ASCC3_HUMAN
ID ASCC3_HUMAN Reviewed; 2202 AA.
AC Q8N3C0; E7EW23; O43738; Q4G1A0; Q5VTN2; Q9H1I9; Q9H5A2; Q9NTR0;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Activating signal cointegrator 1 complex subunit 3;
DE EC=3.6.4.12 {ECO:0000269|PubMed:22055184};
DE AltName: Full=ASC-1 complex subunit p200 {ECO:0000303|PubMed:12077347};
DE Short=ASC1p200;
DE AltName: Full=Helicase, ATP binding 1;
DE AltName: Full=Trip4 complex subunit p200 {ECO:0000303|PubMed:12077347};
GN Name=ASCC3; Synonyms=HELIC1, RQT2 {ECO:0000303|PubMed:32099016};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PHE-146.
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Skin, and Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 277-2202, PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP VARIANT CYS-1995, IDENTIFICATION OF THE ASC-1 COMPLEX, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Cervix carcinoma;
RX PubMed=12077347; DOI=10.1128/mcb.22.14.5203-5211.2002;
RA Jung D.-J., Sung H.-S., Goo Y.-W., Lee H.M., Park O.K., Jung S.-Y., Lim J.,
RA Kim H.-J., Lee S.-K., Kim T.S., Lee J.W., Lee Y.C.;
RT "Novel transcription coactivator complex containing activating signal
RT cointegrator 1.";
RL Mol. Cell. Biol. 22:5203-5211(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1012-2202, AND VARIANT CYS-1995.
RC TISSUE=Melanoma;
RA Baurain J.-F.;
RT "The immunodominant antigen recognized by autologous CTL on a human
RT melanoma is generated by a point mutation in a new member of the RNA
RT helicase gene family.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-572, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH ALKBH3, AND MUTAGENESIS OF
RP GLY-1354.
RX PubMed=22055184; DOI=10.1016/j.molcel.2011.08.039;
RA Dango S., Mosammaparast N., Sowa M.E., Xiong L.J., Wu F., Park K.,
RA Rubin M., Gygi S., Harper J.W., Shi Y.;
RT "DNA unwinding by ASCC3 helicase is coupled to ALKBH3-dependent DNA
RT alkylation repair and cancer cell proliferation.";
RL Mol. Cell 44:373-384(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-2195, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION
RP IN A COMPLEX WITH ASCC1 AND ASCC2, AND INTERACTION WITH ASCC2 AND ALKBH3.
RX PubMed=29144457; DOI=10.1038/nature24484;
RA Brickner J.R., Soll J.M., Lombardi P.M., Vaagboe C.B., Mudge M.C.,
RA Oyeniran C., Rabe R., Jackson J., Sullender M.E., Blazosky E., Byrum A.K.,
RA Zhao Y., Corbett M.A., Gecz J., Field M., Vindigni A., Slupphaug G.,
RA Wolberger C., Mosammaparast N.;
RT "A ubiquitin-dependent signalling axis specific for ALKBH-mediated DNA
RT dealkylation repair.";
RL Nature 551:389-393(2017).
RN [15]
RP FUNCTION, INTERACTION WITH ZNF598 AND RPS3, AND SUBCELLULAR LOCATION.
RX PubMed=28757607; DOI=10.1038/s41467-017-00188-1;
RA Matsuo Y., Ikeuchi K., Saeki Y., Iwasaki S., Schmidt C., Udagawa T.,
RA Sato F., Tsuchiya H., Becker T., Tanaka K., Ingolia N.T., Beckmann R.,
RA Inada T.;
RT "Ubiquitination of stalled ribosome triggers ribosome-associated quality
RT control.";
RL Nat. Commun. 8:159-159(2017).
RN [16]
RP INTERACTION WITH ASCC1 AND ASCC2, IDENTIFICATION IN THE ASCC COMPLEX, AND
RP SUBCELLULAR LOCATION.
RX PubMed=29997253; DOI=10.1074/jbc.ra117.000114;
RA Soll J.M., Brickner J.R., Mudge M.C., Mosammaparast N.;
RT "RNA ligase-like domain in activating signal cointegrator 1 complex subunit
RT 1 (ASCC1) regulates ASCC complex function during alkylation damage.";
RL J. Biol. Chem. 293:13524-13533(2018).
RN [17]
RP INTERACTION WITH ZCCHC4.
RX PubMed=31799605; DOI=10.1093/nar/gkz1147;
RA Pinto R., Vaagboe C.B., Jakobsson M.E., Kim Y., Baltissen M.P.,
RA O'Donohue M.F., Guzman U.H., Malecki J.M., Wu J., Kirpekar F., Olsen J.V.,
RA Gleizes P.E., Vermeulen M., Leidel S.A., Slupphaug G., Falnes P.O.;
RT "The human methyltransferase ZCCHC4 catalyses N6-methyladenosine
RT modification of 28S ribosomal RNA.";
RL Nucleic Acids Res. 48:830-846(2020).
RN [18]
RP FUNCTION, IDENTIFICATION IN THE RQT COMPLEX, INTERACTION WITH ASCC2 AND
RP TRIP4, AND MUTAGENESIS OF LYS-505.
RX PubMed=32099016; DOI=10.1038/s41598-020-60241-w;
RA Hashimoto S., Sugiyama T., Yamazaki R., Nobuta R., Inada T.;
RT "Identification of a novel trigger complex that facilitates ribosome-
RT associated quality control in mammalian cells.";
RL Sci. Rep. 10:3422-3422(2020).
CC -!- FUNCTION: 3'-5' DNA helicase involved in repair of alkylated DNA
CC (PubMed:22055184). Promotes DNA unwinding to generate single-stranded
CC substrate needed for ALKBH3, enabling ALKBH3 to process alkylated N3-
CC methylcytosine (3mC) within double-stranded regions (PubMed:22055184).
CC Also involved in activation of the ribosome quality control (RQC)
CC pathway, a pathway that degrades nascent peptide chains during
CC problematic translation (PubMed:28757607, PubMed:32099016). Drives the
CC splitting of stalled ribosomes, as part of the ribosome quality control
CC trigger (RQT) complex (PubMed:28757607, PubMed:32099016). Part of the
CC ASC-1 complex that enhances NF-kappa-B, SRF and AP1 transactivation
CC (PubMed:12077347). {ECO:0000269|PubMed:12077347,
CC ECO:0000269|PubMed:22055184, ECO:0000269|PubMed:28757607,
CC ECO:0000269|PubMed:32099016}.
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:0000269|PubMed:22055184};
CC -!- SUBUNIT: Identified in the ASCC complex that contains ASCC1, ASCC2 and
CC ASCC3 (PubMed:12077347, PubMed:29144457, PubMed:29997253). Functions as
CC scaffolding subunit that interacts directly with both ASCC1 and ASCC2
CC (PubMed:29144457, PubMed:29997253). Interacts directly with ALKBH3, and
CC thereby recruits ALKBH3 to the ASCC complex (PubMed:22055184,
CC PubMed:29144457). Part of the ASC-1/TRIP4 complex, that contains TRIP4,
CC ASCC1, ASCC2 and ASCC3 (PubMed:12077347). Identified in the RQT
CC (ribosome quality control trigger) complex, that contains ASCC2, ASCC3
CC and TRIP4 (PubMed:32099016). Interacts with ASCC2 (PubMed:32099016).
CC Interacts with TRIP4 (PubMed:32099016). Interacts with ZCCHC4
CC (PubMed:31799605). Interacts with ZNF598 (PubMed:28757607). Interacts
CC with RPS3 (PubMed:28757607). Associates with ribosomes
CC (PubMed:32099016). {ECO:0000269|PubMed:12077347,
CC ECO:0000269|PubMed:22055184, ECO:0000269|PubMed:28757607,
CC ECO:0000269|PubMed:29144457, ECO:0000269|PubMed:29997253,
CC ECO:0000269|PubMed:31799605}.
CC -!- INTERACTION:
CC Q8N3C0; Q8N9N2-2: ASCC1; NbExp=4; IntAct=EBI-1210710, EBI-10962548;
CC Q8N3C0; Q9H1I8: ASCC2; NbExp=6; IntAct=EBI-1210710, EBI-711197;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12077347,
CC ECO:0000269|PubMed:29144457}. Nucleus speckle
CC {ECO:0000269|PubMed:29144457, ECO:0000269|PubMed:29997253}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:28757607}. Note=Colocalizes with ALKBH3 and
CC ASCC2 in nuclear foci when cells have been exposed to alkylating agents
CC that cause DNA damage. {ECO:0000269|PubMed:29144457}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8N3C0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N3C0-3; Sequence=VSP_042955, VSP_042956;
CC Name=3;
CC IsoId=Q8N3C0-4; Sequence=VSP_042957, VSP_042958;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12077347}.
CC -!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG45474.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA11679.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA11679.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL834463; CAD39122.1; -; mRNA.
DR EMBL; AK315197; BAG37637.1; -; mRNA.
DR EMBL; AL121965; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356122; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL591585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z86062; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48449.1; -; Genomic_DNA.
DR EMBL; BC050681; AAH50681.1; -; mRNA.
DR EMBL; BC125211; AAI25212.1; -; mRNA.
DR EMBL; BC125212; AAI25213.1; -; mRNA.
DR EMBL; BC026066; AAH26066.1; -; mRNA.
DR EMBL; AY013288; AAG45474.1; ALT_FRAME; mRNA.
DR EMBL; AJ223948; CAA11679.1; ALT_SEQ; mRNA.
DR CCDS; CCDS5046.1; -. [Q8N3C0-1]
DR CCDS; CCDS5047.1; -. [Q8N3C0-3]
DR CCDS; CCDS75497.1; -. [Q8N3C0-4]
DR RefSeq; NP_001271200.1; NM_001284271.1. [Q8N3C0-4]
DR RefSeq; NP_006819.2; NM_006828.3. [Q8N3C0-1]
DR RefSeq; NP_071374.1; NM_022091.4. [Q8N3C0-3]
DR PDB; 6YXQ; X-ray; 2.70 A; A=1-207.
DR PDBsum; 6YXQ; -.
DR AlphaFoldDB; Q8N3C0; -.
DR SMR; Q8N3C0; -.
DR BioGRID; 116170; 179.
DR ComplexPortal; CPX-6641; ASCC DNA alkylation repair complex.
DR ComplexPortal; CPX-6642; RQT ribosome-associated quality control trigger complex.
DR CORUM; Q8N3C0; -.
DR IntAct; Q8N3C0; 39.
DR MINT; Q8N3C0; -.
DR STRING; 9606.ENSP00000358159; -.
DR CarbonylDB; Q8N3C0; -.
DR iPTMnet; Q8N3C0; -.
DR MetOSite; Q8N3C0; -.
DR PhosphoSitePlus; Q8N3C0; -.
DR BioMuta; ASCC3; -.
DR DMDM; 158518649; -.
DR EPD; Q8N3C0; -.
DR jPOST; Q8N3C0; -.
DR MassIVE; Q8N3C0; -.
DR MaxQB; Q8N3C0; -.
DR PaxDb; Q8N3C0; -.
DR PeptideAtlas; Q8N3C0; -.
DR PRIDE; Q8N3C0; -.
DR ProteomicsDB; 71786; -. [Q8N3C0-1]
DR ProteomicsDB; 71787; -. [Q8N3C0-3]
DR ProteomicsDB; 71788; -. [Q8N3C0-4]
DR Antibodypedia; 32044; 94 antibodies from 19 providers.
DR DNASU; 10973; -.
DR Ensembl; ENST00000369143.2; ENSP00000358139.2; ENSG00000112249.14. [Q8N3C0-3]
DR Ensembl; ENST00000369162.7; ENSP00000358159.2; ENSG00000112249.14. [Q8N3C0-1]
DR Ensembl; ENST00000522650.5; ENSP00000430769.1; ENSG00000112249.14. [Q8N3C0-4]
DR GeneID; 10973; -.
DR KEGG; hsa:10973; -.
DR MANE-Select; ENST00000369162.7; ENSP00000358159.2; NM_006828.4; NP_006819.2.
DR UCSC; uc003pqk.5; human. [Q8N3C0-1]
DR CTD; 10973; -.
DR DisGeNET; 10973; -.
DR GeneCards; ASCC3; -.
DR HGNC; HGNC:18697; ASCC3.
DR HPA; ENSG00000112249; Low tissue specificity.
DR MIM; 614217; gene.
DR neXtProt; NX_Q8N3C0; -.
DR OpenTargets; ENSG00000112249; -.
DR PharmGKB; PA134890913; -.
DR VEuPathDB; HostDB:ENSG00000112249; -.
DR eggNOG; KOG0952; Eukaryota.
DR GeneTree; ENSGT00940000155377; -.
DR HOGENOM; CLU_000335_2_1_1; -.
DR InParanoid; Q8N3C0; -.
DR OMA; GTHHAGM; -.
DR OrthoDB; 154891at2759; -.
DR PhylomeDB; Q8N3C0; -.
DR TreeFam; TF105778; -.
DR PathwayCommons; Q8N3C0; -.
DR Reactome; R-HSA-112126; ALKBH3 mediated reversal of alkylation damage.
DR SignaLink; Q8N3C0; -.
DR BioGRID-ORCS; 10973; 186 hits in 1085 CRISPR screens.
DR ChiTaRS; ASCC3; human.
DR GeneWiki; ASCC3; -.
DR GenomeRNAi; 10973; -.
DR Pharos; Q8N3C0; Tbio.
DR PRO; PR:Q8N3C0; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q8N3C0; protein.
DR Bgee; ENSG00000112249; Expressed in decidua and 193 other tissues.
DR ExpressionAtlas; Q8N3C0; baseline and differential.
DR Genevisible; Q8N3C0; HS.
DR GO; GO:0099053; C:activating signal cointegrator 1 complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:1990391; C:DNA repair complex; IPI:ComplexPortal.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IMP:UniProtKB.
DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IDA:UniProtKB.
DR GO; GO:0032508; P:DNA duplex unwinding; IDA:UniProtKB.
DR GO; GO:0072344; P:rescue of stalled ribosome; IMP:UniProtKB.
DR GO; GO:0032790; P:ribosome disassembly; IC:ComplexPortal.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IMP: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 3D-structure; Acetylation; Alternative splicing; ATP-binding; Coiled coil;
KW Cytoplasm; Direct protein sequencing; DNA damage; DNA repair; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation.
FT CHAIN 1..2202
FT /note="Activating signal cointegrator 1 complex subunit 3"
FT /id="PRO_0000102093"
FT DOMAIN 486..669
FT /note="Helicase ATP-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 728..914
FT /note="Helicase C-terminal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 978..1287
FT /note="SEC63 1"
FT DOMAIN 1336..1511
FT /note="Helicase ATP-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1544..1739
FT /note="Helicase C-terminal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1812..2176
FT /note="SEC63 2"
FT REGION 1..400
FT /note="Required for interaction with ASCC2"
FT /evidence="ECO:0000269|PubMed:29997253"
FT COILED 18..79
FT /evidence="ECO:0000255"
FT COILED 328..356
FT /evidence="ECO:0000255"
FT MOTIF 611..614
FT /note="DEVH box"
FT MOTIF 1453..1456
FT /note="DEIH box"
FT BINDING 499..506
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1349..1356
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:0007744|PubMed:23186163"
FT MOD_RES 572
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 2195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 81..111
FT /note="VGTDNGREAIESGAAFLFMTFHLKDSVGHKE -> EVNCPFQKRRLDGKEED
FT EKMSRASDRFRGLR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_042955"
FT VAR_SEQ 112..2202
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_042956"
FT VAR_SEQ 719..731
FT /note="MVFVHARNATVRT -> HLFYLLLHLFICF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042957"
FT VAR_SEQ 732..2202
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042958"
FT VARIANT 146
FT /note="L -> F (in dbSNP:rs9390698)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_034859"
FT VARIANT 344
FT /note="E -> K (in dbSNP:rs6918004)"
FT /id="VAR_049339"
FT VARIANT 478
FT /note="N -> S (in dbSNP:rs7750940)"
FT /id="VAR_049340"
FT VARIANT 1016
FT /note="S -> C (in dbSNP:rs57534235)"
FT /id="VAR_061212"
FT VARIANT 1050
FT /note="V -> I (in dbSNP:rs9497983)"
FT /id="VAR_034860"
FT VARIANT 1425
FT /note="V -> A (in dbSNP:rs17246013)"
FT /id="VAR_049341"
FT VARIANT 1497
FT /note="R -> T (in dbSNP:rs17305382)"
FT /id="VAR_049342"
FT VARIANT 1800
FT /note="C -> W (in dbSNP:rs35011147)"
FT /id="VAR_034861"
FT VARIANT 1930
FT /note="V -> M (in dbSNP:rs3213542)"
FT /id="VAR_034862"
FT VARIANT 1995
FT /note="S -> C (in dbSNP:rs240780)"
FT /evidence="ECO:0000269|PubMed:12077347, ECO:0000269|Ref.7"
FT /id="VAR_034863"
FT VARIANT 2176
FT /note="Y -> C (in dbSNP:rs240768)"
FT /id="VAR_034864"
FT MUTAGEN 505
FT /note="K->R: Defective activation of the ribosome quality
FT control (RQC) pathway. Impairs its association with
FT ribosomes."
FT /evidence="ECO:0000269|PubMed:32099016"
FT MUTAGEN 1354
FT /note="G->D: Abolishes 3'-5' DNA helicase activity and
FT ability to promote DNA repair."
FT /evidence="ECO:0000269|PubMed:22055184"
FT CONFLICT 86
FT /note="G -> E (in Ref. 5; AAH26066)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="P -> S (in Ref. 1; CAD39122)"
FT /evidence="ECO:0000305"
FT CONFLICT 582
FT /note="V -> A (in Ref. 5; AAH26066)"
FT /evidence="ECO:0000305"
FT CONFLICT 750
FT /note="P -> S (in Ref. 1; CAD39122)"
FT /evidence="ECO:0000305"
FT CONFLICT 1187
FT /note="S -> F (in Ref. 7; CAA11679)"
FT /evidence="ECO:0000305"
FT CONFLICT 1343
FT /note="C -> S (in Ref. 7; CAA11679)"
FT /evidence="ECO:0000305"
FT HELIX 6..14
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 16..19
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 26..35
FT /evidence="ECO:0007829|PDB:6YXQ"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 47..57
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 60..81
FT /evidence="ECO:0007829|PDB:6YXQ"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 87..101
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 109..119
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 124..138
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 143..159
FT /evidence="ECO:0007829|PDB:6YXQ"
FT TURN 163..166
FT /evidence="ECO:0007829|PDB:6YXQ"
SQ SEQUENCE 2202 AA; 251460 MW; 9F074E6E5853399C CRC64;
MALPRLTGAL RSFSNVTKQD NYNEEVADLK IKRSKLHEQV LDLGLTWKKI IKFLNEKLEK
SKMQSINEDL KDILHAAKQI VGTDNGREAI ESGAAFLFMT FHLKDSVGHK ETKAIKQMFG
PFPSSSATAA CNATNRIISH FSQDDLTALV QMTEKEHGDR VFFGKNLAFS FDMHDLDHFD
ELPINGETQK TISLDYKKFL NEHLQEACTP ELKPVEKTNG SFLWCEVEKY LNSTLKEMTE
VPRVEDLCCT LYDMLASIKS GDELQDELFE LLGPEGLELI EKLLQNRITI VDRFLNSSND
HRFQALQDNC KKILGENAKP NYGCQVTIQS EQEKQLMKQY RREEKRIARR EKKAGEDLEV
SEGLMCFDPK ELRIQREQAL LNARSVPILS RQRDADVEKI HYPHVYDSQA EAMKTSAFIA
GAKMILPEGI QRENNKLYEE VRIPYSEPMP LSFEEKPVYI QDLDEIGQLA FKGMKRLNRI
QSIVFETAYN TNENMLICAP TGAGKTNIAM LTVLHEIRQH FQQGVIKKNE FKIVYVAPMK
ALAAEMTDYF SRRLEPLGII VKELTGDMQL SKSEILRTQM LVTTPEKWDV VTRKSVGDVA
LSQIVRLLIL DEVHLLHEDR GPVLESIVAR TLRQVESTQS MIRILGLSAT LPNYLDVATF
LHVNPYIGLF FFDGRFRPVP LGQTFLGIKC ANKMQQLNNM DEVCYENVLK QVKAGHQVMV
FVHARNATVR TAMSLIERAK NCGHIPFFFP TQGHDYVLAE KQVQRSRNKQ VRELFPDGFS
IHHAGMLRQD RNLVENLFSN GHIKVLVCTA TLAWGVNLPA HAVIIKGTQI YAAKRGSFVD
LGILDVMQIF GRAGRPQFDK FGEGIIITTH DKLSHYLTLL TQRNPIESQF LESLADNLNA
EIALGTVTNV EEAVKWISYT YLYVRMRANP LAYGISHKAY QIDPTLRKHR EQLVIEVGRK
LDKAQMIRFE ERTGYFSSTD LGRTASHYYI KYNTIETFNE LFDAHKTEGD IFAIVSKAEE
FDQIKVREEE IEELDTLLSN FCELSTPGGV ENSYGKINIL LQTYISRGEM DSFSLISDSA
YVAQNAARIV RALFEIALRK RWPTMTYRLL NLSKVIDKRL WGWASPLRQF SILPPHILTR
LEEKKLTVDK LKDMRKDEIG HILHHVNIGL KVKQCVHQIP SVMMEASIQP ITRTVLRVTL
SIYADFTWND QVHGTVGEPW WIWVEDPTND HIYHSEYFLA LKKQVISKEA QLLVFTIPIF
EPLPSQYYIR AVSDRWLGAE AVCIINFQHL ILPERHPPHT ELLDLQPLPI TALGCKAYEA
LYNFSHFNPV QTQIFHTLYH TDCNVLLGAP TGSGKTVAAE LAIFRVFNKY PTSKAVYIAP
LKALVRERMD DWKVRIEEKL GKKVIELTGD VTPDMKSIAK ADLIVTTPEK WDGVSRSWQN
RNYVQQVTIL IIDEIHLLGE ERGPVLEVIV SRTNFISSHT EKPVRIVGLS TALANARDLA
DWLNIKQMGL FNFRPSVRPV PLEVHIQGFP GQHYCPRMAS MNKPAFQAIR SHSPAKPVLI
FVSSRRQTRL TALELIAFLA TEEDPKQWLN MDEREMENII ATVRDSNLKL TLAFGIGMHH
AGLHERDRKT VEELFVNCKV QVLIATSTLA WGVNFPAHLV IIKGTEYYDG KTRRYVDFPI
TDVLQMMGRA GRPQFDDQGK AVILVHDIKK DFYKKFLYEP FPVESSLLGV LSDHLNAEIA
GGTITSKQDA LDYITWTYFF RRLIMNPSYY NLGDVSHDSV NKFLSHLIEK SLIELELSYC
IEIGEDNRSI EPLTYGRIAS YYYLKHQTVK MFKDRLKPEC STEELLSILS DAEEYTDLPV
RHNEDHMNSE LAKCLPIESN PHSFDSPHTK AHLLLQAHLS RAMLPCPDYD TDTKTVLDQA
LRVCQAMLDV AANQGWLVTV LNITNLIQMV IQGRWLKDSS LLTLPNIENH HLHLFKKWKP
IMKGPHARGR TSIESLPELI HACGGKDHVF SSMVESELHA AKTKQAWNFL SHLPVINVGI
SVKGSWDDLV EGHNELSVST LTADKRDDNK WIKLHADQEY VLQVSLQRVH FGFHKGKPES
CAVTPRFPKS KDEGWFLILG EVDKRELIAL KRVGYIRNHH VASLSFYTPE IPGRYIYTLY
FMSDCYLGLD QQYDIYLNVT QASLSAQVNT KVSDSLTDLA LK
