ASCC2_MOUSE
ID ASCC2_MOUSE Reviewed; 749 AA.
AC Q91WR3; Q5NCK1; Q8BKM9; Q8BX60; Q8R1B9;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Activating signal cointegrator 1 complex subunit 2;
DE AltName: Full=ASC-1 complex subunit p100;
DE AltName: Full=Trip4 complex subunit p100;
GN Name=Ascc2; Synonyms=Asc1p100;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Eye, and Spinal ganglion;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND PARTIAL NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Eye, and Kidney;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Pancreas, and 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).
CC -!- FUNCTION: Plays a role in DNA damage repair as component of the ASCC
CC complex (By similarity). Recruits ASCC3 and ALKBH3 to sites of DNA
CC damage by binding to polyubiquitinated proteins that have 'Lys-63'-
CC linked polyubiquitin chains (By similarity). Part of the ASC-1 complex
CC that enhances NF-kappa-B, SRF and AP1 transactivation (By similarity).
CC Involved in activation of the ribosome quality control (RQC) pathway, a
CC pathway that degrades nascent peptide chains during problematic
CC translation (By similarity). As part of the ribosome quality control
CC trigger (RQT) complex, recognizes ZNF598-dependent ubiquitination of
CC stalled ribosomes (By similarity). {ECO:0000250|UniProtKB:P53137,
CC ECO:0000250|UniProtKB:Q9H1I8}.
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. Interacts (via CUE domain) with 'Lys-63'-linked polyubiquitin
CC chains, but not with 'Lys-48'-linked polyubiquitin chains. Part of the
CC ASC-1 complex, that contains TRIP4, ASCC1, ASCC2 and ASCC3. Component
CC of the RQT (ribosome quality control trigger) complex, that contains
CC ASCC2, ASCC3 and TRIP4. Interacts with TRIP4. Interacts with CSRP1.
CC Interacts with PRPF8, a component of the spliceosome. Interacts with
CC ZCCHC4 (By similarity). {ECO:0000250|UniProtKB:Q9H1I8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H1I8}. Nucleus
CC speckle {ECO:0000250|UniProtKB:Q9H1I8}. Note=Colocalizes with the
CC spliceosomal components PRPF8 and SNRNP200/BRR2 in nuclear foci when
CC cells have been exposed to alkylating agents that cause DNA damage.
CC Colocalizes with RNF113A and 'Lys-63'-linked polyubiquitinated
CC proteins, ALKBH3 and ASCC3 in nuclear foci when cells have been exposed
CC to alkylating agents that cause DNA damage.
CC {ECO:0000250|UniProtKB:Q9H1I8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q91WR3-1; Sequence=Displayed;
CC Name=2; Synonyms=100S;
CC IsoId=Q91WR3-2; Sequence=VSP_011012;
CC Name=3;
CC IsoId=Q91WR3-3; Sequence=VSP_011013;
CC -!- MISCELLANEOUS: [Isoform 3]: Incomplete sequence. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ASCC2 family. {ECO:0000305}.
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DR EMBL; AK048876; BAC33480.1; -; mRNA.
DR EMBL; AK051387; BAC34621.1; -; mRNA.
DR EMBL; AL606521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC013537; AAH13537.1; -; mRNA.
DR EMBL; BC024840; AAH24840.1; -; mRNA.
DR CCDS; CCDS24387.1; -. [Q91WR3-1]
DR RefSeq; NP_083567.1; NM_029291.1. [Q91WR3-1]
DR AlphaFoldDB; Q91WR3; -.
DR SMR; Q91WR3; -.
DR BioGRID; 217491; 2.
DR STRING; 10090.ENSMUSP00000063272; -.
DR iPTMnet; Q91WR3; -.
DR PhosphoSitePlus; Q91WR3; -.
DR EPD; Q91WR3; -.
DR MaxQB; Q91WR3; -.
DR PaxDb; Q91WR3; -.
DR PeptideAtlas; Q91WR3; -.
DR PRIDE; Q91WR3; -.
DR ProteomicsDB; 277254; -. [Q91WR3-1]
DR ProteomicsDB; 277255; -. [Q91WR3-2]
DR ProteomicsDB; 277256; -. [Q91WR3-3]
DR Antibodypedia; 224; 180 antibodies from 26 providers.
DR Ensembl; ENSMUST00000070257; ENSMUSP00000063272; ENSMUSG00000020412. [Q91WR3-1]
DR Ensembl; ENSMUST00000109930; ENSMUSP00000105556; ENSMUSG00000020412. [Q91WR3-2]
DR GeneID; 75452; -.
DR KEGG; mmu:75452; -.
DR UCSC; uc007hva.2; mouse. [Q91WR3-1]
DR UCSC; uc011xqz.2; mouse. [Q91WR3-2]
DR CTD; 84164; -.
DR MGI; MGI:1922702; Ascc2.
DR VEuPathDB; HostDB:ENSMUSG00000020412; -.
DR eggNOG; KOG4501; Eukaryota.
DR GeneTree; ENSGT00390000018806; -.
DR HOGENOM; CLU_012749_0_0_1; -.
DR InParanoid; Q91WR3; -.
DR OMA; DYQRQFP; -.
DR OrthoDB; 311659at2759; -.
DR PhylomeDB; Q91WR3; -.
DR TreeFam; TF323459; -.
DR BioGRID-ORCS; 75452; 11 hits in 76 CRISPR screens.
DR ChiTaRS; Ascc2; mouse.
DR PRO; PR:Q91WR3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q91WR3; protein.
DR Bgee; ENSMUSG00000020412; Expressed in paneth cell and 250 other tissues.
DR Genevisible; Q91WR3; MM.
DR GO; GO:0099053; C:activating signal cointegrator 1 complex; ISO:MGI.
DR GO; GO:1990391; C:DNA repair complex; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0072344; P:rescue of stalled ribosome; ISS:UniProtKB.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; ISS: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 Alternative splicing; DNA damage; DNA repair; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..749
FT /note="Activating signal cointegrator 1 complex subunit 2"
FT /id="PRO_0000064690"
FT DOMAIN 465..508
FT /note="CUE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00468"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 606..675
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 689..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 712..734
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 233
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1I8"
FT MOD_RES 625
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H1I8"
FT VAR_SEQ 522..561
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011012"
FT VAR_SEQ 733..749
FT /note="NRRTMADRKRSKGMIPS -> KSFCAPEMDYERPEGLRRGAELAVCPWCLSS
FT GCVCPC (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_011013"
SQ SEQUENCE 749 AA; 85653 MW; 9923D4BE00B7C3AB CRC64;
MPALPLDQLQ ITHKDPKTGQ PKTSAALNPE QKADRYFVLY KPPPKDNIPA LVEEYLERAN
FVANDLDWLL ALPHDKFWCQ VIFDETLQKC LDSYLHYVPR KFDEWVAPTP EVADMQNHLH
RSVFLTFLRM STHKESKDHF ISPSAFGEIL YNNFLFDIPK ILDLCVLFGK GNSPLLQKMI
GNIFTQQPSY YTDLDETIPT ILQVFSNILQ HCGLQGDGTS TTPQKLGERS PLTPSDMPLL
ELKDIVLYLC DTSTTLWAFL DIFPLACQTF QKHDFCYRLA SFYEMAIPEL ESAIKKRRLE
DSKLLGDMWQ RLSHSKKKLM EVFHIILNQI CLLPILESSC DNIQGFIEEF LQIFSSLLQE
KRFLRDYDTF SPVAEDISLL QQASSALDET RTAYILQAVE SAWEGVDRQK IKDIKDPPRA
KGSNNEVTVT AEPVSEMPSQ LENLEEDEEC MGAAAALGPA VSGVELDSLI SQVKDLLPDL
GEGFILACLE HYSYDSEQVI NNILEDRLAP ELSQLDRGLE RQVKPDPTPL LSSRHNIFQN
DEFDVFSRDS VDLSRVHKGR RKEENVRSLV NDKQAVVAQW QRYQKYSVVV EEVPLQPGEY
QADDYEDEYD DTYDGNQVGA NDADSDDELI SRRPFTIPQV LRTKMPGEVQ EEEWDEEDEV
EEEAPKPDHF IQDPAVLREK AEARRMAFLA RKGYRPENST AVTGGPRGHG QSRETTQERR
KKEANKAARA NHNRRTMADR KRSKGMIPS
