XRCC5_MOUSE
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 03-AUG-2022, entry version 192.
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 SX-
RT 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 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 -!- 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}.
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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; 20.
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 EPD; P27641; -.
DR jPOST; P27641; -.
DR MaxQB; P27641; -.
DR PaxDb; P27641; -.
DR PeptideAtlas; P27641; -.
DR PRIDE; P27641; -.
DR ProteomicsDB; 275224; -.
DR Antibodypedia; 3849; 1169 antibodies from 47 providers.
DR DNASU; 22596; -.
DR Ensembl; ENSMUST00000027379; ENSMUSP00000027379; ENSMUSG00000026187.
DR GeneID; 22596; -.
DR KEGG; mmu:22596; -.
DR UCSC; uc007bkl.2; mouse.
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; 598957at2759; -.
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; 17 hits in 111 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 247 other tissues.
DR Genevisible; P27641; MM.
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: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; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0003691; F:double-stranded telomeric DNA binding; ISO:MGI.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
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:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0071475; P:cellular hyperosmotic salinity response; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
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: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:1904430; P:negative regulation of t-circle formation; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; IMP:MGI.
DR GO; GO:0050769; P:positive regulation of neurogenesis; IMP:MGI.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; ISO:MGI.
DR GO; GO:0032212; P:positive regulation of telomere maintenance via telomerase; ISO:MGI.
DR GO; GO:0000725; P:recombinational repair; IC: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 Gene3D; 1.25.40.240; -; 1.
DR Gene3D; 2.40.290.10; -; 1.
DR Gene3D; 3.40.50.410; -; 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 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; SSF100939; SSF100939; 1.
DR SUPFAM; SSF101420; SSF101420; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
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 251..460
FT /note="Ku"
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
