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Entry version 159 (18 Sep 2019)
Sequence version 1 (01 Aug 1992)
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Protein

Atypical kinase COQ8, mitochondrial

Gene

COQ8

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

Atypical kinase involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration (PubMed:27499294). Affects the molecular organization and function of COQ3, possibly through kinase activity towards COQ3, COQ5 and/or COQ7 (PubMed:11279158, PubMed:15063807, PubMed:1648478, PubMed:18801050, PubMed:19002377, PubMed:21296186, PubMed:9210471, PubMed:9266513, PubMed:25498144). Its substrate specificity is unclear: does not show any protein kinase activity (PubMed:27499294). Probably acts as a small molecule kinase, possibly a lipid kinase that phosphorylates a prenyl lipid in the ubiquinone biosynthesis pathway, as suggested by its ability to bind coenzyme Q lipid intermediates (By similarity).By similarity10 Publications

Miscellaneous

Present with 952 molecules/cell in log phase SD medium.1 Publication

Caution

Able to autophosphorylate in cis in vitro. This activity may not be relevant in vivo and only reflects in vitro conditions. Probably does not act as a protein kinase as it is unable to act in trans (PubMed:27499294).1 Publication
Was originally (PubMed:1648478) isolated as a multicopy suppressor of a yeast strain harboring a mutation in a cytochrome b translational activator (cbs2-223). But more recently it has been shown (PubMed:15063807) that a tRNA(Trp) gene located downstream of COQ8 mediates suppression of the cbs2-223 mutation. The inability of COQ8 to suppress the cbs2-223 allele in multicopy indicates it may not be a chaperone as previously reported.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: ubiquinone biosynthesis

This protein is involved in the pathway ubiquinone biosynthesis, which is part of Cofactor biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway ubiquinone biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei198ATPBy similarity1
Binding sitei216ATPBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei346Proton acceptorBy similarity1
Binding sitei351ATPBy similarity1
Binding sitei365ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi303 – 306ATPBy similarity4

<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 functionKinase, Transferase
Biological processUbiquinone biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-30616-MONOMER

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00232

<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:
Atypical kinase COQ8, mitochondrialBy similarity (EC:2.7.-.-By similarity)
Alternative name(s):
Activity of bc1 complex protein 1
Coenzyme Q protein 8
Ubiquinone biosynthesis protein COQ8
<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:COQ8
Synonyms:ABC1
Ordered Locus Names:YGL119W
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome VII

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YGL119W

Saccharomyces Genome Database

More...
SGDi
S000003087 COQ8

<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

Membrane, Mitochondrion, Mitochondrion inner membrane

<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

Decreases COQ3 O-methyltransferase activity.1 Publication

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>Mutagenesisi89G → D in coq8-2; impairs growth on ethanol and/or glycerol as a carbon source, but retains steady-state levels of COQ8. 1 Publication1
Mutagenesisi130G → D in coq8-5; impairs growth on ethanol and/or glycerol as a carbon source, but retains steady-state levels of COQ8. Impairs coenzyme Q6 biosynthesis. 1 Publication1
Mutagenesisi134K → A, H, R or S: Abolishes coenzyme Q biosynthesis. Able to autophosphorylate in cis. 2 Publications1
Mutagenesisi137Q → E: Abolishes coenzyme Q biosynthesis. 1 Publication1
Mutagenesisi197A → G or S: Abolishes coenzyme Q biosynthesis. Able to autophosphorylate in cis. 2 Publications1
Mutagenesisi197A → V in coq8-3; impairs growth on ethanol and/or glycerol as a carbon source, but retains steady-state levels of COQ8. Impairs coenzyme Q6 biosynthesis. 1 Publication1
Mutagenesisi198S → A: Decreased coenzyme Q biosynthesis. 1 Publication1
Mutagenesisi216K → A: Impairs coenzyme Q biosynthesis. 1 Publication1
Mutagenesisi216K → R: Abolishes coenzyme Q biosynthesis. 1 Publication1
Mutagenesisi229D → N in coq8-6; impairs growth on ethanol and/or glycerol as a carbon source, but retains steady-state levels of COQ8. 1 Publication1
Mutagenesisi269E → Q: Abolishes coenzyme Q biosynthesis. 1 Publication1
Mutagenesisi346D → N: Abolishes coenzyme Q biosynthesis. 1 Publication1
Mutagenesisi346D → N in coq8-2; impairs growth on ethanol and/or glycerol as a carbon source, but retains steady-state levels of COQ8. 1 Publication1
Mutagenesisi348N → Y in coq8-4; impairs growth on ethanol and/or glycerol as a carbon source, but retains steady-state levels of COQ8. 1 Publication1
Mutagenesisi351N → A: Abolishes coenzyme Q biosynthesis. 1 Publication1
Mutagenesisi365D → N: Abolishes coenzyme Q biosynthesis. Enhanced autophosphorylation in cis. 2 Publications1
Mutagenesisi471R → E: Abolishes coenzyme Q biosynthesis. 1 Publication1
Mutagenesisi475G → N in coq8-8; impairs growth on ethanol and/or glycerol as a carbon source, but retains steady-state levels of COQ8. 1 Publication1

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 29MitochondrionSequence analysisAdd BLAST29
<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_000000026030 – 501Atypical kinase COQ8, mitochondrialAdd BLAST472

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P27697

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

More...
PaxDbi
P27697

PRoteomics IDEntifications database

More...
PRIDEi
P27697

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P27697

<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

Forms homopolymers. Predominantly associated with a complex of about 500 kDa.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
33132, 125 interactors

Database of interacting proteins

More...
DIPi
DIP-5113N

Protein interaction database and analysis system

More...
IntActi
P27697, 4 interactors

Molecular INTeraction database

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MINTi
P27697

STRING: functional protein association networks

More...
STRINGi
4932.YGL119W

<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

3D structure databases

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

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SMRi
P27697

Database of comparative protein structure models

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ModBasei
Search...

<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>Domaini188 – 501Protein kinaseAdd BLAST314

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi134 – 137KxGQ motifBy similarity4
Motifi195 – 198AAAS motifBy similarity4

<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

Adopts an atypical protein kinase-like fold: while it adopts a core fold similar to that of well-characterized protein kinase-like domains. The KxGQ motif completely occludes the typical substrate binding pocket. Nucleotide-binding opens the substrate binding pocket and flips the active site from inside the hydrophobic core into a catalytically competent, solvent-exposed posture.By similarity

<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

Transit peptide

Phylogenomic databases

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P27697

KEGG Orthology (KO)

More...
KOi
K08869

Identification of Orthologs from Complete Genome Data

More...
OMAi
PLDKCFD

Family and domain databases

Conserved Domains Database

More...
CDDi
cd13970 ABC1_ADCK3, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR034646 ADCK3_UbiB
IPR011009 Kinase-like_dom_sf
IPR004147 UbiB_dom

The PANTHER Classification System

More...
PANTHERi
PTHR43851 PTHR43851, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03109 ABC1, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56112 SSF56112, 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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

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

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

P27697-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVTNMVKLRN LRRLYCSSRL LRTIQNGRIS SVSSISLSKK YTTKSAKEGE
60 70 80 90 100
ENVERKHEEE KKDTLKSSSV PTSRISRLFH YGSLAAGVGM NAAAKGISEV
110 120 130 140 150
AKGNSPTWKS LILSDSNIDR ITNKFSKMRG VALKIGQLLS FQDEKVLPKE
160 170 180 190 200
LYEILSRVQN SANHMPQRQL EKVMAKELGA NWKTKFSKFD KIPMAAASIG
210 220 230 240 250
QVHAAELPSG QRVVVKIQYP GVKESIDSDL NSLLMLLTAS SLLPKGLFLD
260 270 280 290 300
KTIANARTEL KWECDYNREA RALQKFEALL KDDPAFEVPH VFPEYTTDNI
310 320 330 340 350
ITMTRMEGTE IMKLPKASQE TKNFISENIM RLCLEEIATF KYMQTDPNWA
360 370 380 390 400
NFLYNGRTKK IELLDFGASR PFAEDFILKY RKLLTYATLR DRKGAYEMSV
410 420 430 440 450
QLGYLTGLES QSMKDAHVDS VLTLGEPFRG DVDKSFDFKD QTVSDRIRGN
460 470 480 490 500
IGLMLNERLC PPPEETYSLH RKFSGIFLLC ARMGASVHCA KLFKEIFAYK

V
Length:501
Mass (Da):56,742
Last modified:August 1, 1992 - 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:iC91D1EEE5A7ACC9C
GO

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
X59027 Genomic DNA Translation: CAA41759.1
Z72641 Genomic DNA Translation: CAA96827.1
BK006941 Genomic DNA Translation: DAA07990.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S16711

NCBI Reference Sequences

More...
RefSeqi
NP_011396.1, NM_001180984.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YGL119W_mRNA; YGL119W; YGL119W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
852758

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YGL119W

<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
X59027 Genomic DNA Translation: CAA41759.1
Z72641 Genomic DNA Translation: CAA96827.1
BK006941 Genomic DNA Translation: DAA07990.1
PIRiS16711
RefSeqiNP_011396.1, NM_001180984.1

3D structure databases

SMRiP27697
ModBaseiSearch...

Protein-protein interaction databases

BioGridi33132, 125 interactors
DIPiDIP-5113N
IntActiP27697, 4 interactors
MINTiP27697
STRINGi4932.YGL119W

PTM databases

iPTMnetiP27697

Proteomic databases

MaxQBiP27697
PaxDbiP27697
PRIDEiP27697

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL119W_mRNA; YGL119W; YGL119W
GeneIDi852758
KEGGisce:YGL119W

Organism-specific databases

EuPathDBiFungiDB:YGL119W
SGDiS000003087 COQ8

Phylogenomic databases

InParanoidiP27697
KOiK08869
OMAiPLDKCFD

Enzyme and pathway databases

UniPathwayiUPA00232
BioCyciYEAST:G3O-30616-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P27697

Family and domain databases

CDDicd13970 ABC1_ADCK3, 1 hit
InterProiView protein in InterPro
IPR034646 ADCK3_UbiB
IPR011009 Kinase-like_dom_sf
IPR004147 UbiB_dom
PANTHERiPTHR43851 PTHR43851, 1 hit
PfamiView protein in Pfam
PF03109 ABC1, 1 hit
SUPFAMiSSF56112 SSF56112, 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 nameiCOQ8_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: P27697
Secondary accession number(s): D6VU29
<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: August 1, 1992
Last sequence update: August 1, 1992
Last modified: September 18, 2019
This is version 159 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

Complete proteome, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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