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Database: UniProt
Entry: Q8N3C0
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Original site: Q8N3C0 
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   16-OCT-2019, entry version 169.
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;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
RP   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.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., 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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   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.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R.M., Hubbard T., Sulston J.E., Dunham I., 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 277-2202, PARTIAL PROTEIN SEQUENCE,
RP   FUNCTION, VARIANT CYS-1995, IDENTIFICATION OF THE ASC-1 COMPLEX,
RP   SUBCELLULAR 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.,
RA   Lim J., 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.,
RA   Mann M.;
RT   "Proteomic characterization of the human centrosome by protein
RT   correlation profiling.";
RL   Nature 426:570-574(2003).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-572, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA   Walther T.C., 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.,
RA   Buerckstuemmer T., 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
RP   OF 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.,
RA   Wang L., Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human
RT   liver phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [14]
RP   SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY,
RP   IDENTIFICATION IN A COMPLEX WITH ASCC1 AND ASCC2, AND INTERACTION WITH
RP   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.,
RA   Byrum A.K., Zhao Y., Corbett M.A., Gecz J., Field M., Vindigni A.,
RA   Slupphaug G., 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   INTERACTION WITH ASCC1 AND ASCC2, IDENTIFICATION IN THE ASCC COMPLEX,
RP   AND 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
RT   subunit 1 (ASCC1) regulates ASCC complex function during alkylation
RT   damage.";
RL   J. Biol. Chem. 293:13524-13533(2018).
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
CC       (PubMed:22055184). Part of the ASC-1 complex that enhances NF-
CC       kappa-B, SRF and AP1 transactivation (PubMed:12077347).
CC       {ECO:0000269|PubMed:12077347, ECO:0000269|PubMed:22055184}.
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
CC       and ASCC3 (PubMed:12077347, PubMed:29144457, PubMed:29997253).
CC       Functions as scaffolding subunit that interacts directly with both
CC       ASCC1 and ASCC2 (PubMed:29144457, PubMed:29997253). Interacts
CC       directly with ALKBH3, and thereby recruits ALKBH3 to the ASCC
CC       complex (PubMed:22055184, PubMed:29144457). Part of the ASC-
CC       1/TRIP4 complex, that contains TRIP4, ASCC1, ASCC2 and ASCC3
CC       (PubMed:12077347). {ECO:0000269|PubMed:12077347,
CC       ECO:0000269|PubMed:22055184, ECO:0000269|PubMed:29144457,
CC       ECO:0000269|PubMed:29997253}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12077347,
CC       ECO:0000269|PubMed:29144457}. Nucleus speckle
CC       {ECO:0000269|PubMed:29144457, ECO:0000269|PubMed:29997253}.
CC       Note=Colocalizes with ALKBH3 and ASCC2 in nuclear foci when cells
CC       have been exposed to alkylating agents that cause DNA damage.
CC       {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};
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   SMR; Q8N3C0; -.
DR   BioGrid; 116170; 75.
DR   CORUM; Q8N3C0; -.
DR   IntAct; Q8N3C0; 31.
DR   MINT; Q8N3C0; -.
DR   STRING; 9606.ENSP00000358159; -.
DR   CarbonylDB; Q8N3C0; -.
DR   iPTMnet; 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   DNASU; 10973; -.
DR   Ensembl; ENST00000369143; ENSP00000358139; ENSG00000112249. [Q8N3C0-3]
DR   Ensembl; ENST00000369162; ENSP00000358159; ENSG00000112249. [Q8N3C0-1]
DR   Ensembl; ENST00000522650; ENSP00000430769; ENSG00000112249. [Q8N3C0-4]
DR   GeneID; 10973; -.
DR   KEGG; hsa:10973; -.
DR   UCSC; uc003pqk.5; human. [Q8N3C0-1]
DR   CTD; 10973; -.
DR   DisGeNET; 10973; -.
DR   GeneCards; ASCC3; -.
DR   HGNC; HGNC:18697; ASCC3.
DR   HPA; HPA031608; -.
DR   HPA; HPA031609; -.
DR   HPA; HPA031610; -.
DR   MIM; 614217; gene.
DR   neXtProt; NX_Q8N3C0; -.
DR   OpenTargets; ENSG00000112249; -.
DR   PharmGKB; PA134890913; -.
DR   eggNOG; KOG0952; Eukaryota.
DR   eggNOG; COG1204; LUCA.
DR   GeneTree; ENSGT00940000155377; -.
DR   HOGENOM; HOG000152625; -.
DR   InParanoid; Q8N3C0; -.
DR   KO; K18663; -.
DR   OMA; YKTLNRM; -.
DR   OrthoDB; 154891at2759; -.
DR   PhylomeDB; Q8N3C0; -.
DR   TreeFam; TF105778; -.
DR   Reactome; R-HSA-112126; ALKBH3 mediated reversal of alkylation damage.
DR   ChiTaRS; ASCC3; human.
DR   GeneWiki; ASCC3; -.
DR   GenomeRNAi; 10973; -.
DR   Pharos; Q8N3C0; -.
DR   PRO; PR:Q8N3C0; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   Bgee; ENSG00000112249; Expressed in 213 organ(s), highest expression level in decidua.
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:HPA.
DR   GO; GO:0005622; C:intracellular; IDA:LIFEdb.
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: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   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; Direct protein sequencing; DNA damage; DNA repair;
KW   Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Polymorphism; Reference proteome; Repeat; Transcription;
KW   Transcription regulation.
FT   CHAIN         1   2202       Activating signal cointegrator 1 complex
FT                                subunit 3.
FT                                /FTId=PRO_0000102093.
FT   DOMAIN      486    669       Helicase ATP-binding 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN      728    914       Helicase C-terminal 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN      978   1287       SEC63 1.
FT   DOMAIN     1336   1511       Helicase ATP-binding 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1544   1739       Helicase C-terminal 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN     1812   2176       SEC63 2.
FT   NP_BIND     499    506       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   NP_BIND    1349   1356       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   REGION        1    400       Required for interaction with ASCC2.
FT                                {ECO:0000269|PubMed:29997253}.
FT   COILED       18     79       {ECO:0000255}.
FT   COILED      328    356       {ECO:0000255}.
FT   MOTIF       611    614       DEVH box.
FT   MOTIF      1453   1456       DEIH box.
FT   MOD_RES      12     12       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   MOD_RES     572    572       N6-acetyllysine.
FT                                {ECO:0000244|PubMed:19608861}.
FT   MOD_RES    2195   2195       Phosphoserine.
FT                                {ECO:0000244|PubMed:23186163}.
FT   VAR_SEQ      81    111       VGTDNGREAIESGAAFLFMTFHLKDSVGHKE -> EVNCPF
FT                                QKRRLDGKEEDEKMSRASDRFRGLR (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_042955.
FT   VAR_SEQ     112   2202       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_042956.
FT   VAR_SEQ     719    731       MVFVHARNATVRT -> HLFYLLLHLFICF (in
FT                                isoform 3).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_042957.
FT   VAR_SEQ     732   2202       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_042958.
FT   VARIANT     146    146       L -> F (in dbSNP:rs9390698).
FT                                {ECO:0000269|PubMed:17974005}.
FT                                /FTId=VAR_034859.
FT   VARIANT     344    344       E -> K (in dbSNP:rs6918004).
FT                                /FTId=VAR_049339.
FT   VARIANT     478    478       N -> S (in dbSNP:rs7750940).
FT                                /FTId=VAR_049340.
FT   VARIANT    1016   1016       S -> C (in dbSNP:rs57534235).
FT                                /FTId=VAR_061212.
FT   VARIANT    1050   1050       V -> I (in dbSNP:rs9497983).
FT                                /FTId=VAR_034860.
FT   VARIANT    1425   1425       V -> A (in dbSNP:rs17246013).
FT                                /FTId=VAR_049341.
FT   VARIANT    1497   1497       R -> T (in dbSNP:rs17305382).
FT                                /FTId=VAR_049342.
FT   VARIANT    1800   1800       C -> W (in dbSNP:rs35011147).
FT                                /FTId=VAR_034861.
FT   VARIANT    1930   1930       V -> M (in dbSNP:rs3213542).
FT                                /FTId=VAR_034862.
FT   VARIANT    1995   1995       S -> C (in dbSNP:rs240780).
FT                                {ECO:0000269|PubMed:12077347,
FT                                ECO:0000269|Ref.7}.
FT                                /FTId=VAR_034863.
FT   VARIANT    2176   2176       Y -> C (in dbSNP:rs240768).
FT                                /FTId=VAR_034864.
FT   MUTAGEN    1354   1354       G->D: Abolishes 3'-5' DNA helicase
FT                                activity and ability to promote DNA
FT                                repair. {ECO:0000269|PubMed:22055184}.
FT   CONFLICT     86     86       G -> E (in Ref. 5; AAH26066).
FT                                {ECO:0000305}.
FT   CONFLICT    444    444       P -> S (in Ref. 1; CAD39122).
FT                                {ECO:0000305}.
FT   CONFLICT    582    582       V -> A (in Ref. 5; AAH26066).
FT                                {ECO:0000305}.
FT   CONFLICT    750    750       P -> S (in Ref. 1; CAD39122).
FT                                {ECO:0000305}.
FT   CONFLICT   1187   1187       S -> F (in Ref. 7; CAA11679).
FT                                {ECO:0000305}.
FT   CONFLICT   1343   1343       C -> S (in Ref. 7; CAA11679).
FT                                {ECO:0000305}.
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
//
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