PBP1_YEAST
ID PBP1_YEAST Reviewed; 722 AA.
AC P53297; D6VUW2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=PAB1-binding protein 1 {ECO:0000305};
DE AltName: Full=Poly(A)-binding protein-binding protein {ECO:0000305};
GN Name=PBP1; Synonyms=MRS16; OrderedLocusNames=YGR178C;
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].
RC STRAIN=ATCC 44774 / DBY747;
RA Mecklenbrauker I.;
RT "Sequencing and characterization of a suppressor of the pet- phenotype in a
RT Saccharomyces cerevisiae strain without mitochondrial group II introns.";
RL Thesis (1996), Vienna Biocentre, Austria.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
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 FUNCTION, INTERACTION WITH PAB1, AND DISRUPTION PHENOTYPE.
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 [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP INTERACTION WITH LSM12 AND PBP4, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16702403; DOI=10.1101/gad.1422006;
RA Fleischer T.C., Weaver C.M., McAfee K.J., Jennings J.L., Link A.J.;
RT "Systematic identification and functional screens of uncharacterized
RT proteins associated with eukaryotic ribosomal complexes.";
RL Genes Dev. 20:1294-1307(2006).
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 SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [9]
RP FUNCTION, INTERACTION WITH MKT1, SUBUNIT, SUBCELLULAR LOCATION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=15082763; DOI=10.1128/mcb.24.9.3670-3681.2004;
RA Tadauchi T., Inada T., Matsumoto K., Irie K.;
RT "Posttranscriptional regulation of HO expression by the Mkt1-Pbp1
RT complex.";
RL Mol. Cell. Biol. 24:3670-3681(2004).
RN [10]
RP FUNCTION, AND INTERACTION WITH FIR1 AND PBP4.
RX PubMed=15121841; DOI=10.1128/mcb.24.10.4196-4206.2004;
RA Mangus D.A., Smith M.M., McSweeney J.M., Jacobson A.;
RT "Identification of factors regulating poly(A) tail synthesis and
RT maturation.";
RL Mol. Cell. Biol. 24:4196-4206(2004).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-436, AND
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106; SER-215 AND SER-436, AND
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND THR-193, AND
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).
RN [14]
RP INTERACTION WITH IGO1.
RX PubMed=20471941; DOI=10.1016/j.molcel.2010.02.039;
RA Talarek N., Cameroni E., Jaquenoud M., Luo X., Bontron S., Lippman S.,
RA Devgan G., Snyder M., Broach J.R., De Virgilio C.;
RT "Initiation of the TORC1-regulated G0 program requires Igo1/2, which
RT license specific mRNAs to evade degradation via the 5'-3' mRNA decay
RT pathway.";
RL Mol. Cell 38:345-355(2010).
RN [15]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-344, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22106047; DOI=10.1002/pmic.201100166;
RA Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL Proteomics 12:236-240(2012).
CC -!- FUNCTION: Involved in pre-mRNA polyadenylation (PubMed:15121841,
CC PubMed:9819425). May act to repress the ability of PAB1 to negatively
CC regulate polyadenylation (PubMed:9819425). Negative regulator of
CC poly(A) nuclease (PAN) activity (PubMed:15121841). Promotes mating-type
CC switching in mother cells by positively regulating HO mRNA translation
CC (PubMed:15082763). Localizes MKT1 to polysomes (PubMed:15082763).
CC {ECO:0000269|PubMed:15082763, ECO:0000269|PubMed:15121841,
CC ECO:0000269|PubMed:9819425}.
CC -!- SUBUNIT: Interacts (via C-terminus) with MKT1 (via C-terminus)
CC (PubMed:15082763). Interacts with FIR1, IGO1, LSM12, PBP4 and PAB1
CC (PubMed:15121841, PubMed:16702403, PubMed:20471941, PubMed:9819425).
CC {ECO:0000269|PubMed:15082763, ECO:0000269|PubMed:15121841,
CC ECO:0000269|PubMed:16702403, ECO:0000269|PubMed:20471941,
CC ECO:0000269|PubMed:9819425}.
CC -!- INTERACTION:
CC P53297; P38828: LSM12; NbExp=4; IntAct=EBI-12961, EBI-24700;
CC P53297; P40850: MKT1; NbExp=3; IntAct=EBI-12961, EBI-10983;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15082763}. Nucleus {ECO:0000269|PubMed:14562095}.
CC Mitochondrion {ECO:0000269|PubMed:14576278}. Note=Localizes to
CC polysomes. {ECO:0000269|PubMed:15082763}.
CC -!- DISRUPTION PHENOTYPE: Abnormal mRNA processing; 3' termini are cleaved
CC but transcripts lack full-length poly(A) tails (PubMed:9819425).
CC Decreases HO mRNA translation (PubMed:15082763).
CC {ECO:0000269|PubMed:15082763, ECO:0000269|PubMed:9819425}.
CC -!- MISCELLANEOUS: Present with 2870 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ataxin-2 family. {ECO:0000305}.
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DR EMBL; U46931; AAB94294.1; -; Genomic_DNA.
DR EMBL; Z72963; CAA97204.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08273.1; -; Genomic_DNA.
DR PIR; S64492; S64492.
DR RefSeq; NP_011694.3; NM_001181307.3.
DR AlphaFoldDB; P53297; -.
DR SMR; P53297; -.
DR BioGRID; 33430; 278.
DR ComplexPortal; CPX-1295; MKT1-PBP1 translation regulation complex.
DR DIP; DIP-2464N; -.
DR IntAct; P53297; 25.
DR MINT; P53297; -.
DR STRING; 4932.YGR178C; -.
DR iPTMnet; P53297; -.
DR MaxQB; P53297; -.
DR PaxDb; P53297; -.
DR PRIDE; P53297; -.
DR EnsemblFungi; YGR178C_mRNA; YGR178C; YGR178C.
DR GeneID; 853089; -.
DR KEGG; sce:YGR178C; -.
DR SGD; S000003410; PBP1.
DR VEuPathDB; FungiDB:YGR178C; -.
DR eggNOG; KOG2375; Eukaryota.
DR GeneTree; ENSGT00940000174882; -.
DR HOGENOM; CLU_009985_0_0_1; -.
DR InParanoid; P53297; -.
DR OMA; YFTAPTW; -.
DR BioCyc; YEAST:G3O-30871-MON; -.
DR PRO; PR:P53297; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P53297; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0005844; C:polysome; IDA:SGD.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0043621; F:protein self-association; IDA:SGD.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0043007; P:maintenance of rDNA; IMP:SGD.
DR GO; GO:1904262; P:negative regulation of TORC1 signaling; IMP:SGD.
DR GO; GO:1900365; P:positive regulation of mRNA polyadenylation; IMP:SGD.
DR GO; GO:0045727; P:positive regulation of translation; IMP:SGD.
DR GO; GO:0031494; P:regulation of mating type switching; IC:ComplexPortal.
DR GO; GO:1901524; P:regulation of mitophagy; IMP:SGD.
DR GO; GO:0006417; P:regulation of translation; IC:ComplexPortal.
DR GO; GO:0034063; P:stress granule assembly; IMP:SGD.
DR InterPro; IPR045117; ATXN2-like.
DR InterPro; IPR009604; LsmAD_domain.
DR InterPro; IPR025852; SM_dom_ATX.
DR PANTHER; PTHR12854; PTHR12854; 1.
DR Pfam; PF06741; LsmAD; 1.
DR Pfam; PF14438; SM-ATX; 1.
DR SMART; SM01272; LsmAD; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Isopeptide bond; Mitochondrion; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..722
FT /note="PAB1-binding protein 1"
FT /id="PRO_0000058244"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 703..722
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 193
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 215
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 436
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956"
FT CROSSLNK 344
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0007744|PubMed:22106047"
SQ SEQUENCE 722 AA; 78781 MW; 92005F3A2346193E CRC64;
MKGNFRKRDS STNSRKGGNS DSNYTNGGVP NQNNSSMFYE NPEITRNFDD RQDYLLANSI
GSDVTVTVTS GVKYTGLLVS CNLESTNGID VVLRFPRVAD SGVSDSVDDL AKTLGETLLI
HGEDVAELEL KNIDLSLDEK WENSKAQETT PARTNIEKER VNGESNEVTK FRTDVDISGS
GREIKERKLE KWTPEEGAEH FDINKGKALE DDSASWDQFA VNEKKFGVKS TFDEHLYTTK
INKDDPNYSK RLQEAERIAK EIESQGTSGN IHIAEDRGII IDDSGLDEED LYSGVDRRGD
ELLAALKSNS KPNSNKGNRY VPPTLRQQPH HMDPAIISSS NSNKNENAVS TDTSTPAAAG
APEGKPPQKT SKNKKSLSSK EAQIEELKKF SEKFKVPYDI PKDMLEVLKR SSSTLKSNSS
LPPKPISKTP SAKTVSPTTQ ISAGKSESRR SGSNISQGQS STGHTTRSST SLRRRNHGSF
FGAKNPHTND AKRVLFGKSF NMFIKSKEAH DEKKKGDDAS ENMEPFFIEK PYFTAPTWLN
TIEESYKTFF PDEDTAIQEA QTRFQQRQLN SMGNAVPGMN PAMGMNMGGM MGFPMGGPSA
SPNPMMNGFA AGSMGMYMPF QPQPMFYHPS MPQMMPVMGS NGAEEGGGNI SPHVPAGFMA
AGPGAPMGAF GYPGGIPFQG MMGSGPSGMP ANGSAMHSHG HSRNYHQTSH HGHHNSSTSG
HK
