ID TERF1_HUMAN Reviewed; 439 AA. AC P54274; A7XP29; Q15553; Q8NHT6; Q93029; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 3. DT 05-OCT-2010, entry version 124. DE RecName: Full=Telomeric repeat-binding factor 1; DE AltName: Full=NIMA-interacting protein 2; DE AltName: Full=TTAGGG repeat-binding factor 1; DE AltName: Full=Telomeric protein Pin2/TRF1; GN Name=TERF1; Synonyms=PIN2, TRBF1, TRF, TRF1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Cervix carcinoma; RX MEDLINE=96099400; PubMed=7502076; DOI=10.1126/science.270.5242.1663; RA Chong L., van Steensel B., Broccoli D., Erdjument-Bromage H., RA Hanish J., Tempst P., de Lange T.; RT "A human telomeric protein."; RL Science 270:1663-1667(1995). RN [2] RP SEQUENCE REVISION TO 14. RA de Lange T.; RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE RP [GENOMIC DNA] OF 1-138 (ISOFORM1/2). RX MEDLINE=97467741; PubMed=9326950; DOI=10.1038/ng1097-231; RA Broccoli D., Smogorzewska A., Chong L., de Lange T.; RT "Human telomeres contain two distinct Myb-related proteins, TRF1 and RT TRF2."; RL Nat. Genet. 17:231-235(1997). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Cervix carcinoma; RX MEDLINE=98054283; PubMed=9391075; DOI=10.1073/pnas.94.25.13618; RA Shen M., Haggblom C., Vogt M., Hunter T., Lu K.P.; RT "Characterization and cell cycle regulation of the related human RT telomeric proteins Pin2 and TRF1 suggest a role in mitosis."; RL Proc. Natl. Acad. Sci. U.S.A. 94:13618-13623(1997). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG NIEHS SNPs program; RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T., RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., RA Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., RA Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Liver; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 329-439 (ISOFORMS 1/2). RC TISSUE=Cervix carcinoma; RX MEDLINE=96188864; PubMed=8614633; DOI=10.1093/nar/24.7.1294; RA Bilaud T., Koering C.E., Binet-Brasselet E., Ancelin K., Pollice A., RA Gasser S.M., Gilson E.; RT "The telobox, a Myb-related telomeric DNA binding motif found in RT proteins from yeast, plants and human."; RL Nucleic Acids Res. 24:1294-1303(1996). RN [9] RP MUTAGENESIS OF SER-219, PHOSPHORYLATION AT SER-219, AND INTERACTION RP WITH ATM. RX MEDLINE=21369915; PubMed=11375976; DOI=10.1074/jbc.M011534200; RA Kishi S., Zhou X.Z., Ziv Y., Khoo C., Hill D.E., Shiloh Y., Lu K.P.; RT "Telomeric protein Pin2/TRF1 as an important ATM target in response to RT double strand DNA breaks."; RL J. Biol. Chem. 276:29282-29291(2001). RN [10] RP INTERACTION WITH MAPRE1 AND WITH THE MITOTIC SPINDLE. RX MEDLINE=21940533; PubMed=11943150; DOI=10.1016/S0014-5793(02)02363-3; RA Nakamura M., Zhen Zhou X., Kishi S., Ping Lu K.; RT "Involvement of the telomeric protein Pin2/TRF1 in the regulation of RT the mitotic spindle."; RL FEBS Lett. 514:193-198(2002). RN [11] RP ADP-RIBOSYLATION. RX MEDLINE=21602874; PubMed=11739745; DOI=10.1128/MCB.22.1.332-342.2002; RA Cook B.D., Dynek J.N., Chang W., Shostak G., Smith S.; RT "Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2 RT at human telomeres."; RL Mol. Cell. Biol. 22:332-342(2002). RN [12] RP IDENTIFICATION IN A COMPLEX WITH POT1; TINF2 AND TNKS1. RX PubMed=12768206; DOI=10.1038/nature01688; RA Loayza D., De Lange T.; RT "POT1 as a terminal transducer of TRF1 telomere length control."; RL Nature 423:1013-1018(2003). RN [13] RP IDENTIFICATION IN THE SHELTERIN COMPLEX. RX PubMed=15316005; DOI=10.1074/jbc.M409047200; RA Ye J.Z.-S., Donigian J.R., van Overbeek M., Loayza D., Luo Y., RA Krutchinsky A.N., Chait B.T., de Lange T.; RT "TIN2 binds TRF1 and TRF2 simultaneously and stabilizes the TRF2 RT complex on telomeres."; RL J. Biol. Chem. 279:47264-47271(2004). RN [14] RP IDENTIFICATION IN THE SHELTERIN COMPLEX. RX PubMed=15383534; DOI=10.1074/jbc.M409293200; RA Liu D., O'Connor M.S., Qin J., Songyang Z.; RT "Telosome, a mammalian telomere-associated complex formed by multiple RT telomeric proteins."; RL J. Biol. Chem. 279:51338-51342(2004). RN [15] RP FUNCTION OF THE SHELTERIN COMPLEX. RX PubMed=16166375; DOI=10.1101/gad.1346005; RA de Lange T.; RT "Shelterin: the protein complex that shapes and safeguards human RT telomeres."; RL Genes Dev. 19:2100-2110(2005). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-434; SER-435 AND RP SER-437, AND MASS SPECTROMETRY. 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 [18] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-11, AND MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [19] RP INTERACTION WITH RLIM, SUBCELLULAR LOCATION, AND UBIQUITINATION. RX PubMed=19164295; DOI=10.1074/jbc.M806702200; RA Her Y.R., Chung I.K.; RT "Ubiquitin ligase RLIM modulates telomere length homeostasis through a RT proteolysis of TRF1."; RL J. Biol. Chem. 284:8557-8566(2009). RN [20] RP STRUCTURE BY NMR OF 378-430. RX MEDLINE=98416700; PubMed=9739097; DOI=10.1016/S0969-2126(98)00106-3; RA Nishikawa T., Nagadoi A., Yoshimura S., Aimoto S., Nishimura Y.; RT "Solution structure of the DNA-binding domain of human telomeric RT protein, hTRF1."; RL Structure 6:1057-1065(1998). RN [21] RP STRUCTURE BY NMR OF 371-439. RX MEDLINE=21605735; PubMed=11738049; DOI=10.1016/S0969-2126(01)00688-8; RA Nishikawa T., Okamura H., Nagadoi A., Koenig P., Rhodes D., RA Nishimura Y.; RT "Solution structure of a telomeric DNA complex of human TRF1."; RL Structure 9:1237-1251(2001). RN [22] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 48-268, AND MUTAGENESIS OF RP ALA-74; ALA-75; TRP-77 AND PHE-81. RX MEDLINE=21431982; PubMed=11545737; DOI=10.1016/S1097-2765(01)00321-5; RA Fairall L., Chapman L., Moss H., de Lange T., Rhodes D.; RT "Structure of the TRFH dimerization domain of the human telomeric RT proteins TRF1 and TRF2."; RL Mol. Cell 8:351-361(2001). RN [23] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 379-431 IN COMPLEX WITH RP TELOMERIC DNA, AND SUBUNIT. RX PubMed=15608617; DOI=10.1038/sj.embor.7400314; RA Court R., Chapman L., Fairall L., Rhodes D.; RT "How the human telomeric proteins TRF1 and TRF2 recognize telomeric RT DNA: a view from high-resolution crystal structures."; RL EMBO Rep. 6:39-45(2005). RN [24] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 58-268 IN COMPLEX WITH TINF2, RP INTERACTION WITH TINF2 AND PINX1, DOMAIN TRFH DIMERIZATION, AND RP SUBUNIT. RX PubMed=18202258; DOI=10.1126/science.1151804; RA Chen Y., Yang Y., van Overbeek M., Donigian J.R., Baciu P., RA de Lange T., Lei M.; RT "A shared docking motif in TRF1 and TRF2 used for differential RT recruitment of telomeric proteins."; RL Science 319:1092-1096(2008). RN [25] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 58-268 IN COMPLEX WITH FBXO4, RP MUTAGENESIS OF LEU-115 AND LEU-120, INTERACTION WITH TINF2, SUBUNIT, RP AND UBIQUITINATION. RX PubMed=20159592; DOI=10.1016/j.devcel.2010.01.007; RA Zeng Z., Wang W., Yang Y., Chen Y., Yang X., Diehl J.A., Liu X., RA Lei M.; RT "Structural basis of selective ubiquitination of TRF1 by SCFFbx4."; RL Dev. Cell 18:214-225(2010). CC -!- FUNCTION: Binds the telomeric double-stranded TTAGGG repeat and CC negatively regulates telomere length. Involved in the regulation CC of the mitotic spindle. Component of the shelterin complex CC (telosome) that is involved in the regulation of telomere length CC and protection. Shelterin associates with arrays of double- CC stranded TTAGGG repeats added by telomerase and protects CC chromosome ends; without its protective activity, telomeres are no CC longer hidden from the DNA damage surveillance and chromosome ends CC are inappropriately processed by DNA repair pathways. CC -!- SUBUNIT: Homodimer; can contain both isoforms. Found in a complex CC with POT1; TINF2 and TNKS1. Interacts with ATM, TINF2, TNKS1, CC TNKS2, PINX1, NEK2 and MAPRE1. Component of the shelterin complex CC (telosome) composed of TERF1, TERF2, TINF2, TERF2IP ACD and POT1. CC Interacts with RLIM (via N-terminus). Interacts with FBXO4. CC Interaction with TINF2 protects against interaction with FBXO4 and CC subsequent polyubiquitination and proteasomal degradation. CC -!- INTERACTION: CC Self; NbExp=3; IntAct=EBI-710997, EBI-710997; CC P00519:ABL1; NbExp=1; IntAct=EBI-710997, EBI-375543; CC Q13315:ATM; NbExp=6; IntAct=EBI-710997, EBI-495465; CC P54132:BLM; NbExp=2; IntAct=EBI-710997, EBI-621372; CC Q9UKT5:FBXO4; NbExp=5; IntAct=EBI-710997, EBI-960409; CC Q15691:MAPRE1; NbExp=3; IntAct=EBI-710997, EBI-1004115; CC Q9BSI4:TINF2; NbExp=1; IntAct=EBI-710997, EBI-717399; CC Q9H2D6:TRIOBP; NbExp=1; IntAct=EBI-710997, EBI-715619; CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, spindle. CC Chromosome, telomere. Note=Colocalizes with telomeric DNA in CC interphase and metaphase cells and is located at chromosome ends CC during metaphase. Associates with the mitotic spindle. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=TRF1; CC IsoId=P54274-1; Sequence=Displayed; CC Name=2; Synonyms=Pin2; CC IsoId=P54274-2; Sequence=VSP_003303; CC -!- TISSUE SPECIFICITY: Highly expressed and ubiquitous. Isoform Pin2 CC predominates. CC -!- INDUCTION: Pin2 expression is tightly regulated during the cell CC cycle; levels are low in G1 and S phase and increase during G2 CC phase and mitosis. CC -!- DOMAIN: The acidic N-terminal domain binds to the ankyrin repeats CC of TNKS1 and TNKS2. The C-terminal domain binds microtubules. CC -!- DOMAIN: The TRFH dimerization region mediates the interaction with CC TINF2. CC -!- PTM: Phosphorylated preferentially on Ser-219 in an ATM-dependent CC manner in response to ionizing DNA damage. CC -!- PTM: ADP-ribosylation by TNKS1 or TNKS2 diminishes its ability to CC bind to telomeric DNA. CC -!- PTM: Ubiquitinated by RLIM/RNF12, leading to its degradation by CC the proteasome. Ubiquitinated by a SCF (SKP1-CUL1-F-box protein) CC ubiquitin-protein ligase complex, leading to its degradation by CC the proteasome. CC -!- SIMILARITY: Contains 1 HTH myb-type DNA-binding domain. CC -!- WEB RESOURCE: Name=NIEHS SNPs; CC URL="http://egp.gs.washington.edu/data/terf1/"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U40705; AAB54036.1; -; mRNA. DR EMBL; AF003001; AAB81137.1; -; mRNA. DR EMBL; U70993; AAB17975.1; -; Genomic_DNA. DR EMBL; U70992; AAB17975.1; JOINED; Genomic_DNA. DR EMBL; U74382; AAB53363.1; -; mRNA. DR EMBL; EU088287; ABV02580.1; -; Genomic_DNA. DR EMBL; AC022893; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC029378; AAH29378.1; -; mRNA. DR EMBL; X93511; CAA63768.1; -; mRNA. DR IPI; IPI00005539; -. DR IPI; IPI00220583; -. DR PIR; A57573; A57573. DR RefSeq; NP_003209.2; -. DR RefSeq; NP_059523.2; -. DR UniGene; Hs.442707; -. DR PDB; 1BA5; NMR; -; A=378-430. DR PDB; 1H6O; X-ray; 2.90 A; A=62-265. DR PDB; 1ITY; NMR; -; A=371-439. DR PDB; 1IV6; NMR; -; A=371-439. DR PDB; 1W0T; X-ray; 2.00 A; A/B=379-431. DR PDB; 3BQO; X-ray; 2.00 A; A=58-268. DR PDB; 3L82; X-ray; 2.40 A; A=58-268. DR PDBsum; 1BA5; -. DR PDBsum; 1H6O; -. DR PDBsum; 1ITY; -. DR PDBsum; 1IV6; -. DR PDBsum; 1W0T; -. DR PDBsum; 3BQO; -. DR PDBsum; 3L82; -. DR ProteinModelPortal; P54274; -. DR DIP; DIP-29412N; -. DR IntAct; P54274; 63. DR MINT; MINT-221323; -. DR STRING; P54274; -. DR PhosphoSite; P54274; -. DR PRIDE; P54274; -. DR Ensembl; ENST00000276603; ENSP00000276603; ENSG00000147601. DR GeneID; 7013; -. DR KEGG; hsa:7013; -. DR CTD; 7013; -. DR GeneCards; GC08P073921; -. DR H-InvDB; HIX0007582; -. DR HGNC; HGNC:11728; TERF1. DR MIM; 600951; gene. DR PharmGKB; PA36445; -. DR eggNOG; prNOG13496; -. DR HOGENOM; HBG125883; -. DR HOVERGEN; HBG054097; -. DR InParanoid; P54274; -. DR OMA; SKILSHY; -. DR OrthoDB; EOG9G4K9K; -. DR PhylomeDB; P54274; -. DR Pathway_Interaction_DB; telomerasepathway; Regulation of Telomerase. DR Reactome; REACT_22172; Chromosome Maintenance. DR ArrayExpress; P54274; -. DR Bgee; P54274; -. DR CleanEx; HS_TERF1; -. DR Genevestigator; P54274; -. DR GermOnline; ENSG00000147601; Homo sapiens. DR GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0000783; C:nuclear telomere cap complex; IDA:BHF-UCL. DR GO; GO:0005654; C:nucleoplasm; EXP:Reactome. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell. DR GO; GO:0008656; F:caspase activator activity; IDA:UniProtKB. DR GO; GO:0008301; F:DNA bending activity; IDA:BHF-UCL. DR GO; GO:0003691; F:double-stranded telomeric DNA binding; IDA:UniProtKB. DR GO; GO:0008017; F:microtubule binding; IDA:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB. DR GO; GO:0010521; F:telomerase inhibitor activity; IGI:BHF-UCL. DR GO; GO:0042162; F:telomeric DNA binding; IDA:UniProtKB. DR GO; GO:0006919; P:activation of caspase activity; IDA:UniProtKB. DR GO; GO:0001309; P:age-dependent telomere shortening; IDA:UniProtKB. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IEP:UniProtKB. DR GO; GO:0006917; P:induction of apoptosis; IDA:UniProtKB. DR GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW. DR GO; GO:0007094; P:mitotic cell cycle spindle assembly checkpoint; IMP:UniProtKB. DR GO; GO:0051974; P:negative regulation of telomerase activity; IGI:BHF-UCL. DR GO; GO:0032211; P:negative regulation of telomere maintenance...; IGI:BHF-UCL. DR GO; GO:0032214; P:negative regulation of telomere maintenance...; NAS:BHF-UCL. DR GO; GO:0031116; P:positive regulation of microtubule polymeri...; IDA:UniProtKB. DR GO; GO:0045840; P:positive regulation of mitosis; IMP:UniProtKB. DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:UniProtKB. DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB. DR GO; GO:0045449; P:regulation of transcription; IEA:InterPro. DR GO; GO:0007004; P:telomere maintenance via telomerase; IMP:UniProtKB. DR GO; GO:0007004; P:telomere maintenance via telomerase; NAS:UniProtKB. DR GO; GO:0010834; P:telomere maintenance via telomere shortening; IMP:BHF-UCL. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR012287; Homeodomain-rel. DR InterPro; IPR017930; HTH_Myb-type_DNA-bd. DR InterPro; IPR014778; Myb_DNA-bd. DR InterPro; IPR001005; SANT_DNA-bd. DR InterPro; IPR017357; Telomere_repeat-bd-1_Pin2. DR InterPro; IPR013867; Telomere_rpt-bd_fac_dimer_dom. DR Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 1. DR Gene3D; G3DSA:1.25.40.210; Telomere_repeat-bd_fac_dimer; 1. DR Pfam; PF00249; Myb_DNA-binding; 1. DR Pfam; PF08558; TRF; 1. DR PIRSF; PIRSF038016; Telomere_bd-1_Pin2; 1. DR ProDom; PD014243; Telomere_repeat-bd_fac_dimer; 1. DR SMART; SM00717; SANT; 1. DR SUPFAM; SSF46689; Homeodomain_like; 1. DR SUPFAM; SSF63600; Telo_rept_bnd_D; 1. DR PROSITE; PS51294; HTH_MYB; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ADP-ribosylation; Alternative splicing; KW Cell cycle; Cell division; Chromosome; Complete proteome; Cytoplasm; KW Cytoskeleton; Direct protein sequencing; DNA-binding; Mitosis; KW Nucleus; Phosphoprotein; Telomere; Ubl conjugation. FT INIT_MET 1 1 Removed. FT CHAIN 2 439 Telomeric repeat-binding factor 1. FT /FTId=PRO_0000197129. FT DOMAIN 375 432 HTH myb-type. FT DNA_BIND 403 428 H-T-H motif. FT REGION 58 268 TRFH dimerization. FT REGION 265 378 Interaction with RLIM. FT MOTIF 337 356 Nuclear localization signal (Potential). FT COMPBIAS 2 71 Asp/Glu-rich (acidic). FT COMPBIAS 55 62 Poly-Glu. FT MOD_RES 2 2 N-acetylalanine. FT MOD_RES 11 11 Phosphoserine. FT MOD_RES 219 219 Phosphoserine; by ATM. FT MOD_RES 434 434 Phosphoserine. FT MOD_RES 435 435 Phosphoserine. FT MOD_RES 437 437 Phosphoserine. FT VAR_SEQ 296 315 Missing (in isoform 2). FT /FTId=VSP_003303. FT MUTAGEN 74 74 A->D: Abolishes dimerization and telomere FT binding; when associated with P-75. FT MUTAGEN 75 75 A->P: Abolishes dimerization and telomere FT binding; when associated with D-74. FT MUTAGEN 77 77 W->P: Abolishes telomere binding. FT MUTAGEN 81 81 F->P: Abolishes telomere binding. FT MUTAGEN 90 90 F->P: Diminishes telomere binding. FT MUTAGEN 115 115 L->R: Loss of interaction with FBXO4. FT MUTAGEN 120 120 L->R: Loss of interaction with FBXO4. FT MUTAGEN 219 219 S->A: Loss of phosphorylation; induction FT of mitotic entry and apoptosis and FT increased radiation hypersensitivity of FT ataxia-telangiectasia cells. FT MUTAGEN 219 219 S->D,E: Fails to induce apoptosis and FT decreases radiation hypersensitivity of FT ataxia-telangiectasia cells (phospho- FT mimicking mutants). FT CONFLICT 14 14 G -> R (in Ref. 1; AAB54036, 3; AAB17975/ FT AAB81137 and 4; AAB53363). FT CONFLICT 338 338 K -> E (in Ref. 8; CAA63768). FT HELIX 63 92 FT HELIX 95 110 FT HELIX 117 133 FT TURN 134 136 FT STRAND 143 145 FT HELIX 150 158 FT HELIX 167 186 FT HELIX 190 200 FT HELIX 211 219 FT HELIX 226 230 FT HELIX 233 251 FT HELIX 255 265 FT HELIX 385 398 FT HELIX 403 409 FT HELIX 417 428 SQ SEQUENCE 439 AA; 50246 MW; AB548E7D3124A211 CRC64; MAEDVSSAAP SPRGCADGRD ADPTEEQMAE TERNDEEQFE CQELLECQVQ VGAPEEEEEE EEDAGLVAEA EAVAAGWMLD FLCLSLCRAF RDGRSEDFRR TRNSAEAIIH GLSSLTACQL RTIYICQFLT RIAAGKTLDA QFENDERITP LESALMIWGS IEKEHDKLHE EIQNLIKIQA IAVCMENGNF KEAEEVFERI FGDPNSHMPF KSKLLMIISQ KDTFHSFFQH FSYNHMMEKI KSYVNYVLSE KSSTFLMKAA AKVVESKRTR TITSQDKPSG NDVEMETEAN LDTRKSVSDK QSAVTESSEG TVSLLRSHKN LFLSKLQHGT QQQDLNKKER RVGTPQSTKK KKESRRATES RIPVSKSQPV TPEKHRARKR QAWLWEEDKN LRSGVRKYGE GNWSKILLHY KFNNRTSVML KDRWRTMKKL KLISSDSED //