASU; 10795; -. DR Ensembl; ENST00000228289.9; ENSP00000228289.5; ENSG00000090612.22. [Q14587-1] DR Ensembl; ENST00000536435.7; ENSP00000444412.3; ENSG00000090612.22. [Q14587-1] DR Ensembl; ENST00000539248.6; ENSP00000467781.1; ENSG00000090612.22. [Q14587-6] DR Ensembl; ENST00000588312.2; ENSP00000466622.1; ENSG00000090612.22. [Q14587-7] DR GeneID; 10795; -. DR KEGG; hsa:10795; -. DR MANE-Select; ENST00000536435.7; ENSP00000444412.3; NM_003415.3; NP_003406.1. DR UCSC; uc010tbw.3; human. [Q14587-1] DR AGR; HGNC:13061; -. DR CTD; 10795; -. DR DisGeNET; 10795; -. DR GeneCards; ZNF268; -. DR HGNC; HGNC:13061; ZNF268. DR HPA; ENSG00000090612; Low tissue specificity. DR MIM; 604753; gene. DR neXtProt; NX_Q14587; -. DR OpenTargets; ENSG00000090612; -. DR PharmGKB; PA37639; -. DR VEuPathDB; HostDB:ENSG00000090612; -. DR eggNOG; KOG1721; Eukaryota. DR GeneTree; ENSGT00940000163459; -. DR HOGENOM; CLU_002678_17_1_1; -. DR InParanoid; Q14587; -. DR OMA; AKGYECT; -. DR OrthoDB; 4637982at2759; -. DR PhylomeDB; Q14587; -. DR PathwayCommons; Q14587; -. DR Reactome; R-HSA-212436; Generic Transcription Pathway. DR SignaLink; Q14587; -. DR SIGNOR; Q14587; -. DR BioGRID-ORCS; 10795; 12 hits in 1181 CRISPR screens. DR ChiTaRS; ZNF268; human. DR EvolutionaryTrace; Q14587; -. DR GeneWiki; ZNF268; -. DR GenomeRNAi; 10795; -. DR Pharos; Q14587; Tbio. DR PRO; PR:Q14587; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q14587; Protein. DR Bgee; ENSG00000090612; Expressed in adrenal tissue and 193 other cell types or tissues. DR ExpressionAtlas; Q14587; baseline and differential. DR Genevisible; Q14587; HS. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central. DR GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB. DR GO; GO:0045597; P:positive regulation of cell differentiation; IMP:UniProtKB. DR GO; GO:0030335; P:positive regulation of cell migration; IMP:UniProtKB. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB. DR GO; GO:1901224; P:positive regulation of non-canonical NF-kappaB signal transduction; IDA:UniProtKB. DR GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:UniProtKB. DR GO; GO:0090073; P:positive regulation of protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0051726; P:regulation of cell cycle; IMP:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; NAS:UniProtKB. DR GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:UniProtKB. DR GO; GO:0043497; P:regulation of protein heterodimerization activity; IDA:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd07765; KRAB_A-box; 1. DR Gene3D; 6.10.140.140; -; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 24. DR InterPro; IPR001909; KRAB. DR InterPro; IPR036051; KRAB_dom_sf. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR23226; ZINC FINGER AND SCAN DOMAIN-CONTAINING; 1. DR PANTHER; PTHR23226:SF398; ZINC FINGER PROTEIN 715; 1. DR Pfam; PF01352; KRAB; 1. DR Pfam; PF00096; zf-C2H2; 23. DR SMART; SM00349; KRAB; 1. DR SMART; SM00355; ZnF_C2H2; 24. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 12. DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1. DR PROSITE; PS50805; KRAB; 1. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 24. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 24. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Differentiation; KW DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat; Repressor; KW Transcription; Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1..947 FT /note="Zinc finger protein 268" FT /id="PRO_0000047495" FT DOMAIN 81..152 FT /note="KRAB" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119" FT ZN_FING 276..298 FT /note="C2H2-type 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 304..326 FT /note="C2H2-type 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 332..354 FT /note="C2H2-type 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 360..382 FT /note="C2H2-type 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 388..410 FT /note="C2H2-type 5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 416..438 FT /note="C2H2-type 6" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 444..466 FT /note="C2H2-type 7" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 472..494 FT /note="C2H2-type 8" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 500..522 FT /note="C2H2-type 9" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 528..550 FT /note="C2H2-type 10" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 556..578 FT /note="C2H2-type 11" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 584..606 FT /note="C2H2-type 12" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 612..634 FT /note="C2H2-type 13" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 640..662 FT /note="C2H2-type 14" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 668..690 FT /note="C2H2-type 15" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 696..718 FT /note="C2H2-type 16" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 724..746 FT /note="C2H2-type 17" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 752..774 FT /note="C2H2-type 18" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 780..802 FT /note="C2H2-type 19" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 808..830 FT /note="C2H2-type 20" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 836..858 FT /note="C2H2-type 21" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 864..886 FT /note="C2H2-type 22" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 892..914 FT /note="C2H2-type 23" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT ZN_FING 920..942 FT /note="C2H2-type 24" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042" FT VAR_SEQ 1..161 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:11311945, FT ECO:0000303|PubMed:12200376" FT /id="VSP_006909" FT VAR_SEQ 1..140 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:16865230, FT ECO:0000303|PubMed:18949428" FT /id="VSP_053461" FT VAR_SEQ 12..99 FT /note="VPPLQERNSSWDRIRKLQGQESILGQGTPGLQPLPGTPRQKQKSRRIEKVLE FT WLFISQEQPKITKSWGPLSFMDVFVDFTWEEWQLLD -> GTNTPNLISSSSWNKEKSC FT VWCRPKFQIRPVQTQSGKLMILWIGIRKIKTSWEVWQKALNALHLENYVFLVQSIFQDK FT NLINVARMERV (in isoform 4)" FT /evidence="ECO:0000303|PubMed:16865230, FT ECO:0000303|PubMed:18949428" FT /id="VSP_053462" FT VAR_SEQ 12..78 FT /note="Missing (in isoform 7)" FT /evidence="ECO:0000303|PubMed:16865230, FT ECO:0000303|PubMed:18949428" FT /id="VSP_053463" FT VAR_SEQ 12..44 FT /note="VPPLQERNSSWDRIRKLQGQESILGQGTPGLQP -> GTNTPNLISSSSWNK FT EKSCVWCRPKFQIRPVQF (in isoform 6)" FT /evidence="ECO:0000303|PubMed:16865230, FT ECO:0000303|PubMed:18949428" FT /id="VSP_053464" FT VAR_SEQ 45..947 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:16865230, FT ECO:0000303|PubMed:18949428" FT /id="VSP_053465" FT VAR_SEQ 79..135 FT /note="GPLSFMDVFVDFTWEEWQLLDPAQKCLYRSVMLENYSNLVSLGYQHTKPDII FT FKLEQ -> TQSGKLMILWIGIRKIKTSWEVRQKALNALHLENYVFLVQSIFQDKNLIN FT VARMERV (in isoform 5)" FT /evidence="ECO:0000303|PubMed:16865230, FT ECO:0000303|PubMed:18949428" FT /id="VSP_053466" FT VAR_SEQ 100..947 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:16865230, FT ECO:0000303|PubMed:18949428" FT /id="VSP_053467" FT VAR_SEQ 136..947 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:16865230, FT ECO:0000303|PubMed:18949428" FT /id="VSP_053468" FT VAR_SEQ 153..183 FT /note="NTVWKIDDLMDWHQENKDKLGSTAKSFECTT -> ILKAGKSKAKVLAGLVS FT GEGPLCASKMTPCC (in isoform 7)" FT /evidence="ECO:0000303|PubMed:16865230, FT ECO:0000303|PubMed:18949428" FT /id="VSP_053469" FT VAR_SEQ 184..947 FT /note="Missing (in isoform 7)" FT /evidence="ECO:0000303|PubMed:16865230, FT ECO:0000303|PubMed:18949428" FT /id="VSP_053470" FT VAR_SEQ 222..947 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:16865230, FT ECO:0000303|PubMed:18949428" FT /id="VSP_053471" FT VARIANT 175 FT /note="T -> M (in dbSNP:rs7975069)" FT /id="VAR_033562" FT MUTAGEN 85 FT /note="D->A: Strongly reduces nuclear localization and FT interaction with TRIM28; when associated with A-86." FT /evidence="ECO:0000269|PubMed:23665872" FT MUTAGEN 86 FT /note="V->A: Reduces nuclear localization. Strongly reduces FT nuclear localization and interaction with TRIM28; when FT associated with A-85." FT /evidence="ECO:0000269|PubMed:23665872" FT MUTAGEN 88 FT /note="V->A: Reduces nuclear localization." FT /evidence="ECO:0000269|PubMed:23665872" FT MUTAGEN 90 FT /note="F->A: Reduces nuclear localization." FT /evidence="ECO:0000269|PubMed:23665872" FT MUTAGEN 93 FT /note="E->A: Reduces nuclear localization. Strongly reduces FT nuclear localization; when associated with A-94 and A-95." FT /evidence="ECO:0000269|PubMed:23665872" FT MUTAGEN 94 FT /note="E->A: Reduces nuclear localization. Inhibits nuclear FT localization; when associated with A-93 and A-95." FT /evidence="ECO:0000269|PubMed:23665872" FT MUTAGEN 95 FT /note="W->A: Reduces nuclear localization. Inhibits nuclear FT localization; when associated with A-93 and A-94." FT /evidence="ECO:0000269|PubMed:23665872" FT CONFLICT 323 FT /note="Q -> P (in Ref. 2; AAL99923)" FT /evidence="ECO:0000305" FT CONFLICT 335..336 FT /note="SE -> IN (in Ref. 2; AAL99923)" FT /evidence="ECO:0000305" FT CONFLICT 340 FT /note="T -> A (in Ref. 2; AAL99923)" FT /evidence="ECO:0000305" FT CONFLICT 344 FT /note="H -> Q (in Ref. 2; AAL99923)" FT /evidence="ECO:0000305" FT CONFLICT 363 FT /note="C -> D (in Ref. 2; AAL99923)" FT /evidence="ECO:0000305" FT CONFLICT 409 FT /note="I -> T (in Ref. 2; AAL99923)" FT /evidence="ECO:0000305" FT CONFLICT 860 FT /note="R -> T (in Ref. 2; AAL99923 and 6; CAA55526)" FT /evidence="ECO:0000305" FT STRAND 279..282 FT /evidence="ECO:0007829|PDB:2EMX" FT STRAND 284..287 FT /evidence="ECO:0007829|PDB:2EMX" FT HELIX 288..298 FT /evidence="ECO:0007829|PDB:2EMX" FT STRAND 304..306 FT /evidence="ECO:0007829|PDB:2EMW" FT TURN 307..310 FT /evidence="ECO:0007829|PDB:2EMW" FT STRAND 311..315 FT /evidence="ECO:0007829|PDB:2EMW" FT HELIX 316..323 FT /evidence="ECO:0007829|PDB:2EMW" FT TURN 324..326 FT /evidence="ECO:0007829|PDB:2EMW" FT STRAND 335..337 FT /evidence="ECO:0007829|PDB:2EOI" FT STRAND 340..343 FT /evidence="ECO:0007829|PDB:2EOI" FT HELIX 344..354 FT /evidence="ECO:0007829|PDB:2EOI" FT TURN 363..366 FT /evidence="ECO:0007829|PDB:2EOJ" FT HELIX 372..379 FT /evidence="ECO:0007829|PDB:2EOJ" FT STRAND 382..385 FT /evidence="ECO:0007829|PDB:2EOJ" FT STRAND 391..393 FT /evidence="ECO:0007829|PDB:2EN0" FT STRAND 396..399 FT /evidence="ECO:0007829|PDB:2EN0" FT HELIX 400..411 FT /evidence="ECO:0007829|PDB:2EN0" FT STRAND 415..417 FT /evidence="ECO:0007829|PDB:2EOF" FT TURN 419..421 FT /evidence="ECO:0007829|PDB:2EOF" FT STRAND 424..426 FT /evidence="ECO:0007829|PDB:2EOF" FT HELIX 428..437 FT /evidence="ECO:0007829|PDB:2EOF" FT TURN 438..440 FT /evidence="ECO:0007829|PDB:2EOF" FT STRAND 443..445 FT /evidence="ECO:0007829|PDB:2EOK" FT STRAND 447..449 FT /evidence="ECO:0007829|PDB:2EOK" FT STRAND 452..455 FT /evidence="ECO:0007829|PDB:2EOK" FT HELIX 456..465 FT /evidence="ECO:0007829|PDB:2EOK" FT TURN 466..468 FT /evidence="ECO:0007829|PDB:2EOK" FT STRAND 495..500 FT /evidence="ECO:0007829|PDB:2EN7" FT TURN 503..505 FT /evidence="ECO:0007829|PDB:2EN7" FT HELIX 512..519 FT /evidence="ECO:0007829|PDB:2EN7" FT TURN 520..522 FT /evidence="ECO:0007829|PDB:2EN7" FT STRAND 527..529 FT /evidence="ECO:0007829|PDB:2EPY" FT STRAND 531..533 FT /evidence="ECO:0007829|PDB:2EPY" FT STRAND 536..539 FT /evidence="ECO:0007829|PDB:2EPY" FT HELIX 540..547 FT /evidence="ECO:0007829|PDB:2EPY" FT TURN 548..550 FT /evidence="ECO:0007829|PDB:2EPY" FT STRAND 559..561 FT /evidence="ECO:0007829|PDB:2EMY" FT STRAND 564..567 FT /evidence="ECO:0007829|PDB:2EMY" FT HELIX 568..578 FT /evidence="ECO:0007829|PDB:2EMY" FT TURN 587..589 FT /evidence="ECO:0007829|PDB:2EOL" FT STRAND 592..596 FT /evidence="ECO:0007829|PDB:2EOL" FT HELIX 597..606 FT /evidence="ECO:0007829|PDB:2EOL" FT STRAND 611..613 FT /evidence="ECO:0007829|PDB:2YTF" FT STRAND 615..617 FT /evidence="ECO:0007829|PDB:2YTF" FT STRAND 620..623 FT /evidence="ECO:0007829|PDB:2YTF" FT HELIX 624..632 FT /evidence="ECO:0007829|PDB:2YTF" FT STRAND 639..642 FT /evidence="ECO:0007829|PDB:2EM1" FT TURN 643..646 FT /evidence="ECO:0007829|PDB:2EM1" FT STRAND 647..651 FT /evidence="ECO:0007829|PDB:2EM1" FT HELIX 652..659 FT /evidence="ECO:0007829|PDB:2EM1" FT TURN 660..662 FT /evidence="ECO:0007829|PDB:2EM1" FT STRAND 667..669 FT /evidence="ECO:0007829|PDB:2EL4" FT STRAND 671..674 FT /evidence="ECO:0007829|PDB:2EL4" FT STRAND 676..679 FT /evidence="ECO:0007829|PDB:2EL4" FT HELIX 680..686 FT /evidence="ECO:0007829|PDB:2EL4" FT HELIX 687..689 FT /evidence="ECO:0007829|PDB:2EL4" FT STRAND 690..692 FT /evidence="ECO:0007829|PDB:2EL4" FT STRAND 699..701 FT /evidence="ECO:0007829|PDB:2EOG" FT HELIX 708..719 FT /evidence="ECO:0007829|PDB:2EOG" FT TURN 727..729 FT /evidence="ECO:0007829|PDB:2EOP" FT HELIX 736..743 FT /evidence="ECO:0007829|PDB:2EOP" FT TURN 744..748 FT /evidence="ECO:0007829|PDB:2EOP" FT STRAND 751..753 FT /evidence="ECO:0007829|PDB:2EL5" FT STRAND 755..757 FT /evidence="ECO:0007829|PDB:2EL5" FT STRAND 760..763 FT /evidence="ECO:0007829|PDB:2EL5" FT HELIX 764..771 FT /evidence="ECO:0007829|PDB:2EL5" FT HELIX 772..774 FT /evidence="ECO:0007829|PDB:2EL5" FT STRAND 783..785 FT /evidence="ECO:0007829|PDB:2YTQ" FT HELIX 792..799 FT /evidence="ECO:0007829|PDB:2YTQ" FT TURN 800..802 FT /evidence="ECO:0007829|PDB:2YTQ" FT STRAND 807..809 FT /evidence="ECO:0007829|PDB:2EPV" FT STRAND 811..813 FT /evidence="ECO:0007829|PDB:2EPV" FT STRAND 816..819 FT /evidence="ECO:0007829|PDB:2EPV" FT HELIX 820..827 FT /evidence="ECO:0007829|PDB:2EPV" FT HELIX 828..830 FT /evidence="ECO:0007829|PDB:2EPV" FT STRAND 835..837 FT /evidence="ECO:0007829|PDB:2EL6" FT STRAND 839..842 FT /evidence="ECO:0007829|PDB:2EL6" FT STRAND 844..847 FT /evidence="ECO:0007829|PDB:2EL6" FT HELIX 848..855 FT /evidence="ECO:0007829|PDB:2EL6" FT HELIX 856..858 FT /evidence="ECO:0007829|PDB:2EL6" FT STRAND 862..865 FT /evidence="ECO:0007829|PDB:2EMV" FT STRAND 867..869 FT /evidence="ECO:0007829|PDB:2EMV" FT STRAND 872..875 FT /evidence="ECO:0007829|PDB:2EMV" FT HELIX 876..886 FT /evidence="ECO:0007829|PDB:2EMV" FT TURN 895..897 FT /evidence="ECO:0007829|PDB:2EN6" FT STRAND 900..903 FT /evidence="ECO:0007829|PDB:2EN6" FT HELIX 904..914 FT /evidence="ECO:0007829|PDB:2EN6" FT STRAND 919..921 FT /evidence="ECO:0007829|PDB:2EPW" FT STRAND 923..925 FT /evidence="ECO:0007829|PDB:2EPW" FT STRAND 928..932 FT /evidence="ECO:0007829|PDB:2EPW" FT HELIX 933..941 FT /evidence="ECO:0007829|PDB:2EPW" SQ SEQUENCE 947 AA; 108374 MW; AC78F4824F4BE1A0 CRC64; MATRVRTASI WVPPLQERNS SWDRIRKLQG QESILGQGTP GLQPLPGTPR QKQKSRRIEK VLEWLFISQE QPKITKSWGP LSFMDVFVDF TWEEWQLLDP AQKCLYRSVM LENYSNLVSL GYQHTKPDII FKLEQGEELC MVQAQVPNQT CPNTVWKIDD LMDWHQENKD KLGSTAKSFE CTTFGKLCLL STKYLSRQKP HKCGTHGKSL KYIDFTSDYA RNNPNGFQVH GKSFFHSKHE QTVIGIKYCE SIESGKTVNK KSQLMCQQMY MGEKPFGCSC CEKAFSSKSY LLVHQQTHAE EKPYGCNECG KDFSSKSYLI VHQRIHTGEK LHECSECRKT FSFHSQLVIH QRIHTGENPY ECCECGKVFS RKDQLVSHQK THSGQKPYVC NECGKAFGLK SQLIIHERIH TGEKPYECNE CQKAFNTKSN LMVHQRTHTG EKPYVCSDCG KAFTFKSQLI VHQGIHTGVK PYGCIQCGKG FSLKSQLIVH QRSHTGMKPY VCNECGKAFR SKSYLIIHTR THTGEKLHEC NNCGKAFSFK SQLIIHQRIH TGENPYECHE CGKAFSRKYQ LISHQRTHAG EKPYECTDCG KAFGLKSQLI IHQRTHTGEK PFECSECQKA FNTKSNLIVH QRTHTGEKPY SCNECGKAFT FKSQLIVHKG VHTGVKPYGC SQCAKTFSLK SQLIVHQRSH TGVKPYGCSE CGKAFRSKSY LIIHMRTHTG EKPHECRECG KSFSFNSQLI VHQRIHTGEN PYECSECGKA FNRKDQLISH QRTHAGEKPY GCSECGKAFS SKSYLIIHMR THSGEKPYEC NECGKAFIWK SLLIVHERTH AGVNPYKCSQ CEKSFSGKLR LLVHQRMHTR EKPYECSECG KAFIRNSQLI VHQRTHSGEK PYGCNECGKT FSQKSILSAH QRTHTGEKPC KCTECGKAFC WKSQLIMHQR THVDDKH //