ID XRCC5_MOUSE Reviewed; 732 AA. AC P27641; Q3TE46; Q3TJT0; Q3TN82; Q80UT1; Q8C4N6; Q8K1K7; Q9R169; DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 4. DT 27-MAR-2024, entry version 201. DE RecName: Full=X-ray repair cross-complementing protein 5; DE EC=3.6.4.-; DE AltName: Full=ATP-dependent DNA helicase 2 subunit 2; DE AltName: Full=ATP-dependent DNA helicase II 80 kDa subunit; DE AltName: Full=CTC box-binding factor 85 kDa subunit; DE Short=CTC85; DE Short=CTCBF; DE AltName: Full=DNA repair protein XRCC5; DE AltName: Full=Ku autoantigen protein p86 homolog; DE AltName: Full=Ku80; DE AltName: Full=Nuclear factor IV; GN Name=Xrcc5; Synonyms=G22p2; 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]. RC STRAIN=BALB/cJ; RX PubMed=1641347; DOI=10.1093/nar/20.14.3784; RA Falzon M., Kuff E.L.; RT "The nucleotide sequence of a mouse cDNA encoding the 80 kDa subunit of the RT Ku (p70/p80) autoantigen."; RL Nucleic Acids Res. 20:3784-3784(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Mammary carcinoma; RA Jiang G.C., Yuan L.Z., Wei K.; RT "Ku gene mutation of radiosensitive mouse mammary carcinoma cell line RT SX-9."; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J, and NOD; RC TISSUE=Embryonic head, Embryonic heart, Embryonic liver, Kidney, and RC Thymus; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=129/Sv X 129SvCp, and FVB/N; RC TISSUE=Embryonic stem cell, and 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 [5] RP DEVELOPMENTAL STAGE, AND INDUCTION. RX PubMed=8605992; DOI=10.1016/0014-5793(96)00189-5; RA Oderwald H., Hughes M.J., Jost J.-P.; RT "Non-histone protein 1 (NHP1) is a member of the Ku protein family which is RT upregulated in differentiating mouse myoblasts and human promyelocytes."; RL FEBS Lett. 382:313-318(1996). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Kidney, Liver, Lung, Pancreas, 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 [7] 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: Single-stranded DNA-dependent ATP-dependent helicase that CC plays a key role in DNA non-homologous end joining (NHEJ) by recruiting CC DNA-PK to DNA. Required for double-strand break repair and V(D)J CC recombination. Also has a role in chromosome translocation. The DNA CC helicase II complex binds preferentially to fork-like ends of double- CC stranded DNA in a cell cycle-dependent manner. It works in the 3'-5' CC direction. During NHEJ, the XRCC5-XRRC6 dimer performs the recognition CC step: it recognizes and binds to the broken ends of the DNA and CC protects them from further resection. Binding to DNA may be mediated by CC XRCC6. The XRCC5-XRRC6 dimer acts as a regulatory subunit of the DNA- CC dependent protein kinase complex DNA-PK by increasing the affinity of CC the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5-XRRC6 dimer CC is probably involved in stabilizing broken DNA ends and bringing them CC together. The assembly of the DNA-PK complex to DNA ends is required CC for the NHEJ ligation step. The XRCC5-XRRC6 dimer probably also acts as CC a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the CC beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site CC near double-strand breaks. XRCC5 probably acts as the catalytic subunit CC of 5'-dRP activity, and allows to 'clean' the termini of abasic sites, CC a class of nucleotide damage commonly associated with strand breaks, CC before such broken ends can be joined. The XRCC5-XRRC6 dimer together CC with APEX1 acts as a negative regulator of transcription. In CC association with NAA15, the XRCC5-XRRC6 dimer binds to the osteocalcin CC promoter and activates osteocalcin expression. As part of the DNA-PK CC complex, involved in the early steps of ribosome assembly by promoting CC the processing of precursor rRNA into mature 18S rRNA in the small- CC subunit processome. Binding to U3 small nucleolar RNA, recruits PRKDC CC and XRCC5/Ku86 to the small-subunit processome. Plays a role in the CC regulation of DNA virus-mediated innate immune response by assembling CC into the HDP-RNP complex, a complex that serves as a platform for IRF3 CC phosphorylation and subsequent innate immune response activation CC through the cGAS-STING pathway. {ECO:0000250|UniProtKB:P13010}. CC -!- SUBUNIT: Heterodimer composed of XRCC5/Ku80 and XRCC6/Ku70 (By CC similarity). Component of the core long-range non-homologous end CC joining (NHEJ) complex (also named DNA-PK complex) composed of PRKDC, CC LIG4, XRCC4, XRCC6/Ku70, XRCC5/Ku86 and NHEJ1/XLF (By similarity). CC Additional component of the NHEJ complex includes PAXX (By similarity). CC Following autophosphorylation, PRKDC dissociates from DNA, leading to CC formation of the short-range NHEJ complex, composed of LIG4, XRCC4, CC XRCC6/Ku70, XRCC5/Ku86 and NHEJ1/XLF (By similarity). The XRCC5-XRCC6 CC dimer also associates with NAA15, and this complex displays DNA binding CC activity towards the osteocalcin FGF response element (OCFRE) (By CC similarity). In addition, XRCC5 binds to the osteoblast-specific CC transcription factors MSX2 and RUNX2 (By similarity). Interacts with CC ELF3 (By similarity). Interacts with APLF (via KBM motif) (By CC similarity). The XRCC5/XRCC6 dimer associates in a DNA-dependent manner CC with APEX1 (By similarity). Identified in a complex with DEAF1 and CC XRCC6 (By similarity). Interacts with NR4A3; the DNA-dependent protein CC kinase complex DNA-PK phosphorylates and activates NR4A3 and prevents CC NR4A3 ubiquitinylation and degradation (By similarity). Interacts with CC RNF138 (By similarity). Interacts with CYREN (via KBM motif) CC (PubMed:30017584). Interacts with WRN (via KBM motif) (By similarity). CC Interacts (via N-terminus) with HSF1 (via N-terminus); this interaction CC is direct and prevents XRCC5/XRCC6 heterodimeric binding and non- CC homologous end joining (NHEJ) repair activities induced by ionizing CC radiation (IR) (By similarity). Interacts with DHX9; this interaction CC occurs in a RNA-dependent manner (By similarity). Part of the HDP-RNP CC complex composed of at least HEXIM1, PRKDC, XRCC5, XRCC6, paraspeckle CC proteins (SFPQ, NONO, PSPC1, RBM14, and MATR3) and NEAT1 RNA (By CC similarity). Interacts with ERCC6 (By similarity). Interacts with ATF7 CC (By similarity). The XRCC5-XRCC6 dimer associates with ALKBH2. CC {ECO:0000250|UniProtKB:P13010, ECO:0000269|PubMed:30017584}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P13010}. Nucleus, CC nucleolus {ECO:0000250|UniProtKB:P13010}. Chromosome CC {ECO:0000250|UniProtKB:P13010}. CC -!- DEVELOPMENTAL STAGE: Expression increases during promyelocyte CC differentiation. {ECO:0000269|PubMed:8605992}. CC -!- INDUCTION: Up-regulation during myogenesis is inhibited by cAMP, 3- CC aminobenzamide and sodium butyrate. Expression in myoblasts is CC unaffected by X-rays and UV light. {ECO:0000269|PubMed:8605992}. CC -!- DOMAIN: The EEXXXDDL motif is required for the interaction with CC catalytic subunit PRKDC and its recruitment to sites of DNA damage. CC {ECO:0000250|UniProtKB:P13010}. CC -!- DOMAIN: The VWFA domain interacts with the KBM (Ku-binding motif) found CC in a number of DNA repair proteins. {ECO:0000250|UniProtKB:Q6DDS9}. CC -!- DOMAIN: The N-terminal and C-terminal regions are not required for CC binding to DNA or for degradation of the protein with only the central CC region being required for these processes. CC {ECO:0000250|UniProtKB:Q6DDS9}. CC -!- PTM: ADP-ribosylated by PARP3. {ECO:0000250|UniProtKB:P13010}. CC -!- PTM: Phosphorylated on serine residues. Phosphorylation by PRKDC may CC enhance helicase activity. {ECO:0000250|UniProtKB:P13010}. CC -!- PTM: Sumoylated. {ECO:0000250|UniProtKB:P13010}. CC -!- PTM: Ubiquitinated by RNF8 via 'Lys-48'-linked ubiquitination following CC DNA damage, leading to its degradation and removal from DNA damage CC sites. Ubiquitinated by RNF138, leading to remove the Ku complex from CC DNA breaks. {ECO:0000250|UniProtKB:P13010}. CC -!- SIMILARITY: Belongs to the ku80 family. {ECO:0000305}. 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; X66323; CAA46999.1; -; mRNA. DR EMBL; AF166486; AAD49720.1; -; mRNA. DR EMBL; AK081633; BAC38276.1; -; mRNA. DR EMBL; AK165470; BAE38207.1; -; mRNA. DR EMBL; AK167312; BAE39415.1; -; mRNA. DR EMBL; AK168913; BAE40726.1; -; mRNA. DR EMBL; AK169838; BAE41402.1; -; mRNA. DR EMBL; BC029218; AAH29218.1; -; mRNA. DR EMBL; BC051660; AAH51660.1; -; mRNA. DR CCDS; CCDS35608.1; -. DR PIR; S26303; S26303. DR RefSeq; NP_033559.2; NM_009533.2. DR AlphaFoldDB; P27641; -. DR SMR; P27641; -. DR BioGRID; 204608; 21. DR ComplexPortal; CPX-2047; Ku70:Ku80 complex. DR CORUM; P27641; -. DR IntAct; P27641; 6. DR MINT; P27641; -. DR STRING; 10090.ENSMUSP00000027379; -. DR iPTMnet; P27641; -. DR PhosphoSitePlus; P27641; -. DR SwissPalm; P27641; -. DR EPD; P27641; -. DR jPOST; P27641; -. DR MaxQB; P27641; -. DR PaxDb; 10090-ENSMUSP00000027379; -. DR PeptideAtlas; P27641; -. DR ProteomicsDB; 275224; -. DR Pumba; P27641; -. DR Antibodypedia; 3849; 1300 antibodies from 47 providers. DR DNASU; 22596; -. DR Ensembl; ENSMUST00000027379.10; ENSMUSP00000027379.9; ENSMUSG00000026187.10. DR GeneID; 22596; -. DR KEGG; mmu:22596; -. DR UCSC; uc007bkl.2; mouse. DR AGR; MGI:104517; -. DR CTD; 7520; -. DR MGI; MGI:104517; Xrcc5. DR VEuPathDB; HostDB:ENSMUSG00000026187; -. DR eggNOG; KOG2326; Eukaryota. DR GeneTree; ENSGT00940000153239; -. DR HOGENOM; CLU_010975_2_1_1; -. DR InParanoid; P27641; -. DR OMA; WAMQYVW; -. DR OrthoDB; 5884at2759; -. DR PhylomeDB; P27641; -. DR TreeFam; TF101205; -. DR Reactome; R-MMU-5693571; Nonhomologous End-Joining (NHEJ). DR Reactome; R-MMU-6798695; Neutrophil degranulation. DR BioGRID-ORCS; 22596; 20 hits in 117 CRISPR screens. DR ChiTaRS; Xrcc5; mouse. DR PRO; PR:P27641; -. DR Proteomes; UP000000589; Chromosome 1. DR RNAct; P27641; Protein. DR Bgee; ENSMUSG00000026187; Expressed in saccule of membranous labyrinth and 250 other cell types or tissues. DR GO; GO:0000781; C:chromosome, telomeric region; ISO:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0070418; C:DNA-dependent protein kinase complex; ISO:MGI. DR GO; GO:0005958; C:DNA-dependent protein kinase-DNA ligase 4 complex; ISO:MGI. DR GO; GO:0043564; C:Ku70:Ku80 complex; ISS:UniProtKB. DR GO; GO:0070419; C:nonhomologous end joining complex; 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:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0032993; C:protein-DNA complex; ISO:MGI. DR GO; GO:1990904; C:ribonucleoprotein complex; ISS:UniProtKB. DR GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB. DR GO; GO:0032040; C:small-subunit processome; ISS:UniProtKB. DR GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; ISO:MGI. DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; ISO:MGI. DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro. DR GO; GO:0045027; F:DNA end binding; ISO:MGI. DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro. DR GO; GO:0003691; F:double-stranded telomeric DNA binding; IEA:Ensembl. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB. DR GO; GO:0042162; F:telomeric DNA binding; ISO:MGI. DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:MGI. DR GO; GO:0034511; F:U3 snoRNA binding; ISS:UniProtKB. DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI. DR GO; GO:0002218; P:activation of innate immune response; ISO:MGI. DR GO; GO:0071475; P:cellular hyperosmotic salinity response; ISO:MGI. DR GO; GO:0071398; P:cellular response to fatty acid; IEA:Ensembl. DR GO; GO:0071480; P:cellular response to gamma radiation; ISS:UniProtKB. DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI. DR GO; GO:0071481; P:cellular response to X-ray; ISO:MGI. DR GO; GO:0006974; P:DNA damage response; ISS:UniProtKB. DR GO; GO:0006302; P:double-strand break repair; IMP:MGI. DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; ISS:UniProtKB. DR GO; GO:0060218; P:hematopoietic stem cell differentiation; IMP:MGI. DR GO; GO:0071425; P:hematopoietic stem cell proliferation; IMP:MGI. DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB. DR GO; GO:1904430; P:negative regulation of t-circle formation; ISO:MGI. DR GO; GO:0022008; P:neurogenesis; IMP:MGI. DR GO; GO:0050769; P:positive regulation of neurogenesis; IMP:MGI. DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:MGI. DR GO; GO:0000725; P:recombinational repair; NAS:ComplexPortal. DR GO; GO:0048660; P:regulation of smooth muscle cell proliferation; ISS:UniProtKB. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0034462; P:small-subunit processome assembly; ISS:UniProtKB. DR GO; GO:0000723; P:telomere maintenance; IBA:GO_Central. DR CDD; cd00873; KU80; 1. DR CDD; cd01458; vWA_ku; 1. DR Gene3D; 1.10.1600.10; -; 1. DR Gene3D; 2.40.290.10; -; 1. DR Gene3D; 1.25.40.240; Ku, C-terminal domain; 1. DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1. DR InterPro; IPR006164; Ku70/Ku80_beta-barrel_dom. DR InterPro; IPR024193; Ku80. DR InterPro; IPR005160; Ku_C. DR InterPro; IPR036494; Ku_C_sf. DR InterPro; IPR005161; Ku_N. DR InterPro; IPR014893; Ku_PK_bind. DR InterPro; IPR016194; SPOC-like_C_dom_sf. DR InterPro; IPR036465; vWFA_dom_sf. DR PANTHER; PTHR12604; KU AUTOANTIGEN DNA HELICASE; 1. DR PANTHER; PTHR12604:SF4; X-RAY REPAIR CROSS-COMPLEMENTING PROTEIN 5; 1. DR Pfam; PF02735; Ku; 1. DR Pfam; PF03730; Ku_C; 1. DR Pfam; PF03731; Ku_N; 1. DR Pfam; PF08785; Ku_PK_bind; 1. DR PIRSF; PIRSF016570; Ku80; 1. DR SMART; SM00559; Ku78; 1. DR SUPFAM; SSF101420; C-terminal domain of Ku80; 1. DR SUPFAM; SSF100939; SPOC domain-like; 1. DR SUPFAM; SSF53300; vWA-like; 1. DR Genevisible; P27641; MM. PE 1: Evidence at protein level; KW Acetylation; Activator; ADP-ribosylation; ATP-binding; Chromosome; KW DNA damage; DNA recombination; DNA repair; DNA-binding; Helicase; KW Hydrolase; Immunity; Innate immunity; Isopeptide bond; Nucleotide-binding; KW Nucleus; Phosphoprotein; Reference proteome; Ribosome biogenesis; KW Transcription; Transcription regulation; Ubl conjugation. FT CHAIN 1..732 FT /note="X-ray repair cross-complementing protein 5" FT /id="PRO_0000084341" FT DOMAIN 9..161 FT /note="VWFA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00219" FT DOMAIN 253..453 FT /note="Ku" FT /evidence="ECO:0000255" FT REGION 138..165 FT /note="Leucine-zipper" FT REGION 708..732 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 720..728 FT /note="EEXXXDL motif" FT MOD_RES 258 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P13010" FT MOD_RES 265 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P13010" FT MOD_RES 318 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P13010" FT MOD_RES 332 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P13010" FT MOD_RES 535 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P13010" FT MOD_RES 578 FT /note="Phosphoserine; by PRKDC" FT /evidence="ECO:0000250|UniProtKB:P13010" FT MOD_RES 580 FT /note="Phosphoserine; by PRKDC" FT /evidence="ECO:0000250|UniProtKB:P13010" FT MOD_RES 581 FT /note="Phosphoserine; by PRKDC" FT /evidence="ECO:0000250|UniProtKB:P13010" FT MOD_RES 666 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:P13010" FT MOD_RES 716 FT /note="Phosphothreonine; by PRKDC" FT /evidence="ECO:0000250|UniProtKB:P13010" FT CROSSLNK 195 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P13010" FT CROSSLNK 532 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P13010" FT CROSSLNK 534 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P13010" FT CROSSLNK 567 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P13010" FT CROSSLNK 569 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P13010" FT CROSSLNK 670 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P13010" FT CROSSLNK 689 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:P13010" FT CONFLICT 5 FT /note="G -> V (in Ref. 1; CAA46999)" FT /evidence="ECO:0000305" FT CONFLICT 24 FT /note="F -> I (in Ref. 1; CAA46999)" FT /evidence="ECO:0000305" FT CONFLICT 57 FT /note="V -> A (in Ref. 1; CAA46999)" FT /evidence="ECO:0000305" FT CONFLICT 66..69 FT /note="NALA -> MPLS (in Ref. 1; CAA46999)" FT /evidence="ECO:0000305" FT CONFLICT 120 FT /note="R -> H (in Ref. 2; AAD49720)" FT /evidence="ECO:0000305" FT CONFLICT 139 FT /note="S -> G (in Ref. 3; BAE38207)" FT /evidence="ECO:0000305" FT CONFLICT 139 FT /note="S -> R (in Ref. 1; CAA46999)" FT /evidence="ECO:0000305" FT CONFLICT 144 FT /note="Q -> K (in Ref. 1; CAA46999)" FT /evidence="ECO:0000305" FT CONFLICT 157 FT /note="S -> C (in Ref. 1; CAA46999)" FT /evidence="ECO:0000305" FT CONFLICT 226 FT /note="S -> F (in Ref. 2; AAD49720)" FT /evidence="ECO:0000305" FT CONFLICT 409..410 FT /note="FP -> SL (in Ref. 1; CAA46999)" FT /evidence="ECO:0000305" FT CONFLICT 414 FT /note="D -> G (in Ref. 3; BAC38276)" FT /evidence="ECO:0000305" FT CONFLICT 415 FT /note="A -> T (in Ref. 2; AAD49720)" FT /evidence="ECO:0000305" FT CONFLICT 418 FT /note="C -> R (in Ref. 1; CAA46999)" FT /evidence="ECO:0000305" FT CONFLICT 442 FT /note="K -> M (in Ref. 2; AAD49720)" FT /evidence="ECO:0000305" FT CONFLICT 479 FT /note="T -> A (in Ref. 1; CAA46999)" FT /evidence="ECO:0000305" FT CONFLICT 515..516 FT /note="ML -> IW (in Ref. 1; CAA46999)" FT /evidence="ECO:0000305" FT CONFLICT 524 FT /note="A -> Q (in Ref. 1; CAA46999)" FT /evidence="ECO:0000305" FT CONFLICT 530..531 FT /note="LS -> PL (in Ref. 1; CAA46999)" FT /evidence="ECO:0000305" FT CONFLICT 558 FT /note="N -> H (in Ref. 2; AAD49720)" FT /evidence="ECO:0000305" FT CONFLICT 692 FT /note="G -> A (in Ref. 1; CAA46999)" FT /evidence="ECO:0000305" FT CONFLICT 703 FT /note="T -> K (in Ref. 1; CAA46999)" FT /evidence="ECO:0000305" FT CONFLICT 708 FT /note="P -> H (in Ref. 3; BAE39415)" FT /evidence="ECO:0000305" SQ SEQUENCE 732 AA; 83057 MW; 391F0FAF7EB04288 CRC64; MAWSGNKAAV VLCVDVGVAM GNSFPGEESP IEQAKKVMTM FVQRQVFSES KDEIALVLYG TDGTDNALAG KDQYQNITVC RHLMLPDFDL LEDIGNKIQP SSQQADFLDA LIVCMDLIQR ETIGKKFGKK HIEVFTDLSS PFSQDQLDVI ICNLKKSGIS LQFFLPFPID KNGEPGERGD LDSGLDHLKP SFPQKGLTEQ QKEGIRMVTR VMLSLEGEDG LDEIYSFSES LRQLCVFKKI ERRSMPWPCQ LTIGPNLSIK IVAYKSIVQE KFKKSWVVVD ARTLKKEDIQ KETVYCLNDD DETEVSKEDT IQGYRYGSDI IPFSKVDEEQ MKYKSEGKCF SVLGFCKSSQ VHRRFFMGHQ VLKVFAAKDD EAAAVALSSL VHALDELNMV AIVRYAYDKR SNPQVGVAFP YIKDAYECLV YVQLPFMEDL RQYMFSSLKN NKKCTPTEAQ LSAIDDLIDS MSLVKKNEEE DIVEDLFPTS KIPNPEFQRL YQCLLHRALH LQERLPPIQQ HILNMLDPPT EMKAKCESPL SKVKTLFPLT EVIKKKNQVT AQDVFQDNHE EGPAAKKYKT EKEEDHISIS SLAEGNITKV GSVNPVENFR FLVRQKIASF EEASLQLISH IEQFLDTNET LYFMKSMDCI KAFREEAIQF SEEQRFNSFL EALREKVEIK QLNHFWEIVV QDGVTLITKD EGPGSSITAE EATKFLAPKD KAKEDTTGPE EAGDVDDLLD MI //