ASCC1_MOUSE
ID ASCC1_MOUSE Reviewed; 356 AA.
AC Q9D8Z1; Q3TAC2;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Activating signal cointegrator 1 complex subunit 1;
DE AltName: Full=ASC-1 complex subunit p50;
DE AltName: Full=Trip4 complex subunit p50;
GN Name=Ascc1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Egg, Pancreas, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Retina;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
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).
CC -!- FUNCTION: Plays a role in DNA damage repair as component of the ASCC
CC complex. Part of the ASC-1 complex that enhances NF-kappa-B, SRF and
CC AP1 transactivation. In cells responding to gastrin-activated paracrine
CC signals, it is involved in the induction of SERPINB2 expression by
CC gastrin. May also play a role in the development of neuromuscular
CC junction. {ECO:0000250|UniProtKB:Q8N9N2}.
CC -!- SUBUNIT: Identified in the ASCC complex that contains ASCC1, ASCC2 and
CC ASCC3. Interacts directly with ASCC3. The ASCC complex interacts with
CC ALKBH3. Part of the ASC-1 complex, that contains TRIP4, ASCC1, ASCC2
CC and ASCC3. Interacts with CSRP1. Interacts with ZCCHC4 (By similarity).
CC {ECO:0000250|UniProtKB:Q8N9N2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8N9N2}. Nucleus
CC speckle {ECO:0000250|UniProtKB:Q8N9N2}. Note=Colocalizes with PRPF8 in
CC nuclear speckles in the absence of DNA damage.
CC {ECO:0000250|UniProtKB:Q8N9N2}.
CC -!- TISSUE SPECIFICITY: Expressed in the spinal cord, brain, paraspinal
CC ganglia, thyroid, and submandibular glands.
CC {ECO:0000269|PubMed:26924529}.
CC -!- DEVELOPMENTAL STAGE: Expressed in 17.5-day-old embryos.
CC {ECO:0000269|PubMed:26924529}.
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DR EMBL; AK007519; BAB25087.1; -; mRNA.
DR EMBL; AK139944; BAE24191.1; -; mRNA.
DR EMBL; AK171958; BAE42747.1; -; mRNA.
DR EMBL; BC030905; AAH30905.1; -; mRNA.
DR CCDS; CCDS23870.1; -.
DR RefSeq; NP_001186116.1; NM_001199187.2.
DR RefSeq; NP_081213.1; NM_026937.3.
DR RefSeq; XP_006514103.1; XM_006514040.3.
DR AlphaFoldDB; Q9D8Z1; -.
DR SMR; Q9D8Z1; -.
DR BioGRID; 213222; 3.
DR STRING; 10090.ENSMUSP00000052351; -.
DR iPTMnet; Q9D8Z1; -.
DR PhosphoSitePlus; Q9D8Z1; -.
DR EPD; Q9D8Z1; -.
DR MaxQB; Q9D8Z1; -.
DR PaxDb; Q9D8Z1; -.
DR PeptideAtlas; Q9D8Z1; -.
DR PRIDE; Q9D8Z1; -.
DR ProteomicsDB; 265116; -.
DR Antibodypedia; 29224; 200 antibodies from 22 providers.
DR Ensembl; ENSMUST00000050516; ENSMUSP00000052351; ENSMUSG00000044475.
DR Ensembl; ENSMUST00000164083; ENSMUSP00000126301; ENSMUSG00000044475.
DR GeneID; 69090; -.
DR KEGG; mmu:69090; -.
DR UCSC; uc007feh.2; mouse.
DR CTD; 51008; -.
DR MGI; MGI:1916340; Ascc1.
DR VEuPathDB; HostDB:ENSMUSG00000044475; -.
DR eggNOG; KOG2814; Eukaryota.
DR GeneTree; ENSGT00390000018119; -.
DR HOGENOM; CLU_044606_0_0_1; -.
DR InParanoid; Q9D8Z1; -.
DR OMA; ISERCIH; -.
DR OrthoDB; 675008at2759; -.
DR PhylomeDB; Q9D8Z1; -.
DR TreeFam; TF314479; -.
DR BioGRID-ORCS; 69090; 5 hits in 75 CRISPR screens.
DR ChiTaRS; Ascc1; mouse.
DR PRO; PR:Q9D8Z1; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q9D8Z1; protein.
DR Bgee; ENSMUSG00000044475; Expressed in right kidney and 255 other tissues.
DR Genevisible; Q9D8Z1; MM.
DR GO; GO:1990391; C:DNA repair complex; ISO:MGI.
DR GO; GO:0031594; C:neuromuscular junction; ISS:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; ISO:MGI.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR Gene3D; 3.30.1370.10; -; 1.
DR InterPro; IPR009210; ASCC1.
DR InterPro; IPR004087; KH_dom.
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 SMART; SM00322; KH; 1.
DR SUPFAM; SSF54791; SSF54791; 1.
DR PROSITE; PS50084; KH_TYPE_1; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..356
FT /note="Activating signal cointegrator 1 complex subunit 1"
FT /id="PRO_0000050101"
FT DOMAIN 57..119
FT /note="KH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 1..52
FT /note="Required for interaction with ASCC3"
FT /evidence="ECO:0000250|UniProtKB:Q8N9N2"
SQ SEQUENCE 356 AA; 41280 MW; E3DBC53A80B439AE CRC64;
MDVLRPQIVT FDGRNYRKNP IQEKQYQHEE DEDFYPDSME YSDEPCGAYE VAQTPHGFRA
TVSAPSLLYK HIVGKRGDTK KKIEVETKTS INIPKHGHEG EIVITGQHRN GVVSARTRID
VLLDTFRRRQ PFTHFLSFFL NEVEVQERFL MFQEEVLRKC SKDRGVDSTI FQNPKKLHLT
IGMLVLLSEQ EIQQTCEILQ RCKEEFINDI SGGRPLEVEM AGIEYMNDDP AMVDVLYAKV
HMKDGSNRLQ ELVDRVLERF QSLGLIVKEW TSVKLHATVM NTLLRKDPNA EGRYNLYTAD
GKYIFKERES FDGRNILKTF ENFYFGSLRL NSIHISQRFT VDSFGNYASC GHVDFS
