CWC15_HUMAN
ID CWC15_HUMAN Reviewed; 229 AA.
AC Q9P013; B2RC17; Q05BV9; Q05DM1; Q9UI29;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Spliceosome-associated protein CWC15 homolog;
GN Name=CWC15; Synonyms=C11orf5; ORFNames=AD-002, HSPC148;
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 [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 [LARGE SCALE MRNA].
RC TISSUE=Blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cerebellum;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, Liver, 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 [6]
RP PROTEIN SEQUENCE OF 2-13; 17-28; 45-55; 188-195 AND 210-216, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT THR-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-110 AND SER-121, AND
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-110, AND IDENTIFICATION BY
RP 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 [9]
RP IDENTIFICATION AS A COMPONENT OF THE PRP19-CDC5L COMPLEX, SUBCELLULAR
RP LOCATION, INTERACTION WITH CTNNBL1, AND FUNCTION.
RX PubMed=20176811; DOI=10.1128/mcb.01505-09;
RA Grote M., Wolf E., Will C.L., Lemm I., Agafonov D.E., Schomburg A.,
RA Fischle W., Urlaub H., Luhrmann R.;
RT "Molecular architecture of the human Prp19/CDC5L complex.";
RL Mol. Cell. Biol. 30:2105-2119(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 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-47, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-110 AND SER-121, 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 [14] {ECO:0007744|PDB:5XJC}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
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 [15] {ECO:0007744|PDB:5MQF}
RP STRUCTURE BY ELECTRON MICROSCOPY (5.90 ANGSTROMS), FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, 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).
CC -!- FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome
CC (PubMed:28502770, PubMed:28076346). Component of the PRP19-CDC5L
CC complex that forms an integral part of the spliceosome and is required
CC for activating pre-mRNA splicing. {ECO:0000269|PubMed:20176811,
CC ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770}.
CC -!- SUBUNIT: Identified in the spliceosome C complex (PubMed:28502770,
CC PubMed:28076346). Component of the PRP19-CDC5L splicing complex
CC composed of a core complex comprising a homotetramer of PRPF19, CDC5L,
CC PLRG1 and BCAS2, and at least three less stably associated proteins
CC CTNNBL1, CWC15 and HSPA8 (PubMed:20176811). Interacts directly with
CC CTNNBL1 in the complex (PubMed:20176811). {ECO:0000269|PubMed:20176811,
CC ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770}.
CC -!- INTERACTION:
CC Q9P013; Q8WYA6: CTNNBL1; NbExp=6; IntAct=EBI-2371709, EBI-748128;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20176811,
CC ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770}.
CC -!- SIMILARITY: Belongs to the CWC15 family. {ECO:0000305}.
CC -!- CAUTION: Has been termed C11orf5, but is not the official C11orf5 as
CC defined by HGNC. {ECO:0000305|PubMed:10873569}.
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DR EMBL; AJ250393; CAB96541.1; -; mRNA.
DR EMBL; AF161497; AAF29112.1; -; mRNA.
DR EMBL; AF110775; AAF14858.1; -; mRNA.
DR EMBL; AK314900; BAG37414.1; -; mRNA.
DR EMBL; BC006975; AAH06975.1; ALT_TERM; mRNA.
DR EMBL; BC032629; AAH32629.1; ALT_TERM; mRNA.
DR EMBL; BC040946; AAH40946.1; -; mRNA.
DR CCDS; CCDS73369.1; -.
DR RefSeq; NP_057487.2; NM_016403.3.
DR RefSeq; XP_011541170.1; XM_011542868.2.
DR RefSeq; XP_016873405.1; XM_017017916.1.
DR PDB; 5MQF; EM; 5.90 A; R=1-229.
DR PDB; 5XJC; EM; 3.60 A; P=1-229.
DR PDB; 5YZG; EM; 4.10 A; P=1-229.
DR PDB; 5Z56; EM; 5.10 A; P=1-229.
DR PDB; 5Z57; EM; 6.50 A; P=1-229.
DR PDB; 5Z58; EM; 4.90 A; P=1-229.
DR PDB; 6FF4; EM; 16.00 A; R=1-229.
DR PDB; 6FF7; EM; 4.50 A; R=1-229.
DR PDB; 6ICZ; EM; 3.00 A; P=1-229.
DR PDB; 6ID0; EM; 2.90 A; P=1-229.
DR PDB; 6ID1; EM; 2.86 A; P=1-229.
DR PDB; 6QDV; EM; 3.30 A; P=1-229.
DR PDB; 6ZYM; EM; 3.40 A; R=1-229.
DR PDB; 7AAV; EM; 4.20 A; R=1-229.
DR PDB; 7ABF; EM; 3.90 A; R=1-229.
DR PDB; 7ABG; EM; 7.80 A; R=1-229.
DR PDB; 7ABI; EM; 8.00 A; R=1-229.
DR PDB; 7DVQ; EM; 2.89 A; P=1-229.
DR PDBsum; 5MQF; -.
DR PDBsum; 5XJC; -.
DR PDBsum; 5YZG; -.
DR PDBsum; 5Z56; -.
DR PDBsum; 5Z57; -.
DR PDBsum; 5Z58; -.
DR PDBsum; 6FF4; -.
DR PDBsum; 6FF7; -.
DR PDBsum; 6ICZ; -.
DR PDBsum; 6ID0; -.
DR PDBsum; 6ID1; -.
DR PDBsum; 6QDV; -.
DR PDBsum; 6ZYM; -.
DR PDBsum; 7AAV; -.
DR PDBsum; 7ABF; -.
DR PDBsum; 7ABG; -.
DR PDBsum; 7ABI; -.
DR PDBsum; 7DVQ; -.
DR AlphaFoldDB; Q9P013; -.
DR SMR; Q9P013; -.
DR BioGRID; 119575; 84.
DR ComplexPortal; CPX-5824; PRP19-CDC5L complex.
DR CORUM; Q9P013; -.
DR IntAct; Q9P013; 40.
DR MINT; Q9P013; -.
DR STRING; 9606.ENSP00000475615; -.
DR GlyGen; Q9P013; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9P013; -.
DR MetOSite; Q9P013; -.
DR PhosphoSitePlus; Q9P013; -.
DR BioMuta; CWC15; -.
DR DMDM; 150438891; -.
DR EPD; Q9P013; -.
DR jPOST; Q9P013; -.
DR MassIVE; Q9P013; -.
DR MaxQB; Q9P013; -.
DR PeptideAtlas; Q9P013; -.
DR PRIDE; Q9P013; -.
DR ProteomicsDB; 83532; -.
DR TopDownProteomics; Q9P013; -.
DR Antibodypedia; 70625; 81 antibodies from 17 providers.
DR DNASU; 51503; -.
DR Ensembl; ENST00000279839.8; ENSP00000475615.2; ENSG00000150316.12.
DR GeneID; 51503; -.
DR KEGG; hsa:51503; -.
DR MANE-Select; ENST00000279839.8; ENSP00000475615.2; NM_016403.4; NP_057487.2.
DR UCSC; uc031ybh.1; human.
DR CTD; 51503; -.
DR DisGeNET; 51503; -.
DR GeneCards; CWC15; -.
DR HGNC; HGNC:26939; CWC15.
DR HPA; ENSG00000150316; Low tissue specificity.
DR neXtProt; NX_Q9P013; -.
DR OpenTargets; ENSG00000150316; -.
DR PharmGKB; PA162383026; -.
DR VEuPathDB; HostDB:ENSG00000150316; -.
DR eggNOG; KOG3228; Eukaryota.
DR GeneTree; ENSGT00390000012084; -.
DR HOGENOM; CLU_068312_0_1_1; -.
DR InParanoid; Q9P013; -.
DR OMA; NCARSEP; -.
DR OrthoDB; 1576404at2759; -.
DR PhylomeDB; Q9P013; -.
DR PathwayCommons; Q9P013; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q9P013; -.
DR BioGRID-ORCS; 51503; 37 hits in 250 CRISPR screens.
DR ChiTaRS; CWC15; human.
DR GeneWiki; CWC15; -.
DR GenomeRNAi; 51503; -.
DR Pharos; Q9P013; Tbio.
DR PRO; PR:Q9P013; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9P013; protein.
DR Bgee; ENSG00000150316; Expressed in kidney epithelium and 186 other tissues.
DR Genevisible; Q9P013; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000974; C:Prp19 complex; IPI:ComplexPortal.
DR GO; GO:0005681; C:spliceosomal complex; IDA:UniProtKB.
DR GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA: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; IDA: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 3D-structure; Acetylation; Coiled coil; Direct protein sequencing;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Spliceosome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6"
FT CHAIN 2..229
FT /note="Spliceosome-associated protein CWC15 homolog"
FT /id="PRO_0000291543"
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:0000269|Ref.6"
FT MOD_RES 18
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9JHS9"
FT MOD_RES 47
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 110
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:24275569"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:24275569"
FT CONFLICT 148
FT /note="E -> D (in Ref. 2; AAF29112)"
FT /evidence="ECO:0000305"
FT STRAND 14..22
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 23..26
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 46..49
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 59..77
FT /evidence="ECO:0007829|PDB:6ID1"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:6FF4"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:6ID1"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:6ID1"
FT HELIX 218..227
FT /evidence="ECO:0007829|PDB:6ID1"
SQ SEQUENCE 229 AA; 26624 MW; B21E6EEF46C4427C CRC64;
MTTAARPTFE PARGGRGKGE GDLSQLSKQY SSRDLPSHTK IKYRQTTQDA PEEVRNRDFR
RELEERERAA AREKNRDRPT REHTTSSSVS KKPRLDQIPA ANLDADDPLT DEEDEDFEEE
SDDDDTAALL AELEKIKKER AEEQARKEQE QKAEEERIRM ENILSGNPLL NLTGPSQPQA
NFKVKRRWDD DVVFKNCAKG VDDQKKDKRF VNDTLRSEFH KKFMEKYIK
