ID ASCC1_HUMAN Reviewed; 400 AA. AC Q8N9N2; Q5SW06; Q5SW07; Q96EI8; Q9Y307; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 28-JAN-2026, entry version 190. DE RecName: Full=Activating signal cointegrator 1 complex subunit 1; DE AltName: Full=ASC-1 complex subunit p50 {ECO:0000303|PubMed:12077347}; DE AltName: Full=Trip4 complex subunit p50 {ECO:0000303|PubMed:12077347}; GN Name=ASCC1; ORFNames=CGI-18; 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 2), PARTIAL PROTEIN SEQUENCE, FUNCTION, RP IDENTIFICATION OF THE ASC-1 COMPLEX, SUBCELLULAR LOCATION, AND TISSUE RP 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] (ISOFORM 2). RX PubMed=10810093; DOI=10.1101/gr.10.5.703; RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.; RT "Identification of novel human genes evolutionarily conserved in RT Caenorhabditis elegans by comparative proteomics."; RL Genome Res. 10:703-713(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Astrocyte, and Placenta; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [5] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Ovary; 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 [7] RP FUNCTION. RX PubMed=19074642; DOI=10.1152/ajpgi.90340.2008; RA Almeida-Vega S., Catlow K., Kenny S., Dimaline R., Varro A.; RT "Gastrin activates paracrine networks leading to induction of PAI-2 via MAZ RT and ASC-1."; RL Am. J. Physiol. 296:G414-G423(2009). RN [8] 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 [9] RP INVOLVEMENT IN BE, AND VARIANT SER-318. RX PubMed=21791690; DOI=10.1001/jama.2011.1029; RA Orloff M., Peterson C., He X., Ganapathi S., Heald B., Yang Y.R., Bebek G., RA Romigh T., Song J.H., Wu W., David S., Cheng Y., Meltzer S.J., Eng C.; RT "Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with Barrett RT esophagus and esophageal adenocarcinoma."; RL JAMA 306:410-419(2011). RN [10] 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 [11] RP FUNCTION, INTERACTION WITH CSRP1, SUBCELLULAR LOCATION, AND INVOLVEMENT IN RP SMABF2. 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 IDENTIFICATION IN A COMPLEX WITH ASCC1 AND ASCC3, SUBUNIT, AND RP IDENTIFICATION BY MASS SPECTROMETRY. 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 FUNCTION, SUBUNIT, INTERACTION WITH ASCC3, 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 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). CC -!- FUNCTION: Plays a role in DNA damage repair as component of the ASCC CC complex (PubMed:29997253). Part of the ASC-1 complex that enhances NF- CC kappa-B, SRF and AP1 transactivation (PubMed:12077347). In cells CC responding to gastrin-activated paracrine signals, it is involved in CC the induction of SERPINB2 expression by gastrin. May also play a role CC in the development of neuromuscular junction. CC {ECO:0000269|PubMed:12077347, ECO:0000269|PubMed:19074642, CC ECO:0000269|PubMed:26924529, ECO:0000269|PubMed:29997253}. 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). The ASCC complex interacts with ALKBH3 CC (PubMed:22055184, PubMed:29144457). Part of the ASC-1 complex, that CC contains TRIP4, ASCC1, ASCC2 and ASCC3 (PubMed:12077347). Interacts CC with CSRP1 (PubMed:26924529). Interacts with ZCCHC4 (PubMed:31799605). CC {ECO:0000269|PubMed:12077347, ECO:0000269|PubMed:22055184, CC ECO:0000269|PubMed:26924529, ECO:0000269|PubMed:29144457, CC ECO:0000269|PubMed:29997253, ECO:0000269|PubMed:31799605}. CC -!- INTERACTION: CC Q8N9N2; Q8N3C0: ASCC3; NbExp=4; IntAct=EBI-10268317, EBI-1210710; CC Q8N9N2; Q12933: TRAF2; NbExp=3; IntAct=EBI-10268317, EBI-355744; CC Q8N9N2-2; Q8N3C0: ASCC3; NbExp=4; IntAct=EBI-10962548, EBI-1210710; CC Q8N9N2-2; Q12933: TRAF2; NbExp=3; IntAct=EBI-10962548, EBI-355744; CC Q8N9N2-2; Q13114: TRAF3; NbExp=3; IntAct=EBI-10962548, EBI-357631; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12077347, CC ECO:0000269|PubMed:26924529}. Nucleus speckle CC {ECO:0000269|PubMed:29997253}. Note=Colocalizes with PRPF8 in nuclear CC speckles in the absence of DNA damage. {ECO:0000269|PubMed:29997253}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q8N9N2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8N9N2-2; Sequence=VSP_011007, VSP_011008; CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:12077347}. CC -!- DISEASE: Barrett esophagus (BE) [MIM:614266]: A condition characterized CC by a metaplastic change in which normal esophageal squamous epithelium CC is replaced by a columnar and intestinal-type epithelium. Patients with CC Barrett esophagus have an increased risk of esophageal adenocarcinoma. CC The main cause of Barrett esophagus is gastroesophageal reflux. The CC retrograde movement of acid and bile salts from the stomach into the CC esophagus causes prolonged injury to the esophageal epithelium and CC induces chronic esophagitis, which in turn is believed to trigger the CC pathologic changes. {ECO:0000269|PubMed:21791690}. Note=The gene CC represented in this entry may be involved in disease pathogenesis. CC -!- DISEASE: Spinal muscular atrophy with congenital bone fractures 2 CC (SMABF2) [MIM:616867]: An autosomal recessive neuromuscular disorder CC characterized by prenatal-onset spinal muscular atrophy, multiple CC congenital contractures consistent with arthrogryposis multiplex CC congenita, respiratory distress, and congenital bone fractures. CC {ECO:0000269|PubMed:26924529}. Note=The disease is caused by variants CC affecting the gene represented in this entry. 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; AY013290; AAG45476.1; -; mRNA. DR EMBL; AF132952; AAD27727.1; -; mRNA. DR EMBL; AK094170; BAC04299.1; -; mRNA. DR EMBL; AK023436; BAG51193.1; -; mRNA. DR EMBL; AC022392; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL607035; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471083; EAW54444.1; -; Genomic_DNA. DR EMBL; BC012291; AAH12291.1; -; mRNA. DR CCDS; CCDS31219.1; -. [Q8N9N2-2] DR CCDS; CCDS55713.1; -. [Q8N9N2-1] DR RefSeq; NP_001185727.1; NM_001198798.2. [Q8N9N2-2] DR RefSeq; NP_001185728.1; NM_001198799.3. [Q8N9N2-1] DR RefSeq; NP_001185729.1; NM_001198800.3. [Q8N9N2-2] DR RefSeq; NP_001356022.1; NM_001369093.1. [Q8N9N2-2] DR RefSeq; NP_001356023.1; NM_001369094.1. [Q8N9N2-2] DR RefSeq; NP_001356024.1; NM_001369095.1. [Q8N9N2-2] DR PDB; 8TLY; X-ray; 2.80 A; A/B=162-349. DR PDBsum; 8TLY; -. DR AlphaFoldDB; Q8N9N2; -. DR SMR; Q8N9N2; -. DR BioGRID; 119215; 82. DR ComplexPortal; CPX-6641; ASCC DNA alkylation repair complex. DR CORUM; Q8N9N2; -. DR FunCoup; Q8N9N2; 998. DR IntAct; Q8N9N2; 51. DR STRING; 9606.ENSP00000339404; -. DR BindingDB; Q8N9N2; -. DR GlyGen; Q8N9N2; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q8N9N2; -. DR PhosphoSitePlus; Q8N9N2; -. DR BioMuta; ASCC1; -. DR DMDM; 50400556; -. DR jPOST; Q8N9N2; -. DR MassIVE; Q8N9N2; -. DR PaxDb; 9606-ENSP00000339404; -. DR PeptideAtlas; Q8N9N2; -. DR ProteomicsDB; 72561; -. [Q8N9N2-1] DR ProteomicsDB; 72562; -. [Q8N9N2-2] DR Pumba; Q8N9N2; -. DR Antibodypedia; 29224; 202 antibodies from 23 providers. DR DNASU; 51008; -. DR Ensembl; ENST00000317126.8; ENSP00000320461.4; ENSG00000138303.20. [Q8N9N2-2] DR Ensembl; ENST00000342444.8; ENSP00000339404.4; ENSG00000138303.20. [Q8N9N2-1] DR Ensembl; ENST00000394915.7; ENSP00000378373.3; ENSG00000138303.20. [Q8N9N2-1] DR Ensembl; ENST00000672957.1; ENSP00000500935.1; ENSG00000138303.20. [Q8N9N2-2] DR GeneID; 51008; -. DR KEGG; hsa:51008; -. DR MANE-Select; ENST00000672957.1; ENSP00000500935.1; NM_001198800.3; NP_001185729.1. [Q8N9N2-2] DR UCSC; uc001jst.3; human. [Q8N9N2-1] DR AGR; HGNC:24268; -. DR ClinPGx; PA134974899; -. DR CTD; 51008; -. DR DisGeNET; 51008; -. DR GeneCards; ASCC1; -. DR HGNC; HGNC:24268; ASCC1. DR HPA; ENSG00000138303; Low tissue specificity. DR MalaCards; ASCC1; -. DR MIM; 614215; gene. DR MIM; 614266; phenotype. DR MIM; 616867; phenotype. DR OpenTargets; ENSG00000138303; -. DR Orphanet; 486811; Prenatal-onset spinal muscular atrophy with congenital bone fractures. DR VEuPathDB; HostDB:ENSG00000138303; -. DR eggNOG; KOG0940; Eukaryota. DR eggNOG; KOG2814; Eukaryota. DR GeneTree; ENSGT00390000018119; -. DR HOGENOM; CLU_044606_0_0_1; -. DR InParanoid; Q8N9N2; -. DR OrthoDB; 277832at2759; -. DR PAN-GO; Q8N9N2; 2 GO annotations based on evolutionary models. DR PhylomeDB; Q8N9N2; -. DR PathwayCommons; Q8N9N2; -. DR Reactome; R-HSA-112126; ALKBH3 mediated reversal of alkylation damage. DR SignaLink; Q8N9N2; -. DR Agora; ENSG00000138303; -. DR BioGRID-ORCS; 51008; 26 hits in 1157 CRISPR screens. DR CD-CODE; 232F8A39; P-body. DR CD-CODE; 804901D1; Nuclear speckle. DR CD-CODE; DEE660B4; Stress granule. DR ChiTaRS; ASCC1; human. DR GenomeRNAi; 51008; -. DR Pharos; Q8N9N2; Tbio. DR PRO; PR:Q8N9N2; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; Q8N9N2; protein. DR Bgee; ENSG00000138303; Expressed in calcaneal tendon and 199 other cell types or tissues. DR ExpressionAtlas; Q8N9N2; baseline and differential. 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:0005667; C:transcription regulator complex; IDA:MGI. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. 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:MGI. DR CDD; cd22419; KH-I_ASCC1; 1. DR FunFam; 3.30.1370.10:FF:000101; Activating signal cointegrator 1 complex subunit 1; 1. DR FunFam; 3.90.1140.10:FF:000005; activating signal cointegrator 1 complex subunit 1; 1. DR Gene3D; 3.90.1140.10; Cyclic phosphodiesterase; 1. DR Gene3D; 3.30.1370.10; K Homology domain, type 1; 1. DR InterPro; IPR019510; AKAP7-like_phosphoesterase. DR InterPro; IPR009210; ASCC1. DR InterPro; IPR009097; Cyclic_Pdiesterase. DR InterPro; IPR047538; KH-I_ASCC1. DR InterPro; IPR004088; KH_dom_type_1. DR InterPro; IPR036612; KH_dom_type_1_sf. DR PANTHER; PTHR13360; ACTIVATING SIGNAL COINTEGRATOR 1 COMPLEX SUBUNIT 1; 1. DR PANTHER; PTHR13360:SF1; ACTIVATING SIGNAL COINTEGRATOR 1 COMPLEX SUBUNIT 1; 1. DR Pfam; PF10469; AKAP7_NLS; 1. DR Pfam; PF00013; KH_1; 1. DR PIRSF; PIRSF027019; Euk_LigT; 1. DR SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1. DR SUPFAM; SSF55144; LigT-like; 1. DR PROSITE; PS50084; KH_TYPE_1; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Direct protein sequencing; DNA damage; KW DNA repair; Neurodegeneration; Nucleus; Proteomics identification; KW Reference proteome; Transcription; Transcription regulation. FT CHAIN 1..400 FT /note="Activating signal cointegrator 1 complex subunit 1" FT /id="PRO_0000050100" FT DOMAIN 86..148 FT /note="KH" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117" FT REGION 1..53 FT /note="Required for interaction with ASCC3" FT /evidence="ECO:0000269|PubMed:29997253" FT VAR_SEQ 71..99 FT /note="NLIHLNTSNDCGFQKITLDCQNIYTWKSR -> K (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10810093, FT ECO:0000303|PubMed:12077347, ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_011007" FT VAR_SEQ 348..400 FT /note="SFALLPRLEYNDAISAHCNLCLPGSSDSPASASQVAGITGVSDAYSQSLPGK FT S -> LFENFYFGSLKLNSIHISQRFTVDSFGNYASCGQIDFS (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10810093, FT ECO:0000303|PubMed:12077347, ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_011008" FT VARIANT 34 FT /note="D -> N (in dbSNP:rs11558719)" FT /id="VAR_061278" FT VARIANT 318 FT /note="N -> S (found in patients with Barrett esophagus; FT dbSNP:rs146370051)" FT /evidence="ECO:0000269|PubMed:21791690" FT /id="VAR_066588" FT CONFLICT 11 FT /note="I -> F (in Ref. 1; AAG45476 and 2; AAD27727)" FT /evidence="ECO:0000305" FT CONFLICT 240..243 FT /note="SGGK -> PGR (in Ref. 1; AAG45476 and 2; AAD27727)" FT /evidence="ECO:0000305" FT CONFLICT 250 FT /note="A -> P (in Ref. 1; AAG45476 and 2; AAD27727)" FT /evidence="ECO:0000305" SQ SEQUENCE 400 AA; 45509 MW; DAD067C98CE71DDB CRC64; MEVLRPQLIR IDGRNYRKNP VQEQTYQHEE DEEDFYQGSM ECADEPCDAY EVEQTPQGFR STLRAPSLLY NLIHLNTSND CGFQKITLDC QNIYTWKSRH IVGKRGDTRK KIEMETKTSI SIPKPGQDGE IVITGQHRNG VISARTRIDV LLDTFRRKQP FTHFLAFFLN EVEVQEGFLR FQEEVLAKCS MDHGVDSSIF QNPKKLHLTI GMLVLLSEEE IQQTCEMLQQ CKEEFINDIS GGKPLEVEMA GIEYMNDDPG MVDVLYAKVH MKDGSNRLQE LVDRVLERFQ ASGLIVKEWN SVKLHATVMN TLFRKDPNAE GRYNLYTAEG KYIFKERESF DGRNILKSFA LLPRLEYNDA ISAHCNLCLP GSSDSPASAS QVAGITGVSD AYSQSLPGKS //