TIM_MOUSE
ID TIM_MOUSE Reviewed; 1197 AA.
AC Q9R1X4; Q63ZX9; Q6P204; Q6PDL4; Q7TPV8; Q8R0Q2; Q9R268; Q9Z0E7;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Protein timeless homolog;
DE Short=mTim;
GN Name=Timeless {ECO:0000312|MGI:MGI:1321393};
GN Synonyms=Tim1 {ECO:0000312|EMBL:BAA36500.1},
GN Timeless1 {ECO:0000303|PubMed:9891984};
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] {ECO:0000312|EMBL:BAA36500.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:BAA36500.1}; TISSUE=Brain;
RX PubMed=9891984; DOI=10.1016/s0014-5793(98)01597-x;
RA Koike N., Hida A., Numano R., Hirose M., Sakaki Y., Tei H.;
RT "Identification of the mammalian homologues of the Drosophila timeless
RT gene, Timeless1.";
RL FEBS Lett. 441:427-431(1998).
RN [2] {ECO:0000312|EMBL:AAC80010.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 6), TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, FUNCTION, AND INTERACTION WITH PER1 AND PER2.
RC TISSUE=Embryo;
RX PubMed=9856465; DOI=10.1016/s0896-6273(00)80627-3;
RA Sangoram A.M., Saez L., Antoch M.P., Gekakis N., Staknis D., Whiteley A.,
RA Fruechte E.M., Vitaterna M.H., Shimomura K., King D.P., Young M.W.,
RA Weitz C.J., Takahashi J.S.;
RT "Mammalian circadian autoregulatory loop: a timeless ortholog and mPer1
RT interact and negatively regulate CLOCK-ARTNL/BMAL1-induced transcription.";
RL Neuron 21:1101-1113(1998).
RN [3] {ECO:0000312|EMBL:AAC79687.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=9856466; DOI=10.1016/s0896-6273(00)80628-5;
RA Zylka M.J., Shearman L.P., Levine J.D., Jin X., Weaver D.R., Reppert S.M.;
RT "Molecular analysis of mammalian timeless.";
RL Neuron 21:1115-1122(1998).
RN [4] {ECO:0000312|EMBL:BAA76390.2}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, INDUCTION, AND INTERACTION WITH PER1.
RC STRAIN=BALB/cJ; TISSUE=Brain;
RX PubMed=10231394; DOI=10.1046/j.1365-2443.1999.00238.x;
RA Takumi T., Nagamine Y., Miyake S., Matsubara C., Taguchi K., Takekida S.,
RA Sakakida Y., Nishikawa K., Kishimoto T., Niwa S., Okumura K., Okamura H.;
RT "A mammalian ortholog of Drosophila timeless, highly expressed in SCN and
RT retina, forms a complex with mPER1.";
RL Genes Cells 4:67-75(1999).
RN [5] {ECO:0000312|EMBL:AAD24467.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Heart {ECO:0000312|EMBL:AAD24467.1}, and Kidney;
RX PubMed=10963667; DOI=10.1073/pnas.97.18.10038;
RA Li Z., Stuart R.O., Qiao J., Pavlova A., Bush K.T., Pohl M., Sakurai H.,
RA Nigam S.K.;
RT "A role for Timeless in epithelial morphogenesis during kidney
RT development.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:10038-10043(2000).
RN [6] {ECO:0000312|EMBL:AAH82770.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 5).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH52884.1, ECO:0000312|EMBL:AAH58641.1},
RC and FVB/N {ECO:0000312|EMBL:AAH26526.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH58641.1},
RC Egg {ECO:0000312|EMBL:AAH52884.1},
RC Olfactory epithelium {ECO:0000312|EMBL:AAH82770.1}, and
RC Salivary gland {ECO:0000312|EMBL:AAH26526.1};
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 [7]
RP INTERACTION WITH CRY1 AND CRY2, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RX PubMed=10428031; DOI=10.1016/s0092-8674(00)81014-4;
RA Kume K., Zylka M.J., Sriram S., Shearman L.P., Weaver D.R., Jin X.,
RA Maywood E.S., Hastings M.H., Reppert S.M.;
RT "mCRY1 and mCRY2 are essential components of the negative limb of the
RT circadian clock feedback loop.";
RL Cell 98:193-205(1999).
RN [8]
RP INTERACTION WITH TIPIN, DEVELOPMENTAL STAGE, SUBUNIT, AND FUNCTION.
RX PubMed=12875843; DOI=10.1016/s0022-2836(03)00633-8;
RA Gotter A.L.;
RT "Tipin, a novel timeless-interacting protein, is developmentally co-
RT expressed with timeless and disrupts its self-association.";
RL J. Mol. Biol. 331:167-176(2003).
RN [9]
RP INTERACTION WITH PER1; PER2 AND PER3, AND INDUCTION.
RX PubMed=14564007; DOI=10.1126/science.1086593;
RA Barnes J.W., Tischkau S.A., Barnes J.A., Mitchell J.W., Burgoon P.W.,
RA Hickok J.R., Gillette M.U.;
RT "Requirement of mammalian Timeless for circadian rhythmicity.";
RL Science 302:439-442(2003).
RN [10]
RP ERRATUM OF PUBMED:14564007.
RA Barnes J.W., Tischkau S.A., Barnes J.A., Mitchell J.W., Burgoon P.W.,
RA Hickok J.R., Gillette M.U.;
RL Science 302:1153-1153(2003).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [12]
RP FUNCTION, SUBUNIT, INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH CRY1 AND CHEK1.
RX PubMed=23418588; DOI=10.1371/journal.pone.0056623;
RA Engelen E., Janssens R.C., Yagita K., Smits V.A., van der Horst G.T.,
RA Tamanini F.;
RT "Mammalian TIMELESS is involved in period determination and DNA damage-
RT dependent phase advancing of the circadian clock.";
RL PLoS ONE 8:E56623-E56623(2013).
RN [13]
RP INTERACTION WITH CRY1, AND SUBCELLULAR LOCATION.
RX PubMed=24489120; DOI=10.1093/nar/gku094;
RA Kang T.H., Leem S.H.;
RT "Modulation of ATR-mediated DNA damage checkpoint response by cryptochrome
RT 1.";
RL Nucleic Acids Res. 42:4427-4434(2014).
CC -!- FUNCTION: Plays an important role in the control of DNA replication,
CC maintenance of replication fork stability, maintenance of genome
CC stability throughout normal DNA replication, DNA repair and in the
CC regulation of the circadian clock (PubMed:9856465, PubMed:23418588,
CC PubMed:10428031, PubMed:12875843). Required to stabilize replication
CC forks during DNA replication by forming a complex with TIPIN: this
CC complex regulates DNA replication processes under both normal and
CC stress conditions, stabilizes replication forks and influences both
CC CHEK1 phosphorylation and the intra-S phase checkpoint in response to
CC genotoxic stress (PubMed:12875843). TIMELESS promotes TIPIN nuclear
CC localization (PubMed:12875843). Involved in cell survival after DNA
CC damage or replication stress by promoting DNA repair (PubMed:12875843).
CC In response to double-strand breaks (DSBs), accumulates at DNA damage
CC sites and promotes homologous recombination repair via its interaction
CC with PARP1 (By similarity). May be specifically required for the ATR-
CC CHEK1 pathway in the replication checkpoint induced by hydroxyurea or
CC ultraviolet light (PubMed:23418588). Involved in the determination of
CC period length and in the DNA damage-dependent phase advancing of the
CC circadian clock (PubMed:23418588, PubMed:10428031). Negatively
CC regulates CLOCK|NPAS2-ARTNL/BMAL1|ARTNL2/BMAL2-induced transactivation
CC of PER1 possibly via translocation of PER1 into the nucleus
CC (PubMed:9856465). May also play an important role in epithelial cell
CC morphogenesis and formation of branching tubules (PubMed:10963667).
CC {ECO:0000250|UniProtKB:Q9UNS1, ECO:0000269|PubMed:10428031,
CC ECO:0000269|PubMed:10963667, ECO:0000269|PubMed:12875843,
CC ECO:0000269|PubMed:23418588, ECO:0000269|PubMed:9856465}.
CC -!- SUBUNIT: Homodimer or homomultimer (PubMed:12875843, PubMed:23418588).
CC Component of the circadian core oscillator, which includes the CRY
CC proteins, CLOCK or NPAS2, ARTNL/BMAL1 or ARTNL2/BMAL2, CSKN1D and/or
CC CSNK1E, TIMELESS, and the PER proteins (PubMed:9856465). Interacts
CC directly with PER2; the interaction with PER2 is via its second PAS
CC domain (PubMed:14564007). Interacts directly with PER1 and PER3
CC (PubMed:9856465, PubMed:10231394, PubMed:14564007). Interacts with CRY1
CC (PubMed:10428031, PubMed:23418588, PubMed:24489120). Interacts with
CC CRY2 (PubMed:10428031). Interacts with CHEK1, ATR and ATRIP (By
CC similarity). Interacts with CLSPN (By similarity). Interacts with TIPIN
CC (PubMed:12875843). Interacts with DDX11; this interaction increases
CC recruitment of both proteins onto chromatin in response to replication
CC stress induction by hydroxyurea (By similarity). Interacts with PARP1;
CC interaction is direct and independent of poly-ADP-ribose (By
CC similarity). {ECO:0000250|UniProtKB:Q9UNS1,
CC ECO:0000269|PubMed:10231394, ECO:0000269|PubMed:10428031,
CC ECO:0000269|PubMed:12875843, ECO:0000269|PubMed:14564007,
CC ECO:0000269|PubMed:23418588, ECO:0000269|PubMed:24489120,
CC ECO:0000269|PubMed:9856465}.
CC -!- INTERACTION:
CC Q9R1X4; O35973: Per1; NbExp=3; IntAct=EBI-1793117, EBI-1266764;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10231394,
CC ECO:0000269|PubMed:10428031, ECO:0000269|PubMed:23418588,
CC ECO:0000269|PubMed:24489120}. Chromosome
CC {ECO:0000250|UniProtKB:Q9UNS1}. Note=In response to double-strand
CC breaks (DSBs), accumulates at DNA damage sites via its interaction with
CC PARP1. {ECO:0000250|UniProtKB:Q9UNS1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1 {ECO:0000269|PubMed:10231394, ECO:0000269|PubMed:9856465,
CC ECO:0000269|PubMed:9856466, ECO:0000269|PubMed:9891984};
CC IsoId=Q9R1X4-1; Sequence=Displayed;
CC Name=2 {ECO:0000305};
CC IsoId=Q9R1X4-2; Sequence=VSP_051695;
CC Name=3 {ECO:0000305};
CC IsoId=Q9R1X4-3; Sequence=VSP_051695, VSP_051696;
CC Name=4 {ECO:0000269|PubMed:10963667}; Synonyms=TIM-s;
CC IsoId=Q9R1X4-4; Sequence=VSP_051694, VSP_051695;
CC Name=5 {ECO:0000305};
CC IsoId=Q9R1X4-5; Sequence=VSP_051694;
CC Name=6 {ECO:0000269|PubMed:9856465};
CC IsoId=Q9R1X4-6; Sequence=VSP_051697;
CC -!- TISSUE SPECIFICITY: Predominantly and robustly expressed in
CC proliferative organs (spleen, thymus, intestine and testis) compared to
CC those more differentiated such as kidney and liver (at protein level).
CC Expressed in all tissues examined including brain, heart, lung, liver,
CC skeletal muscle, kidney, placenta, pancreas, spleen, thymus and testis.
CC Strongly expressed in the suprachiasmatic nucleus (SCN) and pars
CC tuberalis, moderately in the cingulate cortex, pyrimidal cell layer of
CC the piriform cortex, periventricular part of the caudate putamen, and
CC granular layer of the cerebellum, and weakly in the cerebral cortex,
CC gyrus dentatus, hippocampus and thalamic nuclei. In embryonic kidney,
CC expression is highest in regions of active ureteric bud cell branching.
CC {ECO:0000269|PubMed:10231394, ECO:0000269|PubMed:10428031,
CC ECO:0000269|PubMed:10963667, ECO:0000269|PubMed:23418588,
CC ECO:0000269|PubMed:9856465, ECO:0000269|PubMed:9856466,
CC ECO:0000269|PubMed:9891984}.
CC -!- DEVELOPMENTAL STAGE: Expression is highest in whole embryos at 11 dpc
CC and gradually decreases as embryonic development progresses. At 7.5
CC dpc, expressed in germ cell layers. At 14.5 dpc, expressed at highest
CC levels in thymus, liver, gastrointestinal tract, lung and the rapidly
CC proliferating ventricular zone of the brain.
CC {ECO:0000269|PubMed:10963667, ECO:0000269|PubMed:12875843,
CC ECO:0000269|PubMed:9856465, ECO:0000269|PubMed:9891984}.
CC -!- INDUCTION: In retina, expression exhibits a circadian rhythm in the
CC presence of light/dark cycles. In the suprachiasmatic nucleus (SCN),
CC isoform 1 exhibited 24 hours oscillation, isoform 4 is constitutively
CC expressed. Shows a circadian expression pattern in the intestine with
CC peaks at ZT4 and ZT8. {ECO:0000269|PubMed:10231394,
CC ECO:0000269|PubMed:10428031, ECO:0000269|PubMed:14564007,
CC ECO:0000269|PubMed:23418588}.
CC -!- SIMILARITY: Belongs to the timeless family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH52884.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH64788.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AB015598; BAA36500.1; -; mRNA.
DR EMBL; AF098161; AAC80010.1; -; mRNA.
DR EMBL; AF071506; AAC79687.1; -; mRNA.
DR EMBL; AB019001; BAA76390.2; -; mRNA.
DR EMBL; AF126480; AAD24467.1; -; mRNA.
DR EMBL; BC026526; AAH26526.1; -; mRNA.
DR EMBL; BC052884; AAH52884.1; ALT_SEQ; mRNA.
DR EMBL; BC058641; AAH58641.1; -; mRNA.
DR EMBL; BC064788; AAH64788.1; ALT_SEQ; mRNA.
DR EMBL; BC082770; AAH82770.1; -; mRNA.
DR CCDS; CCDS24266.1; -. [Q9R1X4-1]
DR CCDS; CCDS48724.1; -. [Q9R1X4-6]
DR CCDS; CCDS48725.1; -. [Q9R1X4-2]
DR PIR; T13956; T13956.
DR RefSeq; NP_001129554.1; NM_001136082.2. [Q9R1X4-2]
DR RefSeq; NP_001157552.1; NM_001164080.1. [Q9R1X4-6]
DR RefSeq; NP_001157553.1; NM_001164081.1. [Q9R1X4-1]
DR RefSeq; NP_035719.1; NM_011589.2. [Q9R1X4-1]
DR RefSeq; XP_006513646.1; XM_006513583.3. [Q9R1X4-1]
DR AlphaFoldDB; Q9R1X4; -.
DR SMR; Q9R1X4; -.
DR BioGRID; 204198; 42.
DR IntAct; Q9R1X4; 26.
DR STRING; 10090.ENSMUSP00000058021; -.
DR iPTMnet; Q9R1X4; -.
DR PhosphoSitePlus; Q9R1X4; -.
DR EPD; Q9R1X4; -.
DR MaxQB; Q9R1X4; -.
DR PaxDb; Q9R1X4; -.
DR PeptideAtlas; Q9R1X4; -.
DR PRIDE; Q9R1X4; -.
DR ProteomicsDB; 262789; -. [Q9R1X4-1]
DR ProteomicsDB; 262790; -. [Q9R1X4-2]
DR ProteomicsDB; 262791; -. [Q9R1X4-3]
DR ProteomicsDB; 262792; -. [Q9R1X4-4]
DR ProteomicsDB; 262793; -. [Q9R1X4-5]
DR ProteomicsDB; 262794; -. [Q9R1X4-6]
DR Antibodypedia; 15850; 213 antibodies from 31 providers.
DR DNASU; 21853; -.
DR Ensembl; ENSMUST00000055539; ENSMUSP00000058021; ENSMUSG00000039994. [Q9R1X4-1]
DR Ensembl; ENSMUST00000105242; ENSMUSP00000100876; ENSMUSG00000039994. [Q9R1X4-2]
DR Ensembl; ENSMUST00000105244; ENSMUSP00000100878; ENSMUSG00000039994. [Q9R1X4-6]
DR Ensembl; ENSMUST00000105245; ENSMUSP00000100879; ENSMUSG00000039994. [Q9R1X4-1]
DR GeneID; 21853; -.
DR KEGG; mmu:21853; -.
DR UCSC; uc007hlv.2; mouse. [Q9R1X4-1]
DR UCSC; uc007hlw.2; mouse. [Q9R1X4-2]
DR CTD; 8914; -.
DR MGI; MGI:1321393; Timeless.
DR VEuPathDB; HostDB:ENSMUSG00000039994; -.
DR eggNOG; KOG1974; Eukaryota.
DR GeneTree; ENSGT00390000015124; -.
DR InParanoid; Q9R1X4; -.
DR OMA; QGPEECG; -.
DR OrthoDB; 839367at2759; -.
DR PhylomeDB; Q9R1X4; -.
DR TreeFam; TF312802; -.
DR Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR BioGRID-ORCS; 21853; 26 hits in 76 CRISPR screens.
DR ChiTaRS; Timeless; mouse.
DR PRO; PR:Q9R1X4; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9R1X4; protein.
DR Bgee; ENSMUSG00000039994; Expressed in lumbar dorsal root ganglion and 195 other tissues.
DR ExpressionAtlas; Q9R1X4; baseline and differential.
DR Genevisible; Q9R1X4; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031298; C:replication fork protection complex; IBA:GO_Central.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; ISO:MGI.
DR GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IMP:MGI.
DR GO; GO:0044770; P:cell cycle phase transition; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:1904976; P:cellular response to bleomycin; ISS:UniProtKB.
DR GO; GO:0072719; P:cellular response to cisplatin; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
DR GO; GO:0072711; P:cellular response to hydroxyurea; ISS:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0000076; P:DNA replication checkpoint signaling; IBA:GO_Central.
DR GO; GO:0001822; P:kidney development; ISO:MGI.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IEP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0042753; P:positive regulation of circadian rhythm; ISO:MGI.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; ISS:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
DR GO; GO:0043111; P:replication fork arrest; IBA:GO_Central.
DR GO; GO:0048478; P:replication fork protection; IBA:GO_Central.
DR InterPro; IPR044998; Timeless.
DR InterPro; IPR007725; TIMELESS_C.
DR InterPro; IPR006906; Timeless_N.
DR PANTHER; PTHR22940; PTHR22940; 1.
DR Pfam; PF04821; TIMELESS; 1.
DR Pfam; PF05029; TIMELESS_C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Biological rhythms; Cell cycle; Cell division;
KW Chromosome; Developmental protein; DNA damage; DNA repair; Mitosis;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1197
FT /note="Protein timeless homolog"
FT /id="PRO_0000072539"
FT REGION 1..309
FT /note="Required for homodimerization and for interaction
FT with CRY1 and CHEK1"
FT /evidence="ECO:0000269|PubMed:23418588"
FT REGION 647..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..1002
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 997..1095
FT /note="Interaction with PARP1"
FT /evidence="ECO:0000250|UniProtKB:Q9UNS1"
FT REGION 1079..1197
FT /note="Required for nuclear localization"
FT /evidence="ECO:0000269|PubMed:23418588"
FT REGION 1088..1197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..674
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..986
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1002
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNS1"
FT MOD_RES 1071
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNS1"
FT MOD_RES 1084
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNS1"
FT MOD_RES 1086
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNS1"
FT MOD_RES 1165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UNS1"
FT VAR_SEQ 1..721
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:10963667,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_051694"
FT VAR_SEQ 952
FT /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:10963667,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_051695"
FT VAR_SEQ 967..1104
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_051696"
FT VAR_SEQ 1177
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:9856465"
FT /id="VSP_051697"
FT CONFLICT 179
FT /note="I -> V (in Ref. 6; AAH64788)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="H -> R (in Ref. 6; AAH64788)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="R -> G (in Ref. 6; AAH64788)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="A -> V (in Ref. 4; BAA76390)"
FT /evidence="ECO:0000305"
FT CONFLICT 744
FT /note="L -> H (in Ref. 5; AAD24467)"
FT /evidence="ECO:0000305"
FT CONFLICT 846
FT /note="H -> Y (in Ref. 5; AAD24467)"
FT /evidence="ECO:0000305"
FT CONFLICT 956
FT /note="K -> R (in Ref. 5; AAD24467)"
FT /evidence="ECO:0000305"
FT CONFLICT 1068
FT /note="P -> L (in Ref. 5; AAD24467)"
FT /evidence="ECO:0000305"
FT CONFLICT 1190
FT /note="F -> L (in Ref. 4; BAA76390)"
FT /evidence="ECO:0000305"
FT CONFLICT 1196
FT /note="D -> G (in Ref. 4; BAA76390)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1197 AA; 137503 MW; DB24B7F0F3D05787 CRC64;
MDLYMMNCEL LATCSALGYL EGGTYHKEPD CLESVKDLIR YLRHEDETRD VRQQLGAAQI
LQSDLLPILT QHRQDKPLFD AVIRLMVNLT QPALLCFGSV PKDSSVRHHF LQVLTYLQAY
KEAFASEKAF GVLSETLYEL LQLGWEDRQE EDNLLIERIL LLVRNILHVP ANLEQEKSID
DDASIHDRLL WAIHLSGMDD LLLFLSSSSA EQQWSLHVLE IISLMFRDQT PEQLAGVGQG
RLAQERSTDV AELEVLRQRE MAEKRARALQ RGNRHSRFGG SYIVQGLKSI GEKDVVFHKG
LHNLQNYSSD LGKQPRRVPK RRQAAQELSV HRRSVLNVRL FLRDFCSEFL ENCYNPLMGA
VKDHLLRERA QQHDETYYMW AMAFFMAFNR AATFRPGLVS ETLSIRTFHF VEQNLTNYYE
MMLTDRKEAA SWARRMHLAL KAYQELLATV NEMDMCPDEA VRESSRIIKN NIFYMMEYRE
LFLALFRKFD ERYHPRSFLR DLVETTHLFL KMLERFCRSR GNLMVQNKRK KRKKKKKVQD
QGVAFSQSPG ELEAMWPALA EQLLQCAQDP ELSVDPVVPF DAASEVPVEE QRVEAMVRIQ
DCLTAGQAPQ ALALLRSARE VWPEGNAFGS PVISPGEEMQ LLKQILSTPL PRQQEPEEGD
AEEEEEEEEE EELQVVQVSE KEFNFLEYLK RFASSTIVRA YVLLLRSYRQ NSAHTNHCIA
KMLHRLAHGL GMEALLFQLS LFCLFNRLLS DPAAAAYKEL VTFAKYIIGK FFALAAVNQK
AFVELLFWKN TAVVREMTQG YGSLDSGSSS HRAPLWSPEE EAQLQELYLA HKDVEGQDVV
ETILAHLKVV PRTRKQVIHH LVRMGLADSV KEFQKRKGTQ IVLWTEDQEL ELQRLFEEFR
DSDDVLGQIM KNITAKRSRA RVVDKLLALG LVSERRQLYK KRRKKLAPSC MQNGEKSPRD
PWQEDPEEED EHLPEDESED EESEEGLPSG QGQGSSSLSA ENLGESLRQE GLSAPLLWLQ
SSLIRAANDR EEDGCSQAIP LVPLTEENEE AMENEQFQHL LRKLGIRPPS SGQETFWRIP
AKLSSTQLRR VAASLSQQEN EEEREEEPEP GVPGEQGPSE EHRTEALRAL LSARKRKAGL
GPTEEEATGE EEWNSAPKKR QLLDSDEEED DEGRRQAVSG TPRVHRKKRF QIEDEDD
