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Pre-mRNA-splicing factor CWC2 (Complexed with CEF1 protein 2) (PRP19-associated complex protein 40) (Synthetic lethal with CLF1 protein 3)

 CWC2_YEAST              Reviewed;         339 AA.
Q12046; D6VRE5;
05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 148.
RecName: Full=Pre-mRNA-splicing factor CWC2;
AltName: Full=Complexed with CEF1 protein 2;
AltName: Full=PRP19-associated complex protein 40;
AltName: Full=Synthetic lethal with CLF1 protein 3;
Name=CWC2; Synonyms=NTC40, SLC3; OrderedLocusNames=YDL209C;
ORFNames=D1041;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 96604 / S288c / FY1679;
PubMed=9046097;
DOI=10.1002/(SICI)1097-0061(199702)13:2<163::AID-YEA54>3.3.CO;2-W;
Bahr A., Moeller-Rieker S., Hankeln T., Kraemer C., Protin U.,
Schmidt E.R.;
"The nucleotide sequence of a 39 kb segment of yeast chromosome IV: 12
new open reading frames, nine known genes and one gene for Gly-tRNA.";
Yeast 13:163-169(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[5]
INTERACTION WITH PRP19.
PubMed=9528791; DOI=10.1128/MCB.18.4.2196;
Chen H.-R., Jan S.-P., Tsao T.Y., Sheu Y.-J., Banroques J.,
Cheng S.-C.;
"Snt309p, a component of the Prp19p-associated complex that interacts
with Prp19p and associates with the spliceosome simultaneously with or
immediately after dissociation of U4 in the same manner as Prp19p.";
Mol. Cell. Biol. 18:2196-2204(1998).
[6]
IDENTIFICATION IN THE CWC COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=11884590; DOI=10.1128/MCB.22.7.2011-2024.2002;
Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L.;
"Proteomics analysis reveals stable multiprotein complexes in both
fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel
pre-mRNA splicing factors, and snRNAs.";
Mol. Cell. Biol. 22:2011-2024(2002).
[7]
INTERACTION WITH PRP19 AND ISY1.
PubMed=12088152; DOI=10.1017/S1355838202025050;
Ohi M.D., Gould K.L.;
"Characterization of interactions among the Cef1p-Prp19p-associated
splicing complex.";
RNA 8:798-815(2002).
[8]
MUTAGENESIS OF GLY-79.
PubMed=12871902;
Vincent K., Wang Q., Jay S., Hobbs K., Rymond B.C.;
"Genetic interactions with CLF1 identify additional pre-mRNA splicing
factors and a link between activators of yeast vesicular transport and
splicing.";
Genetics 164:895-907(2003).
[9]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[10]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[11]
FUNCTION, MUTAGENESIS OF CYS-73; CYS-87 AND PHE-186, AND RNA-BINDING.
PubMed=19435883; DOI=10.1093/nar/gkp341;
McGrail J.C., Krause A., O'Keefe R.T.;
"The RNA binding protein Cwc2 interacts directly with the U6 snRNA to
link the nineteen complex to the spliceosome during pre-mRNA
splicing.";
Nucleic Acids Res. 37:4205-4217(2009).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-336, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[13]
FUNCTION, RNA-BINDING, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=22246180; DOI=10.1038/emboj.2011.502;
Rasche N., Dybkov O., Schmitzova J., Akyildiz B., Fabrizio P.,
Luhrmann R.;
"Cwc2 and its human homologue RBM22 promote an active conformation of
the spliceosome catalytic centre.";
EMBO J. 31:1591-1604(2012).
-!- FUNCTION: Involved in the first step of pre-mRNA splicing.
Required for cell growth and cell cycle control. Plays a role in
the levels of the U1, U4, U5 and U6 snRNAs and the maintenance of
the U4/U6 snRNA complex. May provide the link between the
"nineteen complex" NTC spliceosome protein complex and the
spliceosome through the U6 snRNA. Associates predominantly with U6
snRNAs in assembled active spliceosomes. Binds directly to the
internal stem-loop (ISL) domain of the U6 snRNA and to the pre-
mRNA intron near the 5' splice site during the activation and
catalytic phases of the spliceosome cycle. Binds also to U1, U4,
U5 and U6 snRNAs and to pre-mRNAs, in vitro. Is not required for
the Prp2-mediated remodeling of the activated spliceosome.
{ECO:0000269|PubMed:19435883, ECO:0000269|PubMed:22246180}.
-!- SUBUNIT: Belongs to the CWC complex (or CEF1-associated complex),
a spliceosome subcomplex composed of the U2, U5 and U6 snRNAs and
at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15,
CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3,
ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22,
PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309,
SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Interacts with ISY1 and
PRP19. {ECO:0000269|PubMed:11884590, ECO:0000269|PubMed:12088152,
ECO:0000269|PubMed:9528791}.
-!- INTERACTION:
P32523:PRP19; NbExp=13; IntAct=EBI-553, EBI-493;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}.
-!- DOMAIN: The C-terminus RRM domain and the zinc finger motif are
necessary for RNA-binding.
-!- MISCELLANEOUS: Present with 2650 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the RRM CWC2 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X99000; CAA67482.1; -; Genomic_DNA.
EMBL; Z74257; CAA98787.1; -; Genomic_DNA.
EMBL; AY693022; AAT93041.1; -; Genomic_DNA.
EMBL; BK006938; DAA11655.1; -; Genomic_DNA.
PIR; S67768; S67768.
RefSeq; NP_010072.1; NM_001180269.1.
PDB; 3TP2; X-ray; 2.40 A; A/B=1-227.
PDB; 3U1L; X-ray; 1.64 A; A=1-240.
PDB; 3U1M; X-ray; 1.95 A; A=1-240.
PDB; 5GM6; EM; 3.50 A; R=1-339.
PDB; 5GMK; EM; 3.40 A; R=1-339.
PDB; 5LJ3; EM; 3.80 A; M=1-339.
PDB; 5LJ5; EM; 3.80 A; M=1-339.
PDB; 5LQW; EM; 5.80 A; F=1-339.
PDB; 5MPS; EM; 3.85 A; M=1-339.
PDB; 5MQ0; EM; 4.17 A; M=1-339.
PDB; 5WSG; EM; 4.00 A; R=1-339.
PDBsum; 3TP2; -.
PDBsum; 3U1L; -.
PDBsum; 3U1M; -.
PDBsum; 5GM6; -.
PDBsum; 5GMK; -.
PDBsum; 5LJ3; -.
PDBsum; 5LJ5; -.
PDBsum; 5LQW; -.
PDBsum; 5MPS; -.
PDBsum; 5MQ0; -.
PDBsum; 5WSG; -.
ProteinModelPortal; Q12046; -.
SMR; Q12046; -.
BioGrid; 31837; 107.
DIP; DIP-5164N; -.
IntAct; Q12046; 51.
MINT; MINT-510131; -.
STRING; 4932.YDL209C; -.
iPTMnet; Q12046; -.
MaxQB; Q12046; -.
PRIDE; Q12046; -.
EnsemblFungi; YDL209C; YDL209C; YDL209C.
GeneID; 851318; -.
KEGG; sce:YDL209C; -.
EuPathDB; FungiDB:YDL209C; -.
SGD; S000002368; CWC2.
HOGENOM; HOG000172735; -.
InParanoid; Q12046; -.
OMA; CEYLHHI; -.
OrthoDB; EOG092C4KFZ; -.
BioCyc; YEAST:G3O-29591-MONOMER; -.
PRO; PR:Q12046; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0000974; C:Prp19 complex; IPI:SGD.
GO; GO:0071006; C:U2-type catalytic step 1 spliceosome; IDA:SGD.
GO; GO:0071007; C:U2-type catalytic step 2 spliceosome; IDA:SGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0036002; F:pre-mRNA binding; IDA:UniProtKB.
GO; GO:0017070; F:U6 snRNA binding; IDA:UniProtKB.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IDA:UniProtKB.
GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:SGD.
GO; GO:0045787; P:positive regulation of cell cycle; IMP:UniProtKB.
GO; GO:0033120; P:positive regulation of RNA splicing; IDA:UniProtKB.
GO; GO:0000387; P:spliceosomal snRNP assembly; IDA:UniProtKB.
CDD; cd12360; RRM_cwf2; 1.
InterPro; IPR034181; Cwc2_RRM.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR000504; RRM_dom.
InterPro; IPR032297; Torus.
InterPro; IPR000571; Znf_CCCH.
Pfam; PF00076; RRM_1; 1.
Pfam; PF16131; Torus; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50102; RRM; 1.
PROSITE; PS50103; ZF_C3H1; 1.
1: Evidence at protein level;
3D-structure; Cell cycle; Complete proteome; Metal-binding;
mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
Reference proteome; RNA-binding; Spliceosome; Zinc; Zinc-finger.
CHAIN 1 339 Pre-mRNA-splicing factor CWC2.
/FTId=PRO_0000081552.
DOMAIN 135 228 RRM. {ECO:0000255|PROSITE-
ProRule:PRU00176}.
ZN_FING 67 94 C3H1-type. {ECO:0000255|PROSITE-
ProRule:PRU00723}.
MOD_RES 335 335 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 336 336 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MUTAGEN 73 73 C->Y: Inhibits cell growth.
{ECO:0000269|PubMed:19435883}.
MUTAGEN 79 79 G->D: No effect. Synthetic lethal when
associated with CLF1 lacking a TPR
domain. {ECO:0000269|PubMed:12871902}.
MUTAGEN 87 87 C->H: Inhibits cell growth.
{ECO:0000269|PubMed:19435883}.
MUTAGEN 186 186 F->D: Inhibits cell growth.
{ECO:0000269|PubMed:19435883}.
HELIX 4 6 {ECO:0000244|PDB:3U1L}.
HELIX 15 17 {ECO:0000244|PDB:3U1L}.
STRAND 25 27 {ECO:0000244|PDB:3TP2}.
HELIX 30 39 {ECO:0000244|PDB:3U1L}.
STRAND 41 45 {ECO:0000244|PDB:3U1L}.
HELIX 55 58 {ECO:0000244|PDB:3U1L}.
HELIX 63 66 {ECO:0000244|PDB:3U1L}.
HELIX 74 77 {ECO:0000244|PDB:3U1L}.
HELIX 84 86 {ECO:0000244|PDB:3U1L}.
STRAND 88 92 {ECO:0000244|PDB:3U1L}.
HELIX 96 105 {ECO:0000244|PDB:3U1L}.
STRAND 107 109 {ECO:0000244|PDB:3U1L}.
STRAND 113 115 {ECO:0000244|PDB:3U1L}.
HELIX 117 119 {ECO:0000244|PDB:3U1L}.
STRAND 125 127 {ECO:0000244|PDB:3TP2}.
HELIX 129 133 {ECO:0000244|PDB:3TP2}.
STRAND 136 140 {ECO:0000244|PDB:3U1L}.
HELIX 144 146 {ECO:0000244|PDB:3U1L}.
HELIX 153 165 {ECO:0000244|PDB:3U1L}.
STRAND 170 176 {ECO:0000244|PDB:3U1L}.
HELIX 177 179 {ECO:0000244|PDB:3U1L}.
STRAND 181 188 {ECO:0000244|PDB:3U1L}.
HELIX 189 199 {ECO:0000244|PDB:3U1L}.
STRAND 207 209 {ECO:0000244|PDB:5GMK}.
HELIX 212 217 {ECO:0000244|PDB:3U1L}.
STRAND 222 225 {ECO:0000244|PDB:3U1L}.
HELIX 232 260 {ECO:0000244|PDB:5GMK}.
SEQUENCE 339 AA; 38431 MW; 371734A11DFDB339 CRC64;
MTSWRDKSAK VQVKESELPS SIPAQTGLTF NIWYNKWSQG FAGNTRFVSP FALQPQLHSG
KTRGDNDGQL FFCLFFAKGM CCLGPKCEYL HHIPDEEDIG KLALRTEVLD CFGREKFADY
REDMGGIGSF RKKNKTLYVG GIDGALNSKH LKPAQIESRI RFVFSRLGDI DRIRYVESKN
CGFVKFKYQA NAEFAKEAMS NQTLLLPSDK EWDDRREGTG LLVKWANEDP DPAAQKRLQE
ELKLESLNMM VHLINNNTNS AGTEVNNKNN ERLDRTFPEA SVDNVKKRLL PLDNGMESDD
FIEKLKKVKK NISRENISSK PSVGKLGGPL LDYLSSDED


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San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




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