ASCC2_HUMAN
ID ASCC2_HUMAN Reviewed; 757 AA.
AC Q9H1I8; B7Z8E0; F5H6J9; Q4TT54; Q8TAZ0; Q9H711; Q9H9D6;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Activating signal cointegrator 1 complex subunit 2;
DE AltName: Full=ASC-1 complex subunit p100 {ECO:0000303|PubMed:12077347};
DE AltName: Full=Trip4 complex subunit p100 {ECO:0000303|PubMed:12077347};
GN Name=ASCC2; Synonyms=ASC1P100, RQT3 {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 [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP VARIANT GLN-509, IDENTIFICATION OF THE ASC-1 COMPLEX, SUBCELLULAR LOCATION,
RP 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Colon, Teratocarcinoma, and 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=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-713, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
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 [8]
RP INTERACTION WITH ALKBH3.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-233, AND IDENTIFICATION BY
RP 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-447 AND SER-632, AND
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 [11]
RP INTERACTION WITH CSRP1, AND SUBCELLULAR LOCATION.
RX PubMed=26924529; DOI=10.1016/j.ajhg.2016.01.006;
RA Knierim E., Hirata H., Wolf N.I., Morales-Gonzalez S., Schottmann G.,
RA Tanaka Y., Rudnik-Schoeneborn S., Orgeur M., Zerres K., Vogt S.,
RA van Riesen A., Gill E., Seifert F., Zwirner A., Kirschner J., Goebel H.H.,
RA Huebner C., Stricker S., Meierhofer D., Stenzel W., Schuelke M.;
RT "Mutations in subunits of the activating signal cointegrator 1 complex are
RT associated with prenatal spinal muscular atrophy and congenital bone
RT fractures.";
RL Am. J. Hum. Genet. 98:473-489(2016).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN A COMPLEX WITH ASCC1 AND
RP ASCC3, INTERACTION WITH PRPF8 AND OTHER COMPONENTS OF THE SPLICEOSOME, AND
RP MUTAGENESIS OF 478-LEU-LEU-479 AND LEU-506.
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 [13]
RP INTERACTION WITH ASCC3, IDENTIFICATION IN THE ASCC COMPLEX, AND SUBCELLULAR
RP 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 [14]
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 [15]
RP FUNCTION, IDENTIFICATION IN THE RQT COMPLEX, INTERACTION WITH ASCC3 AND
RP TRIP4, AND MUTAGENESIS OF 479-LEU--LEU-491.
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).
RN [16]
RP STRUCTURE BY NMR OF 463-525.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the CUE domain in the human activating signal
RT cointegrator 1 complex subunit 2 (ASCC2).";
RL Submitted (SEP-2006) to the PDB data bank.
CC -!- FUNCTION: Plays a role in DNA damage repair as component of the ASCC
CC complex. Recruits ASCC3 and ALKBH3 to sites of DNA damage by binding to
CC polyubiquitinated proteins that have 'Lys-63'-linked polyubiquitin
CC chains (PubMed:29144457). Part of the ASC-1 complex that enhances NF-
CC kappa-B, SRF and AP1 transactivation (PubMed:12077347). Involved in
CC activation of the ribosome quality control (RQC) pathway, a pathway
CC that degrades nascent peptide chains during problematic translation
CC (PubMed:32099016). As part of the ribosome quality control trigger
CC (RQT) complex, recognizes ZNF598-dependent ubiquitination of stalled
CC ribosomes (By similarity). {ECO:0000250|UniProtKB:P53137,
CC ECO:0000269|PubMed:12077347, ECO:0000269|PubMed:29144457,
CC ECO:0000269|PubMed:32099016}.
CC -!- SUBUNIT: Identified in the ASCC complex that contains ASCC1, ASCC2 and
CC ASCC3 (PubMed:29144457, PubMed:29997253). Interacts directly with ASCC3
CC (PubMed:29997253, PubMed:32099016). The ASCC complex interacts with
CC ALKBH3 (PubMed:29144457, PubMed:22055184). Interacts (via CUE domain)
CC with 'Lys-63'-linked polyubiquitin chains, but not with 'Lys-48'-linked
CC polyubiquitin chains (PubMed:29144457). Part of the ASC-1 complex, that
CC contains TRIP4, ASCC1, ASCC2 and ASCC3 (PubMed:12077347). Component of
CC the RQT (ribosome quality control trigger) complex, that contains
CC ASCC2, ASCC3 and TRIP4 (PubMed:32099016). Interacts with TRIP4
CC (PubMed:32099016). Interacts with CSRP1 (PubMed:26924529). Interacts
CC with PRPF8, a component of the spliceosome (PubMed:29144457). Interacts
CC with ZCCHC4 (PubMed:31799605). {ECO:0000269|PubMed:12077347,
CC ECO:0000269|PubMed:22055184, ECO:0000269|PubMed:26924529,
CC ECO:0000269|PubMed:29144457, ECO:0000269|PubMed:29997253,
CC ECO:0000269|PubMed:31799605, ECO:0000269|PubMed:32099016}.
CC -!- INTERACTION:
CC Q9H1I8; Q8N3C0: ASCC3; NbExp=6; IntAct=EBI-711197, EBI-1210710;
CC Q9H1I8; Q9BW62: KATNAL1; NbExp=3; IntAct=EBI-711197, EBI-743591;
CC Q9H1I8; Q99633: PRPF18; NbExp=3; IntAct=EBI-711197, EBI-2798416;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12077347,
CC ECO:0000269|PubMed:26924529, ECO:0000269|PubMed:29144457}. Nucleus
CC speckle {ECO:0000269|PubMed:29144457, ECO:0000269|PubMed:29997253}.
CC Note=Colocalizes with the spliceosomal components PRPF8 and
CC SNRNP200/BRR2 in nuclear foci when cells have been exposed to
CC alkylating agents that cause DNA damage. Colocalizes with RNF113A and
CC 'Lys-63'-linked polyubiquitinated proteins, ALKBH3 and ASCC3 in nuclear
CC foci when cells have been exposed to alkylating agents that cause DNA
CC damage. {ECO:0000269|PubMed:29144457}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H1I8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H1I8-2; Sequence=VSP_011009, VSP_011010, VSP_011011;
CC Name=3;
CC IsoId=Q9H1I8-3; Sequence=VSP_045878, VSP_045879;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12077347}.
CC -!- SIMILARITY: Belongs to the ASCC2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB15089.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY013289; AAG45475.1; -; mRNA.
DR EMBL; AK022886; BAB14293.1; -; mRNA.
DR EMBL; AK025241; BAB15089.1; ALT_INIT; mRNA.
DR EMBL; AK303257; BAH13926.1; -; mRNA.
DR EMBL; AC004882; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z82171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025368; AAH25368.1; -; mRNA.
DR CCDS; CCDS13869.1; -. [Q9H1I8-1]
DR CCDS; CCDS56226.1; -. [Q9H1I8-3]
DR RefSeq; NP_001229835.1; NM_001242906.1. [Q9H1I8-3]
DR RefSeq; NP_115580.2; NM_032204.4. [Q9H1I8-1]
DR RefSeq; XP_005261832.1; XM_005261775.2.
DR RefSeq; XP_016884487.1; XM_017028998.1. [Q9H1I8-1]
DR RefSeq; XP_016884488.1; XM_017028999.1.
DR RefSeq; XP_016884489.1; XM_017029000.1.
DR PDB; 2DI0; NMR; -; A=463-526.
DR PDB; 6YXQ; X-ray; 2.70 A; B=2-434.
DR PDBsum; 2DI0; -.
DR PDBsum; 6YXQ; -.
DR AlphaFoldDB; Q9H1I8; -.
DR SMR; Q9H1I8; -.
DR BioGRID; 123921; 128.
DR ComplexPortal; CPX-6641; ASCC DNA alkylation repair complex.
DR ComplexPortal; CPX-6642; RQT ribosome-associated quality control trigger complex.
DR CORUM; Q9H1I8; -.
DR IntAct; Q9H1I8; 64.
DR MINT; Q9H1I8; -.
DR STRING; 9606.ENSP00000380877; -.
DR GlyGen; Q9H1I8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H1I8; -.
DR PhosphoSitePlus; Q9H1I8; -.
DR BioMuta; ASCC2; -.
DR DMDM; 92090990; -.
DR EPD; Q9H1I8; -.
DR jPOST; Q9H1I8; -.
DR MassIVE; Q9H1I8; -.
DR MaxQB; Q9H1I8; -.
DR PaxDb; Q9H1I8; -.
DR PeptideAtlas; Q9H1I8; -.
DR PRIDE; Q9H1I8; -.
DR ProteomicsDB; 27212; -.
DR ProteomicsDB; 80413; -. [Q9H1I8-1]
DR ProteomicsDB; 80414; -. [Q9H1I8-2]
DR Antibodypedia; 224; 180 antibodies from 26 providers.
DR DNASU; 84164; -.
DR Ensembl; ENST00000307790.8; ENSP00000305502.3; ENSG00000100325.15. [Q9H1I8-1]
DR Ensembl; ENST00000397771.6; ENSP00000380877.2; ENSG00000100325.15. [Q9H1I8-1]
DR Ensembl; ENST00000542393.5; ENSP00000437570.1; ENSG00000100325.15. [Q9H1I8-3]
DR GeneID; 84164; -.
DR KEGG; hsa:84164; -.
DR MANE-Select; ENST00000307790.8; ENSP00000305502.3; NM_032204.5; NP_115580.2.
DR UCSC; uc003agr.4; human. [Q9H1I8-1]
DR CTD; 84164; -.
DR DisGeNET; 84164; -.
DR GeneCards; ASCC2; -.
DR HGNC; HGNC:24103; ASCC2.
DR HPA; ENSG00000100325; Low tissue specificity.
DR MIM; 614216; gene.
DR neXtProt; NX_Q9H1I8; -.
DR OpenTargets; ENSG00000100325; -.
DR PharmGKB; PA134916940; -.
DR VEuPathDB; HostDB:ENSG00000100325; -.
DR eggNOG; KOG4501; Eukaryota.
DR GeneTree; ENSGT00390000018806; -.
DR HOGENOM; CLU_012749_0_0_1; -.
DR InParanoid; Q9H1I8; -.
DR OMA; DYQRQFP; -.
DR OrthoDB; 311659at2759; -.
DR PhylomeDB; Q9H1I8; -.
DR TreeFam; TF323459; -.
DR PathwayCommons; Q9H1I8; -.
DR Reactome; R-HSA-112126; ALKBH3 mediated reversal of alkylation damage.
DR SignaLink; Q9H1I8; -.
DR BioGRID-ORCS; 84164; 17 hits in 1078 CRISPR screens.
DR ChiTaRS; ASCC2; human.
DR EvolutionaryTrace; Q9H1I8; -.
DR GeneWiki; ASCC2; -.
DR GenomeRNAi; 84164; -.
DR Pharos; Q9H1I8; Tbio.
DR PRO; PR:Q9H1I8; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q9H1I8; protein.
DR Bgee; ENSG00000100325; Expressed in lower esophagus mucosa and 188 other tissues.
DR ExpressionAtlas; Q9H1I8; baseline and differential.
DR Genevisible; Q9H1I8; HS.
DR GO; GO:0099053; C:activating signal cointegrator 1 complex; IDA:UniProtKB.
DR GO; GO:1990391; C:DNA repair complex; IPI:ComplexPortal.
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:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IC:ComplexPortal.
DR GO; GO:0032508; P:DNA duplex unwinding; IC:ComplexPortal.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; 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 CDD; cd14364; CUE_ASCC2; 1.
DR InterPro; IPR041800; ASCC2_CUE.
DR InterPro; IPR003892; CUE.
DR InterPro; IPR009060; UBA-like_sf.
DR Pfam; PF02845; CUE; 1.
DR SMART; SM00546; CUE; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR PROSITE; PS51140; CUE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing; DNA damage;
KW DNA repair; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..757
FT /note="Activating signal cointegrator 1 complex subunit 2"
FT /id="PRO_0000064689"
FT DOMAIN 467..510
FT /note="CUE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT REGION 617..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 657..671
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..687
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..742
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 233
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 447
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 713
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:20068231"
FT VAR_SEQ 1..114
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011009"
FT VAR_SEQ 28..80
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045878"
FT VAR_SEQ 137..159
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045879"
FT VAR_SEQ 483..484
FT /note="GE -> EK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011010"
FT VAR_SEQ 485..757
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_011011"
FT VARIANT 96
FT /note="R -> C (in dbSNP:rs1894473)"
FT /id="VAR_050675"
FT VARIANT 123
FT /note="V -> I (in dbSNP:rs11549795)"
FT /id="VAR_050676"
FT VARIANT 407
FT /note="D -> H (in dbSNP:rs28265)"
FT /id="VAR_025512"
FT VARIANT 423
FT /note="P -> S (in dbSNP:rs36571)"
FT /id="VAR_025513"
FT VARIANT 509
FT /note="R -> Q (in dbSNP:rs4823054)"
FT /evidence="ECO:0000269|PubMed:12077347"
FT /id="VAR_019464"
FT VARIANT 546
FT /note="D -> G (in dbSNP:rs34833047)"
FT /id="VAR_050677"
FT VARIANT 588
FT /note="E -> K (in dbSNP:rs34062345)"
FT /id="VAR_050678"
FT VARIANT 639
FT /note="R -> L (in dbSNP:rs6006259)"
FT /id="VAR_025514"
FT MUTAGEN 478..479
FT /note="LL->AA: Loss of ubiquitin binding."
FT /evidence="ECO:0000269|PubMed:29144457"
FT MUTAGEN 479..491
FT /note="LPDLGEGFILACL->AADLGEGFALACA: Decreases ubiquitin
FT binding."
FT /evidence="ECO:0000269|PubMed:32099016"
FT MUTAGEN 506
FT /note="L->A: Loss of ubiquitin binding."
FT /evidence="ECO:0000269|PubMed:29144457"
FT CONFLICT 344
FT /note="Q -> H (in Ref. 2; BAB15089)"
FT /evidence="ECO:0000305"
FT CONFLICT 526
FT /note="K -> N (in Ref. 2; BAB15089)"
FT /evidence="ECO:0000305"
FT CONFLICT 586
FT /note="R -> C (in Ref. 2; BAB15089)"
FT /evidence="ECO:0000305"
FT CONFLICT 639
FT /note="R -> G (in Ref. 2; BAH13926)"
FT /evidence="ECO:0000305"
FT CONFLICT 645
FT /note="P -> L (in Ref. 1; AAG45475)"
FT /evidence="ECO:0000305"
FT CONFLICT 653
FT /note="P -> L (in Ref. 1; AAG45475)"
FT /evidence="ECO:0000305"
FT CONFLICT 661
FT /note="D -> G (in Ref. 2; BAH13926)"
FT /evidence="ECO:0000305"
FT CONFLICT 744
FT /note="T -> I (in Ref. 2; BAH13926)"
FT /evidence="ECO:0000305"
FT HELIX 6..8
FT /evidence="ECO:0007829|PDB:6YXQ"
FT STRAND 10..14
FT /evidence="ECO:0007829|PDB:6YXQ"
FT STRAND 21..27
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 49..71
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 85..97
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 110..131
FT /evidence="ECO:0007829|PDB:6YXQ"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 143..152
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 158..168
FT /evidence="ECO:0007829|PDB:6YXQ"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 173..186
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 189..211
FT /evidence="ECO:0007829|PDB:6YXQ"
FT TURN 234..236
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 239..262
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 267..271
FT /evidence="ECO:0007829|PDB:6YXQ"
FT TURN 272..274
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 275..296
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 302..330
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 332..336
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 344..355
FT /evidence="ECO:0007829|PDB:6YXQ"
FT TURN 356..359
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 361..370
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 373..383
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 390..404
FT /evidence="ECO:0007829|PDB:6YXQ"
FT HELIX 466..478
FT /evidence="ECO:0007829|PDB:2DI0"
FT HELIX 484..493
FT /evidence="ECO:0007829|PDB:2DI0"
FT TURN 494..496
FT /evidence="ECO:0007829|PDB:2DI0"
FT HELIX 498..506
FT /evidence="ECO:0007829|PDB:2DI0"
FT TURN 512..516
FT /evidence="ECO:0007829|PDB:2DI0"
SQ SEQUENCE 757 AA; 86360 MW; BB1DCE21E3068E64 CRC64;
MPALPLDQLQ ITHKDPKTGK LRTSPALHPE QKADRYFVLY KPPPKDNIPA LVEEYLERAT
FVANDLDWLL ALPHDKFWCQ VIFDETLQKC LDSYLRYVPR KFDEGVASAP EVVDMQKRLH
RSVFLTFLRM STHKESKDHF ISPSAFGEIL YNNFLFDIPK ILDLCVLFGK GNSPLLQKMI
GNIFTQQPSY YSDLDETLPT ILQVFSNILQ HCGLQGDGAN TTPQKLEERG RLTPSDMPLL
ELKDIVLYLC DTCTTLWAFL DIFPLACQTF QKHDFCYRLA SFYEAAIPEM ESAIKKRRLE
DSKLLGDLWQ RLSHSRKKLM EIFHIILNQI CLLPILESSC DNIQGFIEEF LQIFSSLLQE
KRFLRDYDAL FPVAEDISLL QQASSVLDET RTAYILQAVE SAWEGVDRRK ATDAKDPSVI
EEPNGEPNGV TVTAEAVSQA SSHPENSEEE ECMGAAAAVG PAMCGVELDS LISQVKDLLP
DLGEGFILAC LEYYHYDPEQ VINNILEERL APTLSQLDRN LDREMKPDPT PLLTSRHNVF
QNDEFDVFSR DSVDLSRVHK GKSTRKEENT RSLLNDKRAV AAQRQRYEQY SVVVEEVPLQ
PGESLPYHSV YYEDEYDDTY DGNQVGANDA DSDDELISRR PFTIPQVLRT KVPREGQEED
DDDEEDDADE EAPKPDHFVQ DPAVLREKAE ARRMAFLAKK GYRHDSSTAV AGSPRGHGQS
RETTQERRKK EANKATRANH NRRTMADRKR SKGMIPS
