Polyadenylate-binding protein, cytoplasmic and nuclear - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P04147 (PABP_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 163. History...

Clusters with 100%, 90%, 50% identity |

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Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Polyadenylate-binding protein, cytoplasmic and nuclear
Short name=PABP
Short name=Poly(A)-binding protein

Alternative name(s):
ARS consensus-binding protein ACBP-67
Polyadenylate tail-binding protein

Gene names

Name:	PAB1
Ordered Locus Names:	YER165W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	577 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds the poly(A) tail of mRNA. Appears to be an important mediator of the multiple roles of the poly(A) tail in mRNA biogenesis, stability and translation. In the nucleus, interacts with the nuclear cleavage factor IA (CFIA), which is required for both mRNA cleavage and polyadenylation. Is also required for efficient mRNA export to the cytoplasm. Acts in concert with a poly(A)-specific nuclease (PAN) to affect poly(A) tail shortening, which may occur concomitantly with either nucleocytoplasmic mRNA transport or translational initiation. Regulates PAN activity via interaction with the stimulator PAN3 or the inhibitor PBP1. In the cytoplasm, affects both translation and mRNA decay. Stimulates translation by interaction with translation initiation factor eIF4G, a subunit of the cap-binding complex eIF4F, bringing the 5'- and 3'-ends of the mRNA in proximity. The formation of this circular mRNP structure appears to be critical for the synergistic effects of the cap and the poly(A) tail in facilitating translation initiation, recycling of ribosomes, and mRNA stability. Also regulates translation termination by recruiting eukaryotic release factor 3 (eRF3). Interaction with eRF3 is also required for regulation of normal mRNA decay through translation termination-coupled poly(A) shortening, probably mediated by PAN. Loss of PAB1 from the mRNP after deadenylation triggers mRNA degradation. Inhibits the major cytoplasmic mRNA deadenylase CCR4-NOT complex. Is also associated peripherally with COPI vesicles through its interaction with ARF1, and this is required for correct localization of the asymmetrically distributed ASH1 mRNA. Ref.8 Ref.9 Ref.12 Ref.16 Ref.17 Ref.19 Ref.23 Ref.26 Ref.27 Ref.29 Ref.32 Ref.33 Ref.35 Ref.36
Subunit structure	Binds to poly(A) mRNA to form a periodic structure with a packing density of one molecule per 25 adenylate residues. Interacts with the nuclear export factor CRM1 and with the importin SXM1. Interacts with RNA15, a component of the cleavage factor IA (CFIA) complex. Interacts with translation initiation factor eIF4G (TIF4631 or TIF4632) and release factor eRF3 (SUP35). Interacts with the PAB-dependent poly(A)-nuclease (PAN) complex regulatory subunit PAN3. Interacts with ARF1, DCP1, PBP1, the Hsp70 chaperone SSA1, and TPA1. Interacts with PAT1 in a RNA-dependent manner. Ref.13 Ref.16 Ref.18 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.28 Ref.29 Ref.31 Ref.32 Ref.33 Ref.34 Ref.36 Ref.37
Subcellular location	Cytoplasm. Nucleus. Note: Predominantly cytoplasmic. Rapidly shuttles between the nucleus and the cytoplasm. Can be exported from the nucleus through at least 2 distinct pathways, the main being dependent on the exportin CRM1, and the second requiring MEX67 and ongoing mRNA export. Import is mediated by the importin SXM1. Ref.2 Ref.11 Ref.35 Ref.36
Domain	RNA recognition motifs (RRMs) 1 and 2 bind specifically to the poly(A) tail, whereas RRMs 3 and 4 bind non-specifically to polypyrimidine RNAs and may serve to bind to a different part of the messenger or to other RNAs. RRM 2 also mediates interaction with eIF-4G. Ref.10
Miscellaneous	Present with 198000 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the polyadenylate-binding protein type-1 family. Contains 1 PABC domain. Contains 4 RRM (RNA recognition motif) domains.

Ontologies

Keywords
Biological process	Translation regulation Transport mRNA processing mRNA transport
Cellular component	Cytoplasm Nucleus
Domain	Repeat
Ligand	RNA-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW mRNA transport Inferred from electronic annotation. Source: UniProtKB-KW regulation of nuclear-transcribed mRNA poly(A) tail shortening Inferred from mutant phenotype PubMed 17766253. Source: SGD regulation of translational initiation Inferred from mutant phenotype Ref.23. Source: SGD
Cellular_component	cytoplasmic stress granule Inferred from direct assay PubMed 17908917 PubMed 18981231 PubMed 19470581. Source: SGD nucleus Inferred from direct assay PubMed 11914276 Ref.35 Ref.36. Source: SGD ribosome Inferred from direct assay PubMed 8631901. Source: SGD
Molecular_function	nucleotide binding Inferred from electronic annotation. Source: InterPro poly(A) RNA binding Inferred from mutant phenotype Ref.15. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TIF4631	P39935	2	EBI-12823,EBI-9002
TIF4632	P39936	2	EBI-12823,EBI-9006

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 577

576

Polyadenylate-binding protein, cytoplasmic and nuclear

PRO_0000081720

Regions

Domain

38 – 116

RRM 1

Domain

126 – 203

RRM 2

Domain

219 – 296

RRM 3

Domain

322 – 399

RRM 4

Domain

489 – 568

PABC

Region

9 – 61

Required and sufficient for nuclear export Potential

Region

281 – 317

Required and sufficient for nuclear import Potential

Region

473 – 577

105

Interaction with SUP35

Motif

12 – 17

Nuclear export signal Potential

Compositional bias

422 – 431

Poly-Ala

Amino acid modifications

Modified residue

N-acetylalanine Ref.14

Modified residue

Phosphoserine Ref.38

Modified residue

125

Phosphoserine Ref.38

Modified residue

249

Phosphoserine Ref.38

Modified residue

405

Phosphoserine Ref.38

Experimental info

Mutagenesis

L → A: Impairs nuclear export; when associated with A-15. Ref.35

Mutagenesis

L → A: Impairs nuclear export; when associated with A-12. Ref.35

Mutagenesis

L → A in PAB1-14; fails to bind poly(U), but not poly(A) RNA; when associated with Q-166; Q-259 and Q-362. Ref.15

Mutagenesis

Y → V in PAB1-16; reduces affinity for oligo(A) about 100-fold, impairs poly(A)-dependent translation, but still interacts with eIF4G; when associated with V-170. In PAB1-15; fails to bind RNA; when associated with V-170; V-263 and V-366. Ref.15 Ref.21

Mutagenesis

134 – 136

HPD → DKS in PAB1-134. Ref.23

Mutagenesis

148

V → A in PAB1-148; greatly reduces poly(A)-dependent translation and moderately reduces stimulation of cap-dependent translation in vitro; when associated with N-151. Ref.23

Mutagenesis

151

D → N in PAB1-148; greatly reduces poly(A)-dependent translation and moderately reduces stimulation of cap-dependent translation in vitro; when associated with A-148. Ref.23

Mutagenesis

157 – 159

IAT → VVC in PAB1-157; greatly reduces poly(A)-dependent translation and stimulation of cap-dependent translation in vitro. Ref.23

Mutagenesis

166

K → Q in PAB1-14; fails to bind poly(U), but not poly(A) RNA; when associated with A-79; Q-259 and Q-362. Ref.15

Mutagenesis

170

F → V in PAB1-6; selectively reduces poly(A) RNA binding. In PAB1-16; reduces affinity for oligo(A) about 100-fold, impairs poly(A)-dependent translation, but still interacts with eIF4G; when associated with V-83. In PAB1-15; fails to bind RNA; when associated with V-83; V-263 and V-366. Ref.15 Ref.21

Mutagenesis

175 – 177

EEG → TQE in PAB1-175; greatly reduces poly(A)-dependent translation and stimulation of cap-dependent translation in vitro. Ref.23

Mutagenesis

180 – 181

KE → ER in PAB1-180; abolishes poly(A)-dependent translation and greatly reduces stimulation of cap-dependent translation in vitro. Impairs interaction with eIF4G.

Mutagenesis

184 – 186

DAL → EKM in PAB1-184; abolishes poly(A)-dependent translation and moderately reduces stimulation of cap-dependent translation in vitro. Impairs interaction with eIF4G. Ref.23

Mutagenesis

193 – 197

GQEIY → DRKVF in PAB1-193; moderately reduces stimulation of cap-dependent translation in vitro. Ref.23

Mutagenesis

199 – 202

APHL → GRFK in PAB1-199; moderately reduces poly(A)-dependent translation and stimulation of cap-dependent translation in vitro. Ref.23

Mutagenesis

259

K → Q in PAB1-14; fails to bind poly(U), but not poly(A) RNA; when associated with A-79; Q-166 and Q-362. Ref.15

Mutagenesis

263

F → V in PAB1-7. In PAB1-15; fails to bind RNA; when associated with V-83; V-170 and V-366. Ref.15 Ref.21

Mutagenesis

362

K → Q in PAB1-14; fails to bind poly(U), but not poly(A) RNA; when associated with A-79; Q-166 and Q-259. Ref.15

Mutagenesis

366

F → V in PAB1-8; selectively reduces poly(U) RNA binding. In PAB1-15; fails to bind RNA; when associated with V-83; V-170 and V-263. Ref.15 Ref.21

Sequence conflict

426

A → R in AAA34838. Ref.1

Secondary structure

577

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P04147 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 4F97E494753E17C7
Show »

FASTA

577

64,344

        10         20         30         40         50         60 
MADITDKTAE QLENLNIQDD QKQAATGSES QSVENSSASL YVGDLEPSVS EAHLYDIFSP 

        70         80         90        100        110        120 
IGSVSSIRVC RDAITKTSLG YAYVNFNDHE AGRKAIEQLN YTPIKGRLCR IMWSQRDPSL 

       130        140        150        160        170        180 
RKKGSGNIFI KNLHPDIDNK ALYDTFSVFG DILSSKIATD ENGKSKGFGF VHFEEEGAAK 

       190        200        210        220        230        240 
EAIDALNGML LNGQEIYVAP HLSRKERDSQ LEETKAHYTN LYVKNINSET TDEQFQELFA 

       250        260        270        280        290        300 
KFGPIVSASL EKDADGKLKG FGFVNYEKHE DAVKAVEALN DSELNGEKLY VGRAQKKNER 

       310        320        330        340        350        360 
MHVLKKQYEA YRLEKMAKYQ GVNLFVKNLD DSVDDEKLEE EFAPYGTITS AKVMRTENGK 

       370        380        390        400        410        420 
SKGFGFVCFS TPEEATKAIT EKNQQIVAGK PLYVAIAQRK DVRRSQLAQQ IQARNQMRYQ 

       430        440        450        460        470        480 
QATAAAAAAA AGMPGQFMPP MFYGVMPPRG VPFNGPNPQQ MNPMGGMPKN GMPPQFRNGP 

       490        500        510        520        530        540 
VYGVPPQGGF PRNANDNNQF YQQKQRQALG EQLYKKVSAK TSNEEAAGKI TGMILDLPPQ 

       550        560        570 
EVFPLLESDE LFEQHYKEAS AAYESFKKEQ EQQTEQA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A single gene from yeast for both nuclear and cytoplasmic polyadenylate-binding proteins: domain structure and expression." Sachs A.B., Bond M.W., Kornberg R.D. Cell 45:827-835(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 9-29.
[2]	"mRNA polyadenylate-binding protein: gene isolation and sequencing and identification of a ribonucleoprotein consensus sequence." Adam S.A., Nakagawa T., Swanson M.S., Woodruff T.K., Dreyfuss G. Mol. Cell. Biol. 6:2932-2943(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION.
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome V." Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. Davis R.W. Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." 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. LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	"The yeast protein encoded by PUB1 binds T-rich single stranded DNA." Cockell M., Frutiger S., Hughes G.J., Gasser S.M. Nucleic Acids Res. 22:32-40(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 8-17; 167-173 AND 242-248, CHARACTERIZATION.
[7]	"A single domain of yeast poly(A)-binding protein is necessary and sufficient for RNA binding and cell viability." Sachs A.B., Davis R.W., Kornberg R.D. Mol. Cell. Biol. 7:3268-3276(1987) [PubMed] [Europe PMC] [Abstract] Cited for: RNA-BINDING.
[8]	"The poly(A) binding protein is required for poly(A) shortening and 60S ribosomal subunit-dependent translation initiation." Sachs A.B., Davis R.W. Cell 58:857-867(1989) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN TRANSLATION INITIATION.
[9]	"The poly(A)-poly(A)-binding protein complex is a major determinant of mRNA stability in vitro." Bernstein P., Peltz S.W., Ross J. Mol. Cell. Biol. 9:659-670(1989) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN MRNA STABILIZATION.
[10]	"The multiple RNA-binding domains of the mRNA poly(A)-binding protein have different RNA-binding activities." Burd C.G., Matunis E.L., Dreyfuss G. Mol. Cell. Biol. 11:3419-3424(1991) [PubMed] [Europe PMC] [Abstract] Cited for: RNA-BINDING, DOMAINS.
[11]	"PUB1 is a major nuclear and cytoplasmic polyadenylated RNA-binding protein in Saccharomyces cerevisiae." Anderson J.T., Paddy M.R., Swanson M.S. Mol. Cell. Biol. 13:6102-6113(1993) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[12]	"Multiple functions for the poly(A)-binding protein in mRNA decapping and deadenylation in yeast." Caponigro G., Parker R. Genes Dev. 9:2421-2432(1995) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[13]	"Association of the yeast poly(A) tail binding protein with translation initiation factor eIF-4G." Tarun S.Z. Jr., Sachs A.B. EMBO J. 15:7168-7177(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TIF4632.
[14]	"Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins." Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., Payne W.E. Electrophoresis 18:1347-1360(1997) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION AT ALA-2.
[15]	"Differential effects of aromatic and charged residue substitutions in the RNA binding domains of the yeast poly(A)-binding protein." Deardorff J.A., Sachs A.B. J. Mol. Biol. 269:67-81(1997) [PubMed] [Europe PMC] [Abstract] Cited for: RNA-BINDING, MUTAGENESIS OF LEU-79; TYR-83; LYS-166; PHE-170; LYS-259; PHE-263; LYS-362 AND PHE-366.
[16]	"Yeast Pab1 interacts with Rna15 and participates in the control of the poly(A) tail length in vitro." Amrani N., Minet M., Le Gouar M., Lacroute F., Wyers F. Mol. Cell. Biol. 17:3694-3701(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN MRNA MATURATION, INTERACTION WITH RNA15.
[17]	"The major yeast poly(A)-binding protein is associated with cleavage factor IA and functions in premessenger RNA 3'-end formation." Minvielle-Sebastia L., Preker P.J., Wiederkehr T., Strahm Y., Keller W. Proc. Natl. Acad. Sci. U.S.A. 94:7897-7902(1997) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN MRNA MATURATION.
[18]	"Translation initiation factor eIF4G mediates in vitro poly(A) tail-dependent translation." Tarun S.Z. Jr., Wells S.E., Deardorff J.A., Sachs A.B. Proc. Natl. Acad. Sci. U.S.A. 94:9046-9051(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TIF4631 AND TIF4632.
[19]	"mRNA stabilization by poly(A) binding protein is independent of poly(A) and requires translation." Coller J.M., Gray N.K., Wickens M.P. Genes Dev. 12:3226-3235(1998) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN MRNA STABILITY.
[20]	"Circularization of mRNA by eukaryotic translation initiation factors." Wells S.E., Hillner P.E., Vale R.D., Sachs A.B. Mol. Cell 2:135-140(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TIF4631, ATOMIC FORCE MICROSCOPY OF CIRCULAR MRNP STRUCTURE.
[21]	"RNA recognition motif 2 of yeast Pab1p is required for its functional interaction with eukaryotic translation initiation factor 4G." Kessler S.H., Sachs A.B. Mol. Cell. Biol. 18:51-57(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TIF4632, MUTAGENESIS OF TYR-83 AND PHE-170.
[22]	"Pbp1p, a factor interacting with Saccharomyces cerevisiae poly(A)-binding protein, regulates polyadenylation." Mangus D.A., Amrani N., Jacobson A. Mol. Cell. Biol. 18:7383-7396(1998) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PBP1.
[23]	"The yeast poly(A)-binding protein Pab1p stimulates in vitro poly(A)-dependent and cap-dependent translation by distinct mechanisms." Otero L.J., Ashe M.P., Sachs A.B. EMBO J. 18:3153-3163(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN TRANSLATION STIMULATION, MUTAGENESIS OF 134-HIS--ASP-136; VAL-148; ASP-151; 157-ILE--THR-159; 175-GLU--GLY-177; 180-LYS-GLU-181; 184-ASP--LEU-186; 193-GLY--TYR-197 AND 199-ALA--LEU-202, INTERACTION WITH TIF4631 AND TIF4632.
[24]	"The eukaryotic mRNA decapping protein Dcp1 interacts physically and functionally with the eIF4F translation initiation complex." Vilela C., Velasco C., Ptushkina M., McCarthy J.E.G. EMBO J. 19:4372-4382(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH DCP1 AND TIF4631.
[25]	"The yeast hsp70 homologue Ssa is required for translation and interacts with Sis1 and Pab1 on translating ribosomes." Horton L.E., James P., Craig E.A., Hensold J.O. J. Biol. Chem. 276:14426-14433(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SSA1.
[26]	"Targeting an mRNA for decapping: displacement of translation factors and association of the Lsm1p-7p complex on deadenylated yeast mRNAs." Tharun S., Parker R. Mol. Cell 8:1075-1083(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN MRNA DECAY, INTERACTION WITH PAT1.
[27]	"Ccr4p is the catalytic subunit of a Ccr4p/Pop2p/Notp mRNA deadenylase complex in Saccharomyces cerevisiae." Tucker M., Staples R.R., Valencia-Sanchez M.A., Muhlrad D., Parker R. EMBO J. 21:1427-1436(2002) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN REGULATION OF CCR4-NOT.
[28]	"Poly(A)-binding protein acts in translation termination via eukaryotic release factor 3 interaction and does not influence [PSI(+)] propagation." Cosson B., Couturier A., Chabelskaya S., Kiktev D., Inge-Vechtomov S.G., Philippe M., Zhouravleva G. Mol. Cell. Biol. 22:3301-3315(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SUP35.
[29]	"Translation termination factor eRF3 mediates mRNA decay through the regulation of deadenylation." Hosoda N., Kobayashi T., Uchida N., Funakoshi Y., Kikuchi Y., Hoshino S., Katada T. J. Biol. Chem. 278:38287-38291(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN MRNA DECAY, INTERACTION WITH SUP35.
[30]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[31]	"The GTP-binding release factor eRF3 as a key mediator coupling translation termination to mRNA decay." Kobayashi T., Funakoshi Y., Hoshino S., Katada T. J. Biol. Chem. 279:45693-45700(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SUP35.
[32]	"Arf1p provides an unexpected link between COPI vesicles and mRNA in Saccharomyces cerevisiae." Trautwein M., Dengjel J., Schirle M., Spang A. Mol. Biol. Cell 15:5021-5037(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN MRNA TRANSPORT, INTERACTION WITH ARF1.
[33]	"Positive and negative regulation of poly(A) nuclease." Mangus D.A., Evans M.C., Agrin N.S., Smith M.M., Gongidi P., Jacobson A. Mol. Cell. Biol. 24:5521-5533(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PAN REGULATION, INTERACTION WITH PAN3 AND PBP1.
[34]	"A faux 3'-UTR promotes aberrant termination and triggers nonsense-mediated mRNA decay." Amrani N., Ganesan R., Kervestin S., Mangus D.A., Ghosh S., Jacobson A. Nature 432:112-118(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SUP35.
[35]	"Yeast poly(A)-binding protein, Pab1, and PAN, a poly(A) nuclease complex recruited by Pab1, connect mRNA biogenesis to export." Dunn E.F., Hammell C.M., Hodge C.A., Cole C.N. Genes Dev. 19:90-103(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN MRNA EXPORT, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-12 AND LEU-15.
[36]	"Yeast poly(A)-binding protein Pab1 shuttles between the nucleus and the cytoplasm and functions in mRNA export." Brune C., Munchel S.E., Fischer N., Podtelejnikov A.V., Weis K. RNA 11:517-531(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN MRNA EXPORT, SUBCELLULAR LOCATION, INTERACTION WITH CRM1 AND SXM1.
[37]	"Tpa1p is part of an mRNP complex that influences translation termination, mRNA deadenylation, and mRNA turnover in Saccharomyces cerevisiae." Keeling K.M., Salas-Marco J., Osherovich L.Z., Bedwell D.M. Mol. Cell. Biol. 26:5237-5248(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH TPA1.
[38]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63; SER-125; SER-249 AND SER-405, MASS SPECTROMETRY.
[39]	"Solution structure of the orphan PABC domain from Saccharomyces cerevisiae poly(A)-binding protein." Kozlov G., Siddiqui N., Coillet-Matillon S., Trempe J.-F., Ekiel I., Sprules T., Gehring K. J. Biol. Chem. 277:22822-22828(2002) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 489-577.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M12780 Genomic DNA. Translation: AAA34838.1.
M13371 Genomic DNA. Translation: AAA34787.1.
D00023 Genomic DNA. Translation: BAA00017.1.
U18922 Genomic DNA. Translation: AAB64692.1.
AY692854 Genomic DNA. Translation: AAT92873.1.
BK006939 Genomic DNA. Translation: DAA07827.1.

PIR

DNBYPA. A25221.

RefSeq

NP_011092.1. NM_001179055.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IFW	NMR	-	A	491-577	[»]

ProteinModelPortal

P04147.

SMR

P04147. Positions 38-414, 489-577.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-2275N.

IntAct

P04147. 164 interactions.

MINT

MINT-693056.

STRING

4932.YER165W.

Proteomic databases

PaxDb

P04147.

PeptideAtlas

P04147.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YER165W; YER165W; YER165W.

GeneID

856912.

KEGG

sce:YER165W.

Organism-specific databases

SGD

S000000967. PAB1.

Phylogenomic databases

eggNOG

COG0724.

GeneTree

ENSGT00640000091232.

HOGENOM

HOG000217922.

K13126.

OMA

ITEKNQQ.

OrthoDB

EOG4QJVWJ.

Enzyme and pathway databases

BioCyc

YEAST:G3O-30326-MONOMER.

Gene expression databases

Genevestigator

P04147.

GermOnline

YER165W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

1.10.1900.10. 1 hit.
3.30.70.330. 4 hits.

InterPro

IPR012677. Nucleotide-bd_a/b_plait.
IPR006515. PABP_1234.
IPR002004. PABP_HYD.
IPR000504. RRM_dom.
[Graphical view]

Pfam

PF00658. PABP. 1 hit.
PF00076. RRM_1. 4 hits.
[Graphical view]

SMART

SM00517. PolyA. 1 hit.
SM00360. RRM. 4 hits.
[Graphical view]

SUPFAM

SSF63570. PABP_HYD. 1 hit.

TIGRFAMs

TIGR01628. PABP-1234. 1 hit.

PROSITE

PS51309. PABC. 1 hit.
PS50102. RRM. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P04147.

NextBio

983356.

Entry information

Entry name

PABP_YEAST

Accession

Primary (citable) accession number: P04147
Secondary accession number(s): D3DM73

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1986
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 163 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents