GenomeNet

Database: UniProt
Entry: E9PZJ8
LinkDB: E9PZJ8
Original site: E9PZJ8 
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   16-OCT-2019, entry version 68.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the 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
RT   project: 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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   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,
RC   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
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-573, AND IDENTIFICATION BY
RP   MASS 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.,
RA   Zhang Y., 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
CC       needed for ALKBH3, enabling ALKBH3 to process alkylated N3-
CC       methylcytosine (3mC) within double-stranded regions. Part of the
CC       ASC-1 complex that enhances NF-kappa-B, SRF and AP1
CC       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
CC       and ASCC3. Functions as scaffolding subunit that interacts
CC       directly with both ASCC1 and ASCC2. Interacts directly with
CC       ALKBH3, and thereby recruits ALKBH3 to the ASCC complex. Part of
CC       the ASC-1/TRIP4 complex, that contains TRIP4, ASCC1, ASCC2 and
CC       ASCC3. {ECO:0000250|UniProtKB:Q8N3C0}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N3C0}.
CC       Nucleus speckle {ECO:0000250|UniProtKB:Q8N3C0}. Note=Colocalizes
CC       with ALKBH3 and ASCC2 in nuclear foci when cells have been exposed
CC       to alkylating agents that cause DNA damage.
CC       {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         Note=No experimental confirmation available.;
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};
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   SMR; E9PZJ8; -.
DR   BioGrid; 219071; 4.
DR   IntAct; E9PZJ8; 2.
DR   MINT; E9PZJ8; -.
DR   STRING; 10090.ENSMUSP00000036726; -.
DR   iPTMnet; E9PZJ8; -.
DR   PhosphoSitePlus; E9PZJ8; -.
DR   EPD; E9PZJ8; -.
DR   MaxQB; E9PZJ8; -.
DR   PaxDb; E9PZJ8; -.
DR   PeptideAtlas; E9PZJ8; -.
DR   PRIDE; E9PZJ8; -.
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   eggNOG; KOG0952; Eukaryota.
DR   eggNOG; COG1204; LUCA.
DR   GeneTree; ENSGT00940000155377; -.
DR   HOGENOM; HOG000157749; -.
DR   InParanoid; E9PZJ8; -.
DR   KO; K18663; -.
DR   OMA; YKTLNRM; -.
DR   OrthoDB; 154891at2759; -.
DR   TreeFam; TF105778; -.
DR   ChiTaRS; Ascc3; mouse.
DR   PRO; PR:E9PZJ8; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   Bgee; ENSMUSG00000038774; Expressed in 232 organ(s), highest expression level in lung.
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; 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: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   Gene3D; 2.60.40.150; -; 2.
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; 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;
KW   Complete proteome; DNA damage; DNA repair; Helicase; Hydrolase;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Transcription; Transcription regulation.
FT   CHAIN         1   2198       Activating signal cointegrator 1 complex
FT                                subunit 3.
FT                                /FTId=PRO_0000416915.
FT   DOMAIN      487    670       Helicase ATP-binding 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      697    915       Helicase C-terminal 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      979   1288       SEC63 1.
FT   DOMAIN     1337   1512       Helicase ATP-binding 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1545   1740       Helicase C-terminal 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN     1813   2177       SEC63 2.
FT   NP_BIND     500    507       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   NP_BIND    1350   1357       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   COILED       18     81       {ECO:0000255}.
FT   COILED      328    356       {ECO:0000255}.
FT   MOTIF       612    615       DEVH box.
FT   MOTIF      1454   1457       DEIH box.
FT   MOD_RES      12     12       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8N3C0}.
FT   MOD_RES     573    573       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:23806337}.
FT   VAR_SEQ       1   1070       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_042999.
FT   CONFLICT   1818   1818       R -> L (in Ref. 2; AAH59917).
FT                                {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
//
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