CWC15_MOUSE
ID CWC15_MOUSE Reviewed; 229 AA.
AC Q9JHS9; Q3TH98; Q9CTH0;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Spliceosome-associated protein CWC15 homolog;
DE AltName: Full=Embryonic development factor 1;
DE Short=mED1;
GN Name=Cwc15; Synonyms=Ed1;
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 [MRNA].
RX PubMed=10873569; DOI=10.1006/bbrc.2000.2910;
RA O'Brien K.P., Tapia-Paez I., Staahle-Baeckdahl M., Kedra D., Dumanski J.P.;
RT "Characterization of five novel human genes in the 11q13-q22 region.";
RL Biochem. Biophys. Res. Commun. 273:90-94(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=KM;
RA Duan J.-Z., Zhang J.-P.;
RT "mED1 (mouse embryonic development factor 1).";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Kidney, and Mammary gland;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 THR-110, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Spleen, and Testis;
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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-18, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Involved in pre-mRNA splicing as component of the
CC spliceosome. Component of the PRP19-CDC5L complex that forms an
CC integral part of the spliceosome and is required for activating pre-
CC mRNA splicing. {ECO:0000250|UniProtKB:Q9P013}.
CC -!- SUBUNIT: Identified in the spliceosome C complex. Component of the
CC PRP19-CDC5L splicing complex composed of a core complex comprising a
CC homotetramer of PRPF19, CDC5L, PLRG1 and BCAS2, and at least three less
CC stably associated proteins CTNNBL1, CWC15 and HSPA8. Interacts directly
CC with CTNNBL1 in the complex. {ECO:0000250|UniProtKB:Q9P013}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9P013}.
CC -!- SIMILARITY: Belongs to the CWC15 family. {ECO:0000305}.
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DR EMBL; AJ250394; CAB96547.1; -; mRNA.
DR EMBL; AY842452; AAW32096.1; -; mRNA.
DR EMBL; AK002864; BAB22414.1; -; mRNA.
DR EMBL; AK003202; BAB22638.1; -; mRNA.
DR EMBL; AK003591; BAB22880.1; -; mRNA.
DR EMBL; AK003834; BAB23026.1; -; mRNA.
DR EMBL; AK145249; BAE26327.1; -; mRNA.
DR EMBL; AK167776; BAE39808.1; -; mRNA.
DR EMBL; AK168365; BAE40300.1; -; mRNA.
DR EMBL; BC004726; AAH04726.1; -; mRNA.
DR CCDS; CCDS22823.1; -.
DR RefSeq; NP_075642.1; NM_023153.3.
DR RefSeq; XP_006510600.1; XM_006510537.3.
DR AlphaFoldDB; Q9JHS9; -.
DR BioGRID; 211192; 21.
DR ComplexPortal; CPX-5825; PRP19-CDC5L complex.
DR IntAct; Q9JHS9; 3.
DR MINT; Q9JHS9; -.
DR STRING; 10090.ENSMUSP00000004200; -.
DR iPTMnet; Q9JHS9; -.
DR PhosphoSitePlus; Q9JHS9; -.
DR EPD; Q9JHS9; -.
DR jPOST; Q9JHS9; -.
DR MaxQB; Q9JHS9; -.
DR PaxDb; Q9JHS9; -.
DR PeptideAtlas; Q9JHS9; -.
DR PRIDE; Q9JHS9; -.
DR ProteomicsDB; 284069; -.
DR Antibodypedia; 70625; 81 antibodies from 17 providers.
DR DNASU; 66070; -.
DR Ensembl; ENSMUST00000004200; ENSMUSP00000004200; ENSMUSG00000004096.
DR Ensembl; ENSMUST00000213913; ENSMUSP00000149476; ENSMUSG00000004096.
DR GeneID; 66070; -.
DR KEGG; mmu:66070; -.
DR UCSC; uc009oeo.1; mouse.
DR CTD; 51503; -.
DR MGI; MGI:1913320; Cwc15.
DR VEuPathDB; HostDB:ENSMUSG00000004096; -.
DR eggNOG; KOG3228; Eukaryota.
DR GeneTree; ENSGT00390000012084; -.
DR HOGENOM; CLU_068312_0_1_1; -.
DR InParanoid; Q9JHS9; -.
DR OMA; NCARSEP; -.
DR OrthoDB; 1576404at2759; -.
DR PhylomeDB; Q9JHS9; -.
DR TreeFam; TF321323; -.
DR Reactome; R-MMU-72163; mRNA Splicing - Major Pathway.
DR BioGRID-ORCS; 66070; 20 hits in 74 CRISPR screens.
DR ChiTaRS; Cwc15; mouse.
DR PRO; PR:Q9JHS9; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9JHS9; protein.
DR Bgee; ENSMUSG00000004096; Expressed in ventricular zone and 262 other tissues.
DR ExpressionAtlas; Q9JHS9; baseline and differential.
DR Genevisible; Q9JHS9; MM.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0000974; C:Prp19 complex; ISO:MGI.
DR GO; GO:0005681; C:spliceosomal complex; ISS:UniProtKB.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; ISS:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; ISS:UniProtKB.
DR InterPro; IPR006973; Cwf_Cwc_15.
DR PANTHER; PTHR12718; PTHR12718; 1.
DR Pfam; PF04889; Cwf_Cwc_15; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Spliceosome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9P013"
FT CHAIN 2..229
FT /note="Spliceosome-associated protein CWC15 homolog"
FT /id="PRO_0000291544"
FT REGION 1..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 123..165
FT /evidence="ECO:0000255"
FT COMPBIAS 35..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..127
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P013"
FT MOD_RES 18
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 47
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9P013"
FT MOD_RES 110
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P013"
FT CONFLICT 223
FT /note="F -> L (in Ref. 3; BAE40300/BAE39808)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 229 AA; 26624 MW; A8AE6F44423EA7DC CRC64;
MTTAARPTFE PARGGRGKGE GDLSQLSKQY SSRDLPSHTK IKYRQTTQDA PEEVRNRDFR
RELEERERAA ARDKNRDRPT REHTTSSSVS KKPRLDQIPA ANLDADDPLT DEEDEDFEEE
SDDDDTAALL AELEKIKKER AEEQARKEQE QKAEEERIRM ENILSGNPLL NLTGPSQPQA
NFKVKRRWDD DVVFKNCAKG IDDQKKDKRF VNDTLRSEFH KKFMEKYIK
