XRCC4_MOUSE
ID XRCC4_MOUSE Reviewed; 326 AA.
AC Q924T3; Q8BKC9; Q8BU02; Q9D6U6;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=DNA repair protein XRCC4 {ECO:0000305};
DE AltName: Full=X-ray repair cross-complementing protein 4 {ECO:0000303|PubMed:11738935};
DE Contains:
DE RecName: Full=Protein XRCC4, C-terminus {ECO:0000305|PubMed:33725486};
DE Short=XRCC4/C {ECO:0000303|PubMed:33725486};
GN Name=Xrcc4 {ECO:0000303|PubMed:11738935, ECO:0000312|MGI:MGI:1333799};
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] (ISOFORM 1).
RX PubMed=11738935; DOI=10.1016/s0921-8777(01)00107-0;
RA Mori M., Itsukaichi H., Nakamura A., Sato K.;
RT "Molecular characterization of ionizing radiation-hypersensitive mutant M10
RT cells.";
RL Mutat. Res. 487:85-92(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Eye, Thymus, and Tongue;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC 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 FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=9875844; DOI=10.1016/s0092-8674(00)81714-6;
RA Gao Y., Sun Y., Frank K.M., Dikkes P., Fujiwara Y., Seidl K.J.,
RA Sekiguchi J.M., Rathbun G.A., Swat W., Wang J., Bronson R.T., Malynn B.A.,
RA Bryans M., Zhu C., Chaudhuri J., Davidson L., Ferrini R., Stamato T.,
RA Orkin S.H., Greenberg M.E., Alt F.W.;
RT "A critical role for DNA end-joining proteins in both lymphogenesis and
RT neurogenesis.";
RL Cell 95:891-902(1998).
RN [5]
RP PHOSPHORYLATION AT SER-53; SER-193; SER-254; SER-295; SER-307; SER-312;
RP THR-315; SER-319 AND SER-320, AND MUTAGENESIS OF SER-53; SER-193; SER-254;
RP SER-295; SER-307; SER-312; THR-315; SER-319 AND SER-320.
RX PubMed=14599745; DOI=10.1016/s1568-7864(03)00143-5;
RA Yu Y., Wang W., Ding Q., Ye R., Chen D., Merkle D., Schriemer D., Meek K.,
RA Lees-Miller S.P.;
RT "DNA-PK phosphorylation sites in XRCC4 are not required for survival after
RT radiation or for V(D)J recombination.";
RL DNA Repair 2:1239-1252(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-244; THR-315; SER-319 AND
RP SER-320, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 FUNCTION.
RX PubMed=33725486; DOI=10.1016/j.molcel.2021.02.025;
RA Maruoka M., Zhang P., Mori H., Imanishi E., Packwood D.M., Harada H.,
RA Kosako H., Suzuki J.;
RT "Caspase cleavage releases a nuclear protein fragment that stimulates
RT phospholipid scrambling at the plasma membrane.";
RL Mol. Cell 81:1397-1410(2021).
CC -!- FUNCTION: [DNA repair protein XRCC4]: DNA non-homologous end joining
CC (NHEJ) core factor, required for double-strand break repair and V(D)J
CC recombination (PubMed:9875844). Acts as a scaffold protein that
CC regulates recruitment of other proteins to DNA double-strand breaks
CC (DSBs). Associates with NHEJ1/XLF to form alternating helical filaments
CC that bridge DNA and act like a bandage, holding together the broken DNA
CC until it is repaired. The XRCC4-NHEJ1/XLF subcomplex binds to the DNA
CC fragments of a DSB in a highly diffusive manner and robustly bridges
CC two independent DNA molecules, holding the broken DNA fragments in
CC close proximity to one other. The mobility of the bridges ensures that
CC the ends remain accessible for further processing by other repair
CC factors. Plays a key role in the NHEJ ligation step of the broken DNA
CC during DSB repair via direct interaction with DNA ligase IV (LIG4): the
CC LIG4-XRCC4 subcomplex reseals the DNA breaks after the gap filling is
CC completed. XRCC4 stabilizes LIG4, regulates its subcellular
CC localization and enhances LIG4's joining activity. Binding of the LIG4-
CC XRCC4 subcomplex to DNA ends is dependent on the assembly of the DNA-
CC dependent protein kinase complex DNA-PK to these DNA ends. Promotes
CC displacement of PNKP from processed strand break termini (By
CC similarity). {ECO:0000250|UniProtKB:Q13426,
CC ECO:0000269|PubMed:9875844}.
CC -!- FUNCTION: [Protein XRCC4, C-terminus]: Acts as an activator of the
CC phospholipid scramblase activity of XKR4 (PubMed:33725486). This form,
CC which is generated upon caspase-3 (CASP3) cleavage, translocates into
CC the cytoplasm and interacts with XKR4, thereby promoting
CC phosphatidylserine scramblase activity of XKR4 and leading to
CC phosphatidylserine exposure on apoptotic cell surface
CC (PubMed:33725486). {ECO:0000269|PubMed:33725486}.
CC -!- SUBUNIT: [DNA repair protein XRCC4]: Homodimer and homotetramer in
CC solution. Interacts with NHEJ1/XLF; the interaction is direct and is
CC mediated via a head-to-head interaction between N-terminal head
CC regions. Interacts with LIG4; the LIG4-XRCC4 subcomplex has a 1:2
CC stoichiometry and XRCC4 is required for LIG4 stability. Component of
CC the core long-range non-homologous end joining (NHEJ) complex (also
CC named DNA-PK complex) composed of PRKDC, LIG4, XRCC4, XRCC6/Ku70,
CC XRCC5/Ku86 and NHEJ1/XLF. Additional component of the NHEJ complex
CC includes PAXX. Following autophosphorylation, PRKDC dissociates from
CC DNA, leading to formation of the short-range NHEJ complex, composed of
CC LIG4, XRCC4, XRCC6/Ku70, XRCC5/Ku86 and NHEJ1/XLF. Interacts with
CC PRKDC; the interaction is direct. Interacts with XRCC6/Ku70; the
CC interaction is direct. Interacts with APTX and APLF. Forms a
CC heterotetramer with IFFO1; the interaction involves LIG4-free XRCC4 and
CC leads to the relocalization of IFFO1 to the sites of DNA damage.
CC Interacts with PNKP; mainly interacts with PNKP when phosphorylated at
CC Thr-231, but is also able to interact at much lower level with PNKP
CC when not unphosphorylated. Interacts with POLL (DNA polymerase lambda).
CC {ECO:0000250|UniProtKB:Q13426}.
CC -!- SUBUNIT: [Protein XRCC4, C-terminus]: Interacts with XKR4; interacts
CC with the processed form of XKR4, which is cleaved by caspase.
CC {ECO:0000250|UniProtKB:Q13426}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13426}.
CC Chromosome {ECO:0000250|UniProtKB:Q13426}. Note=Localizes to site of
CC double-strand breaks. {ECO:0000250|UniProtKB:Q13426}.
CC -!- SUBCELLULAR LOCATION: [Protein XRCC4, C-terminus]: Cytoplasm
CC {ECO:0000250|UniProtKB:Q13426}. Note=Translocates from the nucleus to
CC the cytoplasm following cleavage by caspase-3 (CASP3).
CC {ECO:0000250|UniProtKB:Q13426}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q924T3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q924T3-2; Sequence=VSP_009475;
CC -!- PTM: Phosphorylated by PRKDC at the C-terminus in response to DNA
CC damage; Ser-254 and Ser-312 constitute the main phosphorylation sites
CC (PubMed:14599745). Phosphorylation by PRKDC at the C-terminus of XRCC4
CC and NHEJ1/XLF are highly redundant and regulate ability of the XRCC4-
CC NHEJ1/XLF subcomplex to bridge DNA (By similarity). Phosphorylation by
CC PRKDC does not prevent interaction with NHEJ1/XLF but disrupts ability
CC to bridge DNA and promotes detachment from DNA (By similarity).
CC Phosphorylation at Ser-319 and Ser-320 by PRKDC promotes recognition by
CC the SCF(FBXW7) complex and subsequent ubiquitination via 'Lys-63'-
CC linked ubiquitin (By similarity). Phosphorylation at Thr-231 by CK2
CC promotes interaction with PNKP; regulating PNKP activity and
CC localization to DNA damage sites (By similarity). Phosphorylation by
CC CK2 promotes interaction with APTX (By similarity).
CC {ECO:0000250|UniProtKB:Q13426, ECO:0000269|PubMed:14599745}.
CC -!- PTM: Ubiquitinated at Lys-290 by the SCF(FBXW7) complex via 'Lys-63'-
CC linked ubiquitination, thereby promoting double-strand break repair:
CC the SCF(FBXW7) complex specifically recognizes XRCC4 when
CC phosphorylated at Ser-319 and Ser-320 by PRKDC, and 'Lys-63'-linked
CC ubiquitination facilitates DNA non-homologous end joining (NHEJ) by
CC enhancing association with XRCC5/Ku80 and XRCC6/Ku70.
CC Monoubiquitinated. {ECO:0000250|UniProtKB:Q13426}.
CC -!- PTM: [DNA repair protein XRCC4]: Undergoes proteolytic processing by
CC caspase-3 (CASP3). This generates the protein XRCC4, C-terminus
CC (XRCC4/C), which translocates to the cytoplasm and activates
CC phospholipid scramblase activity of XKR4, thereby promoting
CC phosphatidylserine exposure on apoptotic cell surface.
CC {ECO:0000250|UniProtKB:Q13426}.
CC -!- DISRUPTION PHENOTYPE: Mice show growth defects, premature senescence,
CC IR sensitivity, and inability to support V(D)J recombination
CC (PubMed:9875844). XRCC4 deficiency causes late embryonic lethality
CC accompanied by defective lymphogenesis and defective neurogenesis
CC manifested by extensive apoptotic death of newly generated postmitotic
CC neuronal cells (PubMed:9875844). {ECO:0000269|PubMed:9875844}.
CC -!- SIMILARITY: Belongs to the XRCC4-XLF family. XRCC4 subfamily.
CC {ECO:0000305}.
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DR EMBL; AB055154; BAB62316.1; -; mRNA.
DR EMBL; AK009951; BAB26604.1; -; mRNA.
DR EMBL; AK053612; BAC35447.1; -; mRNA.
DR EMBL; AK088281; BAC40256.1; -; mRNA.
DR EMBL; BC025538; AAH25538.1; -; mRNA.
DR CCDS; CCDS26673.1; -. [Q924T3-1]
DR RefSeq; NP_082288.1; NM_028012.4.
DR RefSeq; XP_006517104.1; XM_006517041.3.
DR RefSeq; XP_006517105.1; XM_006517042.2.
DR RefSeq; XP_006517106.1; XM_006517043.3.
DR AlphaFoldDB; Q924T3; -.
DR SMR; Q924T3; -.
DR CORUM; Q924T3; -.
DR ELM; Q924T3; -.
DR STRING; 10090.ENSMUSP00000022115; -.
DR iPTMnet; Q924T3; -.
DR PhosphoSitePlus; Q924T3; -.
DR EPD; Q924T3; -.
DR jPOST; Q924T3; -.
DR MaxQB; Q924T3; -.
DR PaxDb; Q924T3; -.
DR PeptideAtlas; Q924T3; -.
DR PRIDE; Q924T3; -.
DR ProteomicsDB; 297570; -. [Q924T3-1]
DR ProteomicsDB; 297571; -. [Q924T3-2]
DR DNASU; 108138; -.
DR GeneID; 108138; -.
DR KEGG; mmu:108138; -.
DR UCSC; uc007rjn.2; mouse. [Q924T3-1]
DR CTD; 7518; -.
DR MGI; MGI:1333799; Xrcc4.
DR eggNOG; ENOG502QWJA; Eukaryota.
DR InParanoid; Q924T3; -.
DR OrthoDB; 940052at2759; -.
DR PhylomeDB; Q924T3; -.
DR TreeFam; TF101204; -.
DR Reactome; R-MMU-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-MMU-5693571; Nonhomologous End-Joining (NHEJ).
DR BioGRID-ORCS; 108138; 7 hits in 113 CRISPR screens.
DR ChiTaRS; Xrcc4; mouse.
DR PRO; PR:Q924T3; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q924T3; protein.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0032807; C:DNA ligase IV complex; ISO:MGI.
DR GO; GO:0005958; C:DNA-dependent protein kinase-DNA ligase 4 complex; IDA:MGI.
DR GO; GO:0070522; C:ERCC4-ERCC1 complex; IDA:BHF-UCL.
DR GO; GO:0070419; C:nonhomologous end joining complex; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0070975; F:FHA domain binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0007417; P:central nervous system development; IMP:MGI.
DR GO; GO:1904155; P:DN2 thymocyte differentiation; IMP:MGI.
DR GO; GO:0006266; P:DNA ligation; IDA:MGI.
DR GO; GO:0051103; P:DNA ligation involved in DNA repair; 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; IMP:BHF-UCL.
DR GO; GO:0048144; P:fibroblast proliferation; IMP:MGI.
DR GO; GO:0033152; P:immunoglobulin V(D)J recombination; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0045190; P:isotype switching; IMP:MGI.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:MGI.
DR GO; GO:1905765; P:negative regulation of protection from non-homologous end joining at telomere; IMP:BHF-UCL.
DR GO; GO:0022008; P:neurogenesis; IMP:MGI.
DR GO; GO:0051402; P:neuron apoptotic process; IMP:MGI.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IMP:MGI.
DR GO; GO:0051351; P:positive regulation of ligase activity; ISO:MGI.
DR GO; GO:0050769; P:positive regulation of neurogenesis; IMP:MGI.
DR GO; GO:1905782; P:positive regulation of phosphatidylserine exposure on apoptotic cell surface; ISS:UniProtKB.
DR GO; GO:0002328; P:pro-B cell differentiation; IMP:MGI.
DR GO; GO:1990166; P:protein localization to site of double-strand break; ISS:UniProtKB.
DR GO; GO:0010332; P:response to gamma radiation; IMP:MGI.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:MGI.
DR GO; GO:0010165; P:response to X-ray; IMP:MGI.
DR GO; GO:0061819; P:telomeric DNA-containing double minutes formation; IMP:BHF-UCL.
DR GO; GO:0033151; P:V(D)J recombination; IMP:MGI.
DR Gene3D; 1.20.5.370; -; 1.
DR Gene3D; 2.170.210.10; -; 1.
DR InterPro; IPR010585; DNA_repair_prot_XRCC4.
DR InterPro; IPR014751; XRCC4-like_C.
DR InterPro; IPR038051; XRCC4-like_N_sf.
DR InterPro; IPR009089; XRCC4_N_sf.
DR PANTHER; PTHR28559; PTHR28559; 1.
DR Pfam; PF06632; XRCC4; 1.
DR SUPFAM; SSF50809; SSF50809; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromosome; Coiled coil; Cytoplasm; DNA damage;
KW DNA recombination; DNA repair; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..326
FT /note="DNA repair protein XRCC4"
FT /id="PRO_0000066048"
FT CHAIN 266..326
FT /note="Protein XRCC4, C-terminus"
FT /evidence="ECO:0000250|UniProtKB:Q13426"
FT /id="PRO_0000453297"
FT REGION 1..212
FT /note="Interaction with IFFO1"
FT /evidence="ECO:0000250|UniProtKB:Q13426"
FT REGION 180..211
FT /note="Interaction with LIG4"
FT /evidence="ECO:0000250|UniProtKB:Q13426"
FT REGION 203..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 131..165
FT /evidence="ECO:0000255"
FT COILED 185..209
FT /evidence="ECO:0000255"
FT MOTIF 264..269
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250|UniProtKB:Q13426"
FT COMPBIAS 205..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 53
FT /note="Phosphoserine; by PRKDC"
FT /evidence="ECO:0000305|PubMed:14599745"
FT MOD_RES 193
FT /note="Phosphoserine; by PRKDC"
FT /evidence="ECO:0000305|PubMed:14599745"
FT MOD_RES 227
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q13426"
FT MOD_RES 230
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13426"
FT MOD_RES 231
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q13426"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13426"
FT MOD_RES 244
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13426"
FT MOD_RES 254
FT /note="Phosphoserine; by PRKDC"
FT /evidence="ECO:0000305|PubMed:14599745"
FT MOD_RES 295
FT /note="Phosphoserine; by PRKDC"
FT /evidence="ECO:0000305|PubMed:14599745"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13426"
FT MOD_RES 307
FT /note="Phosphoserine; by PRKDC"
FT /evidence="ECO:0000305|PubMed:14599745"
FT MOD_RES 312
FT /note="Phosphoserine; by PRKDC"
FT /evidence="ECO:0000305|PubMed:14599745"
FT MOD_RES 315
FT /note="Phosphothreonine; by PRKDC"
FT /evidence="ECO:0000305|PubMed:14599745,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 319
FT /note="Phosphoserine; by PRKDC"
FT /evidence="ECO:0000305|PubMed:14599745,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 320
FT /note="Phosphoserine; by PRKDC"
FT /evidence="ECO:0000305|PubMed:14599745,
FT ECO:0007744|PubMed:21183079"
FT CROSSLNK 290
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q13426"
FT VAR_SEQ 293..326
FT /note="LASSLPQTLKEESTSAENMSLETLRNSSPEDLFD -> KKKYPSIMSTKVQR
FT SLGEGGHG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_009475"
FT MUTAGEN 53
FT /note="S->A: In 9A mutant; abolished phosphorylation by
FT PRKDC; does not affect ability to repair double-strand
FT breaks (DSBs), possibly because of redundancy with
FT NHEJ1/XLF phosphorylation sites; when associated with A-
FT 193, A-254, A-295, A-307, A-312, A-315, A-319 and A-320."
FT /evidence="ECO:0000269|PubMed:14599745"
FT MUTAGEN 193
FT /note="S->A: In 9A mutant; abolished phosphorylation by
FT PRKDC; does not affect ability to repair double-strand
FT breaks (DSBs), possibly because of redundancy with
FT NHEJ1/XLF phosphorylation sites; when associated with A-53,
FT A-254, A-295, A-307, A-312, A-315, A-319 and A-320."
FT /evidence="ECO:0000269|PubMed:14599745"
FT MUTAGEN 254
FT /note="S->A: In 9A mutant; abolished phosphorylation by
FT PRKDC; does not affect ability to repair double-strand
FT breaks (DSBs), possibly because of redundancy with
FT NHEJ1/XLF phosphorylation sites; when associated with A-53,
FT A-193, A-295, A-307, A-312, A-315, A-319 and A-320."
FT /evidence="ECO:0000269|PubMed:14599745"
FT MUTAGEN 295
FT /note="S->A: In 9A mutant; abolished phosphorylation by
FT PRKDC; does not affect ability to repair double-strand
FT breaks (DSBs), possibly because of redundancy with
FT NHEJ1/XLF phosphorylation sites; when associated with A-53,
FT A-193, A-254, A-307, A-312, A-315, A-319 and A-320."
FT /evidence="ECO:0000269|PubMed:14599745"
FT MUTAGEN 307
FT /note="S->A: In 9A mutant; abolished phosphorylation by
FT PRKDC; does not affect ability to repair double-strand
FT breaks (DSBs), possibly because of redundancy with
FT NHEJ1/XLF phosphorylation sites; when associated with A-53,
FT A-193, A-254, A-295, A-312, A-315, A-319 and A-320."
FT /evidence="ECO:0000269|PubMed:14599745"
FT MUTAGEN 312
FT /note="S->A: In 9A mutant; abolished phosphorylation by
FT PRKDC; does not affect ability to repair double-strand
FT breaks (DSBs), possibly because of redundancy with
FT NHEJ1/XLF phosphorylation sites; when associated with A-53,
FT A-193, A-254, A-295, A-307, A-315, A-319 and A-320."
FT /evidence="ECO:0000269|PubMed:14599745"
FT MUTAGEN 315
FT /note="T->A: In 9A mutant; abolished phosphorylation by
FT PRKDC; does not affect ability to repair double-strand
FT breaks (DSBs), possibly because of redundancy with
FT NHEJ1/XLF phosphorylation sites; when associated with A-53,
FT A-193, A-254, A-295, A-307, A-312, A-319 and A-320."
FT /evidence="ECO:0000269|PubMed:14599745"
FT MUTAGEN 319
FT /note="S->A: In 9A mutant; abolished phosphorylation by
FT PRKDC; does not affect ability to repair double-strand
FT breaks (DSBs), possibly because of redundancy with
FT NHEJ1/XLF phosphorylation sites; when associated with A-53,
FT A-193, A-254, A-295, A-307, A-312, A-315 and A-320."
FT /evidence="ECO:0000269|PubMed:14599745"
FT MUTAGEN 320
FT /note="S->A: In 9A mutant; abolished phosphorylation by
FT PRKDC; does not affect ability to repair double-strand
FT breaks (DSBs), possibly because of redundancy with
FT NHEJ1/XLF phosphorylation sites; when associated with A-53,
FT A-193, A-254, A-295, A-307, A-312, A-315 and A-319."
FT /evidence="ECO:0000269|PubMed:14599745"
FT CONFLICT 27
FT /note="A -> T (in Ref. 3; BAB26604/BAC35447)"
FT /evidence="ECO:0000305"
FT CONFLICT 54
FT /note="Q -> P (in Ref. 3; BAC40256)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="Q -> R (in Ref. 3; BAB26604/BAC35447)"
FT /evidence="ECO:0000305"
FT CONFLICT 125
FT /note="E -> D (in Ref. 3; BAB26604/BAC35447)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 326 AA; 37061 MW; 58BD3422F7D2CBDB CRC64;
MERKVSRIYL ASEPNVPYFL QVSWERAIGS GFVITLTDGH SAWTATVSEL EISQEADDMA
MEKGKYIDEL RKALVPGSGA AGTYKFLFSK ESQHFSLEKE LKDVSFRLGS FNLDKVSNSA
EVIRELICYC LDTITEKQAK NEHLQKENER LLRDWNDVQG RFEKCVSAKE ALEADLYQRF
ILVLNEKKTK IRSLHKLLNE VQQLEESTKP ERENPCSDKT PEEHGLYDGS TDEESGAPVQ
AAETLHKDDS IFSSPDVTDI APSRKRRHRM QKNLGTEPKM APQELPLQEK ERLASSLPQT
LKEESTSAEN MSLETLRNSS PEDLFD
