MUD2_YEAST
ID MUD2_YEAST Reviewed; 527 AA.
AC P36084; D6VXL2;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Splicing factor MUD2;
GN Name=MUD2; OrderedLocusNames=YKL074C; ORFNames=YKL358;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7926772; DOI=10.1101/gad.8.7.843;
RA Abovich N., Liao X.C., Rosbash M.;
RT "The yeast MUD2 protein: an interaction with PRP11 defines a bridge between
RT commitment complexes and U2 snRNP addition.";
RL Genes Dev. 8:843-854(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-365.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8091863; DOI=10.1002/yea.320100009;
RA Rasmussen S.W.;
RT "Sequence of a 20.7 kb region of yeast chromosome XI includes the NUP100
RT gene, an open reading frame (ORF) possibly representing a nucleoside
RT diphosphate kinase gene, tRNAs for His, Val and Trp in addition to seven
RT ORFs with weak or no significant similarity to known proteins.";
RL Yeast 10:S69-S74(1994).
RN [5]
RP INTERACTION WITH MSL5 AND PRP40.
RX PubMed=9150140; DOI=10.1016/s0092-8674(00)80221-4;
RA Abovich N., Rosbash M.;
RT "Cross-intron bridging interactions in the yeast commitment complex are
RT conserved in mammals.";
RL Cell 89:403-412(1997).
RN [6]
RP FUNCTION, AND INTERACTION WITH MSL5.
RX PubMed=10376880; DOI=10.1017/s1355838299982286;
RA Rutz B., Seraphin B.;
RT "Transient interaction of BBP/ScSF1 and Mud2 with the splicing machinery
RT affects the kinetics of spliceosome assembly.";
RL RNA 5:819-831(1999).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-49, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
CC -!- FUNCTION: Splicing factor that contacts pre-mRNA directly and is a
CC component of the pre-mRNA-U1 snRNP complex (commitment complex 2) that
CC forms during early spliceosome assembly in yeast extracts.
CC {ECO:0000269|PubMed:10376880}.
CC -!- SUBUNIT: MSL5, MUD2 and PRP40 interact to form the commitment complex 2
CC (CC2), a precursor of mature spliceosomes.
CC -!- INTERACTION:
CC P36084; Q12186: MSL5; NbExp=5; IntAct=EBI-11612, EBI-34012;
CC -!- MISCELLANEOUS: Present with 4170 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; U22449; AAA64215.1; -; Genomic_DNA.
DR EMBL; X75780; CAA53400.1; -; Genomic_DNA.
DR EMBL; Z28074; CAA81911.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09082.1; -; Genomic_DNA.
DR PIR; S37899; S37899.
DR RefSeq; NP_012849.1; NM_001179640.1.
DR AlphaFoldDB; P36084; -.
DR BioGRID; 34057; 394.
DR ComplexPortal; CPX-1417; BBP-MUD2 branchpoint-binding complex.
DR DIP; DIP-758N; -.
DR IntAct; P36084; 11.
DR MINT; P36084; -.
DR STRING; 4932.YKL074C; -.
DR iPTMnet; P36084; -.
DR MaxQB; P36084; -.
DR PaxDb; P36084; -.
DR PRIDE; P36084; -.
DR EnsemblFungi; YKL074C_mRNA; YKL074C; YKL074C.
DR GeneID; 853788; -.
DR KEGG; sce:YKL074C; -.
DR SGD; S000001557; MUD2.
DR VEuPathDB; FungiDB:YKL074C; -.
DR eggNOG; KOG0120; Eukaryota.
DR HOGENOM; CLU_033573_0_0_1; -.
DR InParanoid; P36084; -.
DR OMA; YKETHEG; -.
DR BioCyc; YEAST:G3O-31870-MON; -.
DR PRO; PR:P36084; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P36084; protein.
DR GO; GO:0000243; C:commitment complex; IDA:SGD.
DR GO; GO:0016607; C:nuclear speck; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IC:ComplexPortal.
DR GO; GO:0071004; C:U2-type prespliceosome; IBA:GO_Central.
DR GO; GO:0089701; C:U2AF complex; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0008187; F:poly-pyrimidine tract binding; IBA:GO_Central.
DR GO; GO:0030628; F:pre-mRNA 3'-splice site binding; IBA:GO_Central.
DR GO; GO:0045131; F:pre-mRNA branch point binding; IDA:SGD.
DR GO; GO:0000348; P:mRNA branch site recognition; IMP:SGD.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IMP:ComplexPortal.
DR GO; GO:0000245; P:spliceosomal complex assembly; IC:ComplexPortal.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR003954; RRM_dom_euk.
DR SMART; SM00361; RRM_1; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
PE 1: Evidence at protein level;
KW mRNA processing; mRNA splicing; Phosphoprotein; Reference proteome;
KW RNA-binding.
FT CHAIN 1..527
FT /note="Splicing factor MUD2"
FT /id="PRO_0000081654"
FT DOMAIN 424..511
FT /note="RRM"
FT REGION 36..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT CONFLICT 98
FT /note="A -> R (in Ref. 1; AAA64215)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 527 AA; 60460 MW; 884427AB57A12E12 CRC64;
MADEKRLEDL RSKIMESIGK SEKDVVPIEN KRFNTDNAVI DTHFKRQKSD GELPKAPKSR
NVSHSNNRGP SSIITMSTNR TTYEQTRAGP HRQSYRDASG RSYNRENRYS SHNTGPQWNN
NPYNRQRDER RGRNERFDRR GRNGNGNYDR FNYQRKNEGS KFNGDRDKRQ LQTNKYDMNY
NSQNVMYPGS SFDSPAYYNM ASSKANSRLV ISGLSQSSDP SIVARLKDLL ENFISGLQKT
ESNAEDFKIS NFYIGEGRPD HIIVEFSSQI CSTMVLACRS FFNAKLGTFD LKWRRPNDYV
QQLDHLVDFC RGTVIALENL ENIGEGEDYR MKELFSSLNV TNGTAKPLFY KCSSNTNNTG
KESEFTKCIL LSFEVVTQDI LDKLKPYKWF KPNDGKISQV TSWITFQSLP NLVTQSVRVE
SRVLLLLNCL DPLDLKDETF ITEIKETLKY SIAGADTIKI CQPGVDYRLN FENLASGAGN
IYIKFKTLEA AKHAMEELPG TQFNDRTVLC TYIDEDDFDM MEATQLS
