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Protein

Polyadenylate-binding protein 1

Gene

PABPC1

Organism
Homo sapiens (Human)
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, including that of its own transcript. May be involved in cytoplasmic regulatory processes of mRNA metabolism such as pre-mRNA splicing. Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by PAIP2. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo. Involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Involved in regulation of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons; for the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed. By binding to long poly(A) tails, may protect them from uridylation by ZCCHC6/ZCCHC11 and hence contribute to mRNA stability (PubMed:25480299). Positively regulates the replication of dengue virus (DENV) (PubMed:26735137).6 Publications

Miscellaneous

Many viruses shutoff host mRNA translational machinery by inhibiting cellular PABPC1 activity using different mechanisms. Picornaviruses, caliciviruses or lentiviruses encode proteases that cleave PABPC1 at several defined sites in the proline-rich linker region between RRMs and the C-terminal domain. Rotaviruses, gammherpesviruses and bunyamwera virus relocalize PABPC1 from the cytoplasm to the nucleus thus altering its function. Many of these viruses translate their mRNA in a PABPC1-independent manner and are unaffected by host PABPC1 inhibition.

Caution

Was termed (Ref. 5) polyadenylate binding protein II.Curated

<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

  • mRNA 3'-UTR binding Source: UniProtKB
  • poly(A) binding Source: MGI
  • poly(U) RNA binding Source: MGI
  • protein C-terminus binding Source: UniProtKB
  • RNA binding Source: CAFA
  • translation activator activity Source: UniProtKB

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 splicing, Nonsense-mediated mRNA decay

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-156827 L13a-mediated translational silencing of Ceruloplasmin expression
R-HSA-429947 Deadenylation of mRNA
R-HSA-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-HSA-72649 Translation initiation complex formation
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-975956 Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)
R-HSA-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)

SIGNOR Signaling Network Open Resource

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SIGNORi
P11940

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
P11940 Predicted

<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 1
Short name:
PABP-1
Short name:
Poly(A)-binding protein 1
<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:PABPC1
Synonyms:PAB1, PABP1, PABPC2
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <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 8

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000070756.13

Human Gene Nomenclature Database

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HGNCi
HGNC:8554 PABPC1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
604679 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P11940

<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 Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

<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>Mutagenesisi455R → A: Greatly reduces methylation by CARM1 (in vitro); when associated with A-460. 1 Publication1
Mutagenesisi460R → A: Greatly reduces methylation by CARM1 (in vitro); when associated with A-455. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
26986

Open Targets

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OpenTargetsi
ENSG00000070756

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA32880

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL1293286

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
PABPC1

Domain mapping of disease mutations (DMDM)

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DMDMi
3183544

<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 ‘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_00000816981 – 636Polyadenylate-binding protein 1Add BLAST636

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 residuei1N-acetylmethionineCombined sources1
Modified residuei299N6-methyllysine1 Publication1
Modified residuei315PhosphoserineCombined sources1
Modified residuei319PhosphothreonineCombined sources1
Modified residuei385Omega-N-methylarginineCombined sources1
Modified residuei419Omega-N-methylarginineCombined sources1
Modified residuei432Omega-N-methylarginineCombined sources1
Modified residuei436Omega-N-methylarginineCombined sources1
Modified residuei455Omega-N-methylated arginine; by CARM1; partial1 Publication1
Modified residuei460Omega-N-methylated arginine; by CARM1; partial1 Publication1
Modified residuei475Omega-N-methylarginineBy similarity1
Modified residuei481Omega-N-methylarginineCombined sources1
Modified residuei493Asymmetric dimethylarginine; alternateCombined sources1
Modified residuei493Dimethylated arginine; alternate2 Publications1
Modified residuei493Omega-N-methylarginine; alternateCombined sources2 Publications1
Modified residuei506Omega-N-methylarginineCombined sources1
Modified residuei512N6-acetyllysineCombined sources1
Modified residuei518Omega-N-methylarginineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated by MAPKAPK2.1 Publication
Methylated by CARM1. Arg-493 is dimethylated, probably to asymmetric dimethylarginine.3 Publications

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P11940

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P11940

MaxQB - The MaxQuant DataBase

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MaxQBi
P11940

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

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PaxDbi
P11940

PeptideAtlas

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PeptideAtlasi
P11940

PRoteomics IDEntifications database

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PRIDEi
P11940

ProteomicsDB human proteome resource

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ProteomicsDBi
52814
52815 [P11940-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P11940

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P11940

SwissPalm database of S-palmitoylation events

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SwissPalmi
P11940

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
P11940

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Ubiquitous.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000070756 Expressed in 230 organ(s), highest expression level in testis

CleanEx database of gene expression profiles

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CleanExi
HS_PABPC1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P11940 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P11940 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB011536
HPA045423
HPA067156

<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

May interact with SETX (PubMed:21700224). May form homodimers. Component of a multisubunit autoregulatory ribonucleoprotein complex (ARC), at least composed of IGF2BP1, PABPC1 and CSDE1 (PubMed:16356927). Directly interacts with IGF2BP1. Part of a complex associated with the FOS mCRD domain and consisting of HNRPD, SYNCRIP, PAIP1 and CSDE1/UNR (PubMed:11051545). Interacts with the PABPC1-interacting motif-1 (PAM1) and -2 (PAM2) of PAIP1 and PAIP2 (PubMed:9548260, PubMed:11172725, PubMed:11438674, PubMed:11997512, PubMed:11287632, PubMed:20096703). Interacts with PAIP1 with a 1:1 stoichiometry and with PAIP2 with a 1:2 stoichiometry. The interaction with CSDE1 is direct and RNA-independent. Found in a mRNP complex with YBX2 (By similarity). Interacts with TENT2/GLD2 (By similarity). Identified in the spliceosome C complex (PubMed:11991638). Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and YBX1. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Interacts with NFX1 (PubMed:17267499). Interacts with PIWIL1 (By similarity). Interacts with AGO1, AGO2, GSPT1 and GSPT2 (PubMed:17932509, PubMed:18447585, Ref. 51). Interacts with human cytomegalovirus/HHV-5 protein UL69 (PubMed:20133758). Interacts with LARP4B (Ref. 53). Interacts (via the second and third RRM domains and the C-terminus) with PAIP2B (via central acidic portion and C-terminus) (PubMed:16804161, PubMed:11287632). Interacts with LARP1 (PubMed:20430826, PubMed:24532714, PubMed:25940091). Interacts with RYDEN (PubMed:26735137). Found in a complex with RYDEN and LARP1 (PubMed:26735137). Interacts with LARP4 (PubMed:21098120). Interacts with ZFC3H1 in a RNase-sensitive manner (PubMed:27871484). Interacts with TRIM71 (via NHL repeats) in an RNA-dependent manner (PubMed:23125361). Interacts with TENT5C; the interaction has no effect on TENT5C poly(A) polymerase function (PubMed:28931820).By similarity28 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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
117939, 266 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-1076 mCRD-poly(A)-bridging complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P11940

Database of interacting proteins

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DIPi
DIP-31613N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

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ELMi
P11940

Protein interaction database and analysis system

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IntActi
P11940, 124 interactors

Molecular INTeraction database

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MINTi
P11940

STRING: functional protein association networks

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STRINGi
9606.ENSP00000313007

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P11940

<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

1636
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
1CVJX-ray2.60A/B/C/D/E/F/G/H1-190[»]
1G9LNMR-A498-636[»]
1JGNNMR-A544-636[»]
1JH4NMR-A544-636[»]
2K8GNMR-A90-182[»]
2RQGNMR-B541-623[»]
2RQHNMR-B541-623[»]
2X04X-ray1.49A/B545-619[»]
3KTPX-ray1.50A544-626[»]
3KTRX-ray1.70A544-626[»]
3KUIX-ray2.30A544-626[»]
3KUJX-ray1.40A544-626[»]
3KURX-ray2.50A/B/C/D/E/F/G/H544-617[»]
3KUSX-ray1.40A/B544-626[»]
3KUTX-ray1.50A/B544-626[»]
3PKNX-ray1.80A544-626[»]
3PTHX-ray1.70A543-621[»]
4F02X-ray2.00A/D1-190[»]
4F25X-ray1.90A99-199[»]
4F26X-ray2.00A99-199[»]
5DX1X-ray1.93F/G/H/I449-466[»]
5DX8X-ray1.94E/F/G/H449-466[»]
5DXAX-ray2.07F/G/I449-466[»]
5LGPX-ray2.04E/F/G/H447-458[»]
5LGQX-ray2.11E/F/G/H456-466[»]
5LGRX-ray2.00E/F/G/H447-458[»]
5LGSX-ray2.10E/F/G/H456-464[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P11940

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

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SMRi
P11940

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
P11940

<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>Domaini11 – 89RRM 1PROSITE-ProRule annotationAdd BLAST79
Domaini99 – 175RRM 2PROSITE-ProRule annotationAdd BLAST77
Domaini191 – 268RRM 3PROSITE-ProRule annotationAdd BLAST78
Domaini294 – 370RRM 4PROSITE-ProRule annotationAdd BLAST77
Domaini542 – 619PABCPROSITE-ProRule annotationAdd BLAST78

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>Regioni166 – 289CSDE1-bindingAdd BLAST124

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 biasi495 – 501Poly-Ala7

<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

The RNA-binding domains RRM1 and RRM2 and the C-terminus (last 138 amino acids) regions interact with the PABPC1-interacting motif-1 (PAM1) and -2 (PAM2) of PAIP1, respectively.2 Publications
The RNA-binding domains RRM2 and RRM3 and the C-terminus (last 138 amino acids) regions interact with the PABPC1-interacting motif-1 (PAM1) and -2 (PAM2) of PAIP2, respectively.2 Publications

<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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0123 Eukaryota
ENOG410XR5X LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000153773

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000217922

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG002295

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P11940

KEGG Orthology (KO)

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KOi
K13126

Identification of Orthologs from Complete Genome Data

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OMAi
VTEALCV

Database of Orthologous Groups

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OrthoDBi
1027234at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P11940

TreeFam database of animal gene trees

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TreeFami
TF300458

Family and domain databases

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

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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, 3 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>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<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.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 19 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P11940-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MNPSAPSYPM ASLYVGDLHP DVTEAMLYEK FSPAGPILSI RVCRDMITRR
60 70 80 90 100
SLGYAYVNFQ QPADAERALD TMNFDVIKGK PVRIMWSQRD PSLRKSGVGN
110 120 130 140 150
IFIKNLDKSI DNKALYDTFS AFGNILSCKV VCDENGSKGY GFVHFETQEA
160 170 180 190 200
AERAIEKMNG MLLNDRKVFV GRFKSRKERE AELGARAKEF TNVYIKNFGE
210 220 230 240 250
DMDDERLKDL FGKFGPALSV KVMTDESGKS KGFGFVSFER HEDAQKAVDE
260 270 280 290 300
MNGKELNGKQ IYVGRAQKKV ERQTELKRKF EQMKQDRITR YQGVNLYVKN
310 320 330 340 350
LDDGIDDERL RKEFSPFGTI TSAKVMMEGG RSKGFGFVCF SSPEEATKAV
360 370 380 390 400
TEMNGRIVAT KPLYVALAQR KEERQAHLTN QYMQRMASVR AVPNPVINPY
410 420 430 440 450
QPAPPSGYFM AAIPQTQNRA AYYPPSQIAQ LRPSPRWTAQ GARPHPFQNM
460 470 480 490 500
PGAIRPAAPR PPFSTMRPAS SQVPRVMSTQ RVANTSTQTM GPRPAAAAAA
510 520 530 540 550
ATPAVRTVPQ YKYAAGVRNP QQHLNAQPQV TMQQPAVHVQ GQEPLTASML
560 570 580 590 600
ASAPPQEQKQ MLGERLFPLI QAMHPTLAGK ITGMLLEIDN SELLHMLESP
610 620 630
ESLRSKVDEA VAVLQAHQAK EAAQKAVNSA TGVPTV
Length:636
Mass (Da):70,671
Last modified:July 15, 1998 - v2
<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:i2EB1B02A346132EE
GO
Isoform 2 (identifier: P11940-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     447-535: Missing.

Note: No experimental confirmation available.
Show »
Length:547
Mass (Da):61,181
Checksum:i8088B4F7DFABAFB8
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 19 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E7EQV3E7EQV3_HUMAN
Polyadenylate-binding protein
PABPC1
591Annotation score:

Annotation score:2 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>
E7ERJ7E7ERJ7_HUMAN
Polyadenylate-binding protein
PABPC1
604Annotation score:

Annotation score:2 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>
A0A087WTT1A0A087WTT1_HUMAN
Polyadenylate-binding protein
PABPC1
522Annotation score:

Annotation score:2 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>
H0YB75H0YB75_HUMAN
Polyadenylate-binding protein 1
PABPC1
183Annotation score:

Annotation score:1 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>
H0YAW6H0YAW6_HUMAN
Polyadenylate-binding protein 1
PABPC1
187Annotation score:

Annotation score:1 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>
H0YAR2H0YAR2_HUMAN
Polyadenylate-binding protein 1
PABPC1
284Annotation score:

Annotation score:1 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>
H0YAP2H0YAP2_HUMAN
Polyadenylate-binding protein 1
PABPC1
131Annotation score:

Annotation score:1 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>
E5RHG7E5RHG7_HUMAN
Polyadenylate-binding protein 1
PABPC1
75Annotation score:

Annotation score:1 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>
E5RJB9E5RJB9_HUMAN
Polyadenylate-binding protein 1
PABPC1
129Annotation score:

Annotation score:1 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>
E5RH24E5RH24_HUMAN
Polyadenylate-binding protein 1
PABPC1
118Annotation score:

Annotation score:1 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>
There are more potential isoformsShow all

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 conflicti211 – 213Missing in CAA68428 (PubMed:2885805).Curated3
Sequence conflicti410M → I in CAA88401 (Ref. 5) Curated1
Sequence conflicti428I → V in CAA68428 (PubMed:2885805).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_009846447 – 535Missing in isoform 2. 1 PublicationAdd BLAST89

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Y00345 mRNA Translation: CAA68428.1
U68104
, U68093, U68094, U68095, U68097, U68098, U68099, U68100, U68101, U68102, U68103 Genomic DNA Translation: AAD08718.1
AP001205 Genomic DNA No translation available.
BC015958 mRNA Translation: AAH15958.1
BC023520 mRNA Translation: AAH23520.1
Z48501 mRNA Translation: CAA88401.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS6289.1 [P11940-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A93668 DNHUPA
S52491

NCBI Reference Sequences

More...
RefSeqi
NP_002559.2, NM_002568.3 [P11940-1]
XP_005250918.1, XM_005250861.2 [P11940-1]

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.387804

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000318607; ENSP00000313007; ENSG00000070756 [P11940-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
26986

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:26986

UCSC genome browser

More...
UCSCi
uc003yjs.2 human [P11940-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
Y00345 mRNA Translation: CAA68428.1
U68104
, U68093, U68094, U68095, U68097, U68098, U68099, U68100, U68101, U68102, U68103 Genomic DNA Translation: AAD08718.1
AP001205 Genomic DNA No translation available.
BC015958 mRNA Translation: AAH15958.1
BC023520 mRNA Translation: AAH23520.1
Z48501 mRNA Translation: CAA88401.1
CCDSiCCDS6289.1 [P11940-1]
PIRiA93668 DNHUPA
S52491
RefSeqiNP_002559.2, NM_002568.3 [P11940-1]
XP_005250918.1, XM_005250861.2 [P11940-1]
UniGeneiHs.387804

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CVJX-ray2.60A/B/C/D/E/F/G/H1-190[»]
1G9LNMR-A498-636[»]
1JGNNMR-A544-636[»]
1JH4NMR-A544-636[»]
2K8GNMR-A90-182[»]
2RQGNMR-B541-623[»]
2RQHNMR-B541-623[»]
2X04X-ray1.49A/B545-619[»]
3KTPX-ray1.50A544-626[»]
3KTRX-ray1.70A544-626[»]
3KUIX-ray2.30A544-626[»]
3KUJX-ray1.40A544-626[»]
3KURX-ray2.50A/B/C/D/E/F/G/H544-617[»]
3KUSX-ray1.40A/B544-626[»]
3KUTX-ray1.50A/B544-626[»]
3PKNX-ray1.80A544-626[»]
3PTHX-ray1.70A543-621[»]
4F02X-ray2.00A/D1-190[»]
4F25X-ray1.90A99-199[»]
4F26X-ray2.00A99-199[»]
5DX1X-ray1.93F/G/H/I449-466[»]
5DX8X-ray1.94E/F/G/H449-466[»]
5DXAX-ray2.07F/G/I449-466[»]
5LGPX-ray2.04E/F/G/H447-458[»]
5LGQX-ray2.11E/F/G/H456-466[»]
5LGRX-ray2.00E/F/G/H447-458[»]
5LGSX-ray2.10E/F/G/H456-464[»]
ProteinModelPortaliP11940
SMRiP11940
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117939, 266 interactors
ComplexPortaliCPX-1076 mCRD-poly(A)-bridging complex
CORUMiP11940
DIPiDIP-31613N
ELMiP11940
IntActiP11940, 124 interactors
MINTiP11940
STRINGi9606.ENSP00000313007

Chemistry databases

BindingDBiP11940
ChEMBLiCHEMBL1293286

Protein family/group databases

MoonDBiP11940 Predicted

PTM databases

iPTMnetiP11940
PhosphoSitePlusiP11940
SwissPalmiP11940

Polymorphism and mutation databases

BioMutaiPABPC1
DMDMi3183544

Proteomic databases

EPDiP11940
jPOSTiP11940
MaxQBiP11940
PaxDbiP11940
PeptideAtlasiP11940
PRIDEiP11940
ProteomicsDBi52814
52815 [P11940-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
26986
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000318607; ENSP00000313007; ENSG00000070756 [P11940-1]
GeneIDi26986
KEGGihsa:26986
UCSCiuc003yjs.2 human [P11940-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
26986
DisGeNETi26986
EuPathDBiHostDB:ENSG00000070756.13

GeneCards: human genes, protein and diseases

More...
GeneCardsi
PABPC1
HGNCiHGNC:8554 PABPC1
HPAiCAB011536
HPA045423
HPA067156
MIMi604679 gene
neXtProtiNX_P11940
OpenTargetsiENSG00000070756
PharmGKBiPA32880

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0123 Eukaryota
ENOG410XR5X LUCA
GeneTreeiENSGT00940000153773
HOGENOMiHOG000217922
HOVERGENiHBG002295
InParanoidiP11940
KOiK13126
OMAiVTEALCV
OrthoDBi1027234at2759
PhylomeDBiP11940
TreeFamiTF300458

Enzyme and pathway databases

ReactomeiR-HSA-156827 L13a-mediated translational silencing of Ceruloplasmin expression
R-HSA-429947 Deadenylation of mRNA
R-HSA-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-HSA-72649 Translation initiation complex formation
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-975956 Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)
R-HSA-975957 Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)
SIGNORiP11940

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
PABPC1 human
EvolutionaryTraceiP11940

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
PABPC1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
26986
PMAP-CutDBiP11940

Protein Ontology

More...
PROi
PR:P11940

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000070756 Expressed in 230 organ(s), highest expression level in testis
CleanExiHS_PABPC1
ExpressionAtlasiP11940 baseline and differential
GenevisibleiP11940 HS

Family and domain databases

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, 3 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

More...
ProtoNeti
Search...

<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 nameiPABP1_HUMAN
<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: P11940
Secondary accession number(s): Q15097, Q93004
<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: October 1, 1989
Last sequence update: July 15, 1998
Last modified: January 16, 2019
This is version 231 of the entry and version 2 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 programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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