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UniProtKB - P32783 (MCES_YEAST)

Entry version 162 (31 Jul 2019)
Sequence version 1 (01 Oct 1993)
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Protein

mRNA cap guanine-N7 methyltransferase

Gene

ABD1

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

Responsible for methylating the 5'-cap structure of mRNAs.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

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 sitei154S-adenosyl-L-methioninePROSITE-ProRule annotation1
Binding sitei172S-adenosyl-L-methionine; via carbonyl oxygenPROSITE-ProRule annotation1
<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>Sitei175mRNA cap bindingPROSITE-ProRule annotation1
Sitei181mRNA cap bindingPROSITE-ProRule annotation1
Binding sitei194S-adenosyl-L-methioninePROSITE-ProRule annotation1
Sitei206mRNA cap bindingPROSITE-ProRule annotation1
Binding sitei223S-adenosyl-L-methionine; via amide nitrogenBy similarity1
Binding sitei249S-adenosyl-L-methionine; via carbonyl oxygenBy similarity1
Sitei253mRNA cap bindingPROSITE-ProRule annotation1
Binding sitei254S-adenosyl-L-methionineBy similarity1
Sitei347mRNA cap bindingPROSITE-ProRule annotation1
Sitei416mRNA cap bindingPROSITE-ProRule annotation1

<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 functionMethyltransferase, RNA-binding, Transferase
Biological processmRNA capping, mRNA processing
LigandS-adenosyl-L-methionine

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:G3O-29167-MONOMER
YEAST:G3O-29167-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.1.1.56 984

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-SCE-72086 mRNA Capping
R-SCE-77075 RNA Pol II CTD phosphorylation and interaction with CE

<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:
mRNA cap guanine-N7 methyltransferase (EC:2.1.1.56By similarity)
Alternative name(s):
mRNA (guanine-N(7)-)-methyltransferase
mRNA cap methyltransferase
<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:ABD1
Ordered Locus Names:YBR236C
ORF Names:YBR1602
<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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<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 II

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		FungiDB:YBR236C

Saccharomyces Genome Database

More...SGDi		S000000440 ABD1

<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

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_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>Mutagenesisi168V → A: Still viable; normal growth. 1 Publication1
Mutagenesisi170E → A: Non-viable; reduced enzyme activity to 8% of wild-type. 2 Publications1
Mutagenesisi170E → D: Still viable; increase in activity. 2 Publications1
Mutagenesisi170E → Q: Non-viable; reduced enzyme activity to 8% of wild-type. 2 Publications1
Mutagenesisi172G → A: Still viable; normal growth. 1 Publication1
Mutagenesisi174G → A: Non viable; no growth. 1 Publication1
Mutagenesisi176G → A: Still viable; normal growth. 1 Publication1
Mutagenesisi178D → A: Microcolony formation. 1 Publication1
Mutagenesisi181K → A: Still viable; normal growth. 1 Publication1
Mutagenesisi182Y → A: Still viable; normal growth. 1 Publication1
Mutagenesisi194D → A: Lethal; no enzyme activity. 2 Publications1
Mutagenesisi194D → E: Still viable; activity near to wild-type. 2 Publications1
Mutagenesisi194D → N: Lethal; no enzyme activity. 2 Publications1
Mutagenesisi206R → A: Lethal. 2 Publications1
Mutagenesisi206R → K: Still viable; little change in enzyme activity. 2 Publications1
Mutagenesisi253H → A: Still viable; normal growth. 1 Publication1
Mutagenesisi254Y → A: Non viable; no growth. 2 Publications1
Mutagenesisi254Y → F: Still viable; slow growth; near to wild-type enzyme activity. 2 Publications1
Mutagenesisi254Y → S: Lethal; Enzyme activity 10% of wild-type. 2 Publications1
Mutagenesisi276G → A: Still viable; normal growth. 1 Publication1
Mutagenesisi277G → A: Still viable; normal growth. 1 Publication1
Mutagenesisi282T → A: Still viable; normal growth. 1 Publication1
Mutagenesisi287E → A: Still viable; normal growth. 1 Publication1
Mutagenesisi347E → A: Still viable; normal growth. 1 Publication1
Mutagenesisi348Y → A: Still viable; normal growth. 1 Publication1
Mutagenesisi349V → A: Still viable; normal growth. 1 Publication1
Mutagenesisi350V → A: Still viable; normal growth. 1 Publication1
Mutagenesisi361E → A: Still viable; normal growth. 1 Publication1
Mutagenesisi362Y → A: Still viable; normal growth. 1 Publication1
Mutagenesisi363G → A: Still viable; normal growth. 1 Publication1
Mutagenesisi366L → A: Still viable; normal growth. 1 Publication1
Mutagenesisi367V → A: Still viable; normal growth. 1 Publication1
Mutagenesisi372F → A: Still viable; normal growth. 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 polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002101341 – 436mRNA cap guanine-N7 methyltransferaseAdd BLAST436

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P32783

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

More...PaxDbi		P32783

PRoteomics IDEntifications database

More...PRIDEi		P32783

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P32783

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		32931, 344 interactors

Database of interacting proteins

More...DIPi		DIP-2503N

Protein interaction database and analysis system

More...IntActi		P32783, 10 interactors

Molecular INTeraction database

More...MINTi		P32783

STRING: functional protein association networks

More...STRINGi		4932.YBR236C

<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

More...SMRi		P32783

Database of comparative protein structure models

More...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>Domaini101 – 430mRNA cap 0 methyltransferasePROSITE-ProRule annotationAdd BLAST330

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>Regioni150 – 151mRNA cap bindingPROSITE-ProRule annotation2

<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 class I-like SAM-binding methyltransferase superfamily. mRNA cap 0 methyltransferase family.PROSITE-ProRule annotation

Phylogenomic databases

Ensembl GeneTree

More...GeneTreei		ENSGT00390000002368

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000242614

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P32783

KEGG Orthology (KO)

More...KOi		K00565

Identification of Orthologs from Complete Genome Data

More...OMAi		LNLVSCQ

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR004971 mRNA_G-N7_MeTrfase_dom
IPR016899 mRNA_G-N7_MeTrfase_euk
IPR039753 RG7MT1
IPR029063 SAM-dependent_MTases

The PANTHER Classification System

More...PANTHERi		PTHR12189 PTHR12189, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF03291 Pox_MCEL, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF028762 ABD1, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53335 SSF53335, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51562 RNA_CAP0_MT, 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.

P32783-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSTKPEKPIW MSQEDYDRQY GSITGDESST VSKKDSKVTA NAPGDGNGSL 
        60         70         80         90        100
PVLQSSSILT SKVSDLPIEA ESGFKIQKRR HERYDQEERL RKQRAQKLRE 
       110        120        130        140        150
EQLKRHEIEM TANRSINVDQ IVREHYNERT IIANRAKRNL SPIIKLRNFN 
       160        170        180        190        200
NAIKYMLIDK YTKPGDVVLE LGCGKGGDLR KYGAAGISQF IGIDISNASI 
       210        220        230        240        250
QEAHKRYRSM RNLDYQVVLI TGDCFGESLG VAVEPFPDCR FPCDIVSTQF 
       260        270        280        290        300
CLHYAFETEE KARRALLNVA KSLKIGGHFF GTIPDSEFIR YKLNKFPKEV 
       310        320        330        340        350
EKPSWGNSIY KVTFENNSYQ KNDYEFTSPY GQMYTYWLED AIDNVPEYVV 
       360        370        380        390        400
PFETLRSLAD EYGLELVSQM PFNKFFVQEI PKWIERFSPK MREGLQRSDG 
       410        420        430 
RYGVEGDEKE AASYFYTMFA FRKVKQYIEP ESVKPN
Length:436
Mass (Da):50,341
Last modified:October 1, 1993 - 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:iEA5A68F0C4A57C4C
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 conflicti126Y → C in AAT92789 (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
L12000 Genomic DNA Translation: AAA34383.1
Z36105 Genomic DNA Translation: CAA85199.1
AY692770 Genomic DNA Translation: AAT92789.1
BK006936 Genomic DNA Translation: DAA07352.1

Protein sequence database of the Protein Information Resource

More...PIRi		S41782

NCBI Reference Sequences

More...RefSeqi		NP_009795.3, NM_001178584.3

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YBR236C_mRNA; YBR236C_mRNA; YBR236C

Database of genes from NCBI RefSeq genomes

More...GeneIDi		852538

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YBR236C

<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
L12000 Genomic DNA Translation: AAA34383.1
Z36105 Genomic DNA Translation: CAA85199.1
AY692770 Genomic DNA Translation: AAT92789.1
BK006936 Genomic DNA Translation: DAA07352.1
PIRiS41782
RefSeqiNP_009795.3, NM_001178584.3

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
1IC3model-A140-424[»]
SMRiP32783
ModBaseiSearch...

Protein-protein interaction databases

BioGridi32931, 344 interactors
DIPiDIP-2503N
IntActiP32783, 10 interactors
MINTiP32783
STRINGi4932.YBR236C

PTM databases

iPTMnetiP32783

Proteomic databases

MaxQBiP32783
PaxDbiP32783
PRIDEiP32783

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBR236C_mRNA; YBR236C_mRNA; YBR236C
GeneIDi852538
KEGGisce:YBR236C

Organism-specific databases

EuPathDBiFungiDB:YBR236C
SGDiS000000440 ABD1

Phylogenomic databases

GeneTreeiENSGT00390000002368
HOGENOMiHOG000242614
InParanoidiP32783
KOiK00565
OMAiLNLVSCQ

Enzyme and pathway databases

BioCyciMetaCyc:G3O-29167-MONOMER
YEAST:G3O-29167-MONOMER
BRENDAi2.1.1.56 984
ReactomeiR-SCE-72086 mRNA Capping
R-SCE-77075 RNA Pol II CTD phosphorylation and interaction with CE

Miscellaneous databases

Protein Ontology

More...PROi		PR:P32783

Family and domain databases

InterProiView protein in InterPro
IPR004971 mRNA_G-N7_MeTrfase_dom
IPR016899 mRNA_G-N7_MeTrfase_euk
IPR039753 RG7MT1
IPR029063 SAM-dependent_MTases
PANTHERiPTHR12189 PTHR12189, 1 hit
PfamiView protein in Pfam
PF03291 Pox_MCEL, 1 hit
PIRSFiPIRSF028762 ABD1, 1 hit
SUPFAMiSSF53335 SSF53335, 1 hit
PROSITEiView protein in PROSITE
PS51562 RNA_CAP0_MT, 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 nameiMCES_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: P32783
Secondary accession number(s): D6VQN2, Q6B2G0
<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: October 1, 1993
Last sequence update: October 1, 1993
Last modified: July 31, 2019
This is version 162 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, Complete proteome, Reference proteome

Documents

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