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Entry version 151 (16 Oct 2019)
Sequence version 2 (13 Apr 2004)
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Protein

Crossover junction endonuclease MMS4

Gene

MMS4

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

Interacts with MUS81 to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. Typical substrates include 3'-flap structures, D-loops, replication forks with regressed leading strands and nicked Holliday junctions. Cleavage probably occurs approximately half a helical turn upstream of the free 5'-end in these structures. May be required in mitosis for the processing of stalled replication fork intermediates arising spontaneously or subsequent to treatment with DNA damaging agents such as methylmethane sulfonate (MMS), camptothecin (CPT) or UV. May be required in meiosis for the repair of meiosis-specific double strand breaks subsequent to single-end invasion (SEI). This involves consecutive cleavage of D-loops and nicked Holliday junctions leading to sister chromatid crossover. In contrast to MSH4-MSH5 dependent crossover, double Holliday junctions do not seem to be involved. Spore formation and viability are severely impaired in deletion strains.11 Publications

Miscellaneous

Two distinct classes of meiotic crossovers have been demonstrated in budding yeast. Class I crossovers exhibit crossover interference and require MSH4 and MSH5 for their resolution, while class II crossovers exhibit no crossover interference and require MUS81 and MMS4. While class I crossovers represent the majority of crossovers in S.cerevisiae, they are virtually absent in S.pombe which lacks orthologs of MSH4 and MSH5.

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

Mg2+1 Publication, Mn2+1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=31.1 nM for a nicked Holliday junction1 Publication
  2. KM=6.84 nM for a regressed leading strand replication fork1 Publication
  3. KM=4.8 nM for a 3'-flap structure1 Publication
  4. KM=3.45 nM for a nicked duplex1 Publication
  5. KM=14.0 nM for a regressed lagging strand replication fork1 Publication
  6. KM=245 nM for a Y structure1 Publication
  7. KM=173 nM for a double flap structure1 Publication
  1. Vmax=55.6 nmol/min/ng enzyme with a nicked Holliday junction as substrate1 Publication
  2. Vmax=31.3 nmol/min/ng enzyme with a regressed leading strand replication fork as substrate1 Publication
  3. Vmax=24.4 nmol/min/ng enzyme with a 3'-flap structure as substrate1 Publication
  4. Vmax=2.21 nmol/min/ng enzyme with a nicked duplex as substrate1 Publication
  5. Vmax=0.832 nmol/min/ng enzyme with a regressed lagging strand replication fork as subsystrate1 Publication
  6. Vmax=0.0468 nmol/min/ng enzyme with a Y structure as substrate1 Publication
  7. Vmax=0.0879 nmol/min/ng enzyme with a double flap structure as substrate1 Publication

pH dependencei

Optimum pH is 8.0 for cleavage of a 3'-flap structure.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 functionEndonuclease, Hydrolase, Nuclease
Biological processDNA damage, DNA recombination, DNA repair, Meiosis
LigandMagnesium, Manganese, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-29062-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-5693568 Resolution of D-loop Structures through Holliday Junction Intermediates

<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:
Crossover junction endonuclease MMS4 (EC:3.1.22.-)
<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:MMS4
Synonyms:SLX2
Ordered Locus Names:YBR098W
ORF Names:YBR0826, YBR0829, YBR100W
<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 II

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YBR098W

Saccharomyces Genome Database

More...
SGDi
S000000302 MMS4

<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>Mutagenesisi173G → R in allele MMS4-1; loss of activity. 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 <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<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_00000965162 – 691Crossover junction endonuclease MMS4Add BLAST690

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 residuei2N-acetylserineCombined sources1
Modified residuei48PhosphoserineCombined sources1
Modified residuei49PhosphoserineCombined sources1
Modified residuei61PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P38257

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

More...
PaxDbi
P38257

PRoteomics IDEntifications database

More...
PRIDEi
P38257

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P38257

<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

Interacts with MUS81.

4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
32804, 213 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1670 Deoxyribonuclease complex MUS81-MMS4

Database of interacting proteins

More...
DIPi
DIP-2927N

Protein interaction database and analysis system

More...
IntActi
P38257, 9 interactors

Molecular INTeraction database

More...
MINTi
P38257

STRING: functional protein association networks

More...
STRINGi
4932.YBR098W

<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

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>Regioni598 – 691Interaction with MUS81Add BLAST94

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili364 – 391Sequence analysisAdd BLAST28
Coiled coili507 – 529Sequence analysisAdd BLAST23

<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 EME1/MMS4 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000113612

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P38257

Identification of Orthologs from Complete Genome Data

More...
OMAi
SHMEFIN

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006166 ERCC4_domain
IPR033310 Mms4/EME1/EME2

The PANTHER Classification System

More...
PANTHERi
PTHR21077 PTHR21077, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02732 ERCC4, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00891 ERCC4, 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.

P38257-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSQIVDFVED KDSRNDASIQ IIDGPSNVEI IALSESMDQD ECKRAHVSSA
60 70 80 90 100
EMIPSSPQRK SVSNDVENVD LNKSIELSAP FFQDISISKL DDFSTTVNSI
110 120 130 140 150
IDSSLRNENN AKGNAKKLLD DLISDEWSAD LESSGKKHNK SQYNLRDIAE
160 170 180 190 200
KWGVQSLKNP EPIAVDCEYK TQGIGKTNSD ISDSPKSQIG AADILFDFPL
210 220 230 240 250
SPVKHENPTE EKHNSIANEN SSPDNSLKPA GKQNHGEDGT SMAKRVYNKG
260 270 280 290 300
EDEQEHLPKG KKRTIALSRT LINSTKLPDT VELNLSKFLD SSDSITTDVL
310 320 330 340 350
STPAKGSNIV RTGSQPIFSN ANCFQEAKRS KTLTAEDPKC TKNTAREVSQ
360 370 380 390 400
LENYIAYGQY YTREDSKNKI RHLLKENKNA FKRVNQIYRD NIKARSQMII
410 420 430 440 450
EFSPSLLQLF KKGDSDLQQQ LAPAVVQSSY NDSMPLLRFL RKCDSIYDFS
460 470 480 490 500
NDFYYPCDPK IVEENVLILY YDAQEFFEQY TSQKKELYRK IRFFSKNGKH
510 520 530 540 550
VILILSDINK LKRAIFQLEN EKYKARVEQR LSGTEEALRP RSKKSSQVGK
560 570 580 590 600
LGIKKFDLEQ RLRFIDREWH VKIHTVNSHM EFINSLPNLV SLIGKQRMDP
610 620 630 640 650
AIRYMKYAHL NVKSAQDSTE TLKKTFHQIG RMPEMKANNV VSLYPSFQSL
660 670 680 690
LEDIEKGRLQ SDNEGKYLMT EAVEKRLYKL FTCTDPNDTI E
Length:691
Mass (Da):78,764
Last modified:April 13, 2004 - v2
<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:i3B3918DD3B2E7E0C
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAT92950 differs from that shown. Reason: Frameshift.Curated
The sequence CAA55603 differs from that shown. Reason: Frameshift.Curated
The sequence CAA85051 differs from that shown. Reason: Frameshift.Curated
The sequence CAA85054 differs from that shown. Reason: Erroneous initiation.Curated

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
U14000 Genomic DNA Translation: AAF06816.1
X78993 Genomic DNA Translation: CAA55603.1 Frameshift.
Z35967 Genomic DNA Translation: CAA85051.1 Frameshift.
Z35968 Genomic DNA Translation: CAA85054.1 Different initiation.
AY692931 Genomic DNA Translation: AAT92950.1 Frameshift.
BK006936 Genomic DNA Translation: DAA07219.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S45968
S48265

NCBI Reference Sequences

More...
RefSeqi
NP_009656.2, NM_001178446.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YBR098W_mRNA; YBR098W; YBR098W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
852395

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YBR098W

<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
U14000 Genomic DNA Translation: AAF06816.1
X78993 Genomic DNA Translation: CAA55603.1 Frameshift.
Z35967 Genomic DNA Translation: CAA85051.1 Frameshift.
Z35968 Genomic DNA Translation: CAA85054.1 Different initiation.
AY692931 Genomic DNA Translation: AAT92950.1 Frameshift.
BK006936 Genomic DNA Translation: DAA07219.1
PIRiS45968
S48265
RefSeqiNP_009656.2, NM_001178446.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

BioGridi32804, 213 interactors
ComplexPortaliCPX-1670 Deoxyribonuclease complex MUS81-MMS4
DIPiDIP-2927N
IntActiP38257, 9 interactors
MINTiP38257
STRINGi4932.YBR098W

PTM databases

iPTMnetiP38257

Proteomic databases

MaxQBiP38257
PaxDbiP38257
PRIDEiP38257

Genome annotation databases

EnsemblFungiiYBR098W_mRNA; YBR098W; YBR098W
GeneIDi852395
KEGGisce:YBR098W

Organism-specific databases

EuPathDBiFungiDB:YBR098W
SGDiS000000302 MMS4

Phylogenomic databases

HOGENOMiHOG000113612
InParanoidiP38257
OMAiSHMEFIN

Enzyme and pathway databases

BioCyciYEAST:G3O-29062-MONOMER
ReactomeiR-SCE-5693568 Resolution of D-loop Structures through Holliday Junction Intermediates

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P38257

Family and domain databases

InterProiView protein in InterPro
IPR006166 ERCC4_domain
IPR033310 Mms4/EME1/EME2
PANTHERiPTHR21077 PTHR21077, 1 hit
PfamiView protein in Pfam
PF02732 ERCC4, 1 hit
SMARTiView protein in SMART
SM00891 ERCC4, 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 nameiMMS4_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: P38257
Secondary accession number(s): D6VQ99
, P38259, Q6B1Z9, Q9URQ2
<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, 1994
Last sequence update: April 13, 2004
Last modified: October 16, 2019
This is version 151 of the entry and version 2 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. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names
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