ZN268_HUMAN
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 03-AUG-2022, entry version 206.
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}.
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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; 12.
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; Q14587; -.
DR PeptideAtlas; Q14587; -.
DR PRIDE; Q14587; -.
DR ProteomicsDB; 60060; -. [Q14587-1]
DR ProteomicsDB; 60061; -. [Q14587-2]
DR Antibodypedia; 834; 148 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 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; 1318335at2759; -.
DR PhylomeDB; Q14587; -.
DR PathwayCommons; Q14587; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q14587; -.
DR SIGNOR; Q14587; -.
DR BioGRID-ORCS; 10795; 11 hits in 1103 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 191 other 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 NIK/NF-kappaB signaling; 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: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 GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 20.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 24.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 12.
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
