CWC22_HUMAN
ID CWC22_HUMAN Reviewed; 908 AA.
AC Q9HCG8; Q05DC2; Q4G135; Q52LF0; Q6PEX2; Q7Z6I0; Q9H5L3; Q9H6Q6;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Pre-mRNA-splicing factor CWC22 homolog;
DE AltName: Full=Nucampholin homolog;
DE AltName: Full=fSAPb;
GN Name=CWC22; Synonyms=KIAA1604, NCM;
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].
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hepatoma;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Eye, Lymph, Placenta, and Testis;
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 IDENTIFICATION IN THE SPLICEOSOME, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=12226669; DOI=10.1038/nature01031;
RA Zhou Z., Licklider L.J., Gygi S.P., Reed R.;
RT "Comprehensive proteomic analysis of the human spliceosome.";
RL Nature 419:182-185(2002).
RN [6]
RP IDENTIFICATION IN SPLICEOSOME C COMPLEX, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=11991638; DOI=10.1017/s1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [7]
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-829, AND IDENTIFICATION BY
RP 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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61 AND SER-829, 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 [12]
RP FUNCTION, INTERACTION WITH EIF4A3, AND MUTAGENESIS OF 171-ASN-LYS-172.
RX PubMed=22959432; DOI=10.1016/j.celrep.2012.08.017;
RA Steckelberg A.L., Boehm V., Gromadzka A.M., Gehring N.H.;
RT "CWC22 connects pre-mRNA splicing and exon junction complex assembly.";
RL Cell Rep. 2:454-461(2012).
RN [13]
RP FUNCTION, INTERACTION WITH EIF4A3, IDENTIFICATION IN SPLICEOSOME C COMPLEX,
RP AND SUBCELLULAR LOCATION.
RX PubMed=22961380; DOI=10.1038/nsmb.2380;
RA Barbosa I., Haque N., Fiorini F., Barrandon C., Tomasetto C.,
RA Blanchette M., Le Hir H.;
RT "Human CWC22 escorts the helicase eIF4AIII to spliceosomes and promotes
RT exon junction complex assembly.";
RL Nat. Struct. Mol. Biol. 19:983-990(2012).
RN [14]
RP FUNCTION, INTERACTION WITH EIF4A3, AND MUTAGENESIS OF GLY-168; ARG-331 AND
RP TYR-334.
RX PubMed=23236153; DOI=10.1073/pnas.1219725110;
RA Alexandrov A., Colognori D., Shu M.D., Steitz J.A.;
RT "Human spliceosomal protein CWC22 plays a role in coupling splicing to exon
RT junction complex deposition and nonsense-mediated decay.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:21313-21318(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39 AND SER-786, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16] {ECO:0007744|PDB:4C9B}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 116-406 IN COMPLEX WITH EIF4A3.
RX PubMed=24218557; DOI=10.1073/pnas.1314684110;
RA Buchwald G., Schussler S., Basquin C., Le Hir H., Conti E.;
RT "Crystal structure of the human eIF4AIII-CWC22 complex shows how a DEAD-box
RT protein is inhibited by a MIF4G domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E4611-E4618(2013).
RN [17] {ECO:0007744|PDB:5XJC}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=28502770; DOI=10.1016/j.cell.2017.04.033;
RA Zhang X., Yan C., Hang J., Finci L.I., Lei J., Shi Y.;
RT "An Atomic Structure of the Human Spliceosome.";
RL Cell 169:918-929(2017).
RN [18] {ECO:0007744|PDB:5MQF}
RP STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=28076346; DOI=10.1038/nature21079;
RA Bertram K., Agafonov D.E., Liu W.T., Dybkov O., Will C.L., Hartmuth K.,
RA Urlaub H., Kastner B., Stark H., Luhrmann R.;
RT "Cryo-EM structure of a human spliceosome activated for step 2 of
RT splicing.";
RL Nature 542:318-323(2017).
RN [19] {ECO:0007744|PDB:5Z56, ECO:0007744|PDB:5Z57, ECO:0007744|PDB:5Z58}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.90 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
RX PubMed=29360106; DOI=10.1038/cr.2018.14;
RA Zhang X., Yan C., Zhan X., Li L., Lei J., Shi Y.;
RT "Structure of the human activated spliceosome in three conformational
RT states.";
RL Cell Res. 28:307-322(2018).
RN [20] {ECO:0007744|PDB:5YZG}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.10 ANGSTROMS), FUNCTION, SUBCELLULAR
RP LOCATION, AND SUBUNIT.
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: Required for pre-mRNA splicing as component of the
CC spliceosome (PubMed:12226669, PubMed:11991638, PubMed:22961380,
CC PubMed:28502770, PubMed:28076346, PubMed:29360106, PubMed:29301961).
CC Promotes exon-junction complex (EJC) assembly (PubMed:22959432,
CC PubMed:22961380). Hinders EIF4A3 from non-specifically binding RNA and
CC escorts it to the splicing machinery to promote EJC assembly on mature
CC mRNAs. Through its role in EJC assembly, required for nonsense-mediated
CC mRNA decay. {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:12226669,
CC ECO:0000269|PubMed:22959432, ECO:0000269|PubMed:22961380,
CC ECO:0000269|PubMed:23236153, ECO:0000269|PubMed:28076346,
CC ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961,
CC ECO:0000269|PubMed:29360106}.
CC -!- SUBUNIT: Component of the pre-catalytic spliceosome B and the catalytic
CC spliceosome C complexes (PubMed:11991638, PubMed:22961380,
CC PubMed:28502770, PubMed:28076346, PubMed:29360106, PubMed:29301961).
CC Interacts with EIF4A3 and PRPF19 in an RNA-independent manner. Direct
CC interaction with EIF4A3 is mediated by the MIF4G domain
CC (PubMed:24218557). Full interaction with EIF4A3 occurs only when EIF4A3
CC is not part of the EJC and prevents EIF4A3 binding to RNA.
CC {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:12226669,
CC ECO:0000269|PubMed:22959432, ECO:0000269|PubMed:22961380,
CC ECO:0000269|PubMed:23236153, ECO:0000269|PubMed:24218557,
CC ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770,
CC ECO:0000269|PubMed:29301961, ECO:0000269|PubMed:29360106}.
CC -!- INTERACTION:
CC Q9HCG8; P38919: EIF4A3; NbExp=6; IntAct=EBI-373289, EBI-299104;
CC Q9HCG8; Q9Y421: FAM32A; NbExp=2; IntAct=EBI-373289, EBI-726146;
CC Q9HCG8; Q14331: FRG1; NbExp=2; IntAct=EBI-373289, EBI-2515248;
CC Q9HCG8; O95198: KLHL2; NbExp=3; IntAct=EBI-373289, EBI-746999;
CC Q9HCG8; Q16825: PTPN21; NbExp=3; IntAct=EBI-373289, EBI-2860264;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:29301961,
CC ECO:0000269|PubMed:29360106}. Nucleus speckle
CC {ECO:0000269|PubMed:22961380}. Note=Concentrates around speckles, which
CC are sites of pre-mRNA synthesis and processing, where it colocalizes
CC with EJC core proteins. {ECO:0000269|PubMed:22961380}.
CC -!- SIMILARITY: Belongs to the CWC22 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH16651.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH31216.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH57826.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAB13430.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB15197.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB15612.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB046824; BAB13430.1; ALT_INIT; mRNA.
DR EMBL; AK025635; BAB15197.1; ALT_FRAME; mRNA.
DR EMBL; AK026978; BAB15612.1; ALT_INIT; mRNA.
DR EMBL; AC068194; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC096587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016651; AAH16651.1; ALT_SEQ; mRNA.
DR EMBL; BC031216; AAH31216.1; ALT_SEQ; mRNA.
DR EMBL; BC053573; AAH53573.1; -; mRNA.
DR EMBL; BC057826; AAH57826.1; ALT_SEQ; mRNA.
DR EMBL; BC093952; AAH93952.1; -; mRNA.
DR EMBL; BC093954; AAH93954.1; -; mRNA.
DR CCDS; CCDS46465.1; -.
DR RefSeq; NP_065994.1; NM_020943.2.
DR RefSeq; XP_005246783.1; XM_005246726.2.
DR PDB; 4C9B; X-ray; 2.00 A; B=116-406.
DR PDB; 5MQF; EM; 5.90 A; T=1-908.
DR PDB; 5XJC; EM; 3.60 A; V=1-908.
DR PDB; 5YZG; EM; 4.10 A; V=1-908.
DR PDB; 5Z56; EM; 5.10 A; V=1-908.
DR PDB; 5Z57; EM; 6.50 A; V=1-908.
DR PDB; 5Z58; EM; 4.90 A; V=1-908.
DR PDB; 6FF7; EM; 4.50 A; T=1-908.
DR PDB; 6ICZ; EM; 3.00 A; V=1-908.
DR PDB; 6QDV; EM; 3.30 A; H=1-908.
DR PDB; 6YVH; X-ray; 3.19 A; A/B/D/F=119-406.
DR PDB; 6ZYM; EM; 3.40 A; T=1-908.
DR PDB; 7A5P; EM; 5.00 A; T=1-908.
DR PDB; 7DVQ; EM; 2.89 A; V=1-908.
DR PDBsum; 4C9B; -.
DR PDBsum; 5MQF; -.
DR PDBsum; 5XJC; -.
DR PDBsum; 5YZG; -.
DR PDBsum; 5Z56; -.
DR PDBsum; 5Z57; -.
DR PDBsum; 5Z58; -.
DR PDBsum; 6FF7; -.
DR PDBsum; 6ICZ; -.
DR PDBsum; 6QDV; -.
DR PDBsum; 6YVH; -.
DR PDBsum; 6ZYM; -.
DR PDBsum; 7A5P; -.
DR PDBsum; 7DVQ; -.
DR AlphaFoldDB; Q9HCG8; -.
DR SMR; Q9HCG8; -.
DR BioGRID; 121727; 102.
DR CORUM; Q9HCG8; -.
DR DIP; DIP-31268N; -.
DR IntAct; Q9HCG8; 40.
DR MINT; Q9HCG8; -.
DR STRING; 9606.ENSP00000387006; -.
DR iPTMnet; Q9HCG8; -.
DR MetOSite; Q9HCG8; -.
DR PhosphoSitePlus; Q9HCG8; -.
DR BioMuta; CWC22; -.
DR DMDM; 296439380; -.
DR EPD; Q9HCG8; -.
DR jPOST; Q9HCG8; -.
DR MassIVE; Q9HCG8; -.
DR MaxQB; Q9HCG8; -.
DR PaxDb; Q9HCG8; -.
DR PeptideAtlas; Q9HCG8; -.
DR PRIDE; Q9HCG8; -.
DR ProteomicsDB; 81712; -.
DR Antibodypedia; 33977; 155 antibodies from 21 providers.
DR DNASU; 57703; -.
DR Ensembl; ENST00000410053.8; ENSP00000387006.3; ENSG00000163510.14.
DR GeneID; 57703; -.
DR KEGG; hsa:57703; -.
DR MANE-Select; ENST00000410053.8; ENSP00000387006.3; NM_020943.3; NP_065994.1.
DR UCSC; uc010frh.2; human.
DR CTD; 57703; -.
DR DisGeNET; 57703; -.
DR GeneCards; CWC22; -.
DR HGNC; HGNC:29322; CWC22.
DR HPA; ENSG00000163510; Low tissue specificity.
DR MIM; 615186; gene.
DR neXtProt; NX_Q9HCG8; -.
DR OpenTargets; ENSG00000163510; -.
DR PharmGKB; PA164718415; -.
DR VEuPathDB; HostDB:ENSG00000163510; -.
DR eggNOG; KOG2140; Eukaryota.
DR GeneTree; ENSGT00940000153458; -.
DR InParanoid; Q9HCG8; -.
DR OMA; NIFKFDA; -.
DR OrthoDB; 996017at2759; -.
DR PhylomeDB; Q9HCG8; -.
DR TreeFam; TF300510; -.
DR PathwayCommons; Q9HCG8; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q9HCG8; -.
DR BioGRID-ORCS; 57703; 776 hits in 1088 CRISPR screens.
DR ChiTaRS; CWC22; human.
DR GenomeRNAi; 57703; -.
DR Pharos; Q9HCG8; Tbio.
DR PRO; PR:Q9HCG8; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q9HCG8; protein.
DR Bgee; ENSG00000163510; Expressed in epithelial cell of pancreas and 188 other tissues.
DR ExpressionAtlas; Q9HCG8; baseline and differential.
DR Genevisible; Q9HCG8; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IDA:UniProtKB.
DR GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IDA:UniProtKB.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0071005; C:U2-type precatalytic spliceosome; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IC:UniProtKB.
DR IDEAL; IID00595; -.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003891; Initiation_fac_eIF4g_MI.
DR InterPro; IPR003890; MIF4G-like_typ-3.
DR Pfam; PF02847; MA3; 1.
DR SMART; SM00544; MA3; 1.
DR SMART; SM00543; MIF4G; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51366; MI; 1.
PE 1: Evidence at protein level;
KW 3D-structure; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Spliceosome.
FT CHAIN 1..908
FT /note="Pre-mRNA-splicing factor CWC22 homolog"
FT /id="PRO_0000302005"
FT DOMAIN 163..346
FT /note="MIF4G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT DOMAIN 454..570
FT /note="MI"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00698"
FT REGION 1..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 654..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..437
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 715..773
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..908
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C5N3"
FT MOD_RES 786
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 829
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT VARIANT 656
FT /note="A -> V (in dbSNP:rs17778270)"
FT /id="VAR_057513"
FT VARIANT 741
FT /note="D -> V (in dbSNP:rs11903115)"
FT /id="VAR_057514"
FT VARIANT 794
FT /note="R -> Q (in dbSNP:rs1046356)"
FT /id="VAR_057515"
FT MUTAGEN 168
FT /note="G->Y: No effect on EIF4A3 incorporation into EJCs."
FT /evidence="ECO:0000269|PubMed:23236153"
FT MUTAGEN 171..174
FT /note="NKVN->AAVA: Loss of EIF4A3-binding."
FT MUTAGEN 171..172
FT /note="NK->DE: Loss of EIF4A3-binding."
FT /evidence="ECO:0000269|PubMed:22959432"
FT MUTAGEN 331
FT /note="R->A: Decreased EIF4A3-binding; when associated with
FT A-334."
FT /evidence="ECO:0000269|PubMed:23236153"
FT MUTAGEN 334
FT /note="Y->A: Decreased EIF4A3-binding; when associated with
FT A-331."
FT /evidence="ECO:0000269|PubMed:23236153"
FT CONFLICT 270
FT /note="H -> Y (in Ref. 2; BAB15197)"
FT /evidence="ECO:0000305"
FT CONFLICT 550
FT /note="M -> V (in Ref. 2; BAB15197)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="E -> G (in Ref. 4; AAH31216)"
FT /evidence="ECO:0000305"
FT CONFLICT 685
FT /note="S -> F (in Ref. 4; AAH16651)"
FT /evidence="ECO:0000305"
FT CONFLICT 701
FT /note="S -> G (in Ref. 4; AAH31216)"
FT /evidence="ECO:0000305"
FT CONFLICT 742
FT /note="R -> K (in Ref. 4; AAH31216)"
FT /evidence="ECO:0000305"
FT CONFLICT 773
FT /note="S -> R (in Ref. 2; BAB15612 and 4; AAH53573/
FT AAH93952/AAH93954)"
FT /evidence="ECO:0000305"
FT HELIX 136..140
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 150..172
FT /evidence="ECO:0007829|PDB:4C9B"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 178..186
FT /evidence="ECO:0007829|PDB:4C9B"
FT TURN 190..193
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 194..207
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 212..225
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 227..247
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 250..265
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 272..283
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 287..307
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 309..324
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 330..344
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:4C9B"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 380..383
FT /evidence="ECO:0007829|PDB:4C9B"
FT HELIX 391..405
FT /evidence="ECO:0007829|PDB:4C9B"
FT STRAND 444..446
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 450..465
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 469..479
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 483..485
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 486..498
FT /evidence="ECO:0007829|PDB:7DVQ"
FT STRAND 500..502
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 505..517
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 519..534
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 535..538
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 541..556
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 562..567
FT /evidence="ECO:0007829|PDB:7DVQ"
FT TURN 572..574
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 577..594
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 596..603
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 604..606
FT /evidence="ECO:0007829|PDB:6ZYM"
FT TURN 607..610
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 611..613
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 621..634
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 638..640
FT /evidence="ECO:0007829|PDB:7DVQ"
FT HELIX 641..648
FT /evidence="ECO:0007829|PDB:7DVQ"
SQ SEQUENCE 908 AA; 105466 MW; 00EF9B361B5F55AB CRC64;
MKSSVAQIKP SSGHDRRENL NSYQRNSSPE DRYEEQERSP RDRDYFDYSR SDYEHSRRGR
SYDSSMESRN RDREKRRERE RDTDRKRSRK SPSPGRRNPE TSVTQSSSAQ DEPATKKKKD
ELDPLLTRTG GAYIPPAKLR MMQEQITDKN SLAYQRMSWE ALKKSINGLI NKVNISNISI
IIQELLQENI VRGRGLLSRS VLQAQSASPI FTHVYAALVA IINSKFPQIG ELILKRLILN
FRKGYRRNDK QLCLTASKFV AHLINQNVAH EVLCLEMLTL LLERPTDDSV EVAIGFLKEC
GLKLTQVSPR GINAIFERLR NILHESEIDK RVQYMIEVMF AVRKDGFKDH PIILEGLDLV
EEDDQFTHML PLEDDYNPED VLNVFKMDPN FMENEEKYKA IKKEILDEGD TDSNTDQDAG
SSEEDEEEEE EEGEEDEEGQ KVTIHDKTEI NLVSFRRTIY LAIQSSLDFE ECAHKLLKME
FPESQTKELC NMILDCCAQQ RTYEKFFGLL AGRFCMLKKE YMESFEGIFK EQYDTIHRLE
TNKLRNVAKM FAHLLYTDSL PWSVLECIKL SEETTTSSSR IFVKIFFQEL CEYMGLPKLN
ARLKDETLQP FFEGLLPRDN PRNTRFAINF FTSIGLGGLT DELREHLKNT PKVIVAQKPD
VEQNKSSPSS SSSASSSSES DSSDSDSDSS DSSSESSSEE SDSSSISSHS SASANDVRKK
GHGKTRSKEV DKLIRNQQTN DRKQKERRQE HGHQETRTER ERRSEKHRDQ NSSGSNWRDP
ITKYTSDKDV PSERNNYSRV ANDRDQEMHI DLENKHGDPK KKRGERRNSF SENEKHTHRI
KDSENFRRKD RSKSKEMNRK HSGSRSDEDR YQNGAERRWE KSSRYSEQSR ESKKNQDRRR
EKSPAKQK
