CTCF_HUMAN
ID CTCF_HUMAN Reviewed; 727 AA.
AC P49711; B5MC38; Q53XI7; Q59EL8;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Transcriptional repressor CTCF;
DE AltName: Full=11-zinc finger protein;
DE AltName: Full=CCCTC-binding factor;
DE AltName: Full=CTCFL paralog;
GN Name=CTCF;
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] (ISOFORM 1), FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8649389; DOI=10.1128/mcb.16.6.2802;
RA Filippova G.N., Fagerlie S., Klenova E.M., Myers C., Dehner Y., Goodwin G.,
RA Neiman P.E., Collins S.J., Lobanenkov V.V.;
RT "An exceptionally conserved transcriptional repressor, CTCF, employs
RT different combinations of zinc fingers to bind diverged promoter sequences
RT of avian and mammalian c-myc oncogenes.";
RL Mol. Cell. Biol. 16:2802-2813(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=9591631;
RX DOI=10.1002/(sici)1098-2264(199805)22:1<26::aid-gcc4>3.0.co;2-9;
RA Filippova G.N., Lindblom A., Meincke L.J., Klenova E.M., Neiman P.E.,
RA Collins S.J., Doggett N.A., Lobanenkov V.V.;
RT "A widely expressed transcription factor with multiple DNA sequence
RT specificity, CTCF, is localized at chromosome segment 16q22.1 within one of
RT the smallest regions of overlap for common deletions in breast and prostate
RT cancers.";
RL Genes Chromosomes Cancer 22:26-36(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS WILMS TUMOR TRP-339 AND
RP GLN-448, VARIANT BREAST TUMOR GLU-344, AND VARIANT PROSTATE TUMOR ARG-345.
RX PubMed=11782357;
RA Filippova G.N., Qi C.-F., Ulmer J.E., Moore J.M., Ward M.D., Hu Y.J.,
RA Loukinov D.I., Pugacheva E.M., Klenova E.M., Grundy P.E., Feinberg A.P.,
RA Cleton-Jansen A.-M., Moerland E.W., Cornelisse C.J., Suzuki H., Komiya A.,
RA Lindblom A., Dorion-Bonnet F., Neiman P.E., Morse H.C. III, Collins S.J.,
RA Lobanenkov V.V.;
RT "Tumor-associated zinc finger mutations in the CTCF transcription factor
RT selectively alter its DNA-binding specificity.";
RL Cancer Res. 62:48-52(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RT "Homo sapiens protein coding cDNA.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [7]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [9]
RP PROTEIN SEQUENCE OF 471-479 AND 483-487, AND TRANSCRIPTIONAL ACTIVATION OF
RP APP.
RX PubMed=9407128; DOI=10.1074/jbc.272.52.33353;
RA Vostrov A.A., Quitschke W.W.;
RT "The zinc finger protein CTCF binds to the APBbeta domain of the amyloid
RT beta-protein precursor promoter. Evidence for a role in transcriptional
RT activation.";
RL J. Biol. Chem. 272:33353-33359(1997).
RN [10]
RP REVIEW.
RX PubMed=12191639; DOI=10.1016/s1044-579x(02)00060-3;
RA Klenova E.M., Morse H.C. III, Ohlsson R., Lobanenkov V.V.;
RT "The novel BORIS + CTCF gene family is uniquely involved in the epigenetics
RT of normal biology and cancer.";
RL Semin. Cancer Biol. 12:399-414(2002).
RN [11]
RP FUNCTION.
RX PubMed=11743158; DOI=10.1126/science.1065982;
RA Chao W., Huynh K.D., Spencer R.J., Davidow L.S., Lee J.T.;
RT "CTCF, a candidate trans-acting factor for X-inactivation choice.";
RL Science 295:345-347(2002).
RN [12]
RP SUBCELLULAR LOCATION, AND ASSOCIATION WITH H19 ICR.
RX PubMed=16107875; DOI=10.1038/sj.emboj.7600793;
RA Burke L.J., Zhang R., Bartkuhn M., Tiwari V.K., Tavoosidana G.,
RA Kurukuti S., Weth C., Leers J., Galjart N., Ohlsson R., Renkawitz R.;
RT "CTCF binding and higher order chromatin structure of the H19 locus are
RT maintained in mitotic chromatin.";
RL EMBO J. 24:3291-3300(2005).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=16595548; DOI=10.1242/jcs.02890;
RA Torrano V., Navascues J., Docquier F., Zhang R., Burke L.J., Chernukhin I.,
RA Farrar D., Leon J., Berciano M.T., Renkawitz R., Klenova E., Lafarga M.,
RA Delgado M.D.;
RT "Targeting of CTCF to the nucleolus inhibits nucleolar transcription
RT through a poly(ADP-ribosyl)ation-dependent mechanism.";
RL J. Cell Sci. 119:1746-1759(2006).
RN [14]
RP INTERACTION WITH CHD8.
RX PubMed=16949368; DOI=10.1016/j.molcel.2006.08.008;
RA Ishihara K., Oshimura M., Nakao M.;
RT "CTCF-dependent chromatin insulator is linked to epigenetic remodeling.";
RL Mol. Cell 23:733-742(2006).
RN [15]
RP FUNCTION.
RX PubMed=16815976; DOI=10.1073/pnas.0600326103;
RA Kurukuti S., Tiwari V.K., Tavoosidana G., Pugacheva E., Murrell A.,
RA Zhao Z., Lobanenkov V., Reik W., Ohlsson R.;
RT "CTCF binding at the H19 imprinting control region mediates maternally
RT inherited higher-order chromatin conformation to restrict enhancer access
RT to Igf2.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:10684-10689(2006).
RN [16]
RP FUNCTION.
RX PubMed=17827499; DOI=10.1074/jbc.m706213200;
RA Renda M., Baglivo I., Burgess-Beusse B., Esposito S., Fattorusso R.,
RA Felsenfeld G., Pedone P.V.;
RT "Critical DNA binding interactions of the insulator protein CTCF: a small
RT number of zinc fingers mediate strong binding, and a single finger-DNA
RT interaction controls binding at imprinted loci.";
RL J. Biol. Chem. 282:33336-33345(2007).
RN [17]
RP FUNCTION.
RX PubMed=18413740; DOI=10.1158/0008-5472.can-07-6654;
RA Sun L., Huang L., Nguyen P., Bisht K.S., Bar-Sela G., Ho A.S.,
RA Bradbury C.M., Yu W., Cui H., Lee S., Trepel J.B., Feinberg A.P., Gius D.;
RT "DNA methyltransferase 1 and 3B activate BAG-1 expression via recruitment
RT of CTCFL/BORIS and modulation of promoter histone methylation.";
RL Cancer Res. 68:2726-2735(2008).
RN [18]
RP FUNCTION.
RX PubMed=18347100; DOI=10.1084/jem.20071843;
RA Majumder P., Gomez J.A., Chadwick B.P., Boss J.M.;
RT "The insulator factor CTCF controls MHC class II gene expression and is
RT required for the formation of long-distance chromatin interactions.";
RL J. Exp. Med. 205:785-798(2008).
RN [19]
RP FUNCTION.
RX PubMed=18654629; DOI=10.1371/journal.pgen.1000138;
RA Fu Y., Sinha M., Peterson C.L., Weng Z.;
RT "The insulator binding protein CTCF positions 20 nucleosomes around its
RT binding sites across the human genome.";
RL PLoS Genet. 4:E1000138-E1000138(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-374; SER-402; SER-609;
RP SER-610 AND SER-612, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [21]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18550811; DOI=10.1073/pnas.0801273105;
RA Rubio E.D., Reiss D.J., Welcsh P.L., Disteche C.M., Filippova G.N.,
RA Baliga N.S., Aebersold R., Ranish J.A., Krumm A.;
RT "CTCF physically links cohesin to chromatin.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:8309-8314(2008).
RN [22]
RP FUNCTION.
RX PubMed=19322193; DOI=10.1038/emboj.2009.81;
RA Mishiro T., Ishihara K., Hino S., Tsutsumi S., Aburatani H., Shirahige K.,
RA Kinoshita Y., Nakao M.;
RT "Architectural roles of multiple chromatin insulators at the human
RT apolipoprotein gene cluster.";
RL EMBO J. 28:1234-1245(2009).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [24]
RP IDENTIFICATION BY MASS 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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-289; THR-317; SER-609;
RP SER-610 AND SER-612, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-609; SER-610 AND SER-612, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [29]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-689, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [30]
RP FUNCTION, INTERACTION WITH CENPE, AND SUBCELLULAR LOCATION.
RX PubMed=26321640; DOI=10.1016/j.celrep.2015.08.005;
RA Xiao T., Wongtrakoongate P., Trainor C., Felsenfeld G.;
RT "CTCF recruits centromeric protein CENP-E to the
RT pericentromeric/centromeric regions of chromosomes through unusual CTCF-
RT binding sites.";
RL Cell Rep. 12:1704-1714(2015).
RN [31]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-18; LYS-219 AND LYS-689, 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 [32]
RP STRUCTURE BY NMR OF 399-589.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of zinc finger domains of transcriptional repressor
RT CTCF protein.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [33]
RP VARIANT MRD21 TRP-567.
RX PubMed=23746550; DOI=10.1016/j.ajhg.2013.05.007;
RA Gregor A., Oti M., Kouwenhoven E.N., Hoyer J., Sticht H., Ekici A.B.,
RA Kjaergaard S., Rauch A., Stunnenberg H.G., Uebe S., Vasileiou G., Reis A.,
RA Zhou H., Zweier C.;
RT "De novo mutations in the genome organizer CTCF cause intellectual
RT disability.";
RL Am. J. Hum. Genet. 93:124-131(2013).
RN [34]
RP VARIANTS 19-GLY--ARG-727 DEL; CYS-278; HIS-342 AND THR-365,
RP CHARACTERIZATION OF VARIANTS CYS-278; HIS-342 AND THR-365, AND SUBCELLULAR
RP LOCATION.
RX PubMed=28319062; DOI=10.1038/onc.2017.25;
RA Marshall A.D., Bailey C.G., Champ K., Vellozzi M., O'Young P., Metierre C.,
RA Feng Y., Thoeng A., Richards A.M., Schmitz U., Biro M., Jayasinghe R.,
RA Ding L., Anderson L., Mardis E.R., Rasko J.E.J.;
RT "CTCF genetic alterations in endometrial carcinoma are pro-tumorigenic.";
RL Oncogene 36:4100-4110(2017).
CC -!- FUNCTION: Chromatin binding factor that binds to DNA sequence specific
CC sites. Involved in transcriptional regulation by binding to chromatin
CC insulators and preventing interaction between promoter and nearby
CC enhancers and silencers. Acts as transcriptional repressor binding to
CC promoters of vertebrate MYC gene and BAG1 gene. Also binds to the PLK
CC and PIM1 promoters. Acts as a transcriptional activator of APP.
CC Regulates APOA1/C3/A4/A5 gene cluster and controls MHC class II gene
CC expression. Plays an essential role in oocyte and preimplantation
CC embryo development by activating or repressing transcription. Seems to
CC act as tumor suppressor. Plays a critical role in the epigenetic
CC regulation. Participates in the allele-specific gene expression at the
CC imprinted IGF2/H19 gene locus. On the maternal allele, binding within
CC the H19 imprinting control region (ICR) mediates maternally inherited
CC higher-order chromatin conformation to restrict enhancer access to
CC IGF2. Plays a critical role in gene silencing over considerable
CC distances in the genome. Preferentially interacts with unmethylated
CC DNA, preventing spreading of CpG methylation and maintaining
CC methylation-free zones. Inversely, binding to target sites is prevented
CC by CpG methylation. Plays an important role in chromatin remodeling.
CC Can dimerize when it is bound to different DNA sequences, mediating
CC long-range chromatin looping. Mediates interchromosomal association
CC between IGF2/H19 and WSB1/NF1 and may direct distant DNA segments to a
CC common transcription factory. Causes local loss of histone acetylation
CC and gain of histone methylation in the beta-globin locus, without
CC affecting transcription. When bound to chromatin, it provides an anchor
CC point for nucleosomes positioning. Seems to be essential for homologous
CC X-chromosome pairing. May participate with Tsix in establishing a
CC regulatable epigenetic switch for X chromosome inactivation. May play a
CC role in preventing the propagation of stable methylation at the escape
CC genes from X- inactivation. Involved in sister chromatid cohesion.
CC Associates with both centromeres and chromosomal arms during metaphase
CC and required for cohesin localization to CTCF sites. Regulates
CC asynchronous replication of IGF2/H19. Plays a role in the recruitment
CC of CENPE to the pericentromeric/centromeric regions of the chromosome
CC during mitosis (PubMed:26321640). {ECO:0000269|PubMed:11743158,
CC ECO:0000269|PubMed:16815976, ECO:0000269|PubMed:17827499,
CC ECO:0000269|PubMed:18347100, ECO:0000269|PubMed:18413740,
CC ECO:0000269|PubMed:18550811, ECO:0000269|PubMed:18654629,
CC ECO:0000269|PubMed:19322193, ECO:0000269|PubMed:26321640,
CC ECO:0000269|PubMed:8649389, ECO:0000269|PubMed:9591631}.
CC -!- SUBUNIT: Interacts with CHD8 (PubMed:16949368). Interacts with LLPH (By
CC similarity). Interacts with CENPE (PubMed:26321640).
CC {ECO:0000250|UniProtKB:Q61164, ECO:0000269|PubMed:16949368,
CC ECO:0000269|PubMed:26321640}.
CC -!- INTERACTION:
CC P49711; P05067: APP; NbExp=3; IntAct=EBI-932887, EBI-77613;
CC P49711; Q00341: HDLBP; NbExp=4; IntAct=EBI-932887, EBI-1049478;
CC P49711; Q9UGL1: KDM5B; NbExp=8; IntAct=EBI-932887, EBI-2514978;
CC P49711; Q01860: POU5F1; NbExp=2; IntAct=EBI-932887, EBI-475687;
CC P49711; Q12933: TRAF2; NbExp=3; IntAct=EBI-932887, EBI-355744;
CC P49711; Q5VZL5: ZMYM4; NbExp=3; IntAct=EBI-932887, EBI-2514659;
CC P49711; O95789-4: ZMYM6; NbExp=3; IntAct=EBI-932887, EBI-12949277;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:28319062}. Chromosome
CC {ECO:0000269|PubMed:26321640}. Chromosome, centromere
CC {ECO:0000269|PubMed:26321640}. Note=May translocate to the nucleolus
CC upon cell differentiation. Associates with both centromeres and
CC chromosomal arms during metaphase. Associates with the H19 ICR in
CC mitotic chromosomes. May be preferentially excluded from
CC heterochromatin during interphase.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P49711-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P49711-2; Sequence=VSP_045350;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Absent in primary spermatocytes.
CC {ECO:0000269|PubMed:9591631}.
CC -!- DOMAIN: The 11 zinc fingers are highly conserved among vertebrates,
CC exhibiting almost identical amino acid sequences. Different subsets or
CC combination of individual zinc fingers gives the ability to CTCF to
CC recognize multiple DNA target sites.
CC -!- PTM: Sumoylated on Lys-74 and Lys-689; sumoylation of CTCF contributes
CC to the repressive function of CTCF on the MYC P2 promoter.
CC {ECO:0000250|UniProtKB:Q61164}.
CC -!- DISEASE: Intellectual developmental disorder, autosomal dominant 21
CC (MRD21) [MIM:615502]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period.
CC Additional MRD21 features include short stature, microcephaly, and
CC developmental delay. {ECO:0000269|PubMed:23746550}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: More than 13'00 CTCF-binding sites in potential
CC insulators were identified in the human genome.
CC -!- SIMILARITY: Belongs to the CTCF zinc-finger protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD93030.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/CTCFID40187ch16q22.html";
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DR EMBL; U25435; AAB07788.1; -; mRNA.
DR EMBL; AF145477; AAF31318.1; -; Genomic_DNA.
DR EMBL; AF145468; AAF31318.1; JOINED; Genomic_DNA.
DR EMBL; AF145469; AAF31318.1; JOINED; Genomic_DNA.
DR EMBL; AF145470; AAF31318.1; JOINED; Genomic_DNA.
DR EMBL; AF145471; AAF31318.1; JOINED; Genomic_DNA.
DR EMBL; AF145472; AAF31318.1; JOINED; Genomic_DNA.
DR EMBL; AF145473; AAF31318.1; JOINED; Genomic_DNA.
DR EMBL; AF145474; AAF31318.1; JOINED; Genomic_DNA.
DR EMBL; AF145475; AAF31318.1; JOINED; Genomic_DNA.
DR EMBL; AF145476; AAF31318.1; JOINED; Genomic_DNA.
DR EMBL; BT009915; AAP88917.1; -; mRNA.
DR EMBL; AB209793; BAD93030.1; ALT_INIT; mRNA.
DR EMBL; AC009095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC027682; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471092; EAW83142.1; -; Genomic_DNA.
DR EMBL; BC014267; AAH14267.1; -; mRNA.
DR CCDS; CCDS10841.1; -. [P49711-1]
DR CCDS; CCDS54029.1; -. [P49711-2]
DR PIR; G01792; G01792.
DR RefSeq; NP_001177951.1; NM_001191022.1. [P49711-2]
DR RefSeq; NP_006556.1; NM_006565.3. [P49711-1]
DR RefSeq; XP_016878357.1; XM_017022868.1. [P49711-1]
DR PDB; 1X6H; NMR; -; A=515-587.
DR PDB; 2CT1; NMR; -; A=399-462.
DR PDB; 5K5H; X-ray; 3.11 A; A=348-464.
DR PDB; 5K5I; X-ray; 2.19 A; A=378-489.
DR PDB; 5K5J; X-ray; 2.29 A; A=378-489.
DR PDB; 5K5L; X-ray; 3.12 A; E/F/G=405-492.
DR PDB; 5KKQ; X-ray; 1.74 A; A/D=321-465.
DR PDB; 5T00; X-ray; 2.19 A; A/D=321-465.
DR PDB; 5T0U; X-ray; 3.20 A; A/D=294-465.
DR PDB; 5UND; X-ray; 2.55 A; A/B=348-547.
DR PDB; 5YEF; X-ray; 2.81 A; A/B/G/J=292-490.
DR PDB; 5YEG; X-ray; 2.00 A; A=349-490, B=349-489.
DR PDB; 5YEH; X-ray; 2.33 A; A/B=349-490.
DR PDB; 5YEL; X-ray; 2.96 A; A/B=405-580.
DR PDB; 6QNX; X-ray; 2.70 A; C=1-727.
DR PDBsum; 1X6H; -.
DR PDBsum; 2CT1; -.
DR PDBsum; 5K5H; -.
DR PDBsum; 5K5I; -.
DR PDBsum; 5K5J; -.
DR PDBsum; 5K5L; -.
DR PDBsum; 5KKQ; -.
DR PDBsum; 5T00; -.
DR PDBsum; 5T0U; -.
DR PDBsum; 5UND; -.
DR PDBsum; 5YEF; -.
DR PDBsum; 5YEG; -.
DR PDBsum; 5YEH; -.
DR PDBsum; 5YEL; -.
DR PDBsum; 6QNX; -.
DR AlphaFoldDB; P49711; -.
DR SMR; P49711; -.
DR BioGRID; 115906; 304.
DR CORUM; P49711; -.
DR DIP; DIP-35252N; -.
DR IntAct; P49711; 77.
DR MINT; P49711; -.
DR STRING; 9606.ENSP00000264010; -.
DR ChEMBL; CHEMBL4523233; -.
DR iPTMnet; P49711; -.
DR PhosphoSitePlus; P49711; -.
DR SwissPalm; P49711; -.
DR BioMuta; CTCF; -.
DR DMDM; 1706179; -.
DR EPD; P49711; -.
DR jPOST; P49711; -.
DR MassIVE; P49711; -.
DR MaxQB; P49711; -.
DR PaxDb; P49711; -.
DR PeptideAtlas; P49711; -.
DR PRIDE; P49711; -.
DR ProteomicsDB; 56053; -. [P49711-1]
DR ProteomicsDB; 5985; -.
DR Antibodypedia; 15816; 449 antibodies from 41 providers.
DR DNASU; 10664; -.
DR Ensembl; ENST00000264010.10; ENSP00000264010.4; ENSG00000102974.16. [P49711-1]
DR Ensembl; ENST00000401394.6; ENSP00000384707.1; ENSG00000102974.16. [P49711-2]
DR Ensembl; ENST00000642819.1; ENSP00000494408.1; ENSG00000102974.16. [P49711-1]
DR Ensembl; ENST00000644753.1; ENSP00000493495.1; ENSG00000102974.16. [P49711-1]
DR Ensembl; ENST00000645699.1; ENSP00000495348.1; ENSG00000102974.16. [P49711-1]
DR Ensembl; ENST00000646076.1; ENSP00000494538.1; ENSG00000102974.16. [P49711-1]
DR GeneID; 10664; -.
DR KEGG; hsa:10664; -.
DR MANE-Select; ENST00000264010.10; ENSP00000264010.4; NM_006565.4; NP_006556.1.
DR UCSC; uc002etl.4; human. [P49711-1]
DR CTD; 10664; -.
DR DisGeNET; 10664; -.
DR GeneCards; CTCF; -.
DR HGNC; HGNC:13723; CTCF.
DR HPA; ENSG00000102974; Low tissue specificity.
DR MalaCards; CTCF; -.
DR MIM; 604167; gene.
DR MIM; 615502; phenotype.
DR neXtProt; NX_P49711; -.
DR OpenTargets; ENSG00000102974; -.
DR Orphanet; 363611; CTCF-related neurodevelopmental disorder.
DR PharmGKB; PA26998; -.
DR VEuPathDB; HostDB:ENSG00000102974; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000156672; -.
DR HOGENOM; CLU_002678_77_1_1; -.
DR InParanoid; P49711; -.
DR OMA; DPDWSKD; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P49711; -.
DR TreeFam; TF106430; -.
DR PathwayCommons; P49711; -.
DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
DR SignaLink; P49711; -.
DR SIGNOR; P49711; -.
DR BioGRID-ORCS; 10664; 797 hits in 1116 CRISPR screens.
DR ChiTaRS; CTCF; human.
DR EvolutionaryTrace; P49711; -.
DR GeneWiki; CTCF; -.
DR GenomeRNAi; 10664; -.
DR Pharos; P49711; Tbio.
DR PRO; PR:P49711; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P49711; protein.
DR Bgee; ENSG00000102974; Expressed in ventricular zone and 212 other tissues.
DR ExpressionAtlas; P49711; baseline and differential.
DR Genevisible; P49711; HS.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:UniProtKB.
DR GO; GO:0000793; C:condensed chromosome; IDA:UniProtKB.
DR GO; GO:0001673; C:male germ cell nucleus; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043035; F:chromatin insulator sequence binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0001221; F:transcription coregulator binding; IPI:ARUK-UCL.
DR GO; GO:0008270; F:zinc ion binding; TAS:UniProtKB.
DR GO; GO:0140588; P:chromatin looping; IDA:GO_Central.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0006306; P:DNA methylation; IEA:Ensembl.
DR GO; GO:0071514; P:genomic imprinting; IDA:GO_Central.
DR GO; GO:0010216; P:maintenance of DNA methylation; IEA:Ensembl.
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:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0071459; P:protein localization to chromosome, centromeric region; IMP:UniProtKB.
DR GO; GO:0070602; P:regulation of centromeric sister chromatid cohesion; NAS:UniProtKB.
DR GO; GO:0006349; P:regulation of gene expression by genomic imprinting; IEA:Ensembl.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:UniProtKB.
DR GO; GO:0035065; P:regulation of histone acetylation; IEA:Ensembl.
DR GO; GO:0031060; P:regulation of histone methylation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 6.
DR SMART; SM00355; ZnF_C2H2; 11.
DR SUPFAM; SSF57667; SSF57667; 7.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing; Centromere;
KW Chromatin regulator; Chromosome; Chromosome partition;
KW Direct protein sequencing; Disease variant; DNA-binding;
KW Intellectual disability; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Tumor suppressor; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..727
FT /note="Transcriptional repressor CTCF"
FT /id="PRO_0000047228"
FT ZN_FING 266..288
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 294..316
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 322..345
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 351..373
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 379..401
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 407..430
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 437..460
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 467..489
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 495..517
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 523..546
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 555..577
FT /note="C2H2-type 11; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 180..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..633
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..650
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 289
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 317
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 374
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 609
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT CROSSLNK 18
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 74
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 219
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 689
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..328
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_045350"
FT VARIANT 19..727
FT /note="Missing (found in an endometrial carcinoma sample;
FT unknown pathological significance)"
FT /evidence="ECO:0000269|PubMed:28319062"
FT /id="VAR_079374"
FT VARIANT 278
FT /note="R -> C (found in an endometrial carcinoma sample; no
FT effect on its nuclear localization; loss of its ability to
FT inhibit cell proliferation; unknown pathological
FT significance; dbSNP:rs1266478000)"
FT /evidence="ECO:0000269|PubMed:28319062"
FT /id="VAR_079375"
FT VARIANT 339
FT /note="R -> W (in a Wilms' tumor; dbSNP:rs1243010179)"
FT /evidence="ECO:0000269|PubMed:11782357"
FT /id="VAR_013141"
FT VARIANT 342
FT /note="R -> H (found in an endometrial carcinoma sample; no
FT effect on its nuclear localization; loss of its ability to
FT inhibit cell proliferation; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28319062"
FT /id="VAR_079376"
FT VARIANT 344
FT /note="K -> E (in a breast tumor; dbSNP:rs1215280530)"
FT /evidence="ECO:0000269|PubMed:11782357"
FT /id="VAR_013142"
FT VARIANT 345
FT /note="H -> R (in a prostate tumor)"
FT /evidence="ECO:0000269|PubMed:11782357"
FT /id="VAR_013143"
FT VARIANT 365
FT /note="K -> T (found in an endometrial carcinoma sample; no
FT effect on its nuclear localization; no loss of its ability
FT to inhibit cell proliferation; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:28319062"
FT /id="VAR_079377"
FT VARIANT 448
FT /note="R -> Q (in a Wilms' tumor)"
FT /evidence="ECO:0000269|PubMed:11782357"
FT /id="VAR_013144"
FT VARIANT 567
FT /note="R -> W (in MRD21; dbSNP:rs879255516)"
FT /evidence="ECO:0000269|PubMed:23746550"
FT /id="VAR_070776"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:6QNX"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:5T0U"
FT STRAND 302..305
FT /evidence="ECO:0007829|PDB:5T0U"
FT HELIX 306..316
FT /evidence="ECO:0007829|PDB:5T0U"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:5YEF"
FT STRAND 330..333
FT /evidence="ECO:0007829|PDB:5KKQ"
FT HELIX 334..344
FT /evidence="ECO:0007829|PDB:5KKQ"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:5KKQ"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:5KKQ"
FT HELIX 363..374
FT /evidence="ECO:0007829|PDB:5KKQ"
FT STRAND 382..385
FT /evidence="ECO:0007829|PDB:5KKQ"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:5KKQ"
FT HELIX 391..402
FT /evidence="ECO:0007829|PDB:5KKQ"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:2CT1"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:5KKQ"
FT STRAND 415..418
FT /evidence="ECO:0007829|PDB:5KKQ"
FT HELIX 419..429
FT /evidence="ECO:0007829|PDB:5KKQ"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:5K5L"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:5KKQ"
FT TURN 440..443
FT /evidence="ECO:0007829|PDB:5KKQ"
FT STRAND 444..448
FT /evidence="ECO:0007829|PDB:5KKQ"
FT HELIX 449..459
FT /evidence="ECO:0007829|PDB:5KKQ"
FT STRAND 460..468
FT /evidence="ECO:0007829|PDB:5YEF"
FT STRAND 470..473
FT /evidence="ECO:0007829|PDB:5YEG"
FT STRAND 475..478
FT /evidence="ECO:0007829|PDB:5YEG"
FT HELIX 479..486
FT /evidence="ECO:0007829|PDB:5YEG"
FT TURN 489..493
FT /evidence="ECO:0007829|PDB:5UND"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:5UND"
FT STRAND 503..506
FT /evidence="ECO:0007829|PDB:5YEL"
FT HELIX 507..514
FT /evidence="ECO:0007829|PDB:5UND"
FT STRAND 526..529
FT /evidence="ECO:0007829|PDB:5YEL"
FT STRAND 531..535
FT /evidence="ECO:0007829|PDB:5YEL"
FT HELIX 536..540
FT /evidence="ECO:0007829|PDB:5YEL"
FT HELIX 541..545
FT /evidence="ECO:0007829|PDB:5YEL"
FT STRAND 558..560
FT /evidence="ECO:0007829|PDB:5YEL"
FT STRAND 563..565
FT /evidence="ECO:0007829|PDB:1X6H"
FT HELIX 567..575
FT /evidence="ECO:0007829|PDB:5YEL"
SQ SEQUENCE 727 AA; 82785 MW; 2110538B65DC5706 CRC64;
MEGDAVEAIV EESETFIKGK ERKTYQRRRE GGQEEDACHL PQNQTDGGEV VQDVNSSVQM
VMMEQLDPTL LQMKTEVMEG TVAPEAEAAV DDTQIITLQV VNMEEQPINI GELQLVQVPV
PVTVPVATTS VEELQGAYEN EVSKEGLAES EPMICHTLPL PEGFQVVKVG ANGEVETLEQ
GELPPQEDPS WQKDPDYQPP AKKTKKTKKS KLRYTEEGKD VDVSVYDFEE EQQEGLLSEV
NAEKVVGNMK PPKPTKIKKK GVKKTFQCEL CSYTCPRRSN LDRHMKSHTD ERPHKCHLCG
RAFRTVTLLR NHLNTHTGTR PHKCPDCDMA FVTSGELVRH RRYKHTHEKP FKCSMCDYAS
VEVSKLKRHI RSHTGERPFQ CSLCSYASRD TYKLKRHMRT HSGEKPYECY ICHARFTQSG
TMKMHILQKH TENVAKFHCP HCDTVIARKS DLGVHLRKQH SYIEQGKKCR YCDAVFHERY
ALIQHQKSHK NEKRFKCDQC DYACRQERHM IMHKRTHTGE KPYACSHCDK TFRQKQLLDM
HFKRYHDPNF VPAAFVCSKC GKTFTRRNTM ARHADNCAGP DGVEGENGGE TKKSKRGRKR
KMRSKKEDSS DSENAEPDLD DNEDEEEPAV EIEPEPEPQP VTPAPPPAKK RRGRPPGRTN
QPKQNQPTAI IQVEDQNTGA IENIIVEVKK EPDAEPAEGE EEEAQPAATD APNGDLTPEM
ILSMMDR
