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Entry version 226 (11 Dec 2019)
Sequence version 4 (23 Jan 2007)
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Protein

Polyadenylate-binding protein, cytoplasmic and nuclear

Gene

PAB1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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.14 Publications

Miscellaneous

Present with 198000 molecules/cell in log phase SD medium.1 Publication

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionRNA-binding
Biological processmRNA processing, mRNA transport, Translation regulation, Transport

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-30326-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-156827 L13a-mediated translational silencing of Ceruloplasmin expression
R-SCE-975956 Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)
R-SCE-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:PAB1
Ordered Locus Names:YER165W
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome V

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YER165W

Saccharomyces Genome Database

More...
SGDi
S000000967 PAB1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi12L → A: Impairs nuclear export; when associated with A-15. 1 Publication1
Mutagenesisi15L → A: Impairs nuclear export; when associated with A-12. 1 Publication1
Mutagenesisi79L → A in PAB1-14; fails to bind poly(U), but not poly(A) RNA; when associated with Q-166; Q-259 and Q-362. 1 Publication1
Mutagenesisi83Y → 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. 2 Publications1
Mutagenesisi134 – 136HPD → DKS in PAB1-134. 1 Publication3
Mutagenesisi148V → 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. 1 Publication1
Mutagenesisi151D → 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. 1 Publication1
Mutagenesisi157 – 159IAT → VVC in PAB1-157; greatly reduces poly(A)-dependent translation and stimulation of cap-dependent translation in vitro. 1 Publication3
Mutagenesisi166K → Q in PAB1-14; fails to bind poly(U), but not poly(A) RNA; when associated with A-79; Q-259 and Q-362. 1 Publication1
Mutagenesisi170F → 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. 2 Publications1
Mutagenesisi175 – 177EEG → TQE in PAB1-175; greatly reduces poly(A)-dependent translation and stimulation of cap-dependent translation in vitro. 1 Publication3
Mutagenesisi180 – 181KE → ER in PAB1-180; abolishes poly(A)-dependent translation and greatly reduces stimulation of cap-dependent translation in vitro. Impairs interaction with eIF4G. 1 Publication2
Mutagenesisi184 – 186DAL → EKM in PAB1-184; abolishes poly(A)-dependent translation and moderately reduces stimulation of cap-dependent translation in vitro. Impairs interaction with eIF4G. 1 Publication3
Mutagenesisi193 – 197GQEIY → DRKVF in PAB1-193; moderately reduces stimulation of cap-dependent translation in vitro. 1 Publication5
Mutagenesisi199 – 202APHL → GRFK in PAB1-199; moderately reduces poly(A)-dependent translation and stimulation of cap-dependent translation in vitro. 1 Publication4
Mutagenesisi259K → Q in PAB1-14; fails to bind poly(U), but not poly(A) RNA; when associated with A-79; Q-166 and Q-362. 1 Publication1
Mutagenesisi263F → V in PAB1-7. In PAB1-15; fails to bind RNA; when associated with V-83; V-170 and V-366. 1 Publication1
Mutagenesisi362K → Q in PAB1-14; fails to bind poly(U), but not poly(A) RNA; when associated with A-79; Q-166 and Q-259. 1 Publication1
Mutagenesisi366F → 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. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000817202 – 577Polyadenylate-binding protein, cytoplasmic and nuclearAdd BLAST576

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei107Omega-N-methylarginine1 Publication1
Modified residuei249PhosphoserineCombined sources1
Modified residuei332PhosphoserineCombined sources1
Cross-linki337Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei405PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P04147

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P04147

PRoteomics IDEntifications database

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PRIDEi
P04147

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P04147

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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 an RNA-dependent manner.

18 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
36918, 648 interactors

Database of interacting proteins

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DIPi
DIP-2275N

Protein interaction database and analysis system

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IntActi
P04147, 217 interactors

Molecular INTeraction database

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MINTi
P04147

STRING: functional protein association networks

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STRINGi
4932.YER165W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
P04147 protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1577
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P04147

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P04147

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini38 – 116RRM 1PROSITE-ProRule annotationAdd BLAST79
Domaini126 – 203RRM 2PROSITE-ProRule annotationAdd BLAST78
Domaini219 – 296RRM 3PROSITE-ProRule annotationAdd BLAST78
Domaini322 – 399RRM 4PROSITE-ProRule annotationAdd BLAST78
Domaini489 – 568PABCPROSITE-ProRule annotationAdd BLAST80

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni9 – 61Required and sufficient for nuclear exportSequence analysisAdd BLAST53
Regioni281 – 317Required and sufficient for nuclear importSequence analysisAdd BLAST37
Regioni473 – 577Interaction with SUP35Add BLAST105

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi12 – 17Nuclear export signalSequence analysis6

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi422 – 431Poly-Ala10

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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.1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000217922

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P04147

KEGG Orthology (KO)

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KOi
K13126

Identification of Orthologs from Complete Genome Data

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OMAi
GRAQKKY

Family and domain databases

Database of protein disorder

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DisProti
DP01538

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.70.330, 4 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR036053 PABP-dom
IPR006515 PABP_1234
IPR002004 PABP_HYD
IPR035979 RBD_domain_sf
IPR000504 RRM_dom
IPR003954 RRM_dom_euk

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00658 PABP, 1 hit
PF00076 RRM_1, 4 hits

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00517 PolyA, 1 hit
SM00360 RRM, 4 hits
SM00361 RRM_1, 4 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF54928 SSF54928, 2 hits
SSF63570 SSF63570, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR01628 PABP-1234, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51309 PABC, 1 hit
PS50102 RRM, 4 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P04147-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MADITDKTAE QLENLNIQDD QKQAATGSES QSVENSSASL YVGDLEPSVS
60 70 80 90 100
EAHLYDIFSP IGSVSSIRVC RDAITKTSLG YAYVNFNDHE AGRKAIEQLN
110 120 130 140 150
YTPIKGRLCR IMWSQRDPSL RKKGSGNIFI KNLHPDIDNK ALYDTFSVFG
160 170 180 190 200
DILSSKIATD ENGKSKGFGF VHFEEEGAAK EAIDALNGML LNGQEIYVAP
210 220 230 240 250
HLSRKERDSQ LEETKAHYTN LYVKNINSET TDEQFQELFA KFGPIVSASL
260 270 280 290 300
EKDADGKLKG FGFVNYEKHE DAVKAVEALN DSELNGEKLY VGRAQKKNER
310 320 330 340 350
MHVLKKQYEA YRLEKMAKYQ GVNLFVKNLD DSVDDEKLEE EFAPYGTITS
360 370 380 390 400
AKVMRTENGK SKGFGFVCFS TPEEATKAIT EKNQQIVAGK PLYVAIAQRK
410 420 430 440 450
DVRRSQLAQQ IQARNQMRYQ QATAAAAAAA AGMPGQFMPP MFYGVMPPRG
460 470 480 490 500
VPFNGPNPQQ MNPMGGMPKN GMPPQFRNGP VYGVPPQGGF PRNANDNNQF
510 520 530 540 550
YQQKQRQALG EQLYKKVSAK TSNEEAAGKI TGMILDLPPQ EVFPLLESDE
560 570
LFEQHYKEAS AAYESFKKEQ EQQTEQA
Length:577
Mass (Da):64,344
Last modified:January 23, 2007 - v4
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4F97E494753E17C7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti426A → R in AAA34838 (PubMed:3518950).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
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

Protein sequence database of the Protein Information Resource

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PIRi
A25221 DNBYPA

NCBI Reference Sequences

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RefSeqi
NP_011092.1, NM_001179055.1

Genome annotation databases

Ensembl fungal genome annotation project

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EnsemblFungii
YER165W_mRNA; YER165W; YER165W

Database of genes from NCBI RefSeq genomes

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GeneIDi
856912

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
sce:YER165W

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
PIRiA25221 DNBYPA
RefSeqiNP_011092.1, NM_001179055.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IFWNMR-A491-577[»]
6R5Kelectron microscopy4.80D/F/H1-577[»]
SMRiP04147
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi36918, 648 interactors
DIPiDIP-2275N
IntActiP04147, 217 interactors
MINTiP04147
STRINGi4932.YER165W

PTM databases

iPTMnetiP04147

Proteomic databases

MaxQBiP04147
PaxDbiP04147
PRIDEiP04147

Genome annotation databases

EnsemblFungiiYER165W_mRNA; YER165W; YER165W
GeneIDi856912
KEGGisce:YER165W

Organism-specific databases

EuPathDBiFungiDB:YER165W
SGDiS000000967 PAB1

Phylogenomic databases

HOGENOMiHOG000217922
InParanoidiP04147
KOiK13126
OMAiGRAQKKY

Enzyme and pathway databases

BioCyciYEAST:G3O-30326-MONOMER
ReactomeiR-SCE-156827 L13a-mediated translational silencing of Ceruloplasmin expression
R-SCE-975956 Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)
R-SCE-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

Miscellaneous databases

EvolutionaryTraceiP04147

Protein Ontology

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PROi
PR:P04147
RNActiP04147 protein

Family and domain databases

DisProtiDP01538
Gene3Di3.30.70.330, 4 hits
InterProiView protein in InterPro
IPR012677 Nucleotide-bd_a/b_plait_sf
IPR036053 PABP-dom
IPR006515 PABP_1234
IPR002004 PABP_HYD
IPR035979 RBD_domain_sf
IPR000504 RRM_dom
IPR003954 RRM_dom_euk
PfamiView protein in Pfam
PF00658 PABP, 1 hit
PF00076 RRM_1, 4 hits
SMARTiView protein in SMART
SM00517 PolyA, 1 hit
SM00360 RRM, 4 hits
SM00361 RRM_1, 4 hits
SUPFAMiSSF54928 SSF54928, 2 hits
SSF63570 SSF63570, 1 hit
TIGRFAMsiTIGR01628 PABP-1234, 1 hit
PROSITEiView protein in PROSITE
PS51309 PABC, 1 hit
PS50102 RRM, 4 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPABP_YEAST
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P04147
Secondary accession number(s): D3DM73
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1986
Last sequence update: January 23, 2007
Last modified: December 11, 2019
This is version 226 of the entry and version 4 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names
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