TERF2_MOUSE
ID TERF2_MOUSE Reviewed; 541 AA.
AC O35144; D3YVG5; Q80VE2; Q8BQJ9;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Telomeric repeat-binding factor 2;
DE AltName: Full=TTAGGG repeat-binding factor 2;
DE AltName: Full=Telomeric DNA-binding protein;
GN Name=Terf2; Synonyms=Trf2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Embryo;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=FVB/N-3; TISSUE=Mammary tumor;
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 30-540 (ISOFORM 1).
RC TISSUE=Brain;
RX 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364 AND SER-367, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, INTERACTION WITH DCLRE1B, AND MUTAGENESIS OF PHE-165.
RX PubMed=20619712; DOI=10.1016/j.molcel.2010.06.031;
RA Wu P., van Overbeek M., Rooney S., de Lange T.;
RT "Apollo contributes to G overhang maintenance and protects leading-end
RT telomeres.";
RL Mol. Cell 39:606-617(2010).
RN [9]
RP FUNCTION, AND INTERACTION WITH TERF2IP.
RX PubMed=20622870; DOI=10.1038/ncb2080;
RA Teo H., Ghosh S., Luesch H., Ghosh A., Wong E.T., Malik N., Orth A.,
RA de Jesus P., Perry A.S., Oliver J.D., Tran N.L., Speiser L.J., Wong M.,
RA Saez E., Schultz P., Chanda S.K., Verma I.M., Tergaonkar V.;
RT "Telomere-independent Rap1 is an IKK adaptor and regulates NF-kappaB-
RT dependent gene expression.";
RL Nat. Cell Biol. 12:758-767(2010).
RN [10]
RP FUNCTION, INTERACTION WITH TERF2IP, MUTAGENESIS OF 335-ALA-PHE-336, AND
RP SUBCELLULAR LOCATION.
RX PubMed=20339076; DOI=10.1126/science.1185100;
RA Sfeir A., Kabir S., van Overbeek M., Celli G.B., de Lange T.;
RT "Loss of Rap1 induces telomere recombination in the absence of NHEJ or a
RT DNA damage signal.";
RL Science 327:1657-1661(2010).
CC -!- FUNCTION: Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and
CC plays a central role in telomere maintenance and protection against
CC end-to-end fusion of chromosomes. In addition to its telomeric DNA-
CC binding role, required to recruit a number of factors and enzymes
CC required for telomere protection, including the shelterin complex,
CC TERF2IP/RAP1 and DCLRE1B/Apollo. Component of the shelterin complex
CC (telosome) that is involved in the regulation of telomere length and
CC protection. Shelterin associates with arrays of double-stranded 5'-
CC TTAGGG-3' repeats added by telomerase and protects chromosome ends;
CC without its protective activity, telomeres are no longer hidden from
CC the DNA damage surveillance and chromosome ends are inappropriately
CC processed by DNA repair pathways. Together with DCLRE1B/Apollo, plays a
CC key role in telomeric loop (T loop) formation by generating 3' single-
CC stranded overhang at the leading end telomeres: T loops have been
CC proposed to protect chromosome ends from degradation and repair.
CC Required both to recruit DCLRE1B/Apollo to telomeres and activate the
CC exonuclease activity of DCLRE1B/Apollo. Preferentially binds to
CC positive supercoiled DNA. Together with DCLRE1B/Apollo, required to
CC control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed
CC for telomere replication during fork passage and prevent aberrant
CC telomere topology. Recruits TERF2IP/RAP1 to telomeres, thereby
CC participating in to repressing homology-directed repair (HDR), which
CC can affect telomere length. {ECO:0000269|PubMed:20339076,
CC ECO:0000269|PubMed:20619712, ECO:0000269|PubMed:20622870}.
CC -!- SUBUNIT: Homodimer. Component of the shelterin complex (telosome)
CC composed of TERF1, TERF2, TINF2, TERF2IP/RAP1, ACD and POT1. Interacts
CC with TERF2IP. Interacts with NBN. Interacts with SLX4/BTBD12. Interacts
CC with DCLRE1B/Apollo; the interaction is direct (By similarity).
CC Interacts with TERF2IP/RAP1; the interaction is direct. {ECO:0000250,
CC ECO:0000269|PubMed:20339076, ECO:0000269|PubMed:20619712,
CC ECO:0000269|PubMed:20622870}.
CC -!- INTERACTION:
CC O35144; Q6ZQJ5: Dna2; NbExp=4; IntAct=EBI-6919263, EBI-6919222;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625,
CC ECO:0000269|PubMed:20339076}. Chromosome, telomere
CC {ECO:0000269|PubMed:20339076}. Note=Colocalizes with telomeric DNA in
CC interphase cells and is located at chromosome ends during metaphase.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O35144-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O35144-2; Sequence=VSP_027086;
CC -!- DOMAIN: The TRFH dimerization region mediates the interaction with
CC DCLRE1B/Apollo but not TINF2. {ECO:0000250}.
CC -!- DOMAIN: The HTH domain is an independent structural unit and mediates
CC binding to telomeric DNA. {ECO:0000250}.
CC -!- PTM: Phosphorylated upon DNA damage, most probably by ATM.
CC Phosphorylated TERF2 is not bound to telomeric DNA, and rapidly
CC localizes to damage sites (By similarity). {ECO:0000250}.
CC -!- PTM: Methylated by PRMT1 at multiple arginines within the N-terminal
CC Arg-rich region. Methylation may control association with telomeres (By
CC similarity). {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB81136.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC33784.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK049507; BAC33784.1; ALT_INIT; mRNA.
DR EMBL; AC123868; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC046284; AAH46284.1; -; mRNA.
DR EMBL; AF003000; AAB81136.1; ALT_INIT; mRNA.
DR CCDS; CCDS52666.1; -. [O35144-2]
DR CCDS; CCDS90457.1; -. [O35144-1]
DR RefSeq; NP_001076587.1; NM_001083118.2. [O35144-2]
DR RefSeq; NP_001273129.1; NM_001286200.1.
DR RefSeq; XP_006530899.1; XM_006530836.3.
DR AlphaFoldDB; O35144; -.
DR SMR; O35144; -.
DR BioGRID; 204117; 16.
DR ComplexPortal; CPX-153; Shelterin complex.
DR ComplexPortal; CPX-498; Slx4-Terf2 complex.
DR IntAct; O35144; 7.
DR MINT; O35144; -.
DR STRING; 10090.ENSMUSP00000118759; -.
DR iPTMnet; O35144; -.
DR PhosphoSitePlus; O35144; -.
DR EPD; O35144; -.
DR jPOST; O35144; -.
DR MaxQB; O35144; -.
DR PaxDb; O35144; -.
DR PeptideAtlas; O35144; -.
DR PRIDE; O35144; -.
DR ProteomicsDB; 258997; -. [O35144-1]
DR ProteomicsDB; 258998; -. [O35144-2]
DR Antibodypedia; 1053; 632 antibodies from 46 providers.
DR DNASU; 21750; -.
DR Ensembl; ENSMUST00000068421; ENSMUSP00000068948; ENSMUSG00000031921. [O35144-1]
DR Ensembl; ENSMUST00000116425; ENSMUSP00000112126; ENSMUSG00000031921. [O35144-2]
DR GeneID; 21750; -.
DR KEGG; mmu:21750; -.
DR UCSC; uc009nhf.2; mouse. [O35144-2]
DR CTD; 7014; -.
DR MGI; MGI:1195972; Terf2.
DR VEuPathDB; HostDB:ENSMUSG00000031921; -.
DR eggNOG; ENOG502RYHN; Eukaryota.
DR GeneTree; ENSGT00940000158316; -.
DR InParanoid; O35144; -.
DR OrthoDB; 605826at2759; -.
DR PhylomeDB; O35144; -.
DR Reactome; R-MMU-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
DR Reactome; R-MMU-110331; Cleavage of the damaged purine.
DR Reactome; R-MMU-171319; Telomere Extension By Telomerase.
DR Reactome; R-MMU-174411; Polymerase switching on the C-strand of the telomere.
DR Reactome; R-MMU-174414; Processive synthesis on the C-strand of the telomere.
DR Reactome; R-MMU-174417; Telomere C-strand (Lagging Strand) Synthesis.
DR Reactome; R-MMU-174430; Telomere C-strand synthesis initiation.
DR Reactome; R-MMU-174437; Removal of the Flap Intermediate from the C-strand.
DR Reactome; R-MMU-2559586; DNA Damage/Telomere Stress Induced Senescence.
DR Reactome; R-MMU-9670095; Inhibition of DNA recombination at telomere.
DR BioGRID-ORCS; 21750; 23 hits in 77 CRISPR screens.
DR ChiTaRS; Terf2; mouse.
DR PRO; PR:O35144; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; O35144; protein.
DR Bgee; ENSMUSG00000031921; Expressed in embryonic post-anal tail and 266 other tissues.
DR ExpressionAtlas; O35144; baseline and differential.
DR Genevisible; O35144; MM.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
DR GO; GO:0001673; C:male germ cell nucleus; IDA:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0000783; C:nuclear telomere cap complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0070187; C:shelterin complex; ISO:MGI.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; IMP:BHF-UCL.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0098505; F:G-rich strand telomeric DNA binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:BHF-UCL.
DR GO; GO:0003720; F:telomerase activity; ISO:MGI.
DR GO; GO:0042162; F:telomeric DNA binding; IDA:BHF-UCL.
DR GO; GO:0008089; P:anterograde axonal transport; IMP:SynGO.
DR GO; GO:0099087; P:anterograde axonal transport of messenger ribonucleoprotein complex; ISO:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:1903770; P:negative regulation of beta-galactosidase activity; ISO:MGI.
DR GO; GO:2000773; P:negative regulation of cellular senescence; ISO:MGI.
DR GO; GO:1905778; P:negative regulation of exonuclease activity; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
DR GO; GO:1904430; P:negative regulation of t-circle formation; ISO:MGI.
DR GO; GO:1904354; P:negative regulation of telomere capping; ISO:MGI.
DR GO; GO:0032205; P:negative regulation of telomere maintenance; ISO:MGI.
DR GO; GO:0032208; P:negative regulation of telomere maintenance via recombination; IMP:BHF-UCL.
DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; ISO:MGI.
DR GO; GO:1904357; P:negative regulation of telomere maintenance via telomere lengthening; ISO:MGI.
DR GO; GO:1905839; P:negative regulation of telomeric D-loop disassembly; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; ISO:MGI.
DR GO; GO:0032206; P:positive regulation of telomere maintenance; IDA:MGI.
DR GO; GO:0031848; P:protection from non-homologous end joining at telomere; IDA:MGI.
DR GO; GO:0070198; P:protein localization to chromosome, telomeric region; ISO:MGI.
DR GO; GO:0032204; P:regulation of telomere maintenance; ISO:MGI.
DR GO; GO:0032210; P:regulation of telomere maintenance via telomerase; ISO:MGI.
DR GO; GO:0016233; P:telomere capping; ISO:MGI.
DR GO; GO:0000723; P:telomere maintenance; IDA:MGI.
DR GO; GO:0061820; P:telomeric D-loop disassembly; ISO:MGI.
DR GO; GO:0031627; P:telomeric loop formation; IMP:BHF-UCL.
DR CDD; cd11654; TRF2_RBM; 1.
DR Gene3D; 1.25.40.210; -; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR013867; Telomere_rpt-bd_fac_dimer_dom.
DR InterPro; IPR036507; Telomere_rpt-bd_fac_dimer_sf.
DR InterPro; IPR017357; TERF1/2.
DR InterPro; IPR030657; TERF2.
DR InterPro; IPR031902; TERF2_RBM.
DR PANTHER; PTHR46833; PTHR46833; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF16772; TERF2_RBM; 1.
DR Pfam; PF08558; TRF; 1.
DR PIRSF; PIRSF038016; Telomere_bd-1_Pin2; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF63600; SSF63600; 1.
DR PROSITE; PS51294; HTH_MYB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Chromosome; DNA-binding; Isopeptide bond;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Telomere;
KW Ubl conjugation.
FT CHAIN 1..541
FT /note="Telomeric repeat-binding factor 2"
FT /id="PRO_0000197132"
FT DOMAIN 483..540
FT /note="HTH myb-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT DNA_BIND 511..536
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00625"
FT REGION 1..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 87..290
FT /note="TRFH dimerization"
FT REGION 291..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 373..377
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 24..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..387
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..431
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 62
FT /note="Asymmetric dimethylarginine; by PRMT1"
FT /evidence="ECO:0000250|UniProtKB:Q15554"
FT MOD_RES 63
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q15554"
FT MOD_RES 233
FT /note="Phosphothreonine; by ATM"
FT /evidence="ECO:0000250|UniProtKB:Q15554"
FT MOD_RES 364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 290
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15554"
FT CROSSLNK 337
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15554"
FT CROSSLNK 355
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15554"
FT CROSSLNK 371
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15554"
FT CROSSLNK 377
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15554"
FT CROSSLNK 452
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15554"
FT VAR_SEQ 448..541
FT /note="ASKDKWNSPNGLEEKEVWLEEDQLFEVQAPGEDRSSSLTRKQKWTIEESEWV
FT KDGVRKYGEGNWAAISKSYPFVNRTAVMIKDRWRTMKKLGMN -> YEDLLCRSLGAGW
FT RAWLGLVLLP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_027086"
FT MUTAGEN 165
FT /note="F->A: Abolishes interaction with DCLRE1B/Apollo,
FT leading to activate the ATM signaling pathway."
FT /evidence="ECO:0000269|PubMed:20619712"
FT MUTAGEN 335..336
FT /note="AF->SS: Abolishes interaction with TERF2IP/RAP1 but
FT does not affect protection of telomeres against non-
FT homologous end-joining (NHEJ)-mediated repair."
FT /evidence="ECO:0000269|PubMed:20339076"
FT CONFLICT 317
FT /note="Missing (in Ref. 4; AAB81136)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="D -> S (in Ref. 4; AAB81136)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="K -> E (in Ref. 3; AAH46284 and 4; AAB81136)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 541 AA; 60263 MW; 2788F7322506182C CRC64;
MAAGAGTAGP ASGPGVVRDP MASQPRKRPS REGGEGGEGE RRSNTMAGGG GSSDSSGRAA
SRRASRSGGR ARRGRHEPGL GGAAERGAGE ARLEEAVNRW VLKFYFHEAL RAFRSSRYRD
FRQIRDIMQA LLVRPLGKEH TVSRLLRVMQ CLSRIEEGEN LDCSFDMEAE LTPLESAINV
LEMIKTEFTL TDSMVESSRK LVKEAAVIIC IKNKEFEKAS KILKKYMSKD PTTQKLRTDL
LNIIREKNLA HPVIQNFSYE VFQQKMLRFL ESHLDDTEPY LLTMAKKALK SESAASSTMR
EEKHPEPVEK PLREPPSRQP QNPPATIGIR TLKAAFKALS TAQDSEAAFA KLDQKDLVLA
NLASPSSPAH KHKRPRKDEH ESAAPAEGEG GSDRQPRNSP MTISRLLLEE DSQSTEPSPG
LNSSHKAMSA SKPRALNQPH PGEKKPKASK DKWNSPNGLE EKEVWLEEDQ LFEVQAPGED
RSSSLTRKQK WTIEESEWVK DGVRKYGEGN WAAISKSYPF VNRTAVMIKD RWRTMKKLGM
N
