YJU2_MOUSE
ID YJU2_MOUSE Reviewed; 314 AA.
AC Q9D6J3;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Splicing factor YJU2 {ECO:0000255|HAMAP-Rule:MF_03226};
DE AltName: Full=Coiled-coil domain-containing protein 94 {ECO:0000305};
GN Name=Yju2 {ECO:0000255|HAMAP-Rule:MF_03226, ECO:0000312|MGI:MGI:1920136};
GN Synonyms=Ccdc94 {ECO:0000312|MGI:MGI:1920136};
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; TISSUE=Hippocampus;
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 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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211 AND SER-213, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211 AND SER-213, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211; SER-213; SER-309;
RP SER-312 AND SER-314, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen, and
RC 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).
CC -!- FUNCTION: Part of the spliceosome which catalyzes two sequential
CC transesterification reactions, first the excision of the non-coding
CC intron from pre-mRNA and then the ligation of the coding exons to form
CC the mature mRNA. Plays a role in stabilizing the structure of the
CC spliceosome catalytic core and docking of the branch helix into the
CC active site, producing 5'-exon and lariat intron-3'-intermediates. May
CC protect cells from TP53-dependent apoptosis upon dsDNA break damage
CC through association with PRP19-CD5L complex. {ECO:0000255|HAMAP-
CC Rule:MF_03226}.
CC -!- SUBUNIT: Component of the spliceosome. Present in the activated B
CC complex, the catalytically activated B* complex which catalyzes the
CC branching, the catalytic step 1 C complex catalyzing the exon ligation,
CC and the postcatalytic P complex containing the ligated exons (mRNA) and
CC the excised lariat intron. {ECO:0000255|HAMAP-Rule:MF_03226}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BW85,
CC ECO:0000255|HAMAP-Rule:MF_03226}.
CC -!- SIMILARITY: Belongs to the CWC16 family. YJU2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03226}.
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DR EMBL; AK013533; BAB28900.1; -; mRNA.
DR EMBL; BC031400; AAH31400.1; -; mRNA.
DR CCDS; CCDS37660.1; -.
DR RefSeq; NP_082657.1; NM_028381.3.
DR AlphaFoldDB; Q9D6J3; -.
DR SMR; Q9D6J3; -.
DR BioGRID; 215624; 1.
DR STRING; 10090.ENSMUSP00000084082; -.
DR iPTMnet; Q9D6J3; -.
DR PhosphoSitePlus; Q9D6J3; -.
DR EPD; Q9D6J3; -.
DR jPOST; Q9D6J3; -.
DR MaxQB; Q9D6J3; -.
DR PaxDb; Q9D6J3; -.
DR PeptideAtlas; Q9D6J3; -.
DR PRIDE; Q9D6J3; -.
DR ProteomicsDB; 281420; -.
DR Antibodypedia; 42411; 130 antibodies from 21 providers.
DR DNASU; 72886; -.
DR Ensembl; ENSMUST00000086869; ENSMUSP00000084082; ENSMUSG00000003208.
DR GeneID; 72886; -.
DR KEGG; mmu:72886; -.
DR UCSC; uc008dak.1; mouse.
DR CTD; 55702; -.
DR MGI; MGI:1920136; Yju2.
DR VEuPathDB; HostDB:ENSMUSG00000003208; -.
DR eggNOG; KOG2989; Eukaryota.
DR GeneTree; ENSGT00530000063615; -.
DR HOGENOM; CLU_053603_0_1_1; -.
DR InParanoid; Q9D6J3; -.
DR OMA; LMTVRLM; -.
DR OrthoDB; 1583452at2759; -.
DR PhylomeDB; Q9D6J3; -.
DR TreeFam; TF315070; -.
DR BioGRID-ORCS; 72886; 24 hits in 71 CRISPR screens.
DR ChiTaRS; Ccdc94; mouse.
DR PRO; PR:Q9D6J3; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9D6J3; protein.
DR Bgee; ENSMUSG00000003208; Expressed in lumbar dorsal root ganglion and 233 other tissues.
DR ExpressionAtlas; Q9D6J3; baseline and differential.
DR Genevisible; Q9D6J3; MM.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000349; P:generation of catalytic spliceosome for first transesterification step; IEA:UniProtKB-UniRule.
DR GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IBA:GO_Central.
DR HAMAP; MF_03226; YJU2; 1.
DR InterPro; IPR007590; Saf4/Yju2.
DR InterPro; IPR043701; Yju2.
DR PANTHER; PTHR12111; PTHR12111; 1.
DR Pfam; PF04502; Saf4_Yju2; 1.
PE 1: Evidence at protein level;
KW Metal-binding; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Spliceosome; Zinc.
FT CHAIN 1..314
FT /note="Splicing factor YJU2"
FT /id="PRO_0000234019"
FT REGION 178..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03226"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03226"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03226"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03226"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BW85"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 314 AA; 35988 MW; 04B5A40B742CBA4A CRC64;
MSERKVLNKY YPPDFDPSKI PKLKLPKDRQ YVVRLMAPFN MRCKTCGEYI YKGKKFNARK
ETVQNEAYLG LPIFRFYIKC TRCLAEITFK TDPENTDYTM EHGATRNFQA EKLLEEEEKR
VQKEREDEEL NNPMKVLENR TKDSKLEMEV LENLQELKDL NQRQAHVDFE AMLRQHRMSQ
EQWQQQQEEE DERETAALLE EARHRRLLED SESEDEAPPS RPRAAARPNP TAILNEVPQT
KRKAEALCSK AQLAGLVVPK KVKTEANGAS EQVGVPTAAG APKSRKADNP TPQTPGTSSL
SQLGAYGDSE DSDS
