ASCC1_HUMAN
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 03-AUG-2022, entry version 173.
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:29144457, PubMed:22055184). 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; 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.
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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_001198799.2. [Q8N9N2-1]
DR RefSeq; NP_001185729.1; NM_001198800.2. [Q8N9N2-2]
DR RefSeq; XP_006717936.1; XM_006717873.3.
DR AlphaFoldDB; Q8N9N2; -.
DR SMR; Q8N9N2; -.
DR BioGRID; 119215; 64.
DR ComplexPortal; CPX-6641; ASCC DNA alkylation repair complex.
DR CORUM; Q8N9N2; -.
DR IntAct; Q8N9N2; 38.
DR STRING; 9606.ENSP00000339404; -.
DR GlyGen; Q8N9N2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8N9N2; -.
DR PhosphoSitePlus; Q8N9N2; -.
DR BioMuta; ASCC1; -.
DR DMDM; 50400556; -.
DR EPD; Q8N9N2; -.
DR jPOST; Q8N9N2; -.
DR MassIVE; Q8N9N2; -.
DR MaxQB; Q8N9N2; -.
DR PaxDb; Q8N9N2; -.
DR PeptideAtlas; Q8N9N2; -.
DR PRIDE; Q8N9N2; -.
DR ProteomicsDB; 72561; -. [Q8N9N2-1]
DR ProteomicsDB; 72562; -. [Q8N9N2-2]
DR Antibodypedia; 29224; 200 antibodies from 22 providers.
DR DNASU; 51008; -.
DR Ensembl; ENST00000317126.8; ENSP00000320461.4; ENSG00000138303.18. [Q8N9N2-2]
DR Ensembl; ENST00000342444.8; ENSP00000339404.4; ENSG00000138303.18. [Q8N9N2-1]
DR Ensembl; ENST00000394915.7; ENSP00000378373.3; ENSG00000138303.18. [Q8N9N2-1]
DR Ensembl; ENST00000394919.5; ENSP00000378377.1; ENSG00000138303.18. [Q8N9N2-2]
DR Ensembl; ENST00000672957.1; ENSP00000500935.1; ENSG00000138303.18. [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 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 neXtProt; NX_Q8N9N2; -.
DR OpenTargets; ENSG00000138303; -.
DR Orphanet; 486811; Prenatal-onset spinal muscular atrophy with congenital bone fractures.
DR PharmGKB; PA134974899; -.
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; 900867at2759; -.
DR PhylomeDB; Q8N9N2; -.
DR TreeFam; TF314479; -.
DR PathwayCommons; Q8N9N2; -.
DR Reactome; R-HSA-112126; ALKBH3 mediated reversal of alkylation damage.
DR SignaLink; Q8N9N2; -.
DR BioGRID-ORCS; 51008; 25 hits in 1079 CRISPR screens.
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 198 other tissues.
DR ExpressionAtlas; Q8N9N2; baseline and differential.
DR Genevisible; Q8N9N2; HS.
DR GO; GO:1990391; C:DNA repair complex; IPI:ComplexPortal.
DR GO; GO:0031594; C:neuromuscular junction; IMP: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:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
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:MGI.
DR Gene3D; 3.30.1370.10; -; 1.
DR InterPro; IPR009210; ASCC1.
DR InterPro; IPR009097; Cyclic_Pdiesterase.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR019510; Kinase-A_anchor_nucl_local_sig.
DR PANTHER; PTHR13360; PTHR13360; 1.
DR Pfam; PF10469; AKAP7_NLS; 1.
DR Pfam; PF00013; KH_1; 1.
DR PIRSF; PIRSF027019; Euk_LigT; 1.
DR SUPFAM; SSF54791; SSF54791; 1.
DR SUPFAM; SSF55144; SSF55144; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Direct protein sequencing; DNA damage; DNA repair;
KW Neurodegeneration; Nucleus; Reference proteome; Transcription;
KW 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
