ID NBN_MOUSE Reviewed; 751 AA. AC Q9R207; O88981; Q3UY57; Q811I6; Q8CCY0; Q9R1X1; DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 173. DE RecName: Full=Nibrin; DE AltName: Full=Cell cycle regulatory protein p95; DE AltName: Full=Nijmegen breakage syndrome protein 1 homolog; GN Name=Nbn; Synonyms=Nbs1; 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 [MRNA]. RX PubMed=10640816; DOI=10.1159/000015396; RA Vissinga C.S., Yeo T.C., Woessner J., Massa H.F., Wilson R.K., Trask B.J., RA Concannon P.; RT "Identification, characterization, and mapping of a mouse homolog of the RT gene mutated in Nijmegen breakage syndrome."; RL Cytogenet. Cell Genet. 87:80-84(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain, and Testis; RA Saito T.; RT "Structure of the mouse Nijmegen breakage syndrome (Nibrin/Nbs1) protein."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain stem; RA Mas C., Bourgeois F., Simonneau M.; RT "Isolation of 50 cDNAs differentially expressed in embryonic forebrain as RT compared to mid and hindbrain: a strategy to identify candidate genes RT involved in human neurodevelopmental diseases."; RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Czech II, and FVB/N; TISSUE=Colon, and Mammary gland; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-613. RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata; 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 [6] RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=10915761; DOI=10.1093/hmg/9.12.1739; RA Wilda M., Demuth I., Concannon P., Sperling K., Hameister H.; RT "Expression pattern of the Nijmegen breakage syndrome gene, Nbs1, during RT murine development."; RL Hum. Mol. Genet. 9:1739-1744(2000). RN [7] RP INTERACTION WITH SP100. RX PubMed=12470659; DOI=10.1016/s0006-291x(02)02755-9; RA Naka K., Ikeda K., Motoyama N.; RT "Recruitment of NBS1 into PML oncogenic domains via interaction with SP100 RT protein."; RL Biochem. Biophys. Res. Commun. 299:863-871(2002). RN [8] RP PHOSPHORYLATION AT SER-343. RX PubMed=17376776; DOI=10.1074/jbc.c700019200; RA Yong W., Bao S., Chen H., Li D., Sanchez E.R., Shou W.; RT "Mice lacking protein phosphatase 5 are defective in ataxia telangiectasia RT mutated (ATM)-mediated cell cycle arrest."; RL J. Biol. Chem. 282:14690-14694(2007). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic fibroblast; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Spleen; 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 [11] RP INTERACTION WITH CYREN. RX PubMed=30017584; DOI=10.1016/j.molcel.2018.06.018; RA Hung P.J., Johnson B., Chen B.R., Byrum A.K., Bredemeyer A.L., RA Yewdell W.T., Johnson T.E., Lee B.J., Deivasigamani S., Hindi I., RA Amatya P., Gross M.L., Paull T.T., Pisapia D.J., Chaudhuri J., RA Petrini J.J.H., Mosammaparast N., Amarasinghe G.K., Zha S., Tyler J.K., RA Sleckman B.P.; RT "MRI is a DNA damage response adaptor during classical non-homologous end RT joining."; RL Mol. Cell 71:332-342(2018). CC -!- FUNCTION: Component of the MRE11-RAD50-NBN (MRN complex) which plays a CC critical role in the cellular response to DNA damage and the CC maintenance of chromosome integrity. The complex is involved in double- CC strand break (DSB) repair, DNA recombination, maintenance of telomere CC integrity, cell cycle checkpoint control and meiosis. The complex CC possesses single-strand endonuclease activity and double-strand- CC specific 3'-5' exonuclease activity, which are provided by MRE11. RAD50 CC may be required to bind DNA ends and hold them in close proximity. NBN CC modulate the DNA damage signal sensing by recruiting PI3/PI4-kinase CC family members ATM, ATR, and probably DNA-PKcs to the DNA damage sites CC and activating their functions. It can also recruit MRE11 and RAD50 to CC the proximity of DSBs by an interaction with the histone H2AX. NBN also CC functions in telomere length maintenance by generating the 3' overhang CC which serves as a primer for telomerase dependent telomere elongation. CC NBN is a major player in the control of intra-S-phase checkpoint and CC there is some evidence that NBN is involved in G1 and G2 checkpoints. CC The roles of NBS1/MRN encompass DNA damage sensor, signal transducer, CC and effector, which enable cells to maintain DNA integrity and genomic CC stability. Forms a complex with RBBP8 to link DNA double-strand break CC sensing to resection. Enhances AKT1 phosphorylation possibly by CC association with the mTORC2 complex (By similarity). CC {ECO:0000250|UniProtKB:O60934}. CC -!- SUBUNIT: Component of the MRN complex composed of two heterodimers CC RAD50/MRE11 associated with a single NBN (By similarity). As part of CC the MRN complex, interacts with MCM9; the interaction recruits the CC complex to DNA repair sites (By similarity). Component of the BASC CC complex, at least composed of BRCA1, MSH2, MSH6, MLH1, ATM, BLM, RAD50, CC MRE11 and NBN (By similarity). Interacts with histone H2AX this CC requires phosphorylation of H2AX on 'Ser-139' (By similarity). CC Interacts with HJURP, INTS3, KPNA2 and TERF2 (By similarity). Interacts CC with RBBP8; the interaction links the role of the MRN complex in DNA CC double-strand break sensing to resection (By similarity). Interacts CC with SP100; recruits NBN to PML bodies (PubMed:12470659). Interacts CC with ATF2 (By similarity). Interacts with MTOR, MAPKAP1 isoform 2 and CC RICTOR; indicative for an association with the mTORC2 complex (By CC similarity). Interacts with MRNIP (By similarity). Interacts with UFL1; CC promoting UFL1 recruitment to double-strand breaks following DNA damage CC (By similarity). Interacts with CYREN (via XLF motif) CC (PubMed:30017584). {ECO:0000250|UniProtKB:O60934, CC ECO:0000269|PubMed:12470659, ECO:0000269|PubMed:30017584}. CC -!- INTERACTION: CC Q9R207; Q61216: Mre11; NbExp=2; IntAct=EBI-2014862, EBI-2014813; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O60934}. Nucleus, CC PML body {ECO:0000250|UniProtKB:O60934}. Chromosome, telomere CC {ECO:0000250|UniProtKB:O60934}. Chromosome CC {ECO:0000250|UniProtKB:O60934}. Note=Localizes to discrete nuclear foci CC after treatment with genotoxic agents. Acetylation of 'Lys-5' of CC histone H2AX (H2AXK5ac) promotes NBN/NBS1 assembly at the sites of DNA CC damage. {ECO:0000250|UniProtKB:O60934}. CC -!- TISSUE SPECIFICITY: High expression in the liver, heart and testis. Low CC expression in all other tissues analyzed. In the cerebellum the CC postmitotic Purkinje cells are marked specifically. CC {ECO:0000269|PubMed:10915761}. CC -!- DEVELOPMENTAL STAGE: A low level of expression is observed in all CC tissues. Highly specific expression was observed in organs with CC physiologic DNA double strand breakage (DSB), such as testis, thymus CC and spleen. Enhanced expression is also found at sites of high CC proliferative activity. These are the subventricular layer of the CC telencephalon and the diencephalon, the liver, lung, kidney and gut, as CC well as striated and smooth muscle cells in various organs. CC {ECO:0000269|PubMed:10915761}. CC -!- DOMAIN: The FHA and BRCT domains are likely to have a crucial role for CC both binding to histone H2AX and for relocalization of MRE11/RAD50 CC complex to the vicinity of DNA damage. {ECO:0000250|UniProtKB:O60934}. CC -!- DOMAIN: The C-terminal domain contains a MRE11-binding site, and this CC interaction is required for the nuclear localization of the MRN CC complex. {ECO:0000250|UniProtKB:O60934}. CC -!- DOMAIN: The EEXXXDDL motif at the C-terminus is required for the CC interaction with ATM and its recruitment to sites of DNA damage and CC promote the phosphorylation of ATM substrates, leading to the events of CC DNA damage response. {ECO:0000250|UniProtKB:O60934}. CC -!- PTM: Phosphorylated by ATM in response of ionizing radiation, and such CC phosphorylation is responsible intra-S phase checkpoint control and CC telomere maintenance. {ECO:0000250|UniProtKB:O60934}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF076687; AAD20943.1; -; mRNA. DR EMBL; AB016988; BAA76298.1; -; mRNA. DR EMBL; AF092840; AAC62113.1; -; mRNA. DR EMBL; BC044773; AAH44773.1; -; mRNA. DR EMBL; BC055061; AAH55061.1; -; mRNA. DR EMBL; AK134960; BAE22356.1; -; mRNA. DR EMBL; AK031933; BAC27610.1; -; mRNA. DR CCDS; CCDS17986.1; -. DR RefSeq; NP_038780.3; NM_013752.3. DR AlphaFoldDB; Q9R207; -. DR BioGRID; 205163; 19. DR ComplexPortal; CPX-4703; MRN complex. DR DIP; DIP-46804N; -. DR IntAct; Q9R207; 2. DR STRING; 10090.ENSMUSP00000029879; -. DR iPTMnet; Q9R207; -. DR PhosphoSitePlus; Q9R207; -. DR SwissPalm; Q9R207; -. DR EPD; Q9R207; -. DR jPOST; Q9R207; -. DR MaxQB; Q9R207; -. DR PaxDb; 10090-ENSMUSP00000029879; -. DR PeptideAtlas; Q9R207; -. DR ProteomicsDB; 286153; -. DR Pumba; Q9R207; -. DR Antibodypedia; 690; 1783 antibodies from 48 providers. DR DNASU; 27354; -. DR Ensembl; ENSMUST00000029879.15; ENSMUSP00000029879.9; ENSMUSG00000028224.15. DR GeneID; 27354; -. DR KEGG; mmu:27354; -. DR UCSC; uc008sbn.1; mouse. DR AGR; MGI:1351625; -. DR CTD; 4683; -. DR MGI; MGI:1351625; Nbn. DR VEuPathDB; HostDB:ENSMUSG00000028224; -. DR eggNOG; ENOG502QQ7Y; Eukaryota. DR GeneTree; ENSGT00390000000521; -. DR InParanoid; Q9R207; -. DR OMA; KKNFKMF; -. DR OrthoDB; 2787263at2759; -. DR PhylomeDB; Q9R207; -. DR TreeFam; TF101103; -. DR Reactome; R-MMU-2559586; DNA Damage/Telomere Stress Induced Senescence. DR Reactome; R-MMU-5685938; HDR through Single Strand Annealing (SSA). DR Reactome; R-MMU-5685939; HDR through MMEJ (alt-NHEJ). DR Reactome; R-MMU-5685942; HDR through Homologous Recombination (HRR). DR Reactome; R-MMU-5693548; Sensing of DNA Double Strand Breaks. DR Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks. DR Reactome; R-MMU-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates. DR Reactome; R-MMU-5693571; Nonhomologous End-Joining (NHEJ). DR Reactome; R-MMU-5693579; Homologous DNA Pairing and Strand Exchange. DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends. DR Reactome; R-MMU-5693616; Presynaptic phase of homologous DNA pairing and strand exchange. DR Reactome; R-MMU-6804756; Regulation of TP53 Activity through Phosphorylation. DR Reactome; R-MMU-69473; G2/M DNA damage checkpoint. DR BioGRID-ORCS; 27354; 15 hits in 120 CRISPR screens. DR ChiTaRS; Nbn; mouse. DR PRO; PR:Q9R207; -. DR Proteomes; UP000000589; Chromosome 4. DR RNAct; Q9R207; Protein. DR Bgee; ENSMUSG00000028224; Expressed in saccule of membranous labyrinth and 290 other cell types or tissues. DR ExpressionAtlas; Q9R207; baseline and differential. DR GO; GO:0070533; C:BRCA1-C complex; ISO:MGI. DR GO; GO:0098687; C:chromosomal region; NAS:ComplexPortal. DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL. DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI. DR GO; GO:0030870; C:Mre11 complex; ISS:UniProtKB. DR GO; GO:0042405; C:nuclear inclusion body; ISS:UniProtKB. DR GO; GO:0005730; C:nucleolus; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IDA:MGI. DR GO; GO:0016605; C:PML body; IDA:BHF-UCL. DR GO; GO:0005657; C:replication fork; IDA:MGI. DR GO; GO:0035861; C:site of double-strand break; ISO:MGI. DR GO; GO:0003684; F:damaged DNA binding; IDA:MGI. DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISS:UniProtKB. DR GO; GO:0001832; P:blastocyst growth; IMP:UniProtKB. DR GO; GO:0000077; P:DNA damage checkpoint signaling; ISO:MGI. DR GO; GO:0000729; P:DNA double-strand break processing; NAS:ComplexPortal. DR GO; GO:0032508; P:DNA duplex unwinding; ISO:MGI. DR GO; GO:0110025; P:DNA strand resection involved in replication fork processing; NAS:ComplexPortal. DR GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central. DR GO; GO:0035825; P:homologous recombination; NAS:ComplexPortal. DR GO; GO:0001701; P:in utero embryonic development; IMP:UniProtKB. DR GO; GO:0097193; P:intrinsic apoptotic signaling pathway; IMP:MGI. DR GO; GO:0045190; P:isotype switching; IDA:UniProtKB. DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW. DR GO; GO:0007095; P:mitotic G2 DNA damage checkpoint signaling; IMP:MGI. DR GO; GO:0044818; P:mitotic G2/M transition checkpoint; NAS:ComplexPortal. DR GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:MGI. DR GO; GO:1904354; P:negative regulation of telomere capping; ISO:MGI. DR GO; GO:0046597; P:negative regulation of viral entry into host cell; ISO:MGI. DR GO; GO:0007405; P:neuroblast proliferation; IMP:MGI. DR GO; GO:0050885; P:neuromuscular process controlling balance; IMP:MGI. DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI. DR GO; GO:0031954; P:positive regulation of protein autophosphorylation; ISO:MGI. DR GO; GO:0032206; P:positive regulation of telomere maintenance; ISO:MGI. DR GO; GO:0048145; P:regulation of fibroblast proliferation; ISS:UniProtKB. DR GO; GO:0090656; P:t-circle formation; ISO:MGI. DR GO; GO:0000723; P:telomere maintenance; ISS:UniProtKB. DR GO; GO:0090737; P:telomere maintenance via telomere trimming; ISO:MGI. DR GO; GO:0031860; P:telomeric 3' overhang formation; ISO:MGI. DR CDD; cd17741; BRCT_nibrin; 1. DR CDD; cd22667; FHA_NBN; 1. DR Gene3D; 2.60.200.20; -; 1. DR Gene3D; 3.40.50.10190; BRCT domain; 1. DR Gene3D; 3.40.50.10980; Nibrin, BRCT2 domain; 1. DR InterPro; IPR036420; BRCT_dom_sf. DR InterPro; IPR000253; FHA_dom. DR InterPro; IPR040227; Nibrin-rel. DR InterPro; IPR032429; Nibrin_BRCT2. DR InterPro; IPR043014; Nibrin_BRCT2_sf. DR InterPro; IPR013908; Nibrin_C. DR InterPro; IPR016592; Nibrin_met. DR InterPro; IPR008984; SMAD_FHA_dom_sf. DR PANTHER; PTHR12162:SF0; NIBRIN; 1. DR PANTHER; PTHR12162; NIBRIN-RELATED; 1. DR Pfam; PF00498; FHA; 1. DR Pfam; PF08599; Nbs1_C; 1. DR Pfam; PF16508; NIBRIN_BRCT_II; 1. DR PIRSF; PIRSF011869; Nibrin_animal; 1. DR SMART; SM00240; FHA; 1. DR SMART; SM01348; Nbs1_C; 1. DR SUPFAM; SSF52113; BRCT domain; 1. DR SUPFAM; SSF49879; SMAD/FHA domain; 1. DR PROSITE; PS50006; FHA_DOMAIN; 1. DR Genevisible; Q9R207; MM. PE 1: Evidence at protein level; KW Cell cycle; Chromosome; DNA damage; DNA repair; Isopeptide bond; Meiosis; KW Nucleus; Phosphoprotein; Reference proteome; Telomere; Ubl conjugation. FT CHAIN 1..751 FT /note="Nibrin" FT /id="PRO_0000231044" FT DOMAIN 24..83 FT /note="FHA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00086" FT DOMAIN 105..181 FT /note="BRCT" FT REGION 111..328 FT /note="Mediates interaction with SP100" FT /evidence="ECO:0000269|PubMed:12470659" FT REGION 221..403 FT /note="Interaction with MTOR, MAPKAP1 and RICTOR" FT /evidence="ECO:0000250|UniProtKB:O60934" FT REGION 389..418 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 444..479 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 491..550 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 576..645 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 731..751 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 461..467 FT /note="Nuclear localization signal" FT /evidence="ECO:0000250|UniProtKB:O60934" FT MOTIF 734..741 FT /note="EEXXXDDL motif" FT /evidence="ECO:0000250|UniProtKB:O60934" FT COMPBIAS 392..418 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 444..460 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 461..477 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 491..517 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 529..550 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 576..601 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 611..629 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 337 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:O60934" FT MOD_RES 343 FT /note="Phosphoserine; by ATM" FT /evidence="ECO:0000269|PubMed:17376776" FT MOD_RES 347 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O60934" FT MOD_RES 398 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332, FT ECO:0007744|PubMed:21183079" FT MOD_RES 433 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O60934" FT MOD_RES 508 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O60934" FT CROSSLNK 569 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O60934" FT CROSSLNK 580 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:O60934" FT CONFLICT 9 FT /note="G -> S (in Ref. 4; AAH44773)" FT /evidence="ECO:0000305" FT CONFLICT 11..12 FT /note="AP -> SL (in Ref. 3; AAC62113)" FT /evidence="ECO:0000305" FT CONFLICT 325 FT /note="P -> Q (in Ref. 5; BAE22356)" FT /evidence="ECO:0000305" FT CONFLICT 366 FT /note="D -> E (in Ref. 2; BAA76298)" FT /evidence="ECO:0000305" FT CONFLICT 455 FT /note="I -> F (in Ref. 2; BAA76298)" FT /evidence="ECO:0000305" FT CONFLICT 513 FT /note="L -> Q (in Ref. 4; AAH44773)" FT /evidence="ECO:0000305" FT CONFLICT 664 FT /note="N -> K (in Ref. 4; AAH44773)" FT /evidence="ECO:0000305" FT CONFLICT 676 FT /note="E -> D (in Ref. 4; AAH44773)" FT /evidence="ECO:0000305" FT CONFLICT 679 FT /note="P -> S (in Ref. 4; AAH44773)" FT /evidence="ECO:0000305" SQ SEQUENCE 751 AA; 83795 MW; C9F597CC08227B2C CRC64; MWKLLPAAGA APGEPYRLLA GVEYVVGRKN CGILIENDQS ISRNHAVLTV NFPVTSLSQT DEIPTLTIKD NSKYGTFVNE EKMQTGLSCT LKTGDRVTFG VFESKFRVEY EPLVVCSSCL DVSGKTVLNQ AILQLGGLTA NNWTEECTHL VMSAVKVTIK TICALICGRP IIKPEYFSEF LKAVESKKQP PDIESFYPPI DEPAIGSKSV DLSGRHERKQ IFKGKTFVFL NAKQHKKLSS AVAFGGGEAR LMAEDDEEEQ SFFSAPGTCV VDVGITNTQL IISHSQKKWI HLIMDTLQRN GLRPIPEAEI GLAVIFMTTE NYCNPQGQPC TELKTTTPGP SLSQVLSANG KIIPSAPVNM TTYVADTESE PADTCMPLSE RPEEVKIPGL EQSSRKLSQE TFNIKEAPKP SSKANNVASD TLVRGKTPSY QLSPMKFPVA NKNKDWTSQQ QQNSIKNYFQ PCTRKRERDE DNPELSSCKS SRMELSCSLL EQTQPAGPSL WKSKEHQSQN ATLDREADTS SVGGMDIELN RKSPDRKPLP TETLRPRKRK DVDLATEEEV LEELLRSTKP ELAVQVKVEK QEADDTIRKK PRMDAERNRP LNGGSEPESN SALQEDEREK KDELQTESWS TKHEIANSDG LQDSSEELPR KLLLTEFRSL VVSNHNSTSR NLCVNECGPL KNFKKFKKAT FPGAGKLPHI IGGSDLVGHH ARKNTELEEW LKQEMEVQKQ QAKEESLADD LFRYNPNVKR R //