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 27-MAR-2024, entry version 188. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 293. 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 GlyGen; P53297; 5 sites, 1 O-linked glycan (5 sites). DR iPTMnet; P53297; -. DR MaxQB; P53297; -. DR PaxDb; 4932-YGR178C; -. DR PeptideAtlas; P53297; -. DR EnsemblFungi; YGR178C_mRNA; YGR178C; YGR178C. DR GeneID; 853089; -. DR KEGG; sce:YGR178C; -. DR AGR; SGD:S000003410; -. 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 OrthoDB; 55807at2759; -. DR BioCyc; YEAST:G3O-30871-MONOMER; -. DR BioGRID-ORCS; 853089; 3 hits in 10 CRISPR screens. 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; IPI:ComplexPortal. DR GO; GO:0003729; F:mRNA binding; HDA:SGD. 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:0045727; P:positive regulation of translation; IMP:SGD. DR GO; GO:0031494; P:regulation of mating type switching; NAS:ComplexPortal. DR GO; GO:1901524; P:regulation of mitophagy; IMP:SGD. DR GO; GO:0006417; P:regulation of translation; NAS:ComplexPortal. DR GO; GO:0034063; P:stress granule assembly; IMP:SGD. DR InterPro; IPR045117; ATXN2-like. DR InterPro; IPR009604; LsmAD_domain. DR InterPro; IPR047575; Sm. DR InterPro; IPR025852; SM_dom_ATX. DR PANTHER; PTHR12854; ATAXIN 2-RELATED; 1. DR PANTHER; PTHR12854:SF7; ATAXIN-2 HOMOLOG; 1. DR Pfam; PF06741; LsmAD; 1. DR Pfam; PF14438; SM-ATX; 1. DR SMART; SM01272; LsmAD; 1. DR PROSITE; PS52002; SM; 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 DOMAIN 51..107 FT /note="Sm" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01346" 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 //