YJU2_HUMAN
ID YJU2_HUMAN Reviewed; 323 AA.
AC Q9BW85; O75270; Q9H862; Q9NW16;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
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|HGNC:HGNC:25518};
GN Synonyms=CCDC94 {ECO:0000312|HGNC:HGNC:25518};
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 [LARGE SCALE MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Barrow I.K.-P., Boguski M.S., Touchman J.W., Spencer F.;
RT "Full-insert sequence of mapped XREF EST.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Lung;
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=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211; SER-213 AND SER-220, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211 AND SER-213, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211 AND SER-213, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211 AND SER-213, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
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=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [11]
RP FUNCTION.
RX PubMed=22952453; DOI=10.1371/journal.pgen.1002922;
RA Sorrells S., Carbonneau S., Harrington E., Chen A.T., Hast B., Milash B.,
RA Pyati U., Major M.B., Zhou Y., Zon L.I., Stewart R.A., Look A.T., Jette C.;
RT "Ccdc94 protects cells from ionizing radiation by inhibiting the expression
RT of p53.";
RL PLoS Genet. 8:E1002922-E1002922(2012).
RN [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (4.1 ANGSTROMS) OF C COMPLEX, SUBCELLULAR
RP LOCATION, AND FUNCTION.
RX PubMed=29301961; DOI=10.1126/science.aar6401;
RA Zhan X., Yan C., Zhang X., Lei J., Shi Y.;
RT "Structure of a human catalytic step I spliceosome.";
RL Science 359:537-545(2018).
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 (PubMed:29301961). Plays a role in stabilizing the
CC structure of the spliceosome catalytic core and docking of the branch
CC helix into the active site, producing 5'-exon and lariat intron-3'-
CC intermediates (By similarity). May protect cells from TP53-dependent
CC apoptosis upon dsDNA break damage through association with PRP19-CD5L
CC complex (PubMed:22952453). {ECO:0000255|HAMAP-Rule:MF_03226,
CC ECO:0000269|PubMed:22952453, ECO:0000269|PubMed:29301961}.
CC -!- SUBUNIT: Component of the spliceosome (PubMed:29301961). Present in the
CC activated B complex, the catalytically activated B* complex which
CC catalyzes the branching, the catalytic step 1 C complex catalyzing the
CC exon ligation, and the postcatalytic P complex containing the ligated
CC exons (mRNA) and the excised lariat intron (By similarity). Identified
CC in the spliceosome C complex; in the complex interacts directly with
CC PRP16 (PubMed:29301961). {ECO:0000255|HAMAP-Rule:MF_03226,
CC ECO:0000269|PubMed:29301961}.
CC -!- INTERACTION:
CC Q9BW85; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-10300345, EBI-11524452;
CC Q9BW85; Q7Z569: BRAP; NbExp=3; IntAct=EBI-10300345, EBI-349900;
CC Q9BW85; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-10300345, EBI-10961624;
CC Q9BW85; Q8NHQ1: CEP70; NbExp=6; IntAct=EBI-10300345, EBI-739624;
CC Q9BW85; O95995: GAS8; NbExp=3; IntAct=EBI-10300345, EBI-1052570;
CC Q9BW85; Q08379: GOLGA2; NbExp=8; IntAct=EBI-10300345, EBI-618309;
CC Q9BW85; Q9NYA3: GOLGA6A; NbExp=3; IntAct=EBI-10300345, EBI-11163335;
CC Q9BW85; Q6IE81: JADE1; NbExp=3; IntAct=EBI-10300345, EBI-954672;
CC Q9BW85; Q6IE81-3: JADE1; NbExp=3; IntAct=EBI-10300345, EBI-12120084;
CC Q9BW85; Q92993: KAT5; NbExp=3; IntAct=EBI-10300345, EBI-399080;
CC Q9BW85; Q9Y6D9: MAD1L1; NbExp=3; IntAct=EBI-10300345, EBI-742610;
CC Q9BW85; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-10300345, EBI-16439278;
CC Q9BW85; Q04864-2: REL; NbExp=3; IntAct=EBI-10300345, EBI-10829018;
CC Q9BW85; Q12800: TFCP2; NbExp=6; IntAct=EBI-10300345, EBI-717422;
CC Q9BW85; Q9C019: TRIM15; NbExp=3; IntAct=EBI-10300345, EBI-2342111;
CC Q9BW85; P19474: TRIM21; NbExp=3; IntAct=EBI-10300345, EBI-81290;
CC Q9BW85; P14373: TRIM27; NbExp=3; IntAct=EBI-10300345, EBI-719493;
CC Q9BW85; P52747: ZNF143; NbExp=3; IntAct=EBI-10300345, EBI-2849334;
CC Q9BW85; Q8TF50: ZNF526; NbExp=3; IntAct=EBI-10300345, EBI-11035148;
CC Q9BW85; Q3KNS6-3: ZNF829; NbExp=3; IntAct=EBI-10300345, EBI-18036029;
CC Q9BW85; A0A384NQ31; NbExp=3; IntAct=EBI-10300345, EBI-12903728;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|HAMAP-Rule:MF_03226,
CC ECO:0000269|PubMed:29301961}.
CC -!- SIMILARITY: Belongs to the CWC16 family. YJU2 subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_03226}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC72949.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK001236; BAA91572.1; -; mRNA.
DR EMBL; AK023988; BAB14757.1; -; mRNA.
DR EMBL; AF091080; AAC72949.1; ALT_FRAME; mRNA.
DR EMBL; BC000561; AAH00561.1; -; mRNA.
DR EMBL; BC019096; AAH19096.1; -; mRNA.
DR CCDS; CCDS12124.1; -.
DR RefSeq; NP_060544.2; NM_018074.5.
DR PDB; 5YZG; EM; 4.10 A; Y=1-323.
DR PDB; 6ZYM; EM; 3.40 A; u=1-178.
DR PDB; 7A5P; EM; 5.00 A; u=1-323.
DR PDBsum; 5YZG; -.
DR PDBsum; 6ZYM; -.
DR PDBsum; 7A5P; -.
DR AlphaFoldDB; Q9BW85; -.
DR SMR; Q9BW85; -.
DR BioGRID; 120827; 70.
DR IntAct; Q9BW85; 58.
DR MINT; Q9BW85; -.
DR STRING; 9606.ENSP00000262962; -.
DR iPTMnet; Q9BW85; -.
DR MetOSite; Q9BW85; -.
DR PhosphoSitePlus; Q9BW85; -.
DR BioMuta; CCDC94; -.
DR DMDM; 74733407; -.
DR EPD; Q9BW85; -.
DR jPOST; Q9BW85; -.
DR MassIVE; Q9BW85; -.
DR MaxQB; Q9BW85; -.
DR PaxDb; Q9BW85; -.
DR PeptideAtlas; Q9BW85; -.
DR PRIDE; Q9BW85; -.
DR ProteomicsDB; 79263; -.
DR Antibodypedia; 42411; 130 antibodies from 21 providers.
DR DNASU; 55702; -.
DR Ensembl; ENST00000262962.12; ENSP00000262962.6; ENSG00000105248.16.
DR GeneID; 55702; -.
DR KEGG; hsa:55702; -.
DR MANE-Select; ENST00000262962.12; ENSP00000262962.6; NM_018074.6; NP_060544.2.
DR UCSC; uc002lzv.5; human.
DR CTD; 55702; -.
DR DisGeNET; 55702; -.
DR GeneCards; YJU2; -.
DR HGNC; HGNC:25518; YJU2.
DR HPA; ENSG00000105248; Low tissue specificity.
DR neXtProt; NX_Q9BW85; -.
DR OpenTargets; ENSG00000105248; -.
DR PharmGKB; PA144596461; -.
DR VEuPathDB; HostDB:ENSG00000105248; -.
DR eggNOG; KOG2989; Eukaryota.
DR GeneTree; ENSGT00530000063615; -.
DR HOGENOM; CLU_053603_0_1_1; -.
DR InParanoid; Q9BW85; -.
DR OMA; LMTVRLM; -.
DR OrthoDB; 1583452at2759; -.
DR PhylomeDB; Q9BW85; -.
DR TreeFam; TF315070; -.
DR PathwayCommons; Q9BW85; -.
DR SignaLink; Q9BW85; -.
DR BioGRID-ORCS; 55702; 780 hits in 1053 CRISPR screens.
DR ChiTaRS; CCDC94; human.
DR GenomeRNAi; 55702; -.
DR Pharos; Q9BW85; Tdark.
DR PRO; PR:Q9BW85; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9BW85; protein.
DR Bgee; ENSG00000105248; Expressed in granulocyte and 166 other tissues.
DR ExpressionAtlas; Q9BW85; baseline and differential.
DR Genevisible; Q9BW85; HS.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IDA: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 3D-structure; Metal-binding; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Spliceosome; Zinc.
FT CHAIN 1..323
FT /note="Splicing factor YJU2"
FT /id="PRO_0000234018"
FT REGION 207..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..323
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:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D6J3"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9D6J3"
FT CONFLICT 105
FT /note="T -> A (in Ref. 1; BAA91572)"
FT /evidence="ECO:0000305"
FT CONFLICT 247
FT /note="W -> R (in Ref. 1; BAB14757)"
FT /evidence="ECO:0000305"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 42..47
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 55..63
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:6ZYM"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:6ZYM"
FT HELIX 134..161
FT /evidence="ECO:0007829|PDB:6ZYM"
FT HELIX 167..175
FT /evidence="ECO:0007829|PDB:6ZYM"
SQ SEQUENCE 323 AA; 37086 MW; 8E1BB92C4A008BB5 CRC64;
MSERKVLNKY YPPDFDPSKI PKLKLPKDRQ YVVRLMAPFN MRCKTCGEYI YKGKKFNARK
ETVQNEVYLG LPIFRFYIKC TRCLAEITFK TDPENTDYTM EHGATRNFQA EKLLEEEEKR
VQKEREDEEL NNPMKVLENR TKDSKLEMEV LENLQELKDL NQRQAHVDFE AMLRQHRLSE
EERRRQQQEE DEQETAALLE EARKRRLLED SDSEDEAAPS PLQPALRPNP TAILDEAPKP
KRKVEVWEQS VGSLGSRPPL SRLVVVKKAK ADPDCSNGQP QAAPTPGAPQ NRKEANPTPL
TPGASSLSQL GAYLDSDDSN GSN
