ID   CTCFL_HUMAN             Reviewed;         663 AA.
AC   Q8NI51; A0S6W1; A1L4C6; A6XGL8; A6XGM2; A6XGM3; A6XGM8; A6XGN0; A6XGN1;
AC   A6XGN2; A6XGN3; A6XGN4; E7EQ27; E7EUE3; E9PBA9; Q5JUG4; Q9BZ30; Q9NQJ3;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   27-MAR-2024, entry version 186.
DE   RecName: Full=Transcriptional repressor CTCFL;
DE   AltName: Full=Brother of the regulator of imprinted sites;
DE   AltName: Full=CCCTC-binding factor;
DE   AltName: Full=CTCF paralog;
DE   AltName: Full=CTCF-like protein;
DE   AltName: Full=Cancer/testis antigen 27;
DE            Short=CT27;
DE   AltName: Full=Zinc finger protein CTCF-T;
GN   Name=CTCFL; Synonyms=BORIS;
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; 2; 3; 4; 5; 6; 7; 8; 9; 10 AND 11),
RP   FUNCTION, AND VARIANT ALA-177.
RC   TISSUE=Testis;
RX   PubMed=12011441; DOI=10.1073/pnas.092123699;
RA   Loukinov D.I., Pugacheva E., Vatolin S., Pack S.D., Moon H., Chernukhin I.,
RA   Mannan P., Larsson E., Kanduri C., Vostrov A.A., Cui H., Niemitz E.L.,
RA   Rasko J.E.J., Docquier F.M., Kistler M., Breen J.J., Zhuang Z.,
RA   Quitschke W.W., Renkawitz R., Klenova E.M., Feinberg A.P., Ohlsson R.,
RA   Morse H.C. III, Lobanenkov V.V.;
RT   "BORIS, a novel male germ-line-specific protein associated with epigenetic
RT   reprogramming events, shares the same 11-zinc-finger domain with CTCF, the
RT   insulator protein involved in reading imprinting marks in the soma.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:6806-6811(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Testis;
RX   PubMed=17048991; DOI=10.1371/journal.pbio.0040355;
RA   Jelinic P., Stehle J.-C., Shaw P.;
RT   "The testis-specific factor CTCFL cooperates with the protein
RT   methyltransferase PRMT7 in H19 imprinting control region methylation.";
RL   PLoS Biol. 4:E355-E355(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ALA-177.
RC   TISSUE=Testis;
RX   PubMed=17962299; DOI=10.1093/nar/gkm896;
RA   Renaud S., Pugacheva E.M., Delgado M.D., Braunschweig R., Abdullaev Z.,
RA   Loukinov D., Benhattar J., Lobanenkov V.;
RT   "Expression of the CTCF-paralogous cancer-testis gene, brother of the
RT   regulator of imprinted sites (BORIS), is regulated by three alternative
RT   promoters modulated by CpG methylation and by CTCF and p53 transcription
RT   factors.";
RL   Nucleic Acids Res. 35:7372-7388(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-177.
RC   TISSUE=Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-177.
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   [8]
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   [9]
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   [10]
RP   FUNCTION, AND INTERACTION WITH BAG6/BAT3 AND SETD1A.
RX   PubMed=18765639; DOI=10.1128/mcb.00568-08;
RA   Nguyen P., Bar-Sela G., Sun L., Bisht K.S., Cui H., Kohn E., Feinberg A.P.,
RA   Gius D.;
RT   "BAT3 and SET1A form a complex with CTCFL/BORIS to modulate H3K4 histone
RT   dimethylation and gene expression.";
RL   Mol. Cell. Biol. 28:6720-6729(2008).
CC   -!- FUNCTION: Testis-specific DNA binding protein responsible for insulator
CC       function, nuclear architecture and transcriptional control, which
CC       probably acts by recruiting epigenetic chromatin modifiers. Plays a key
CC       role in gene imprinting in male germline, by participating in the
CC       establishment of differential methylation at the IGF2/H19 imprinted
CC       control region (ICR). Directly binds the unmethylated H19 ICR and
CC       recruits the PRMT7 methyltransferase, leading to methylate histone H4
CC       'Arg-3' to form H4R3sme2. This probably leads to recruit de novo DNA
CC       methyltransferases at these sites (By similarity). Seems to act as
CC       tumor suppressor. In association with DNMT1 and DNMT3B, involved in
CC       activation of BAG1 gene expression by binding to its promoter. Required
CC       for dimethylation of H3 lysine 4 (H3K4me2) of MYC and BRCA1 promoters.
CC       {ECO:0000250, ECO:0000269|PubMed:12011441, ECO:0000269|PubMed:18413740,
CC       ECO:0000269|PubMed:18765639}.
CC   -!- SUBUNIT: Interacts with histones, PRMT7 and SETD1A. Interacts (via N-
CC       terminus) with BAG6/BAT3. {ECO:0000269|PubMed:18765639}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=11;
CC       Name=1;
CC         IsoId=Q8NI51-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8NI51-2; Sequence=VSP_045158;
CC       Name=3;
CC         IsoId=Q8NI51-3; Sequence=VSP_045160;
CC       Name=4;
CC         IsoId=Q8NI51-4; Sequence=VSP_045157, VSP_045159;
CC       Name=5;
CC         IsoId=Q8NI51-5; Sequence=VSP_045156, VSP_045159;
CC       Name=6;
CC         IsoId=Q8NI51-6; Sequence=VSP_045155, VSP_045160;
CC       Name=7;
CC         IsoId=Q8NI51-7; Sequence=VSP_047059;
CC       Name=8;
CC         IsoId=Q8NI51-8; Sequence=VSP_047058;
CC       Name=9;
CC         IsoId=Q8NI51-9; Sequence=VSP_047725, VSP_047726;
CC       Name=10;
CC         IsoId=Q8NI51-10; Sequence=VSP_045156, VSP_045160;
CC       Name=11;
CC         IsoId=Q8NI51-11; Sequence=VSP_045155, VSP_054899;
CC   -!- TISSUE SPECIFICITY: Testis specific. Specifically expressed in primary
CC       spermatocytes.
CC   -!- DEVELOPMENTAL STAGE: Is up-regulated in primary spermatocytes
CC       (expression overlapping with the genome-wide erasure of methylation) to
CC       become silenced on activation of CTCF in post-meiotic germline cells
CC       (expression corresponding to DNA remethylation).
CC   -!- SIMILARITY: Belongs to the CTCF zinc-finger protein family.
CC       {ECO:0000305}.
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DR   EMBL; AF336042; AAM28645.1; -; mRNA.
DR   EMBL; AY071919; AAL61541.1; -; mRNA.
DR   EMBL; DQ294738; ABB92839.1; -; mRNA.
DR   EMBL; DQ778124; ABH10106.1; -; mRNA.
DR   EMBL; DQ778108; ABH10090.1; -; mRNA.
DR   EMBL; DQ778109; ABH10091.1; -; mRNA.
DR   EMBL; DQ778110; ABH10092.1; -; mRNA.
DR   EMBL; DQ778111; ABH10093.1; -; mRNA.
DR   EMBL; DQ778112; ABH10094.1; -; mRNA.
DR   EMBL; DQ778115; ABH10097.1; -; mRNA.
DR   EMBL; DQ778116; ABH10098.1; -; mRNA.
DR   EMBL; DQ778121; ABH10103.2; -; mRNA.
DR   EMBL; DQ778123; ABH10105.1; -; mRNA.
DR   EMBL; DQ778125; ABH10107.2; -; mRNA.
DR   EMBL; DQ778126; ABH10108.1; -; mRNA.
DR   EMBL; DQ778127; ABH10109.1; -; mRNA.
DR   EMBL; AK128070; BAG54626.1; -; mRNA.
DR   EMBL; AL035541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL160176; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471077; EAW75518.1; -; Genomic_DNA.
DR   EMBL; BC130486; AAI30487.1; -; mRNA.
DR   CCDS; CCDS13459.1; -. [Q8NI51-1]
DR   CCDS; CCDS58776.1; -. [Q8NI51-6]
DR   CCDS; CCDS58777.1; -. [Q8NI51-5]
DR   CCDS; CCDS58778.1; -. [Q8NI51-4]
DR   CCDS; CCDS58779.1; -. [Q8NI51-8]
DR   CCDS; CCDS58780.1; -. [Q8NI51-7]
DR   CCDS; CCDS58781.1; -. [Q8NI51-3]
DR   CCDS; CCDS58782.1; -. [Q8NI51-2]
DR   CCDS; CCDS68161.1; -. [Q8NI51-11]
DR   CCDS; CCDS68162.1; -. [Q8NI51-10]
DR   RefSeq; NP_001255969.1; NM_001269040.1. [Q8NI51-1]
DR   RefSeq; NP_001255970.1; NM_001269041.1. [Q8NI51-1]
DR   RefSeq; NP_001255971.1; NM_001269042.1.
DR   RefSeq; NP_001255972.1; NM_001269043.1. [Q8NI51-7]
DR   RefSeq; NP_001255973.1; NM_001269044.1. [Q8NI51-3]
DR   RefSeq; NP_001255974.1; NM_001269045.1.
DR   RefSeq; NP_001255975.1; NM_001269046.1. [Q8NI51-8]
DR   RefSeq; NP_001255976.1; NM_001269047.1. [Q8NI51-2]
DR   RefSeq; NP_001255977.1; NM_001269048.1. [Q8NI51-4]
DR   RefSeq; NP_001255978.1; NM_001269049.1. [Q8NI51-10]
DR   RefSeq; NP_001255979.1; NM_001269050.1. [Q8NI51-5]
DR   RefSeq; NP_001255980.1; NM_001269051.1.
DR   RefSeq; NP_001255981.1; NM_001269052.1.
DR   RefSeq; NP_001255983.1; NM_001269054.1. [Q8NI51-6]
DR   RefSeq; NP_001255984.1; NM_001269055.1. [Q8NI51-11]
DR   RefSeq; NP_542185.2; NM_080618.3. [Q8NI51-1]
DR   AlphaFoldDB; Q8NI51; -.
DR   SMR; Q8NI51; -.
DR   BioGRID; 126653; 38.
DR   IntAct; Q8NI51; 15.
DR   STRING; 9606.ENSP00000415579; -.
DR   iPTMnet; Q8NI51; -.
DR   PhosphoSitePlus; Q8NI51; -.
DR   BioMuta; CTCFL; -.
DR   DMDM; 313104098; -.
DR   EPD; Q8NI51; -.
DR   jPOST; Q8NI51; -.
DR   MassIVE; Q8NI51; -.
DR   MaxQB; Q8NI51; -.
DR   PaxDb; 9606-ENSP00000415579; -.
DR   PeptideAtlas; Q8NI51; -.
DR   ProteomicsDB; 1764; -.
DR   ProteomicsDB; 1765; -.
DR   ProteomicsDB; 1766; -.
DR   ProteomicsDB; 1767; -.
DR   ProteomicsDB; 1768; -.
DR   ProteomicsDB; 1769; -.
DR   ProteomicsDB; 1770; -.
DR   ProteomicsDB; 18412; -.
DR   ProteomicsDB; 73832; -. [Q8NI51-1]
DR   Pumba; Q8NI51; -.
DR   Antibodypedia; 744; 285 antibodies from 33 providers.
DR   DNASU; 140690; -.
DR   Ensembl; ENST00000243914.8; ENSP00000243914.3; ENSG00000124092.13. [Q8NI51-1]
DR   Ensembl; ENST00000371196.6; ENSP00000360239.2; ENSG00000124092.13. [Q8NI51-1]
DR   Ensembl; ENST00000422109.6; ENSP00000413713.2; ENSG00000124092.13. [Q8NI51-9]
DR   Ensembl; ENST00000422869.6; ENSP00000399061.2; ENSG00000124092.13. [Q8NI51-2]
DR   Ensembl; ENST00000423479.7; ENSP00000415579.2; ENSG00000124092.13. [Q8NI51-7]
DR   Ensembl; ENST00000429804.7; ENSP00000415329.2; ENSG00000124092.13. [Q8NI51-8]
DR   Ensembl; ENST00000432255.6; ENSP00000409344.2; ENSG00000124092.13. [Q8NI51-4]
DR   Ensembl; ENST00000433949.7; ENSP00000392034.3; ENSG00000124092.13. [Q8NI51-10]
DR   Ensembl; ENST00000502686.6; ENSP00000437999.1; ENSG00000124092.13. [Q8NI51-6]
DR   Ensembl; ENST00000539382.5; ENSP00000439998.1; ENSG00000124092.13. [Q8NI51-5]
DR   Ensembl; ENST00000608263.5; ENSP00000476783.1; ENSG00000124092.13. [Q8NI51-1]
DR   Ensembl; ENST00000608440.5; ENSP00000477488.1; ENSG00000124092.13. [Q8NI51-3]
DR   Ensembl; ENST00000608903.5; ENSP00000476718.1; ENSG00000124092.13. [Q8NI51-11]
DR   Ensembl; ENST00000609232.5; ENSP00000476398.1; ENSG00000124092.13. [Q8NI51-1]
DR   GeneID; 140690; -.
DR   KEGG; hsa:140690; -.
DR   MANE-Select; ENST00000243914.8; ENSP00000243914.3; NM_001386993.1; NP_001373922.1.
DR   UCSC; uc010giw.2; human. [Q8NI51-1]
DR   AGR; HGNC:16234; -.
DR   CTD; 140690; -.
DR   DisGeNET; 140690; -.
DR   GeneCards; CTCFL; -.
DR   HGNC; HGNC:16234; CTCFL.
DR   HPA; ENSG00000124092; Tissue enriched (testis).
DR   MIM; 607022; gene.
DR   neXtProt; NX_Q8NI51; -.
DR   OpenTargets; ENSG00000124092; -.
DR   PharmGKB; PA26999; -.
DR   VEuPathDB; HostDB:ENSG00000124092; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000161524; -.
DR   HOGENOM; CLU_643978_0_0_1; -.
DR   InParanoid; Q8NI51; -.
DR   OrthoDB; 5398475at2759; -.
DR   PhylomeDB; Q8NI51; -.
DR   TreeFam; TF106430; -.
DR   PathwayCommons; Q8NI51; -.
DR   SignaLink; Q8NI51; -.
DR   SIGNOR; Q8NI51; -.
DR   BioGRID-ORCS; 140690; 11 hits in 1180 CRISPR screens.
DR   ChiTaRS; CTCFL; human.
DR   GeneWiki; CTCFL; -.
DR   GenomeRNAi; 140690; -.
DR   Pharos; Q8NI51; Tbio.
DR   PRO; PR:Q8NI51; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; Q8NI51; Protein.
DR   Bgee; ENSG00000124092; Expressed in secondary oocyte and 57 other cell types or tissues.
DR   ExpressionAtlas; Q8NI51; baseline and differential.
DR   GO; GO:0005694; C:chromosome; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0016604; C:nuclear body; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0043035; F:chromatin insulator sequence binding; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR   GO; GO:0042393; F:histone binding; ISS: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; 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:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0071169; P:establishment of protein localization to chromatin; IMP:UniProtKB.
DR   GO; GO:0071514; P:genomic imprinting; ISS:UniProtKB.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; IMP:UniProtKB.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 9.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR24388:SF53; COMBGAP, ISOFORM L-RELATED; 1.
DR   PANTHER; PTHR24388; ZINC FINGER PROTEIN; 1.
DR   Pfam; PF00096; zf-C2H2; 4.
DR   SMART; SM00355; ZnF_C2H2; 11.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 7.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 7.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 11.
DR   Genevisible; Q8NI51; HS.
PE   1: Evidence at protein level;
KW   Activator; Alternative splicing; Cell cycle; Chromatin regulator;
KW   Cytoplasm; DNA-binding; Metal-binding; Nucleus; Reference proteome; Repeat;
KW   Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger.
FT   CHAIN           1..663
FT                   /note="Transcriptional repressor CTCFL"
FT                   /id="PRO_0000047226"
FT   ZN_FING         257..279
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         285..307
FT                   /note="C2H2-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         313..336
FT                   /note="C2H2-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         342..364
FT                   /note="C2H2-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         370..392
FT                   /note="C2H2-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         398..421
FT                   /note="C2H2-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         428..451
FT                   /note="C2H2-type 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         458..480
FT                   /note="C2H2-type 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         486..508
FT                   /note="C2H2-type 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         514..537
FT                   /note="C2H2-type 10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         546..568
FT                   /note="C2H2-type 11; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          24..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          221..250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          569..630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..48
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..614
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..262
FT                   /note="Missing (in isoform 6 and isoform 11)"
FT                   /evidence="ECO:0000303|PubMed:12011441"
FT                   /id="VSP_045155"
FT   VAR_SEQ         1..205
FT                   /note="Missing (in isoform 5 and isoform 10)"
FT                   /evidence="ECO:0000303|PubMed:12011441"
FT                   /id="VSP_045156"
FT   VAR_SEQ         354..497
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:12011441"
FT                   /id="VSP_045157"
FT   VAR_SEQ         394..427
FT                   /note="GEKPYECHICHTRFTQSGTMKIHILQKHGENVPK -> EATSKRSLQEIPRC
FT                   KFHPDCLQMLQVWQRLFPLD (in isoform 9)"
FT                   /evidence="ECO:0000303|PubMed:12011441"
FT                   /id="VSP_047725"
FT   VAR_SEQ         395..444
FT                   /note="Missing (in isoform 8)"
FT                   /evidence="ECO:0000303|PubMed:12011441"
FT                   /id="VSP_047058"
FT   VAR_SEQ         428..663
FT                   /note="Missing (in isoform 9)"
FT                   /evidence="ECO:0000303|PubMed:12011441"
FT                   /id="VSP_047726"
FT   VAR_SEQ         559..663
FT                   /note="INLHRHSEKCGSGEAKSAASGKGRRTRKRKQTILKEATKGQKEAAKGWKEAA
FT                   NGDEAAAEEASTTKGEQFPGEMFPVACRETTARVKEEVDEGVTCEMLLNTMDK -> VL
FT                   Y (in isoform 11)"
FT                   /evidence="ECO:0000303|PubMed:12011441"
FT                   /id="VSP_054899"
FT   VAR_SEQ         560..663
FT                   /note="NLHRHSEKCGSGEAKSAASGKGRRTRKRKQTILKEATKGQKEAAKGWKEAAN
FT                   GDEAAAEEASTTKGEQFPGEMFPVACRETTARVKEEVDEGVTCEMLLNTMDK -> TSK
FT                   WSGLKPQTFIT (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:12011441"
FT                   /id="VSP_045158"
FT   VAR_SEQ         560..663
FT                   /note="NLHRHSEKCGSGEAKSAASGKGRRTRKRKQTILKEATKGQKEAAKGWKEAAN
FT                   GDEAAAEEASTTKGEQFPGEMFPVACRETTARVKEEVDEGVTCEMLLNTMDK -> LWV
FT                   GNSEVAELGGPGSGPLLRLQSGCPPGLHHPKAGLGPEDPLPGQLRHTTAGTGLSSLLQG
FT                   PLCRAA (in isoform 4 and isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:12011441"
FT                   /id="VSP_045159"
FT   VAR_SEQ         614..663
FT                   /note="EAAAEEASTTKGEQFPGEMFPVACRETTARVKEEVDEGVTCEMLLNTMDK
FT                   -> GVISAHRNLCLLGSSDSHASVSGAGITDARHHAWLIVLLFLVEMGFYHVSHS (in
FT                   isoform 3, isoform 6 and isoform 10)"
FT                   /evidence="ECO:0000303|PubMed:12011441"
FT                   /id="VSP_045160"
FT   VAR_SEQ         663
FT                   /note="K -> NSAGCTGRMMLVSAWLLGRPQETYNQGRRRRGSRRVTW (in
FT                   isoform 7)"
FT                   /evidence="ECO:0000303|PubMed:12011441"
FT                   /id="VSP_047059"
FT   VARIANT         50
FT                   /note="E -> Q (in dbSNP:rs6070128)"
FT                   /id="VAR_023213"
FT   VARIANT         177
FT                   /note="T -> A (in dbSNP:rs6025606)"
FT                   /evidence="ECO:0000269|PubMed:12011441,
FT                   ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:17962299"
FT                   /id="VAR_023214"
FT   VARIANT         448
FT                   /note="R -> H (in dbSNP:rs6092491)"
FT                   /id="VAR_057374"
FT   VARIANT         525
FT                   /note="Q -> E (in dbSNP:rs6070122)"
FT                   /id="VAR_032766"
FT   CONFLICT        613
FT                   /note="Missing (in Ref. 2; AAL61541)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   663 AA;  75747 MW;  9351E1A85173D085 CRC64;
     MAATEISVLS EQFTKIKELE LMPEKGLKEE EKDGVCREKD HRSPSELEAE RTSGAFQDSV
     LEEEVELVLA PSEESEKYIL TLQTVHFTSE AVELQDMSLL SIQQQEGVQV VVQQPGPGLL
     WLEEGPRQSL QQCVAISIQQ ELYSPQEMEV LQFHALEENV MVASEDSKLA VSLAETTGLI
     KLEEEQEKNQ LLAERTKEQL FFVETMSGDE RSDEIVLTVS NSNVEEQEDQ PTAGQADAEK
     AKSTKNQRKT KGAKGTFHCD VCMFTSSRMS SFNRHMKTHT SEKPHLCHLC LKTFRTVTLL
     RNHVNTHTGT RPYKCNDCNM AFVTSGELVR HRRYKHTHEK PFKCSMCKYA SVEASKLKRH
     VRSHTGERPF QCCQCSYASR DTYKLKRHMR THSGEKPYEC HICHTRFTQS GTMKIHILQK
     HGENVPKYQC PHCATIIARK SDLRVHMRNL HAYSAAELKC RYCSAVFHER YALIQHQKTH
     KNEKRFKCKH CSYACKQERH MTAHIRTHTG EKPFTCLSCN KCFRQKQLLN AHFRKYHDAN
     FIPTVYKCSK CGKGFSRWIN LHRHSEKCGS GEAKSAASGK GRRTRKRKQT ILKEATKGQK
     EAAKGWKEAA NGDEAAAEEA STTKGEQFPG EMFPVACRET TARVKEEVDE GVTCEMLLNT
     MDK
//