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 28-JAN-2026, entry version 179. 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, AND IDENTIFICATION IN THE RQT COMPLEX. RX PubMed=32579943; DOI=10.1016/j.molcel.2020.06.006; RA Juszkiewicz S., Speldewinde S.H., Wan L., Svejstrup J.Q., Hegde R.S.; RT "The ASC-1 complex disassembles collided ribosomes."; RL Mol. Cell 79:603-614(2020). RN [16] RP FUNCTION, IDENTIFICATION IN THE RQT COMPLEX, INTERACTION WITH ASCC3, AND RP 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 [17] RP FUNCTION, IDENTIFICATION IN THE RQT COMPLEX, AND DOMAIN. RX PubMed=36302773; DOI=10.1038/s41467-022-34097-9; RA Narita M., Denk T., Matsuo Y., Sugiyama T., Kikuguchi C., Ito S., Sato N., RA Suzuki T., Hashimoto S., Machova I., Tesina P., Beckmann R., Inada T.; RT "A distinct mammalian disome collision interface harbors K63-linked RT polyubiquitination of uS10 to trigger hRQT-mediated subunit dissociation."; RL Nat. Commun. 13:6411-6411(2022). RN [18] 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: Ubiquitin-binding protein involved in DNA repair and rescue CC of stalled ribosomes (PubMed:29144457, PubMed:32099016, CC PubMed:32579943, PubMed:36302773). Plays a role in DNA damage repair as CC component of the ASCC complex (PubMed:29144457). Recruits ASCC3 and CC ALKBH3 to sites of DNA damage by binding to polyubiquitinated proteins CC that have 'Lys-63'-linked polyubiquitin chains (PubMed:29144457). Part CC of the ASC-1 complex that enhances NF-kappa-B, SRF and AP1 CC transactivation (PubMed:12077347). Involved in activation of the CC ribosome quality control (RQC) pathway, a pathway that degrades nascent CC peptide chains during problematic translation (PubMed:32099016, CC PubMed:32579943, PubMed:36302773). Specifically recognizes and binds CC RPS20/uS10 ubiquitinated by ZNF598, promoting recruitment of the RQT CC (ribosome quality control trigger) complex on stalled ribosomes, CC followed by disassembly of stalled ribosomes (PubMed:36302773). CC {ECO:0000269|PubMed:12077347, ECO:0000269|PubMed:29144457, CC ECO:0000269|PubMed:32099016, ECO:0000269|PubMed:32579943, CC ECO:0000269|PubMed:36302773}. 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:22055184, PubMed:29144457). 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, PubMed:32579943, CC PubMed:36302773). 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 ECO:0000269|PubMed:32579943, ECO:0000269|PubMed:36302773}. CC -!- INTERACTION: CC Q9H1I8; Q8N3C0: ASCC3; NbExp=9; 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 -!- DOMAIN: The CUE domain specifically binds RPS20/uS10 ubiquitinated via CC 'Lys-63'-linked ubiquitin chains by ZNF598. CC {ECO:0000305|PubMed:36302773}. CC -!- SIMILARITY: Belongs to the ASCC2 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAB15089.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_001242906.2. [Q9H1I8-3] DR RefSeq; NP_001356850.1; NM_001369921.1. [Q9H1I8-1] DR RefSeq; NP_001356851.1; NM_001369922.1. [Q9H1I8-1] DR RefSeq; NP_001356852.1; NM_001369923.1. [Q9H1I8-1] DR RefSeq; NP_115580.2; NM_032204.4. [Q9H1I8-1] DR RefSeq; XP_047297496.1; XM_047441540.1. [Q9H1I8-1] DR RefSeq; XP_054181993.1; XM_054326018.1. [Q9H1I8-1] 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; 147. DR ComplexPortal; CPX-6641; ASCC DNA alkylation repair complex. DR ComplexPortal; CPX-6642; RQT ribosome-associated quality control trigger complex. DR CORUM; Q9H1I8; -. DR FunCoup; Q9H1I8; 2416. DR IntAct; Q9H1I8; 97. 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 jPOST; Q9H1I8; -. DR MassIVE; Q9H1I8; -. DR PaxDb; 9606-ENSP00000380877; -. DR PeptideAtlas; Q9H1I8; -. DR ProteomicsDB; 27212; -. DR ProteomicsDB; 80413; -. [Q9H1I8-1] DR ProteomicsDB; 80414; -. [Q9H1I8-2] DR Pumba; Q9H1I8; -. DR Antibodypedia; 224; 184 antibodies from 26 providers. DR DNASU; 84164; -. DR Ensembl; ENST00000307790.8; ENSP00000305502.3; ENSG00000100325.16. [Q9H1I8-1] DR Ensembl; ENST00000397771.6; ENSP00000380877.2; ENSG00000100325.16. [Q9H1I8-1] DR Ensembl; ENST00000542393.5; ENSP00000437570.1; ENSG00000100325.16. [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 AGR; HGNC:24103; -. DR ClinPGx; PA134916940; -. 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 OpenTargets; ENSG00000100325; -. DR VEuPathDB; HostDB:ENSG00000100325; -. DR eggNOG; KOG4501; Eukaryota. DR GeneTree; ENSGT00390000018806; -. DR HOGENOM; CLU_012749_0_0_1; -. DR InParanoid; Q9H1I8; -. DR OMA; LSQHEFW; -. DR OrthoDB; 5577209at2759; -. DR PAN-GO; Q9H1I8; 2 GO annotations based on evolutionary models. DR PhylomeDB; Q9H1I8; -. DR PathwayCommons; Q9H1I8; -. DR Reactome; R-HSA-112126; ALKBH3 mediated reversal of alkylation damage. DR SignaLink; Q9H1I8; -. DR SIGNOR; Q9H1I8; -. DR Agora; ENSG00000100325; -. DR BioGRID-ORCS; 84164; 17 hits in 1154 CRISPR screens. DR CD-CODE; 804901D1; Nuclear speckle. 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 190 other cell types or tissues. DR ExpressionAtlas; Q9H1I8; baseline and differential. DR GO; GO:0022626; C:cytosolic ribosome; IDA:UniProt. 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:0180022; C:RQC-trigger complex; IDA:UniProtKB. DR GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IDA:UniProtKB. DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central. DR GO; GO:0006307; P:DNA alkylation repair; NAS:ComplexPortal. DR GO; GO:0006260; P:DNA replication; NAS:ComplexPortal. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0072344; P:rescue of stalled ribosome; IDA:UniProtKB. DR GO; GO:0032790; P:ribosome disassembly; IDA:UniProtKB. DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IMP:UniProtKB. DR CDD; cd14364; CUE_ASCC2; 1. DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1. DR InterPro; IPR052586; ASCC2. DR InterPro; IPR041800; ASCC2_CUE. DR InterPro; IPR003892; CUE. DR InterPro; IPR009060; UBA-like_sf. DR PANTHER; PTHR21494:SF0; ACTIVATING SIGNAL COINTEGRATOR 1 COMPLEX SUBUNIT 2; 1. DR PANTHER; PTHR21494; ACTIVATING SIGNAL COINTEGRATOR 1 COMPLEX SUBUNIT 2 ASC-1 COMPLEX SUBUNIT P100; 1. DR Pfam; PF02845; CUE; 1. DR SMART; SM00546; CUE; 1. DR SUPFAM; SSF46934; UBA-like; 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; Proteomics identification; KW Reference proteome; Transcription; 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..670 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 671..687 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 719..734 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 //