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UniProtKB - P61829 (ATP9_YEAST)

Entry version 149 (02 Jun 2021)
Sequence version 1 (21 Jul 1986)
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Protein

ATP synthase subunit 9, mitochondrial

Gene

OLI1

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

Mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F0 domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei59Reversibly protonated during proton transportBy similarity1

<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

Biological processHydrogen ion transport, Ion transport, Transport
LigandLipid-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-SCE-163210, Formation of ATP by chemiosmotic coupling
R-SCE-8949613, Cristae formation

Protein family/group databases

Transport Classification Database

More...TCDBi		3.A.2.1.3, the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily

<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:
ATP synthase subunit 9, mitochondrial
Alternative name(s):
Lipid-binding protein
Oligomycin resistance protein 1
<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:OLI1
Synonyms:ATP9, OLI3, PHO2
Ordered Locus Names:Q0130
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates if the gene coding for the protein originates from the hydrogenosome, the mitochondrion, the nucleomorph, different plastids or a plasmid. The absence of this section means that the gene is located in one of the main chromosomal element(s).<p><a href='/help/encoded_on' target='_top'>More...</a></p>Encoded oniMitochondrion
<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: Mitochondrion

Organism-specific databases

Saccharomyces Genome Database

More...SGDi		S000007274, OLI1

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei14 – 34HelicalSequence analysisAdd BLAST21
Transmembranei52 – 72HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

CF(0), Membrane, Mitochondrion

<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_00001122401 – 76ATP synthase subunit 9, mitochondrialAdd BLAST76

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-formylmethionine1 Publication1

Keywords - PTMi

Formylation

Proteomic databases

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

More...PaxDbi		P61829

PRoteomics IDEntifications database

More...PRIDEi		P61829

<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

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. In yeast, the dimeric form of ATP synthase consists of 17 polypeptides: alpha, beta, gamma, delta, epsilon, 4 (B), 5 (OSCP), 6 (A), 8, 9 (C), d, E (Tim11), f, g, h, i/j and k.

<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

P61829
With#Exp.IntAct
itself2EBI-9016907,EBI-9016907

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		34780, 13 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-3281, Mitochondrial proton-transporting ATP synthase complex

Database of interacting proteins

More...DIPi		DIP-3041N

Protein interaction database and analysis system

More...IntActi		P61829, 2 interactors

STRING: functional protein association networks

More...STRINGi		4932.Q0130

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P61829, 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

176
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		P61829

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		P61829

<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 ATPase C chain family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3025, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000176138

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_148047_4_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P61829

Identification of Orthologs from Complete Genome Data

More...OMAi		VGNIWAN

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.20.20.10, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_01396, ATP_synth_c_bact, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000454, ATP_synth_F0_csu
IPR020537, ATP_synth_F0_csu_DDCD_BS
IPR038662, ATP_synth_F0_csu_sf
IPR002379, ATPase_proteolipid_c-like_dom
IPR035921, F/V-ATP_Csub_sf

The PANTHER Classification System

More...PANTHERi		PTHR10031, PTHR10031, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00137, ATP-synt_C, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00124, ATPASEC

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF81333, SSF81333, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00605, ATPASE_C, 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.

P61829-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQLVLAAKYI GAGISTIGLL GAGIGIAIVF AALINGVSRN PSIKDTVFPM 
        60         70 
AILGFALSEA TGLFCLMVSF LLLFGV
Length:76
Mass (Da):7,759
Last modified:July 21, 1986 - 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:i82B4477D6F75D758
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 varianti46T → L in strain: DS400/A3 and KL14-4A. 1
Natural varianti53L → F in strain: DS400/A3, DS401 and oligomycin-resistant mutant. 1
Natural varianti57L → V in oligomycin-resistant mutant and cross-resistance to venturicidin. 1
Natural varianti65C → S in oligomycin-resistant mutant. 1

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
L00007 Genomic DNA Translation: AAA32146.1
J01462 Genomic DNA Translation: AAA32169.1
V00707 Genomic DNA Translation: CAA24079.1
L36899 Genomic DNA Translation: AAA67535.1
X03968 Genomic DNA Translation: CAA27605.1
KP263414 Genomic DNA Translation: AIZ98894.1

Protein sequence database of the Protein Information Resource

More...PIRi		A23024, LWBYA

NCBI Reference Sequences

More...RefSeqi		NP_009319.1, NC_001224.1
YP_009144710.1, NC_027264.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		Q0130_mRNA; Q0130; Q0130

Database of genes from NCBI RefSeq genomes

More...GeneIDi		24573116
854584

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:Q0130

<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
L00007 Genomic DNA Translation: AAA32146.1
J01462 Genomic DNA Translation: AAA32169.1
V00707 Genomic DNA Translation: CAA24079.1
L36899 Genomic DNA Translation: AAA67535.1
X03968 Genomic DNA Translation: CAA27605.1
KP263414 Genomic DNA Translation: AIZ98894.1
PIRiA23024, LWBYA
RefSeqiNP_009319.1, NC_001224.1
YP_009144710.1, NC_027264.1

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
2WPDX-ray3.43J/K/L/M/N/O/P/Q/R/S1-76[»]
2XOKX-ray3.01K/L/M/N/O/P/Q/R/S/T1-76[»]
3U2FX-ray2.00K/L/M/N/O1-76[»]
3U2YX-ray2.50K/L/M/N/O1-76[»]
3U32X-ray2.00K/L/M/N/O1-76[»]
3UD0X-ray2.00K/L/M/N/O1-76[»]
3ZRYX-ray6.50J/K/L/M/N/O/P/Q/R/S1-76[»]
4B2Qelectron microscopy37.00J/K/L/M/N/O/P/Q/R/S/j/k/l/m/n/o/p/q/r/s1-76[»]
4F4SX-ray1.90A/B/C/D/E/K/L/M/N/O1-76[»]
5BPSX-ray2.10A/B/C/D/E/K/L/M/N/O1-76[»]
5BQ6X-ray2.30A/B/C/D/E/K/L/M/N/O1-76[»]
5BQAX-ray2.10A/B/C/D/E/K/L/M/N/O1-76[»]
5BQJX-ray2.10A/B/C/D/E/K/L/M/N/O1-76[»]
6B2Zelectron microscopy3.600/1/2/3/4/5/6/7/8/9/B/C/D/E/F/G/H/I/J/K1-76[»]
6B8Helectron microscopy3.600/1/2/3/4/5/6/7/8/9/J/L/M/N/P/Q/R/S/T/U1-76[»]
6CP3electron microscopy3.80K/L/M/N/O/P/Q/R/S/T1-76[»]
6CP5electron microscopy4.20K/L/M/N/O/P/Q/R/S/T1-76[»]
6CP6electron microscopy3.60K/L/M/N/O/P/Q/R/S/T1-76[»]
6CP7electron microscopy4.10K/L/M/N/O/P/Q/R/S/T1-76[»]
6WTDelectron microscopy4.20K/L/M/N/O/P/Q/R/S/T1-76[»]
SMRiP61829
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi34780, 13 interactors
ComplexPortaliCPX-3281, Mitochondrial proton-transporting ATP synthase complex
DIPiDIP-3041N
IntActiP61829, 2 interactors
STRINGi4932.Q0130

Protein family/group databases

TCDBi3.A.2.1.3, the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily

Proteomic databases

PaxDbiP61829
PRIDEiP61829

Genome annotation databases

EnsemblFungiiQ0130_mRNA; Q0130; Q0130
GeneIDi24573116
854584
KEGGisce:Q0130

Organism-specific databases

SGDiS000007274, OLI1

Phylogenomic databases

eggNOGiKOG3025, Eukaryota
GeneTreeiENSGT00940000176138
HOGENOMiCLU_148047_4_1_1
InParanoidiP61829
OMAiVGNIWAN

Enzyme and pathway databases

ReactomeiR-SCE-163210, Formation of ATP by chemiosmotic coupling
R-SCE-8949613, Cristae formation

Miscellaneous databases

EvolutionaryTraceiP61829

Protein Ontology

More...PROi		PR:P61829
RNActiP61829, protein

Family and domain databases

Gene3Di1.20.20.10, 1 hit
HAMAPiMF_01396, ATP_synth_c_bact, 1 hit
InterProiView protein in InterPro
IPR000454, ATP_synth_F0_csu
IPR020537, ATP_synth_F0_csu_DDCD_BS
IPR038662, ATP_synth_F0_csu_sf
IPR002379, ATPase_proteolipid_c-like_dom
IPR035921, F/V-ATP_Csub_sf
PANTHERiPTHR10031, PTHR10031, 1 hit
PfamiView protein in Pfam
PF00137, ATP-synt_C, 1 hit
PRINTSiPR00124, ATPASEC
SUPFAMiSSF81333, SSF81333, 1 hit
PROSITEiView protein in PROSITE
PS00605, ATPASE_C, 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 nameiATP9_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: P61829
Secondary accession number(s): A0A0A7P075, P00841, Q37750
<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: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 2, 2021
This is version 149 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, Direct protein sequencing, 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
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