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   27-MAR-2024, entry version 148.
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).
RN   [16] {ECO:0007744|PDB:7DVQ}
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.89 ANGSTROMS), AND SUBUNIT.
RX   PubMed=33509932; DOI=10.1126/science.abg0879;
RA   Bai R., Wan R., Wang L., Xu K., Zhang Q., Lei J., Shi Y.;
RT   "Structure of the activated human minor spliceosome.";
RL   Science 371:0-0(2021).
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. As a component of the minor
CC       spliceosome, involved in the splicing of U12-type introns in pre-mRNAs
CC       (Probable). {ECO:0000269|PubMed:20176811, ECO:0000269|PubMed:28076346,
CC       ECO:0000269|PubMed:28502770, ECO:0000305|PubMed:33509932}.
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). Component of the minor
CC       spliceosome, which splices U12-type introns (PubMed:33509932).
CC       {ECO:0000269|PubMed:20176811, ECO:0000269|PubMed:28076346,
CC       ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:33509932}.
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   PDB; 7QTT; EM; 3.10 A; Q=1-229.
DR   PDB; 7W59; EM; 3.60 A; P=1-229.
DR   PDB; 7W5A; EM; 3.60 A; P=1-229.
DR   PDB; 7W5B; EM; 4.30 A; P=1-229.
DR   PDB; 8C6J; EM; 2.80 A; P=1-229.
DR   PDB; 8CH6; EM; 5.90 A; Q=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   PDBsum; 7QTT; -.
DR   PDBsum; 7W59; -.
DR   PDBsum; 7W5A; -.
DR   PDBsum; 7W5B; -.
DR   PDBsum; 8C6J; -.
DR   PDBsum; 8CH6; -.
DR   AlphaFoldDB; Q9P013; -.
DR   EMDB; EMD-11569; -.
DR   EMDB; EMD-11693; -.
DR   EMDB; EMD-11694; -.
DR   EMDB; EMD-11695; -.
DR   EMDB; EMD-11697; -.
DR   EMDB; EMD-14146; -.
DR   EMDB; EMD-16452; -.
DR   EMDB; EMD-16658; -.
DR   EMDB; EMD-30875; -.
DR   EMDB; EMD-32317; -.
DR   EMDB; EMD-32319; -.
DR   EMDB; EMD-32321; -.
DR   EMDB; EMD-3545; -.
DR   EMDB; EMD-4255; -.
DR   EMDB; EMD-4525; -.
DR   EMDB; EMD-6721; -.
DR   EMDB; EMD-6864; -.
DR   EMDB; EMD-6889; -.
DR   EMDB; EMD-6890; -.
DR   EMDB; EMD-6891; -.
DR   EMDB; EMD-9645; -.
DR   EMDB; EMD-9646; -.
DR   EMDB; EMD-9647; -.
DR   SMR; Q9P013; -.
DR   BioGRID; 119575; 132.
DR   ComplexPortal; CPX-5824; PRP19-CDC5L complex.
DR   CORUM; Q9P013; -.
DR   IntAct; Q9P013; 41.
DR   MINT; Q9P013; -.
DR   STRING; 9606.ENSP00000475615; -.
DR   GlyGen; Q9P013; 3 sites, 1 O-linked glycan (3 sites).
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   PaxDb; 9606-ENSP00000475615; -.
DR   PeptideAtlas; Q9P013; -.
DR   ProteomicsDB; 83532; -.
DR   Pumba; Q9P013; -.
DR   TopDownProteomics; Q9P013; -.
DR   Antibodypedia; 70625; 93 antibodies from 18 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   AGR; HGNC:26939; -.
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; KYREHGQ; -.
DR   OrthoDB; 1442599at2759; -.
DR   PhylomeDB; Q9P013; -.
DR   PathwayCommons; Q9P013; -.
DR   Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR   SignaLink; Q9P013; -.
DR   SIGNOR; Q9P013; -.
DR   BioGRID-ORCS; 51503; 45 hits in 307 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 188 other cell types or tissues.
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; CELL CYCLE CONTROL PROTEIN CWF15; 1.
DR   PANTHER; PTHR12718:SF2; SPLICEOSOME-ASSOCIATED PROTEIN CWC15 HOMOLOG; 1.
DR   Pfam; PF04889; Cwf_Cwc_15; 1.
DR   Genevisible; Q9P013; HS.
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          198..200
FT                   /evidence="ECO:0007829|PDB:7QTT"
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
//