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Entry version 183 (07 Oct 2020)
Sequence version 1 (01 Nov 1996)
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Protein

Exosome complex exonuclease RRP6

Gene

RRP6

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

Nuclear-specific 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. 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. RRP6 has 3'-5' exonuclease activity which is not modulated upon association with Exo-9 suggesting that the complex inner RNA-binding path is not used to access its active site.4 Publications

Miscellaneous

Present with 2160 molecules/cell in log phase SD medium.1 Publication

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

GO - Biological processi

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

Molecular functionExonuclease, Hydrolase, Nuclease, RNA-binding
Biological processrRNA processing

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-6791226, Major pathway of rRNA processing in the nucleolus and cytosol

<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 RRP6 (EC:3.1.13.-)
Alternative name(s):
Ribosomal RNA-processing protein 6
<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:RRP6
Synonyms:UNC733
Ordered Locus Names:YOR001W
<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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<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

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YOR001W

Saccharomyces Genome Database

More...
SGDi
S000005527, RRP6

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

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

Keywords - Cellular componenti

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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Deletion mutant is impaired in growth at all temperatures and is nonviable at 37 degrees Celsius. It is defective in the 3' processing of the 5.8S rRNA and accumulates a discrete species, 5.8S + 30, that is 3' extended by about 30 nucleotides. Deletion also causes an accumulation of 7S RNA and 5' ETS and increases the level of poly(A)+ mRNA.3 Publications

<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_00000974561 – 733Exosome complex exonuclease RRP6Add BLAST733

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 residuei138PhosphoserineCombined sources1
Modified residuei520PhosphothreonineCombined sources1
Modified residuei640PhosphoserineCombined sources1
Modified residuei645PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q12149

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

More...
PaxDbi
Q12149

PRoteomics IDEntifications database

More...
PRIDEi
Q12149

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q12149

<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 associates 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. RRP6 specifically is part of the nuclear form of the RNA exosome complex; the association appears to be mediated by Exo-9 and not by DIS3.

Interacts with LRP1.

Interacts with NPL3, NOP53 and PAP1.

6 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
34404, 849 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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

Database of interacting proteins

More...
DIPi
DIP-4560N

Protein interaction database and analysis system

More...
IntActi
Q12149, 28 interactors

Molecular INTeraction database

More...
MINTi
Q12149

STRING: functional protein association networks

More...
STRINGi
4932.YOR001W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q12149, 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

1733
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
Q12149

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
Q12149

<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>Domaini435 – 515HRDCPROSITE-ProRule annotationAdd BLAST81

<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 exosome component 10/RRP6 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2206, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000015408

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_010129_3_2_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q12149

KEGG Orthology (KO)

More...
KOi
K12591

Identification of Orthologs from Complete Genome Data

More...
OMAi
FKAVHQW

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002562, 3'-5'_exonuclease_dom
IPR012588, Exosome-assoc_fac_Rrp6_N
IPR010997, HRDC-like_sf
IPR002121, HRDC_dom
IPR012337, RNaseH-like_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01612, DNA_pol_A_exo1, 1 hit
PF00570, HRDC, 1 hit
PF08066, PMC2NT, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00474, 35EXOc, 1 hit
SM00341, HRDC, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF47819, SSF47819, 1 hit
SSF53098, SSF53098, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50967, HRDC, 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.

Q12149-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTSENPDVLL SRVINVVRAA SSLASQDVDF YKNLDRGFSK DLKSKADKLA
60 70 80 90 100
DMANEIILSI DEHHESFELK EEDISDLWNN FGNIMDNLLE MSDHSLDKLN
110 120 130 140 150
CAINSKSRGS DLQYLGEFSG KNFSPTKRVE KPQLKFKSPI DNSESHPFIP
160 170 180 190 200
LLKEKPNALK PLSESLRLVD DDENNPSHYP HPYEYEIDHQ EYSPEILQIR
210 220 230 240 250
EEIPSKSWDD SVPIWVDTST ELESMLEDLK NTKEIAVDLE HHDYRSYYGI
260 270 280 290 300
VCLMQISTRE RDYLVDTLKL RENLHILNEV FTNPSIVKVF HGAFMDIIWL
310 320 330 340 350
QRDLGLYVVG LFDTYHASKA IGLPRHSLAY LLENFANFKT SKKYQLADWR
360 370 380 390 400
IRPLSKPMTA YARADTHFLL NIYDQLRNKL IESNKLAGVL YESRNVAKRR
410 420 430 440 450
FEYSKYRPLT PSSEVYSPIE KESPWKILMY QYNIPPEREV LVRELYQWRD
460 470 480 490 500
LIARRDDESP RFVMPNQLLA ALVAYTPTDV IGVVSLTNGV TEHVRQNAKL
510 520 530 540 550
LANLIRDALR NIKNTNEEAT PIPSSETKAD GILLETISVP QIRDVMERFS
560 570 580 590 600
VLCNSNISKS RAKPVTNSSI LLGKILPREE HDIAYSKDGL PNKVKTEDIR
610 620 630 640 650
IRAQNFKSAL ANLEDIIFEI EKPLVVPVKL EEIKTVDPAS APNHSPEIDN
660 670 680 690 700
LDDLVVLKKK NIQKKQPAKE KGVTEKDAVD YSKIPNILSN KPGQNNRQQK
710 720 730
KRRFDPSSSD SNGPRAAKKR RPAAKGKNLS FKR
Length:733
Mass (Da):84,039
Last modified:November 1, 1996 - 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:iB19A0B2ED74C6DA7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti402E → G in AAT92869 (PubMed:17322287).Curated1

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
Z74909 Genomic DNA Translation: CAA99189.1
U43491 Genomic DNA Translation: AAC49480.1
AY692850 Genomic DNA Translation: AAT92869.1
BK006948 Genomic DNA Translation: DAA10783.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S61984

NCBI Reference Sequences

More...
RefSeqi
NP_014643.1, NM_001183420.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YOR001W_mRNA; YOR001W; YOR001W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
854162

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YOR001W

<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
Z74909 Genomic DNA Translation: CAA99189.1
U43491 Genomic DNA Translation: AAC49480.1
AY692850 Genomic DNA Translation: AAT92869.1
BK006948 Genomic DNA Translation: DAA10783.1
PIRiS61984
RefSeqiNP_014643.1, NM_001183420.1

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
1M0Ymodel-A207-382[»]
2HBJX-ray2.10A129-536[»]
2HBKX-ray2.25A129-536[»]
2HBLX-ray2.30A129-536[»]
2HBMX-ray2.70A129-536[»]
4IFDX-ray2.80K518-693[»]
4OO1X-ray3.30J129-685[»]
4WFCX-ray2.35A/C/E1-111[»]
4WFDX-ray2.40A/D/G1-111[»]
5C0WX-ray4.60K1-693[»]
5C0XX-ray3.81K1-693[»]
5C0YX-ray2.10A/B122-518[»]
5K36X-ray3.10J129-684[»]
5VZJX-ray3.30J129-684[»]
6FSZelectron microscopy4.60KK1-733[»]
6FT6electron microscopy3.90KK1-733[»]
SMRiQ12149
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi34404, 849 interactors
ComplexPortaliCPX-599, Nuclear/nucleolar exosome complex, DIS3-RRP6 variant
DIPiDIP-4560N
IntActiQ12149, 28 interactors
MINTiQ12149
STRINGi4932.YOR001W

PTM databases

iPTMnetiQ12149

Proteomic databases

MaxQBiQ12149
PaxDbiQ12149
PRIDEiQ12149

Genome annotation databases

EnsemblFungiiYOR001W_mRNA; YOR001W; YOR001W
GeneIDi854162
KEGGisce:YOR001W

Organism-specific databases

EuPathDBiFungiDB:YOR001W
SGDiS000005527, RRP6

Phylogenomic databases

eggNOGiKOG2206, Eukaryota
GeneTreeiENSGT00390000015408
HOGENOMiCLU_010129_3_2_1
InParanoidiQ12149
KOiK12591
OMAiFKAVHQW

Enzyme and pathway databases

ReactomeiR-SCE-6791226, Major pathway of rRNA processing in the nucleolus and cytosol

Miscellaneous databases

EvolutionaryTraceiQ12149

Protein Ontology

More...
PROi
PR:Q12149
RNActiQ12149, protein

Family and domain databases

InterProiView protein in InterPro
IPR002562, 3'-5'_exonuclease_dom
IPR012588, Exosome-assoc_fac_Rrp6_N
IPR010997, HRDC-like_sf
IPR002121, HRDC_dom
IPR012337, RNaseH-like_sf
PfamiView protein in Pfam
PF01612, DNA_pol_A_exo1, 1 hit
PF00570, HRDC, 1 hit
PF08066, PMC2NT, 1 hit
SMARTiView protein in SMART
SM00474, 35EXOc, 1 hit
SM00341, HRDC, 1 hit
SUPFAMiSSF47819, SSF47819, 1 hit
SSF53098, SSF53098, 1 hit
PROSITEiView protein in PROSITE
PS50967, HRDC, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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 nameiRRP6_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: Q12149
Secondary accession number(s): D6W267, Q6B280
<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: June 1, 2001
Last sequence update: November 1, 1996
Last modified: October 7, 2020
This is version 183 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Yeast chromosome XV
    Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names
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