NBN_MOUSE
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 03-AUG-2022, entry version 164.
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}.
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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; Q9R207; -.
DR PeptideAtlas; Q9R207; -.
DR PRIDE; Q9R207; -.
DR ProteomicsDB; 286153; -.
DR Antibodypedia; 690; 1581 antibodies from 48 providers.
DR DNASU; 27354; -.
DR Ensembl; ENSMUST00000029879; ENSMUSP00000029879; ENSMUSG00000028224.
DR GeneID; 27354; -.
DR KEGG; mmu:27354; -.
DR UCSC; uc008sbn.1; mouse.
DR CTD; 4683; -.
DR MGI; MGI:1351625; Nbn.
DR VEuPathDB; HostDB:ENSMUSG00000028224; -.
DR eggNOG; ENOG502QQ7Y; Eukaryota.
DR GeneTree; ENSGT00390000000521; -.
DR InParanoid; Q9R207; -.
DR OMA; LESPHSC; -.
DR OrthoDB; 831679at2759; -.
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 114 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 286 other tissues.
DR ExpressionAtlas; Q9R207; baseline and differential.
DR Genevisible; Q9R207; MM.
DR GO; GO:0070533; C:BRCA1-C complex; ISO:MGI.
DR GO; GO:0098687; C:chromosomal region; IC:ComplexPortal.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
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: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:0047485; F:protein N-terminus binding; ISS:UniProtKB.
DR GO; GO:0001832; P:blastocyst growth; IMP:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IMP:MGI.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; ISO:MGI.
DR GO; GO:0000729; P:DNA double-strand break processing; IC:ComplexPortal.
DR GO; GO:0032508; P:DNA duplex unwinding; ISO:MGI.
DR GO; GO:0110025; P:DNA strand resection involved in replication fork processing; IC: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; IC: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; IC: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:0050885; P:neuromuscular process controlling balance; IMP:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0033674; P:positive regulation of kinase activity; 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; cd00060; FHA; 1.
DR Gene3D; 3.40.50.10190; -; 1.
DR Gene3D; 3.40.50.10980; -; 1.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR013908; DNA-repair_Nbs1_C.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR040227; Nibrin-rel.
DR InterPro; IPR032429; Nibrin_BRCT2.
DR InterPro; IPR043014; Nibrin_BRCT2_sf.
DR InterPro; IPR016592; Nibrin_met.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR12162; PTHR12162; 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; SSF49879; SSF49879; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
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
