TTC5_MOUSE
ID TTC5_MOUSE Reviewed; 440 AA.
AC Q99LG4; Q3TTN5; Q3TZL6;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Tetratricopeptide repeat protein 5 {ECO:0000250|UniProtKB:Q8N0Z6};
DE Short=TPR repeat protein 5 {ECO:0000250|UniProtKB:Q8N0Z6};
DE AltName: Full=Stress-responsive activator of p300 {ECO:0000303|PubMed:18833288};
DE Short=Protein Strap {ECO:0000303|PubMed:11511361};
GN Name=Ttc5 {ECO:0000312|MGI:MGI:2683584};
GN Synonyms=Strap {ECO:0000303|PubMed:11511361};
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor, and Salivary 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 [3]
RP FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH EP300 AND JMY, INDUCTION BY
RP STRESS, AND DOMAIN.
RX PubMed=11511361; DOI=10.1016/s1097-2765(01)00277-5;
RA Demonacos C., Krstic-Demonacos M., La Thangue N.B.;
RT "A TPR motif cofactor contributes to p300 activity in the p53 response.";
RL Mol. Cell 8:71-84(2001).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-203, MUTAGENESIS OF
RP SER-203, AND INTERACTION WITH EP300.
RX PubMed=15448695; DOI=10.1038/ncb1170;
RA Demonacos C., Krstic-Demonacos M., Smith L., Xu D., O'Connor D.P.,
RA Jansson M., La Thangue N.B.;
RT "A new effector pathway links ATM kinase with the DNA damage response.";
RL Nat. Cell Biol. 6:968-976(2004).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY STRESS, PHOSPHORYLATION,
RP MUTAGENESIS OF 13-LEU--TYR-24; SER-203 AND SER-221, AND DOMAIN.
RX PubMed=18833288; DOI=10.1038/embor.2008.186;
RA Adams C.J., Graham A.L., Jansson M., Coutts A.S., Edelmann M., Smith L.,
RA Kessler B., La Thangue N.B.;
RT "ATM and Chk2 kinase target the p53 cofactor Strap.";
RL EMBO Rep. 9:1222-1229(2008).
RN [6]
RP FUNCTION, INDUCTION, AND INTERACTION WITH HSF1 AND EP300.
RX PubMed=18451878; DOI=10.1038/embor.2008.70;
RA Xu D., Zalmas L.P., La Thangue N.B.;
RT "A transcription cofactor required for the heat-shock response.";
RL EMBO Rep. 9:662-669(2008).
RN [7]
RP FUNCTION, AND INTERACTION WITH PRMT5.
RX PubMed=19011621; DOI=10.1038/ncb1802;
RA Jansson M., Durant S.T., Cho E.C., Sheahan S., Edelmann M., Kessler B.,
RA La Thangue N.B.;
RT "Arginine methylation regulates the p53 response.";
RL Nat. Cell Biol. 10:1431-1439(2008).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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 [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ATP5F1B AND TP53.
RX PubMed=25168243; DOI=10.1038/cdd.2014.135;
RA Maniam S., Coutts A.S., Stratford M.R., McGouran J., Kessler B.,
RA La Thangue N.B.;
RT "Cofactor Strap regulates oxidative phosphorylation and mitochondrial p53
RT activity through ATP synthase.";
RL Cell Death Differ. 22:156-163(2015).
RN [10]
RP FUNCTION, INTERACTION WITH JMY, AND SUBCELLULAR LOCATION.
RX PubMed=30420355; DOI=10.1083/jcb.201802157;
RA Hu X., Mullins R.D.;
RT "LC3 and STRAP regulate actin filament assembly by JMY during autophagosome
RT formation.";
RL J. Cell Biol. 218:251-266(2019).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS), PHOSPHORYLATION AT SER-203 AND
RP SER-221, AND TPR REPEATS.
RX PubMed=22362889; DOI=10.1073/pnas.1113731109;
RA Adams C.J., Pike A.C., Maniam S., Sharpe T.D., Coutts A.S., Knapp S.,
RA La Thangue N.B., Bullock A.N.;
RT "The p53 cofactor Strap exhibits an unexpected TPR motif and
RT oligonucleotide-binding (OB)-fold structure.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:3778-3783(2012).
CC -!- FUNCTION: Cofactor involved in the regulation of various cellular
CC mechanisms such as actin regulation, autophagy, chromatin regulation
CC and DNA repair (PubMed:11511361, PubMed:15448695, PubMed:18451878,
CC PubMed:30420355). In physiological conditions, interacts with cofactor
CC JMY in the cytoplasm which prevents JMY's actin nucleation activity and
CC ability to activate the Arp2/3 complex (PubMed:30420355). Acts as a
CC negative regulator of nutrient stress-induced autophagy by inhibiting
CC JMY's interaction with MAP1LC3B, thereby preventing autophagosome
CC formation (PubMed:30420355). Involves in tubulin autoregulation by
CC promoting its degradation in response to excess soluble tubulin (By
CC similarity). To do so, associates with the active ribosome near the
CC ribosome exit tunnel and with nascent tubulin polypeptides early during
CC their translation, triggering tubulin mRNA-targeted degradation (By
CC similarity). Following DNA damage, phosphorylated by DNA damage
CC responsive protein kinases ATM and CHEK2, leading to its nuclear
CC accumulation and stability (PubMed:15448695, PubMed:18833288). Nuclear
CC TTC5/STRAP promotes the assembly of a stress-responsive p53/TP53
CC coactivator complex, which includes the coactivators JMY and p300,
CC thereby increasing p53/TP53-dependent transcription and apoptosis
CC (PubMed:11511361). Also recruits arginine methyltransferase PRMT5 to
CC p53/TP53 when DNA is damaged, allowing PRMT5 to methylate p53/TP53
CC (PubMed:19011621). In DNA stress conditions, also prevents p53/TP53
CC degradation by E3 ubiquitin ligase MDM2 (PubMed:11511361). Upon heat-
CC shock stress, forms a chromatin-associated complex with heat-shock
CC factor 1 HSF1 and p300/EP300 to stimulate heat-shock-responsive
CC transcription, thereby increasing cell survival (PubMed:18451878).
CC Mitochondrial TTC5/STRAP interacts with ATP synthase subunit beta
CC ATP5F1B which decreased ATP synthase activity and lowers mitochondrial
CC ATP production, thereby regulating cellular respiration and
CC mitochondrial-dependent apoptosis (PubMed:25168243). Mitochondrial
CC TTC5/STRAP also regulates p53/TP53-mediated apoptosis
CC (PubMed:25168243). {ECO:0000250|UniProtKB:Q8N0Z6,
CC ECO:0000269|PubMed:11511361, ECO:0000269|PubMed:15448695,
CC ECO:0000269|PubMed:18451878, ECO:0000269|PubMed:18833288,
CC ECO:0000269|PubMed:19011621, ECO:0000269|PubMed:25168243,
CC ECO:0000269|PubMed:30420355}.
CC -!- SUBUNIT: Interacts with JMY and p300/EP300; the interaction occurs in
CC the nucleus and augments the association between JMY and p300/EP300 in
CC response to DNA damage (PubMed:11511361, PubMed:15448695). Interacts
CC with PRMT5; the interaction is DNA damage-dependent and promotes PRMT5
CC interaction with p53/TP53 and subsequent methylation (PubMed:19011621).
CC Forms a complex with HSF1 and p300/EP300; these interactions augment
CC chromatin-bound HSF1 and p300/EP300 histone acetyltransferase activity,
CC resulting in enhanced heat-shock-responsive transcription
CC (PubMed:18451878). Interacts with JMY; the interaction occurs in the
CC cytoplasm and results in the inhibition of JYM's nucleation activity
CC (PubMed:30420355). Interacts with ribosome-coding tubulin (via 60S
CC subunit 28S rRNA and protein uL24/RPL26) and the N-terminal of nascent
CC tubulin polypeptide (via alpha-tubulin MREC motif and beta-tubulin MREI
CC motif); these interactions result in tubulin mRNA-targeted degradation
CC (By similarity). Interacts with ATP5F1B; the interaction occurs in the
CC mitochondria and results in ATP production decrease (PubMed:25168243).
CC Interacts with p53/TP53; the interaction occurs in the mitochondria and
CC results in increased apoptosis (PubMed:25168243).
CC {ECO:0000250|UniProtKB:Q8N0Z6, ECO:0000269|PubMed:11511361,
CC ECO:0000269|PubMed:15448695, ECO:0000269|PubMed:18451878,
CC ECO:0000269|PubMed:19011621, ECO:0000269|PubMed:25168243,
CC ECO:0000269|PubMed:30420355}.
CC -!- INTERACTION:
CC Q99LG4; Q3UA06: Trip13; NbExp=2; IntAct=EBI-21183045, EBI-308990;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15448695,
CC ECO:0000269|PubMed:18833288}. Cytoplasm {ECO:0000269|PubMed:15448695,
CC ECO:0000269|PubMed:18833288, ECO:0000269|PubMed:25168243,
CC ECO:0000269|PubMed:30420355}. Cytoplasmic vesicle
CC {ECO:0000269|PubMed:30420355}. Mitochondrion matrix
CC {ECO:0000269|PubMed:25168243}. Note=Phosphorylation at Ser-203 results
CC in nuclear localization, while unphosphorylated protein localizes to
CC the cytoplasm (PubMed:15448695). Nuclear localization may be necessary
CC for DNA damage-dependent stabilization of the protein (PubMed:15448695,
CC PubMed:18833288). {ECO:0000269|PubMed:15448695,
CC ECO:0000269|PubMed:18833288}.
CC -!- TISSUE SPECIFICITY: Expressed in heart, brain, spleen, lung, liver,
CC skeletal muscle, kidney and testis. {ECO:0000269|PubMed:11511361}.
CC -!- INDUCTION: Stress-responsive protein (PubMed:11511361,
CC PubMed:18833288). Induced upon UV or ionizing irradiation (at protein
CC level) (PubMed:11511361). Induced upon heat-shock stress (at protein
CC level) (PubMed:18451878). {ECO:0000269|PubMed:11511361,
CC ECO:0000269|PubMed:18451878, ECO:0000269|PubMed:18833288}.
CC -!- DOMAIN: The tetratricopep-repeat (TPR) motifs may function as protein
CC interaction domains. {ECO:0000305|PubMed:11511361}.
CC -!- PTM: Phosphorylation by ATM kinase induces nuclear accumulation while
CC interfering with nuclear export, and phosphorylation by CHEK2 kinase
CC enhances nuclear stability. {ECO:0000269|PubMed:15448695,
CC ECO:0000269|PubMed:18833288}.
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DR EMBL; AK157777; BAE34192.1; -; mRNA.
DR EMBL; AK161279; BAE36290.1; -; mRNA.
DR EMBL; BC003272; AAH03272.1; -; mRNA.
DR EMBL; BC025610; AAH25610.1; -; mRNA.
DR EMBL; BC092074; AAH92074.1; -; mRNA.
DR CCDS; CCDS36905.1; -.
DR RefSeq; NP_001074418.1; NM_001080949.2.
DR PDB; 4ABN; X-ray; 2.05 A; A/B=1-440.
DR PDBsum; 4ABN; -.
DR AlphaFoldDB; Q99LG4; -.
DR SMR; Q99LG4; -.
DR BioGRID; 230097; 6.
DR IntAct; Q99LG4; 1.
DR STRING; 10090.ENSMUSP00000006451; -.
DR iPTMnet; Q99LG4; -.
DR PhosphoSitePlus; Q99LG4; -.
DR EPD; Q99LG4; -.
DR MaxQB; Q99LG4; -.
DR PaxDb; Q99LG4; -.
DR PRIDE; Q99LG4; -.
DR ProteomicsDB; 298155; -.
DR Antibodypedia; 6802; 140 antibodies from 27 providers.
DR DNASU; 219022; -.
DR Ensembl; ENSMUST00000006451; ENSMUSP00000006451; ENSMUSG00000006288.
DR GeneID; 219022; -.
DR KEGG; mmu:219022; -.
DR UCSC; uc007tlm.2; mouse.
DR CTD; 91875; -.
DR MGI; MGI:2683584; Ttc5.
DR VEuPathDB; HostDB:ENSMUSG00000006288; -.
DR eggNOG; ENOG502QQ6C; Eukaryota.
DR GeneTree; ENSGT00390000006227; -.
DR HOGENOM; CLU_026886_2_1_1; -.
DR InParanoid; Q99LG4; -.
DR OMA; DECKGYE; -.
DR OrthoDB; 633153at2759; -.
DR PhylomeDB; Q99LG4; -.
DR TreeFam; TF316804; -.
DR Reactome; R-MMU-6804760; Regulation of TP53 Activity through Methylation.
DR BioGRID-ORCS; 219022; 2 hits in 107 CRISPR screens.
DR ChiTaRS; Ttc5; mouse.
DR PRO; PR:Q99LG4; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q99LG4; protein.
DR Bgee; ENSMUSG00000006288; Expressed in embryonic brain and 230 other tissues.
DR ExpressionAtlas; Q99LG4; baseline and differential.
DR Genevisible; Q99LG4; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0043022; F:ribosome binding; ISO:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0009267; P:cellular response to starvation; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0061014; P:positive regulation of mRNA catabolic process; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 2.40.50.550; -; 1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR032076; TTC5_OB.
DR InterPro; IPR038645; TTC5_OB_sf.
DR Pfam; PF16669; TTC5_OB; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Cytoplasmic vesicle; DNA damage; DNA repair;
KW Mitochondrion; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW TPR repeat.
FT CHAIN 1..440
FT /note="Tetratricopeptide repeat protein 5"
FT /id="PRO_0000106382"
FT REPEAT 7..61
FT /note="TPR 1"
FT /evidence="ECO:0000269|PubMed:22362889"
FT REPEAT 68..98
FT /note="TPR 2"
FT /evidence="ECO:0000269|PubMed:22362889"
FT REPEAT 103..130
FT /note="TPR 3"
FT /evidence="ECO:0000269|PubMed:22362889"
FT REPEAT 136..174
FT /note="TPR 4"
FT /evidence="ECO:0000269|PubMed:22362889"
FT REPEAT 179..216
FT /note="TPR 5"
FT /evidence="ECO:0000269|PubMed:22362889"
FT REPEAT 224..253
FT /note="TPR 6"
FT /evidence="ECO:0000269|PubMed:22362889"
FT REGION 285..287
FT /note="Mediates interaction with 28S rRNA of ribosome-
FT coding tubulin"
FT /evidence="ECO:0000250|UniProtKB:Q8N0Z6"
FT MOTIF 13..24
FT /note="Nuclear export signal"
FT /evidence="ECO:0000269|PubMed:18833288"
FT SITE 147
FT /note="Mediates interaction with N-terminal MREI motif of
FT beta-tubulin nascent chain"
FT /evidence="ECO:0000250|UniProtKB:Q8N0Z6"
FT SITE 225
FT /note="Mediates interaction with N-terminal MREI motif of
FT beta-tubulin nascent chain"
FT /evidence="ECO:0000250|UniProtKB:Q8N0Z6"
FT SITE 259
FT /note="Mediates interaction with N-terminal MREI motif of
FT beta-tubulin nascent chain"
FT /evidence="ECO:0000250|UniProtKB:Q8N0Z6"
FT MOD_RES 203
FT /note="Phosphoserine; by ATM"
FT /evidence="ECO:0000269|PubMed:15448695,
FT ECO:0000269|PubMed:22362889"
FT MOD_RES 221
FT /note="Phosphoserine; by CHEK2"
FT /evidence="ECO:0000269|PubMed:18833288,
FT ECO:0000269|PubMed:22362889"
FT MUTAGEN 13..24
FT /note="Missing: Increased nuclear localization in non-
FT stress conditions. No change in protein accumulation and
FT stability in response to DNA damage. No change in
FT subcellular localization in non-stress conditions; when
FT associated with 13-L--Y-24. No change in protein
FT accumulation and stability in response to DNA damage; when
FT associated with 13-L--Y-24."
FT /evidence="ECO:0000269|PubMed:18833288"
FT MUTAGEN 203
FT /note="S->A: Loss of phosphorylation at S-203; decreased
FT nuclear localization in non-stress conditions; loss of
FT nuclear accumulation and stability in response to DNA
FT damage. No change in subcellular localization in non-stress
FT conditions; when associated with 13-L--Y-24. No change in
FT protein accumulation and stability in response to DNA
FT damage; when associated with 13-L--Y-24."
FT /evidence="ECO:0000269|PubMed:15448695,
FT ECO:0000269|PubMed:18833288"
FT MUTAGEN 203
FT /note="S->D: No change in subcellular localization in non-
FT stress conditions. No change in protein accumulation and
FT stability in response to DNA damage."
FT /evidence="ECO:0000269|PubMed:18833288"
FT MUTAGEN 221
FT /note="S->A: Decreased phosphorylation. No change in
FT subcellular localization in non-stress conditions. No
FT change in nuclear accumulation in response to DNA damage.
FT Impaired stability in response to DNA damage."
FT /evidence="ECO:0000269|PubMed:18833288"
FT CONFLICT 120
FT /note="A -> T (in Ref. 2; AAH03272/AAH25610/AAH92074)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="V -> A (in Ref. 2; AAH03272/AAH25610/AAH92074)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="S -> Y (in Ref. 1; BAE34192)"
FT /evidence="ECO:0000305"
FT HELIX 5..28
FT /evidence="ECO:0007829|PDB:4ABN"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:4ABN"
FT HELIX 36..41
FT /evidence="ECO:0007829|PDB:4ABN"
FT HELIX 42..61
FT /evidence="ECO:0007829|PDB:4ABN"
FT HELIX 68..78
FT /evidence="ECO:0007829|PDB:4ABN"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:4ABN"
FT HELIX 86..98
FT /evidence="ECO:0007829|PDB:4ABN"
FT HELIX 103..116
FT /evidence="ECO:0007829|PDB:4ABN"
FT HELIX 119..130
FT /evidence="ECO:0007829|PDB:4ABN"
FT HELIX 136..146
FT /evidence="ECO:0007829|PDB:4ABN"
FT HELIX 154..174
FT /evidence="ECO:0007829|PDB:4ABN"
FT HELIX 179..195
FT /evidence="ECO:0007829|PDB:4ABN"
FT HELIX 200..216
FT /evidence="ECO:0007829|PDB:4ABN"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:4ABN"
FT HELIX 224..236
FT /evidence="ECO:0007829|PDB:4ABN"
FT HELIX 240..253
FT /evidence="ECO:0007829|PDB:4ABN"
FT HELIX 258..280
FT /evidence="ECO:0007829|PDB:4ABN"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:4ABN"
FT HELIX 286..294
FT /evidence="ECO:0007829|PDB:4ABN"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:4ABN"
FT TURN 304..307
FT /evidence="ECO:0007829|PDB:4ABN"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:4ABN"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:4ABN"
FT STRAND 335..345
FT /evidence="ECO:0007829|PDB:4ABN"
FT STRAND 352..362
FT /evidence="ECO:0007829|PDB:4ABN"
FT STRAND 365..369
FT /evidence="ECO:0007829|PDB:4ABN"
FT STRAND 383..388
FT /evidence="ECO:0007829|PDB:4ABN"
FT STRAND 390..398
FT /evidence="ECO:0007829|PDB:4ABN"
FT STRAND 401..411
FT /evidence="ECO:0007829|PDB:4ABN"
FT HELIX 413..415
FT /evidence="ECO:0007829|PDB:4ABN"
FT HELIX 425..427
FT /evidence="ECO:0007829|PDB:4ABN"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:4ABN"
SQ SEQUENCE 440 AA; 48795 MW; 07CB475AD1CEA370 CRC64;
MMADEEEEAK HVLQKLQGLV DRLYCFRDSY FETHSVEDAG RKQQDVQEEM EKTLQQMEEV
LGSAQVEAQA LMLKGKALNV TPDYSPEAEV LLSKAVKLEP ELVEAWNQLG EVYWKKGDVA
SAHTCFSGAL THCKNKVSLQ NLSMVLRQLQ TDSGDEHSRH VMDSVRQAKL AVQMDVLDGR
SWYILGNAYL SLYFNTGQNP KISQQALSAY AQAEKVDRKA SSNPDLHLNR ATLHKYEESY
GEALEGFSQA AALDPVWPEP QQREQQLLEF LSRLTSLLES KGKTKPKKLQ SMLGSLRPAH
LGPCGDGRYQ SASGQKMTLE LKPLSTLQPG VNSGTVVLGK VVFSLTTEEK VPFTFGLVDS
DGPCYAVMVY NVVQSWGVLI GDSVAIPEPN LRHHQIRHKG KDYSFSSVRV ETPLLLVVNG
KPQNSSSQAS ATVASRPQCE
