ASCC3_MOUSE
ID ASCC3_MOUSE Reviewed; 2198 AA.
AC E9PZJ8; Q6PB36; Q8C1G1; Q8C707; Q8K292;
DT 18-APR-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Activating signal cointegrator 1 complex subunit 3;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q8N3C0};
GN Name=Ascc3;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-331 AND 2125-2198.
RC STRAIN=C57BL/6J; TISSUE=Kidney, and 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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 [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-573, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: 3'-5' DNA helicase involved in repair of alkylated DNA.
CC Promotes DNA unwinding to generate single-stranded substrate needed for
CC ALKBH3, enabling ALKBH3 to process alkylated N3-methylcytosine (3mC)
CC within double-stranded regions. Also involved in activation of the
CC ribosome quality control (RQC) pathway, a pathway that degrades nascent
CC peptide chains during problematic translation. Drives the splitting of
CC stalled ribosomes, as part of the ribosome quality control trigger
CC (RQT) complex. Part of the ASC-1 complex that enhances NF-kappa-B, SRF
CC and AP1 transactivation. {ECO:0000250|UniProtKB:Q8N3C0}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000250|UniProtKB:Q8N3C0};
CC -!- SUBUNIT: Identified in the ASCC complex that contains ASCC1, ASCC2 and
CC ASCC3. Functions as scaffolding subunit that interacts directly with
CC both ASCC1 and ASCC2. Interacts directly with ALKBH3, and thereby
CC recruits ALKBH3 to the ASCC complex. Part of the ASC-1/TRIP4 complex,
CC that contains TRIP4, ASCC1, ASCC2 and ASCC3. Identified in the RQT
CC (ribosome quality control trigger) complex, that contains ASCC2, ASCC3
CC and TRIP4. Interacts with ASCC2. Interacts with TRIP4. Interacts with
CC ZCCHC4. Interacts with ZNF598. Interacts with RPS3. Associates with
CC ribosomes (By similarity). {ECO:0000250|UniProtKB:Q8N3C0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N3C0}. Nucleus
CC speckle {ECO:0000250|UniProtKB:Q8N3C0}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q8N3C0}. Note=Colocalizes with ALKBH3 and ASCC2
CC in nuclear foci when cells have been exposed to alkylating agents that
CC cause DNA damage. {ECO:0000250|UniProtKB:Q8N3C0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=E9PZJ8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=E9PZJ8-2; Sequence=VSP_042999;
CC -!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH32189.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC137877; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC153529; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC159114; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032189; AAH32189.1; ALT_INIT; mRNA.
DR EMBL; BC059917; AAH59917.1; -; mRNA.
DR EMBL; AK021027; BAC25644.1; -; mRNA.
DR EMBL; AK052745; BAC35127.1; -; mRNA.
DR CCDS; CCDS48555.1; -. [E9PZJ8-1]
DR RefSeq; NP_932124.2; NM_198007.2. [E9PZJ8-1]
DR AlphaFoldDB; E9PZJ8; -.
DR SMR; E9PZJ8; -.
DR BioGRID; 219071; 5.
DR IntAct; E9PZJ8; 2.
DR MINT; E9PZJ8; -.
DR STRING; 10090.ENSMUSP00000036726; -.
DR iPTMnet; E9PZJ8; -.
DR PhosphoSitePlus; E9PZJ8; -.
DR EPD; E9PZJ8; -.
DR jPOST; E9PZJ8; -.
DR MaxQB; E9PZJ8; -.
DR PaxDb; E9PZJ8; -.
DR PeptideAtlas; E9PZJ8; -.
DR PRIDE; E9PZJ8; -.
DR ProteomicsDB; 281809; -. [E9PZJ8-1]
DR ProteomicsDB; 281810; -. [E9PZJ8-2]
DR Antibodypedia; 32044; 94 antibodies from 19 providers.
DR Ensembl; ENSMUST00000035606; ENSMUSP00000036726; ENSMUSG00000038774. [E9PZJ8-1]
DR GeneID; 77987; -.
DR KEGG; mmu:77987; -.
DR UCSC; uc007fak.2; mouse. [E9PZJ8-1]
DR CTD; 10973; -.
DR MGI; MGI:1925237; Ascc3.
DR VEuPathDB; HostDB:ENSMUSG00000038774; -.
DR eggNOG; KOG0952; Eukaryota.
DR GeneTree; ENSGT00940000155377; -.
DR HOGENOM; CLU_000335_2_1_1; -.
DR InParanoid; E9PZJ8; -.
DR OMA; GTHHAGM; -.
DR OrthoDB; 154891at2759; -.
DR PhylomeDB; E9PZJ8; -.
DR TreeFam; TF105778; -.
DR BioGRID-ORCS; 77987; 13 hits in 110 CRISPR screens.
DR ChiTaRS; Ascc3; mouse.
DR PRO; PR:E9PZJ8; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; E9PZJ8; protein.
DR Bgee; ENSMUSG00000038774; Expressed in spermatid and 219 other tissues.
DR ExpressionAtlas; E9PZJ8; baseline and differential.
DR Genevisible; E9PZJ8; MM.
DR GO; GO:0099053; C:activating signal cointegrator 1 complex; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:1990391; C:DNA repair complex; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; ISS:UniProtKB.
DR GO; GO:0032508; P:DNA duplex unwinding; ISS:UniProtKB.
DR GO; GO:0072344; P:rescue of stalled ribosome; ISS:UniProtKB.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 2.60.40.150; -; 2.
DR Gene3D; 3.40.50.300; -; 4.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004179; Sec63-dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 2.
DR Pfam; PF02889; Sec63; 2.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 2.
DR SMART; SM00973; Sec63; 2.
DR SUPFAM; SSF46785; SSF46785; 2.
DR SUPFAM; SSF52540; SSF52540; 4.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR PROSITE; PS51194; HELICASE_CTER; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ATP-binding; Coiled coil; Cytoplasm;
KW DNA damage; DNA repair; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..2198
FT /note="Activating signal cointegrator 1 complex subunit 3"
FT /id="PRO_0000416915"
FT DOMAIN 487..670
FT /note="Helicase ATP-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 697..915
FT /note="Helicase C-terminal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 979..1288
FT /note="SEC63 1"
FT DOMAIN 1337..1512
FT /note="Helicase ATP-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1545..1740
FT /note="Helicase C-terminal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1813..2177
FT /note="SEC63 2"
FT COILED 18..81
FT /evidence="ECO:0000255"
FT COILED 328..356
FT /evidence="ECO:0000255"
FT MOTIF 612..615
FT /note="DEVH box"
FT MOTIF 1454..1457
FT /note="DEIH box"
FT BINDING 500..507
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1350..1357
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N3C0"
FT MOD_RES 573
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT VAR_SEQ 1..1070
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042999"
FT CONFLICT 1818
FT /note="R -> L (in Ref. 2; AAH59917)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2198 AA; 250557 MW; 39FF851ED47394FD CRC64;
MALPRLTGAL RSFSNVTKQD NYNEEVADLK LKRSKLHEQV LDFGLTWKKI VKFLNEKLEK
NKMQNINEDL KDILQAAKQI VGTDNGREAI ESGAAFLFMT FHMTDSVGYM ETKAIRQTFG
PFPSSSATSA CNATNRIISH FSQDDLTAFV QMAENPCNDR VVFGKNLAFS FDMYDLDHFD
ELPINGESQK TISLDYKKFL NEQFQEPYTP ELKPVEKTNG SLLWCEVEKY LNATLKEMTE
AARVEDLCCT LYDMLASAKS GDELQDELFE LLGPEGLDLI EKLLQNRITI VDRFLNSSSD
HKFQVLQDSC KKILGENSKP NYGCQVTIQS EQEKQLMKQY RREEKRIARR EKKAGEDGEV
SGEGVLPFDP KELRIQREHA LLNARNAPIL GRQRDVEFEK IRYPHVYDSQ AQARETSAFI
AGAKMILPEG IQRENTKLYE EVRIPYGEPM PVGFEEKPVY IKDLDEVGQL AFKGMKRLNR
IQSIVFETAY NTNENMLICA PTGAGKTNIA MLTILHEIRQ HFHQGVIKKN EFKIVYVAPM
KALAAEMTNY FSKRLEPLGI VVKELTGDMQ LSKSEILRTQ MLVTTPEKWD VVTRKSVGDV
ALSQIVKLLI LDEVHLLHED RGPVLESIVA RTLRQVESTQ SMIRILGLSA TLPNYLDVAT
FLHVNPYIGL FYFDGRFRPV PLGQTFLGIK STNKMQQLNN MDEVCYESVL KQVKAGHQVM
VFVHARNATV RTAMSLIERA KNSGQISCFL PTEGPEYGHA LKQVQKSRNK QVRELFSDGF
SIHHAGMLRQ DRNLVENLFS NGHIKVLVCT ATLAWGVNLP AHAVVIKGTQ IYAAKRGSFV
DLGILDVMQI FGRAGRPQFD KFGEGIIITT HDKLSHYLSL LTQQNPIESQ FLESLADNLN
AEIALGTVTN VEEAVRWMSY TYLYVRMRAN PLAYGISHKA YQIDPTLRKH REQLLIEVGQ
KLDKAKMIRF EERTGYFSST DLGRTASHFY IKYNTIETFN ELFDAHKTEG DIFAIVSKAE
EFDQIKVREE EIEELDALLN NFCELSAPGG VENSYGKINI LLQTYISRGE MDSFSLISDS
AYVAQNAARI VRALFEIALR KRWPTMTYRL LNLSKVIDKR LWGWASPLRQ FSVLPPHILT
RLEEKNLTVD KLKDMRKDEI GHILHHVNIG LKVKQCVHQI PSVTMEASIQ PITRTVLRVS
LNIHPDFSWN DQVHGTVGEP WWIWVEDPTN DHIYHSEYFL ALKKQVINKE AQLLVFTIPI
FEPLPSQYYI RAVSDRWLGA EAVCIINFQH LILPERHPPH TELLDLQPLP ITALGCKAYE
ALYNFSHFNP VQTQIFHTLY HTDCNVLLGA PTGSGKTVAA ELAIFRVFNK YPTSKAVYIA
PLKALVRERM DDWKIRIEEK LGKKVIELTG DVTPDMKSIA KADLIVTTPE KWDGVSRSWQ
NRSYVQQVNI LIIDEIHLLG EERGPVLEVI VSRTNFISSH TEKPVRIVGL STALANARDL
ADWLNIKQMG LFNFRPSVRP VPLEVHIQGF PGQHYCPRMA SMNKPAFQAI RSHSPAKPVL
IFVSSRRQTR LTALELIAFL ATEEDPKQWL NMDEQEMDNI IGTVRDSNLK LTLAFGIGMH
HAGLHERDRK TVEELFVNCK VQVLIATSTL AWGVNFPAHL VIIKGTEYYD GKTRRYVDFP
ITDVLQMMGR AGRPQFDDQG KAVILVHDIK KDFYKKFLYE PFPVESSLLG VLSDHLNAEI
AGGTITSKQD AMDYITWTYF FRRLIMNPSY YSLGDVSQDS INKFLSHLIG QSLVELELSH
CIEVGEDNRT IEPLTCGRIA SYYYLKHKTV KMFKDRLKPE CSTEELLSIL SDAEEYTDLP
VRHNEDHTNN ELAKCLPIEL NPHSFDSPHT KAHLLLQAHL SRAMLPCPDY DTDTKTVLDQ
ALRVCQAMLD VAASQGWLVT VLNITHLIQM VIQGRWLKDS SLLTIPNIEQ HHLHLFRKWK
PPVKSSHAKC RTSIECLPEL IHACEGKDHV FSSMVEKELQ PAKTKQAWNF LSRLPVINVG
ISVKGSWDDL VEGHNELSIS TLTADKRDEN KWIKLHADQE YVLQVSLQRV HFGLPKGKHE
NHAVTPRFPK LKDEGWFLIL GEVDKRELMA VKRVGFVRTH HDASISFFTP ETPGRYIFTL
YLMSDCYLGL DQQYDIYLNV IKANISTKDS DVFTDLSV
