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UniProtKB - Q08162 (RRP44_YEAST)

Entry version 180 (25 May 2022)
Sequence version 1 (01 Nov 1997)
Previous versions | rss
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Protein

Exosome complex exonuclease DIS3

Gene

DIS3

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

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 cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and in RNA surveillance pathways, preventing translation of aberrant mRNAs. 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. DIS3 has both 3'-5' exonuclease and endonuclease activities. The exonuclease activity of DIS3 is down-regulated upon association with Exo-9 possibly involving a conformational change in the catalytic domain and threading of the RNA substrate through the complex central channel. Structured substrates can be degraded if they have a 3' single-stranded extension sufficiently long (such as 35 nt poly(A)) to span the proposed complex inner RNA-binding path and to reach the exonuclease site provided by DIS3. Plays a role in mitotic control.

3 Publications

Miscellaneous

Present with 606 molecules/cell in log phase SD medium.1 Publication
Mn2+ doesn't support the hydrolytic activity. Activity is KCl or NaCl dependent and activity is slightly increased in the presence of reducing agents such as DTT or beta-mercaptoethanol and doesn't vary notably between pH 6.8 and 8.8.

Caution

It was originally thought that there are multiple subunits in the exosome that have exonuclease activity but it was later shown (PubMed:17173052 and PubMed:17174896) that only this DIS3/RRP44 subunit of the exosome core has this activity.1 Publication

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionEndonuclease, Exonuclease, Hydrolase, Nuclease, RNA-binding
Biological processrRNA processing

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.1.13.1, 984

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-SCE-429958, mRNA decay by 3' to 5' exoribonuclease
R-SCE-450385, Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA
R-SCE-450513, Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA

<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%5Fand%5Ftaxonomy%5Fsection">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 exonuclease DIS3 (EC:3.1.13.-, EC:3.1.26.-)
Alternative name(s):
Chromosome disjunction protein 3
Ribosomal RNA-processing protein 44
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:DIS3
Synonyms:RRP44
Ordered Locus Names:YOL021C
ORF Names:O2197
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 XV

Organism-specific databases

Saccharomyces Genome Database

More...SGDi		S000005381, DIS3

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:YOL021C

<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

Keywords - Cellular componenti

Cytoplasm, Exosome, Mitochondrion, 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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi47C → S: Slow growth; when associated with S-52 and S-55. 1 Publication1
Mutagenesisi52C → S: Slow growth; when associated with S-47 and S-55. 1 Publication1
Mutagenesisi55C → S: Slow growth; when associated with S-47 and S-52. 1 Publication1
Mutagenesisi171D → A: Abolishes endoribonucleolytic activity; no effect on growth. No growth; when associated with N-551. 1 Publication1
Mutagenesisi198D → A: Abolishes endoribonucleolytic activity; no effect on growth. No growth; when associated with N-551. 1 Publication1
Mutagenesisi551D → N: Exoribonucleolytic activity abolished. Accumulation of partially processed 5.8S rRNA and partially degraded 5' ETS. No growth; when associated with A-171. No growth; when associated with A-198. 3 Publications1

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001664231 – 1001Exosome complex exonuclease DIS3Add BLAST1001

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q08162

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

More...PaxDbi		Q08162

PRoteomics IDEntifications database

More...PRIDEi		Q08162

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the RNA exosome complex. The catalytically inactive RNA exosome core (Exo-9) complex which is believed to associate with catalytic subunits DIS3 and RRP6 in cytoplasmic- and nuclear-specific RNA exosome complex forms. Exo-9 is formed by a hexameric ring of RNase PH domain-containing subunits and peripheral S1 domain-containing components CSL4, RRP4 and RRP40 located on the top of the ring structure. DIS3 associates at the respective bottom side with Exo-9.

Interacts with GSP1.

7 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		34381, 240 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-599, Nuclear/nucleolar exosome complex, DIS3-RRP6 variant
CPX-603, Cytoplasmic exosome complex, DIS3 variant

Database of interacting proteins

More...DIPi		DIP-2355N

Protein interaction database and analysis system

More...IntActi		Q08162, 24 interactors

Molecular INTeraction database

More...MINTi		Q08162

STRING: functional protein association networks

More...STRINGi		4932.YOL021C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q08162, 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

11001
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		Q08162

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

More...SMRi		Q08162

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q08162

<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%5Fand%5Fdomains%5Fsection">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>Domaini904 – 1001S1 motifPROSITE-ProRule annotationAdd BLAST98

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>Regioni1 – 235EndoribonucleaseAdd BLAST235
Regioni343 – 363DisorderedSequence analysisAdd BLAST21

<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 RNR ribonuclease family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2102, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00530000063106

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_002333_5_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q08162

Identification of Orthologs from Complete Genome Data

More...OMAi		VVKRNWR

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.40.50.140, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR041505, Dis3_CSD2
IPR012340, NA-bd_OB-fold
IPR029060, PIN-like_dom_sf
IPR002716, PIN_dom
IPR001900, RNase_II/R
IPR022966, RNase_II/R_CS
IPR033771, Rrp44_CSD1
IPR033770, RRP44_S1
IPR022967, S1_dom
IPR003029, S1_domain

Pfam protein domain database

More...Pfami		View protein in Pfam
PF17849, OB_Dis3, 1 hit
PF13638, PIN_4, 1 hit
PF00773, RNB, 1 hit
PF17216, Rrp44_CSD1, 1 hit
PF17215, Rrp44_S1, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00670, PINc, 1 hit
SM00955, RNB, 1 hit
SM00316, S1, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50249, SSF50249, 4 hits
SSF88723, SSF88723, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS01175, RIBONUCLEASE_II, 1 hit
PS50126, S1, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

Q08162-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSVPAIAPRR KRLADGLSVT QKVFVRSRNG GATKIVREHY LRSDIPCLSR 
        60         70         80         90        100
SCTKCPQIVV PDAQNELPKF ILSDSPLELS APIGKHYVVL DTNVVLQAID 
       110        120        130        140        150
LLENPNCFFD VIVPQIVLDE VRNKSYPVYT RLRTLCRDSD DHKRFIVFHN 
       160        170        180        190        200
EFSEHTFVER LPNETINDRN DRAIRKTCQW YSEHLKPYDI NVVLVTNDRL 
       210        220        230        240        250
NREAATKEVE SNIITKSLVQ YIELLPNADD IRDSIPQMDS FDKDLERDTF 
       260        270        280        290        300
SDFTFPEYYS TARVMGGLKN GVLYQGNIQI SEYNFLEGSV SLPRFSKPVL 
       310        320        330        340        350
IVGQKNLNRA FNGDQVIVEL LPQSEWKAPS SIVLDSEHFD VNDNPDIEAG 
       360        370        380        390        400
DDDDNNESSS NTTVISDKQR RLLAKDAMIA QRSKKIQPTA KVVYIQRRSW 
       410        420        430        440        450
RQYVGQLAPS SVDPQSSSTQ NVFVILMDKC LPKVRIRTRR AAELLDKRIV 
       460        470        480        490        500
ISIDSWPTTH KYPLGHFVRD LGTIESAQAE TEALLLEHDV EYRPFSKKVL 
       510        520        530        540        550
ECLPAEGHDW KAPTKLDDPE AVSKDPLLTK RKDLRDKLIC SIDPPGCVDI 
       560        570        580        590        600
DDALHAKKLP NGNWEVGVHI ADVTHFVKPG TALDAEGAAR GTSVYLVDKR 
       610        620        630        640        650
IDMLPMLLGT DLCSLKPYVD RFAFSVIWEL DDSANIVNVN FMKSVIRSRE 
       660        670        680        690        700
AFSYEQAQLR IDDKTQNDEL TMGMRALLKL SVKLKQKRLE AGALNLASPE 
       710        720        730        740        750
VKVHMDSETS DPNEVEIKKL LATNSLVEEF MLLANISVAR KIYDAFPQTA 
       760        770        780        790        800
MLRRHAAPPS TNFEILNEML NTRKNMSISL ESSKALADSL DRCVDPEDPY 
       810        820        830        840        850
FNTLVRIMST RCMMAAQYFY SGAYSYPDFR HYGLAVDIYT HFTSPIRRYC 
       860        870        880        890        900
DVVAHRQLAG AIGYEPLSLT HRDKNKMDMI CRNINRKHRN AQFAGRASIE 
       910        920        930        940        950
YYVGQVMRNN ESTETGYVIK VFNNGIVVLV PKFGVEGLIR LDNLTEDPNS 
       960        970        980        990       1000
AAFDEVEYKL TFVPTNSDKP RDVYVFDKVE VQVRSVMDPI TSKRKAELLL 

K
Length:1,001
Mass (Da):113,707
Last modified:November 1, 1997 - v1
<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:i00DD31BD2D6904F4
GO

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
D76430 Genomic DNA Translation: BAA11176.1
Z74763 Genomic DNA Translation: CAA99021.1
BK006948 Genomic DNA Translation: DAA10760.1

Protein sequence database of the Protein Information Resource

More...PIRi		S66704

NCBI Reference Sequences

More...RefSeqi		NP_014621.1, NM_001183275.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YOL021C_mRNA; YOL021C; YOL021C

Database of genes from NCBI RefSeq genomes

More...GeneIDi		854138

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YOL021C

<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
D76430 Genomic DNA Translation: BAA11176.1
Z74763 Genomic DNA Translation: CAA99021.1
BK006948 Genomic DNA Translation: DAA10760.1
PIRiS66704
RefSeqiNP_014621.1, NM_001183275.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2VNUX-ray2.30D242-1001[»]
2WP8X-ray3.00J25-1001[»]
4IFDX-ray2.80J1-1001[»]
5C0WX-ray4.60J1-1001[»]
5C0XX-ray3.81J1-1001[»]
5G06electron microscopy4.20J1-1001[»]
5JEAX-ray2.65J1-1001[»]
5K36X-ray3.10K1-1001[»]
5VZJX-ray3.30K1-1001[»]
6FSZelectron microscopy4.60JJ1-1001[»]
6LQSelectron microscopy3.80R41-1001[»]
7AJTelectron microscopy4.60EK1-1001[»]
7AJUelectron microscopy3.80EK1-1001[»]
7D4Ielectron microscopy4.00R41-1001[»]
AlphaFoldDBiQ08162
SMRiQ08162
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi34381, 240 interactors
ComplexPortaliCPX-599, Nuclear/nucleolar exosome complex, DIS3-RRP6 variant
CPX-603, Cytoplasmic exosome complex, DIS3 variant
DIPiDIP-2355N
IntActiQ08162, 24 interactors
MINTiQ08162
STRINGi4932.YOL021C

Proteomic databases

MaxQBiQ08162
PaxDbiQ08162
PRIDEiQ08162

Genome annotation databases

EnsemblFungiiYOL021C_mRNA; YOL021C; YOL021C
GeneIDi854138
KEGGisce:YOL021C

Organism-specific databases

SGDiS000005381, DIS3
VEuPathDBiFungiDB:YOL021C

Phylogenomic databases

eggNOGiKOG2102, Eukaryota
GeneTreeiENSGT00530000063106
HOGENOMiCLU_002333_5_0_1
InParanoidiQ08162
OMAiVVKRNWR

Enzyme and pathway databases

BRENDAi3.1.13.1, 984
ReactomeiR-SCE-429958, mRNA decay by 3' to 5' exoribonuclease
R-SCE-450385, Butyrate Response Factor 1 (BRF1) binds and destabilizes mRNA
R-SCE-450513, Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA

Miscellaneous databases

EvolutionaryTraceiQ08162

Protein Ontology

More...PROi		PR:Q08162
RNActiQ08162, protein

Family and domain databases

Gene3Di2.40.50.140, 1 hit
InterProiView protein in InterPro
IPR041505, Dis3_CSD2
IPR012340, NA-bd_OB-fold
IPR029060, PIN-like_dom_sf
IPR002716, PIN_dom
IPR001900, RNase_II/R
IPR022966, RNase_II/R_CS
IPR033771, Rrp44_CSD1
IPR033770, RRP44_S1
IPR022967, S1_dom
IPR003029, S1_domain
PfamiView protein in Pfam
PF17849, OB_Dis3, 1 hit
PF13638, PIN_4, 1 hit
PF00773, RNB, 1 hit
PF17216, Rrp44_CSD1, 1 hit
PF17215, Rrp44_S1, 1 hit
SMARTiView protein in SMART
SM00670, PINc, 1 hit
SM00955, RNB, 1 hit
SM00316, S1, 1 hit
SUPFAMiSSF50249, SSF50249, 4 hits
SSF88723, SSF88723, 1 hit
PROSITEiView protein in PROSITE
PS01175, RIBONUCLEASE_II, 1 hit
PS50126, S1, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 nameiRRP44_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: Q08162
Secondary accession number(s): D6W244
<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%5Fand%5Fisoforms">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, 1997
Last sequence update: November 1, 1997
Last modified: May 25, 2022
This is version 180 of the entry and version 1 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, Reference proteome

Documents

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