PBP2_YEAST
ID PBP2_YEAST Reviewed; 413 AA.
AC P38151; D6VQM8;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=PAB1-binding protein 2;
GN Name=PBP2; OrderedLocusNames=YBR233W; ORFNames=YBR1531;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [2]
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 [3]
RP PARTIAL CHARACTERIZATION.
RX PubMed=9819425; DOI=10.1128/mcb.18.12.7383;
RA Mangus D.A., Amrani N., Jacobson A.;
RT "Pbp1p, a factor interacting with Saccharomyces cerevisiae poly(A)-binding
RT protein, regulates polyadenylation.";
RL Mol. Cell. Biol. 18:7383-7396(1998).
RN [4]
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- SUBUNIT: Interacts with PAB1.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- MISCELLANEOUS: Present with 1590 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; Z36101; CAA85196.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07348.1; -; Genomic_DNA.
DR PIR; S46109; S46109.
DR RefSeq; NP_009792.3; NM_001178581.3.
DR AlphaFoldDB; P38151; -.
DR SMR; P38151; -.
DR BioGRID; 32927; 72.
DR DIP; DIP-4947N; -.
DR IntAct; P38151; 18.
DR MINT; P38151; -.
DR STRING; 4932.YBR233W; -.
DR iPTMnet; P38151; -.
DR MaxQB; P38151; -.
DR PaxDb; P38151; -.
DR PRIDE; P38151; -.
DR EnsemblFungi; YBR233W_mRNA; YBR233W; YBR233W.
DR GeneID; 852533; -.
DR KEGG; sce:YBR233W; -.
DR SGD; S000000437; PBP2.
DR VEuPathDB; FungiDB:YBR233W; -.
DR eggNOG; KOG2190; Eukaryota.
DR HOGENOM; CLU_022670_9_0_1; -.
DR InParanoid; P38151; -.
DR OMA; ANIHMRC; -.
DR BioCyc; YEAST:G3O-29164-MON; -.
DR PRO; PR:P38151; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38151; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; IDA:SGD.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0051252; P:regulation of RNA metabolic process; IBA:GO_Central.
DR GO; GO:0000723; P:telomere maintenance; IGI:SGD.
DR Gene3D; 3.30.1370.10; -; 3.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR Pfam; PF00013; KH_1; 3.
DR SMART; SM00322; KH; 3.
DR SUPFAM; SSF54791; SSF54791; 3.
DR PROSITE; PS50084; KH_TYPE_1; 3.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome; Repeat; Ribonucleoprotein; RNA-binding.
FT CHAIN 1..413
FT /note="PAB1-binding protein 2"
FT /id="PRO_0000050122"
FT DOMAIN 66..130
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 148..213
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT DOMAIN 330..394
FT /note="KH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 413 AA; 45782 MW; 638846509BCE1840 CRC64;
MSTETTKPSI TTTPTTVLVS PNTLKRKKGE DTSEEQLEAE IKRVALKDAD SHSDNDHDSP
DNVPSDVHLR MLCLVKHASL IVGHKGATIS RIKSETSARI NISNNIRGVP ERIVYVRGTC
DDVAKAYGMI VRALLEEHGN EDNGEDIEIS INLLIPHHLM GCIIGKRGSR LREIEDLSAA
KLFASPNQLL LSNDRILTIN GVPDAIHIAT FYISQTLLNF QMESPQKNVK RSIYYQPTQF
NSVLIDHSQP NTIFHQRNHQ YHPSDKLLSY KPNKNLPISS TLLSMATPQY TTASVANATA
FQPNFVIPNV TVLDGPVISP APGNHLLMNF VQQEIFIDEK FVGNVIGKDG KHINSVKEST
GCSIIIQDPV EGSSERRLTI RGTFMASQAA IMLISNKIEI DRSNAERKRR SPL
