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Protein

Exosome complex component RRP42

Gene

EXOSC7

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

Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes.

Caution

The six exosome core subunits containing a RNase PH-domain are not phosphorolytically active.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

  • 3'-5'-exoribonuclease activity Source: UniProtKB
  • AU-rich element binding Source: GO_Central
  • RNA binding 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 processrRNA processing

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-380994 ATF4 activates genes
R-HSA-429958 mRNA decay by 3' to 5' exoribonuclease
R-HSA-450385 Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA
R-HSA-450513 Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA
R-HSA-450604 KSRP (KHSRP) binds and destabilizes mRNA
R-HSA-6791226 Major pathway of rRNA processing in the nucleolus and cytosol

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

More...
MoonDBi
Q15024 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:
Exosome complex component RRP42
Alternative name(s):
Exosome component 7
Ribosomal RNA-processing protein 42
p8
<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:EXOSC7
Synonyms:KIAA0116, RRP42
<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 3

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000075914.12

Human Gene Nomenclature Database

More...
HGNCi
HGNC:28112 EXOSC7

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
606488 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q15024

<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, Exosome, 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

Organism-specific databases

DisGeNET

More...
DisGeNETi
23016

Open Targets

More...
OpenTargetsi
ENSG00000075914

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA134880567

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
EXOSC7

Domain mapping of disease mutations (DMDM)

More...
DMDMi
322510129

<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 methionineiRemovedCombined sources1 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_00001399632 – 291Exosome complex component RRP42Add BLAST290

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-acetylalanineCombined sources1 Publication1
Modified residuei116N6-acetyllysineCombined sources1
Modified residuei177PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q15024

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q15024

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q15024

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

More...
PaxDbi
Q15024

PeptideAtlas

More...
PeptideAtlasi
Q15024

PRoteomics IDEntifications database

More...
PRIDEi
Q15024

ProteomicsDB human proteome resource

More...
ProteomicsDBi
60375

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
Q15024

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q15024

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

More...
PhosphoSitePlusi
Q15024

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000075914 Expressed in 234 organ(s), highest expression level in oocyte

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q15024 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q15024 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA036182
HPA057980

<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

Component of the RNA exosome complex. Specifically part of the catalytically inactive RNA exosome core (Exo-9) complex which is believed to associate with catalytic subunits EXOSC10, and DIS3 or DIS3L in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits specifically containing the heterodimers EXOSC4-EXOSC9, EXOSC5-EXOSC8 and EXOSC6-EXOSC7, and peripheral S1 domain-containing components EXOSC1, EXOSC2 and EXOSC3 located on the top of the ring structure. Interacts with EXOSC1. Interacts with ZC3HAV1.4 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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
116658, 43 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-476 Nuclear exosome complex, DIS3-EXOSC10 variant
CPX-591 Nucleolar exosome complex, EXOSC10 variant
CPX-592 Cytoplasmic exosome complex, DIS3L variant
CPX-593 Exosome complex, DIS3 variant
CPX-600 Cytoplasmic exosome complex, DIS3L-EXOSC10 variant

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
Q15024

Database of interacting proteins

More...
DIPi
DIP-31266N

Protein interaction database and analysis system

More...
IntActi
Q15024, 32 interactors

Molecular INTeraction database

More...
MINTi
Q15024

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000265564

<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

1291
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
2NN6X-ray3.35E1-291[»]
6D6Qelectron microscopy3.45E1-291[»]
6D6Relectron microscopy3.45E1-291[»]
6H25electron microscopy3.80E1-291[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q15024

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

More...
SMRi
Q15024

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q15024

<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

<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

Belongs to the RNase PH family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1612 Eukaryota
COG2123 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000153590

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000229504

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG051521

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q15024

KEGG Orthology (KO)

More...
KOi
K12589

Identification of Orthologs from Complete Genome Data

More...
OMAi
NPYDCTR

Database of Orthologous Groups

More...
OrthoDBi
965225at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q15024

TreeFam database of animal gene trees

More...
TreeFami
TF320641

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.30.230.70, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001247 ExoRNase_PH_dom1
IPR015847 ExoRNase_PH_dom2
IPR036345 ExoRNase_PH_dom2_sf
IPR027408 PNPase/RNase_PH_dom_sf
IPR020568 Ribosomal_S5_D2-typ_fold

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01138 RNase_PH, 1 hit
PF03725 RNase_PH_C, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54211 SSF54211, 1 hit
SSF55666 SSF55666, 1 hit

<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>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.

Q15024-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASVTLSEAE KVYIVHGVQE DLRVDGRGCE DYRCVEVETD VVSNTSGSAR
60 70 80 90 100
VKLGHTDILV GVKAEMGTPK LEKPNEGYLE FFVDCSASAT PEFEGRGGDD
110 120 130 140 150
LGTEIANTLY RIFNNKSSVD LKTLCISPRE HCWVLYVDVL LLECGGNLFD
160 170 180 190 200
AISIAVKAAL FNTRIPRVRV LEDEEGSKDI ELSDDPYDCI RLSVENVPCI
210 220 230 240 250
VTLCKIGYRH VVDATLQEEA CSLASLLVSV TSKGVVTCMR KVGKGSLDPE
260 270 280 290
SIFEMMETGK RVGKVLHASL QSVVHKEESL GPKRQKVGFL G
Length:291
Mass (Da):31,821
Last modified:February 8, 2011 - v3
<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:iA674F745CEC61BBB
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_032765169R → Q. Corresponds to variant dbSNP:rs34512144Ensembl.1
Natural variantiVAR_014923274V → LCombined sources2 PublicationsCorresponds to variant dbSNP:rs6794Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AC104165 Genomic DNA No translation available.
BC012831 mRNA Translation: AAH12831.1
D29958 mRNA Translation: BAA06226.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS2725.1

NCBI Reference Sequences

More...
RefSeqi
NP_055819.2, NM_015004.3

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.719958

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000265564; ENSP00000265564; ENSG00000075914

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
23016

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:23016

UCSC genome browser

More...
UCSCi
uc003coi.3 human

Keywords - Coding sequence diversityi

Polymorphism

<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
AC104165 Genomic DNA No translation available.
BC012831 mRNA Translation: AAH12831.1
D29958 mRNA Translation: BAA06226.1
CCDSiCCDS2725.1
RefSeqiNP_055819.2, NM_015004.3
UniGeneiHs.719958

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2NN6X-ray3.35E1-291[»]
6D6Qelectron microscopy3.45E1-291[»]
6D6Relectron microscopy3.45E1-291[»]
6H25electron microscopy3.80E1-291[»]
ProteinModelPortaliQ15024
SMRiQ15024
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116658, 43 interactors
ComplexPortaliCPX-476 Nuclear exosome complex, DIS3-EXOSC10 variant
CPX-591 Nucleolar exosome complex, EXOSC10 variant
CPX-592 Cytoplasmic exosome complex, DIS3L variant
CPX-593 Exosome complex, DIS3 variant
CPX-600 Cytoplasmic exosome complex, DIS3L-EXOSC10 variant
CORUMiQ15024
DIPiDIP-31266N
IntActiQ15024, 32 interactors
MINTiQ15024
STRINGi9606.ENSP00000265564

Protein family/group databases

MoonDBiQ15024 Predicted

PTM databases

iPTMnetiQ15024
PhosphoSitePlusiQ15024

Polymorphism and mutation databases

BioMutaiEXOSC7
DMDMi322510129

2D gel databases

SWISS-2DPAGEiQ15024

Proteomic databases

EPDiQ15024
jPOSTiQ15024
MaxQBiQ15024
PaxDbiQ15024
PeptideAtlasiQ15024
PRIDEiQ15024
ProteomicsDBi60375

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
23016
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265564; ENSP00000265564; ENSG00000075914
GeneIDi23016
KEGGihsa:23016
UCSCiuc003coi.3 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
23016
DisGeNETi23016
EuPathDBiHostDB:ENSG00000075914.12

GeneCards: human genes, protein and diseases

More...
GeneCardsi
EXOSC7

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0003236
HGNCiHGNC:28112 EXOSC7
HPAiHPA036182
HPA057980
MIMi606488 gene
neXtProtiNX_Q15024
OpenTargetsiENSG00000075914
PharmGKBiPA134880567

Human Unidentified Gene-Encoded large proteins database

More...
HUGEi
Search...

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1612 Eukaryota
COG2123 LUCA
GeneTreeiENSGT00940000153590
HOGENOMiHOG000229504
HOVERGENiHBG051521
InParanoidiQ15024
KOiK12589
OMAiNPYDCTR
OrthoDBi965225at2759
PhylomeDBiQ15024
TreeFamiTF320641

Enzyme and pathway databases

ReactomeiR-HSA-380994 ATF4 activates genes
R-HSA-429958 mRNA decay by 3' to 5' exoribonuclease
R-HSA-450385 Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA
R-HSA-450513 Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA
R-HSA-450604 KSRP (KHSRP) binds and destabilizes mRNA
R-HSA-6791226 Major pathway of rRNA processing in the nucleolus and cytosol

Miscellaneous databases

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

More...
ChiTaRSi
EXOSC7 human
EvolutionaryTraceiQ15024

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

More...
GenomeRNAii
23016

Protein Ontology

More...
PROi
PR:Q15024

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000075914 Expressed in 234 organ(s), highest expression level in oocyte
ExpressionAtlasiQ15024 baseline and differential
GenevisibleiQ15024 HS

Family and domain databases

Gene3Di3.30.230.70, 1 hit
InterProiView protein in InterPro
IPR001247 ExoRNase_PH_dom1
IPR015847 ExoRNase_PH_dom2
IPR036345 ExoRNase_PH_dom2_sf
IPR027408 PNPase/RNase_PH_dom_sf
IPR020568 Ribosomal_S5_D2-typ_fold
PfamiView protein in Pfam
PF01138 RNase_PH, 1 hit
PF03725 RNase_PH_C, 1 hit
SUPFAMiSSF54211 SSF54211, 1 hit
SSF55666 SSF55666, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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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 nameiEXOS7_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: Q15024
Secondary accession number(s): Q96E72
<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: June 6, 2002
Last sequence update: February 8, 2011
Last modified: January 16, 2019
This is version 180 of the entry and version 3 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 entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
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