CWC25_HUMAN
ID CWC25_HUMAN Reviewed; 425 AA.
AC Q9NXE8; A0JLM3; Q68DK5;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Pre-mRNA-splicing factor CWC25 homolog;
DE AltName: Full=Coiled-coil domain-containing protein 49;
DE AltName: Full=Spliceosome-associated protein homolog CWC25;
GN Name=CWC25; Synonyms=CCDC49;
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] (ISOFORM 1).
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Liver;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, and Uterus;
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=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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218 AND SER-222, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170 AND SER-218, 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 [8]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-391, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [9] {ECO:0007744|PDB:5YZG}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.10 ANGSTROMS), FUNCTION, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
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: Involved in pre-mRNA splicing as component of the
CC spliceosome. {ECO:0000269|PubMed:29301961}.
CC -!- SUBUNIT: Identified in the spliceosome C complex.
CC {ECO:0000269|PubMed:29301961}.
CC -!- INTERACTION:
CC Q9NXE8; Q8IXW7: FMR1; NbExp=3; IntAct=EBI-746052, EBI-11976595;
CC Q9NXE8; O76011: KRT34; NbExp=3; IntAct=EBI-746052, EBI-1047093;
CC Q9NXE8; P19474: TRIM21; NbExp=3; IntAct=EBI-746052, EBI-81290;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:29301961}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NXE8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NXE8-2; Sequence=VSP_025797;
CC -!- SIMILARITY: Belongs to the CWC25 family. {ECO:0000305}.
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DR EMBL; AK000298; BAA91065.1; -; mRNA.
DR EMBL; CR749362; CAH18215.1; -; mRNA.
DR EMBL; BC003085; AAH03085.1; ALT_TERM; mRNA.
DR EMBL; BC008833; AAH08833.1; -; mRNA.
DR CCDS; CCDS45663.1; -. [Q9NXE8-1]
DR RefSeq; NP_060218.1; NM_017748.4. [Q9NXE8-1]
DR PDB; 5YZG; EM; 4.10 A; X=1-425.
DR PDB; 6ZYM; EM; 3.40 A; t=1-425.
DR PDBsum; 5YZG; -.
DR PDBsum; 6ZYM; -.
DR AlphaFoldDB; Q9NXE8; -.
DR SMR; Q9NXE8; -.
DR BioGRID; 120231; 49.
DR IntAct; Q9NXE8; 13.
DR MINT; Q9NXE8; -.
DR STRING; 9606.ENSP00000478070; -.
DR iPTMnet; Q9NXE8; -.
DR PhosphoSitePlus; Q9NXE8; -.
DR BioMuta; CWC25; -.
DR DMDM; 74734693; -.
DR EPD; Q9NXE8; -.
DR jPOST; Q9NXE8; -.
DR MassIVE; Q9NXE8; -.
DR MaxQB; Q9NXE8; -.
DR PaxDb; Q9NXE8; -.
DR PeptideAtlas; Q9NXE8; -.
DR PRIDE; Q9NXE8; -.
DR ProteomicsDB; 83084; -. [Q9NXE8-1]
DR ProteomicsDB; 83085; -. [Q9NXE8-2]
DR Antibodypedia; 74912; 27 antibodies from 12 providers.
DR DNASU; 54883; -.
DR Ensembl; ENST00000614790.5; ENSP00000478070.1; ENSG00000273559.5. [Q9NXE8-1]
DR Ensembl; ENST00000614868.2; ENSP00000477799.1; ENSG00000276761.2. [Q9NXE8-1]
DR GeneID; 54883; -.
DR KEGG; hsa:54883; -.
DR MANE-Select; ENST00000614790.5; ENSP00000478070.1; NM_017748.5; NP_060218.1.
DR UCSC; uc002hqu.5; human. [Q9NXE8-1]
DR CTD; 54883; -.
DR DisGeNET; 54883; -.
DR GeneCards; CWC25; -.
DR HGNC; HGNC:25989; CWC25.
DR HPA; ENSG00000273559; Tissue enhanced (bone).
DR neXtProt; NX_Q9NXE8; -.
DR OpenTargets; ENSG00000273559; -.
DR PharmGKB; PA165431769; -.
DR VEuPathDB; HostDB:ENSG00000273559; -.
DR eggNOG; KOG3869; Eukaryota.
DR GeneTree; ENSGT00440000039055; -.
DR HOGENOM; CLU_025093_1_0_1; -.
DR InParanoid; Q9NXE8; -.
DR OMA; SWHPHTM; -.
DR OrthoDB; 1635950at2759; -.
DR PhylomeDB; Q9NXE8; -.
DR TreeFam; TF320801; -.
DR PathwayCommons; Q9NXE8; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q9NXE8; -.
DR BioGRID-ORCS; 54883; 286 hits in 1075 CRISPR screens.
DR ChiTaRS; CWC25; human.
DR GenomeRNAi; 54883; -.
DR Pharos; Q9NXE8; Tdark.
DR PRO; PR:Q9NXE8; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9NXE8; protein.
DR Bgee; ENSG00000273559; Expressed in sural nerve and 95 other tissues.
DR ExpressionAtlas; Q9NXE8; baseline and differential.
DR Genevisible; Q9NXE8; HS.
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:0071006; C:U2-type catalytic step 1 spliceosome; IDA:UniProtKB.
DR GO; GO:0005684; C:U2-type spliceosomal complex; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:UniProtKB.
DR InterPro; IPR019339; CIR_N_dom.
DR InterPro; IPR022209; CWC25.
DR Pfam; PF10197; Cir_N; 1.
DR Pfam; PF12542; CWC25; 1.
DR SMART; SM01083; Cir_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Isopeptide bond;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Spliceosome; Ubl conjugation.
FT CHAIN 1..425
FT /note="Pre-mRNA-splicing factor CWC25 homolog"
FT /id="PRO_0000288865"
FT REGION 146..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 20..70
FT /evidence="ECO:0000255"
FT COILED 333..377
FT /evidence="ECO:0000255"
FT COMPBIAS 146..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..194
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..270
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..302
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 222
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 391
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..347
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_025797"
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:6ZYM"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:6ZYM"
FT HELIX 17..53
FT /evidence="ECO:0007829|PDB:6ZYM"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:6ZYM"
SQ SEQUENCE 425 AA; 49647 MW; F8288E143A3FF764 CRC64;
MGGGDLNLKK SWHPQTLRNV EKVWKAEQKH EAERKKIEEL QRELREERAR EEMQRYAEDV
GAVKKKEEKL DWMYQGPGGM VNRDEYLLGR PIDKYVFEKM EEKEAGCSSE TGLLPGSIFA
PSGANSLLDM ASKIREDPLF IIRKKEEEKK REVLNNPVKM KKIKELLQMS LEKKEKKKKK
EKKKKHKKHK HRSSSSDRSS SEDEHSAGRS QKKMANSSPV LSKVPGYGLQ VRNSDRNQGL
QGPLTAEQKR GHGMKNHSRS RSSSHSPPRH ASKKSTREAG SRDRRSRSLG RRSRSPRPSK
LHNSKVNRRE TGQTRSPSPK KEVYQRRHAP GYTRKLSAEE LERKRQEMME NAKWREEERL
NILKRHAKDE EREQRLEKLD SRDGKFIHRM KLESASTSSL EDRVKRNIYS LQRTSVALEK
NFMKR
