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UniProtKB - P40340 (ATAD2_YEAST)

Entry version 173 (25 May 2022)
Sequence version 2 (01 Oct 1996)
Previous versions | rss
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Protein

ATPase histone chaperone YTA7

Gene

YTA7

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

Functions as an ATP-dependent nucleosome disassembly factor that helps evict canonical histone H3 from the 5'-end of genes upon their induction (PubMed:25406467).

Also contributes to kinetochore assembly by cooperating with SCM3 to load the histone H3 variant CSE4/CENP-A at centromeres (PubMed:32079723).

Provides a chromatin boundary function at the 5'-end of genes that restricts access by RTT106 and thus prevents ectopic spreading of repressive chromatin into coding regions (PubMed:19683497, PubMed:25406467, PubMed:22156209).

Also prevents heterochromatin spreading downstream of the silent mating-type locus HMR, this function is independent of the tRNA boundary element (PubMed:16079223).

Contributes to appropriate cell cycle regulation of histone gene expression by recruiting RNA polymerase II to histone genes, and subsequent CDK1- and casein kinase II-dependent eviction from chromatin is required to promote transcriptional elongation (PubMed:22156209).

5 Publications

Miscellaneous

Present with 172 molecules/cell in log phase SD medium.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi454 – 461ATPSequence analysis8

<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 functionHydrolase
LigandATP-binding, Nucleotide-binding

<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:
ATPase histone chaperone YTA7By similarity (EC:3.6.1.-1 Publication)
Alternative name(s):
ATPase family AAA domain-containing protein YTA7Curated
Short name:
AAA-ATPaseCurated
Tat-binding homolog 7
<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:YTA71 Publication
Ordered Locus Names:YGR270WImported
<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: Chromosome VII

Organism-specific databases

Saccharomyces Genome Database

More...SGDi		S000003502, YTA7

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:YGR270W

<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

Keywords - Cellular componenti

Centromere, Chromosome, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

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

Decreases the level of CSE4/CENP-A at centromeres (PubMed:32079723). Decreases internucleosome spacing at protein-coding genes (PubMed:25406467). Decreases localization of RNA polymerase II to the histone HTA1-HTB1 gene locus during the G1/S transition (PubMed:22156209). Decreases HTA1 RNA level (PubMed:19683497). Heterochromatin spreading downstream of the silent mating-type locus HMR (PubMed:16079223). Decreases cell population growth; simultaneous disruption of proteins required for maintaining centromere and kinetochore function, including CLH4 and CBF1, enhances the growth defect (PubMed:32079723).5 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi11S → A: Severely decreases phosphorylation, causes a G2/M transition delay, and leads to sensitivity to 6-azauracil (impairs transcriptional elongation); when associated with A-67; A-94; A-212; A-230; A-241; A-259; A-285; A-304; A-369; A-370; A-380 and A-445. 1 Publication1
Mutagenesisi67T → A: Severely decreases phosphorylation, causes a G2/M transition delay, and leads to sensitivity to 6-azauracil (impairs transcriptional elongation); when associated with A-11; A-94; A-212; A-230; A-241; A-259; A-285; A-304; A-369; A-370; A-380 and A-445. 1 Publication1
Mutagenesisi94S → A: Severely decreases phosphorylation, causes a G2/M transition delay, and leads to sensitivity to 6-azauracil (impairs transcriptional elongation); when associated with A-11; A-67; A-212; A-230; A-241; A-259; A-285; A-304; A-369; A-370; A-380 and A-445. 1 Publication1
Mutagenesisi212T → A: Severely decreases phosphorylation, causes a G2/M transition delay, and leads to sensitivity to 6-azauracil (impairs transcriptional elongation); when associated with A-11; A-67; A-94; A-230; A-241; A-259; A-285; A-304; A-369; A-370; A-380 and A-445. 1 Publication1
Mutagenesisi230S → A: Severely decreases phosphorylation, causes a G2/M transition delay, and leads to sensitivity to 6-azauracil (impairs transcriptional elongation); when associated with A-11; A-67; A-94; A-212; A-241; A-259; A-285; A-304; A-369; A-370; A-380 and A-445. 1 Publication1
Mutagenesisi241S → A: Severely decreases phosphorylation, causes a G2/M transition delay, and leads to sensitivity to 6-azauracil (impairs transcriptional elongation); when associated with A-11; A-67; A-94; A-212; A-230; A-259; A-285; A-304; A-369; A-370; A-380 and A-445. 1 Publication1
Mutagenesisi259S → A: Severely decreases phosphorylation, causes a G2/M transition delay, and leads to sensitivity to 6-azauracil (impairs transcriptional elongation); when associated with A-11; A-67; A-94; A-212; A-230; A-241; A-285; A-304; A-369; A-370; A-380 and A-445. 1 Publication1
Mutagenesisi285S → A: Severely decreases phosphorylation, causes a G2/M transition delay, and leads to sensitivity to 6-azauracil (impairs transcriptional elongation); when associated with A-11; A-67; A-94; A-212; A-230; A-241; A-259; A-304; A-369; A-370; A-380 and A-445. 1 Publication1
Mutagenesisi304S → A: Severely decreases phosphorylation, causes a G2/M transition delay, and leads to sensitivity to 6-azauracil (impairs transcriptional elongation); when associated with A-11; A-67; A-94; A-212; A-230; A-241; A-259; A-285; A-369; A-370; A-380 and A-445. 1 Publication1
Mutagenesisi369S → A: Severely decreases phosphorylation, causes a G2/M transition delay, and leads to sensitivity to 6-azauracil (impairs transcriptional elongation); when associated with A-11; A-67; A-94; A-212; A-230; A-241; A-259; A-285; A-304; A-370; A-380 and A-445. 1 Publication1
Mutagenesisi370S → A: Severely decreases phosphorylation, causes a G2/M transition delay, and leads to sensitivity to 6-azauracil (impairs transcriptional elongation); when associated with A-11; A-67; A-94; A-212; A-230; A-241; A-259; A-285; A-304; A-369; A-380 and A-445. 1 Publication1
Mutagenesisi380T → A: Severely decreases phosphorylation, causes a G2/M transition delay, and leads to sensitivity to 6-azauracil (impairs transcriptional elongation); when associated with A-11; A-67; A-94; A-212; A-230; A-241; A-259; A-285; A-304; A-369; A-370 and A-445. 1 Publication1
Mutagenesisi445T → A: Severely decreases phosphorylation, causes a G2/M transition delay, and leads to sensitivity to 6-azauracil (impairs transcriptional elongation); when associated with A-11; A-67; A-94; A-212; A-230; A-241; A-259; A-285; A-304; A-369; A-370 and A-380. 1 Publication1
Mutagenesisi460K → A: Increases YTA7 binding to the HTA1 open reading frame outside of S-phase. Increases localization of RTT106 and RSC8 to the HTA1 gene locus. Increases nucleosome occupancy at core histone loci. Decreases transcription of HTA1. 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%5Fprocessing%5Fsection">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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000847712 – 1379ATPase histone chaperone YTA7Add BLAST1378

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-acetylalanineCombined sources1
Modified residuei11PhosphoserineCombined sources1
Modified residuei17PhosphoserineCombined sources1
Modified residuei94PhosphoserineCombined sources1
Modified residuei212PhosphothreonineCombined sources1
Modified residuei229PhosphothreonineCombined sources1
Modified residuei241PhosphoserineCombined sources1
Modified residuei259PhosphoserineCombined sources1
Modified residuei285PhosphoserineCombined sources1
Modified residuei367PhosphoserineCombined sources1
Modified residuei369PhosphoserineCombined sources1
Modified residuei370PhosphoserineCombined sources1
Modified residuei735PhosphoserineCombined sources1
Modified residuei1142PhosphoserineCombined sources1
Modified residuei1256PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated by CDK1 and casein kinase II during S-phase, which leads to its eviction from histone gene promoters and promotes histone gene transcription.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P40340

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

More...PaxDbi		P40340

PRoteomics IDEntifications database

More...PRIDEi		P40340

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P40340

<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

Interacts with CSE4/CENP-A (PubMed:32079723).

Interacts with SCM3 (PubMed:32079723).

Interacts with SPT16 (PubMed:22156209).

Interacts with POB3 (PubMed:22156209).

Interacts with the casein kinase II complex subunits CKA1, CKA2, CKB1 and CKB2 (PubMed:22156209).

Interacts with RNA polymerase II (PubMed:22156209).

Interacts (via Bromo domain) with histone H3 (PubMed:16079223).

Interacts (via Bromo domain) with histone H4 (PubMed:16079223).

3 Publications

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		33519, 595 interactors

Database of interacting proteins

More...DIPi		DIP-6557N

Protein interaction database and analysis system

More...IntActi		P40340, 88 interactors

Molecular INTeraction database

More...MINTi		P40340

STRING: functional protein association networks

More...STRINGi		4932.YGR270W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P40340, 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

3D structure databases

AlphaFold Protein Structure Database

More...AlphaFoldDBi		P40340

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

More...SMRi		P40340

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%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1044 – 1086BromoPROSITE-ProRule annotationAdd BLAST43

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>Regioni1 – 39DisorderedSequence analysisAdd BLAST39
Regioni54 – 243DisorderedSequence analysisAdd BLAST190
Regioni302 – 330DisorderedSequence analysisAdd BLAST29
Regioni375 – 396DisorderedSequence analysisAdd BLAST22
Regioni450 – 578AAA-ATPase; required for its chromatin boundary function1 PublicationAdd BLAST129
Regioni1233 – 1274DisorderedSequence analysisAdd BLAST42
Regioni1291 – 1316DisorderedSequence analysisAdd BLAST26

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1 – 15Basic and acidic residuesSequence analysisAdd BLAST15
Compositional biasi65 – 84Basic and acidic residuesSequence analysisAdd BLAST20
Compositional biasi93 – 122Basic and acidic residuesSequence analysisAdd BLAST30
Compositional biasi123 – 149Acidic residuesSequence analysisAdd BLAST27
Compositional biasi150 – 171Basic and acidic residuesSequence analysisAdd BLAST22
Compositional biasi225 – 243Basic and acidic residuesSequence analysisAdd BLAST19
Compositional biasi1238 – 1258Basic and acidic residuesSequence analysisAdd BLAST21
Compositional biasi1259 – 1274Polar residuesSequence analysisAdd BLAST16

<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 AAA ATPase family.Curated

Keywords - Domaini

Bromodomain

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0732, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00550000074694

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000536_6_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P40340

Identification of Orthologs from Complete Genome Data

More...OMAi		NAQMGIE

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.20.920.10, 1 hit
3.40.50.300, 2 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR003593, AAA+_ATPase
IPR041569, AAA_lid_3
IPR045199, ATAD2-like
IPR003959, ATPase_AAA_core
IPR003960, ATPase_AAA_CS
IPR001487, Bromodomain
IPR036427, Bromodomain-like_sf
IPR027417, P-loop_NTPase

The PANTHER Classification System

More...PANTHERi		PTHR23069, PTHR23069, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00004, AAA, 2 hits
PF17862, AAA_lid_3, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00382, AAA, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47370, SSF47370, 1 hit
SSF52540, SSF52540, 2 hits

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00674, AAA, 1 hit
PS50014, BROMODOMAIN_2, 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.

<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 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.

P40340-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MARNLRNRRG SDVEDASNAK VGYETQIKDE NGIIHTTTRS LRKINYAEIE 
        60         70         80         90        100
KVFDFLEDDQ VMDKDETPVD VTSDEHHNNN QKGDDEDDDV DLVSPHENAR 
       110        120        130        140        150
TNEELTNERN LRKRKAHDPE EDDESFHEED VDDDEEEEEA DEFEDEYLDE 
       160        170        180        190        200
DSKDNNRRRR AADRKFVVPD PDDDEEYDED DEEGDRISHS ASSKRLKRAN 
       210        220        230        240        250
SRRTRSSRHP ETPPPVRRAL RSRTRHSRTS NEENDDENDN SRNEALTLAD 
       260        270        280        290        300
EIRELQEDSP IREKRFLRER TKPVNYKLPP PLTASNAEEF IDKNNNALSF 
       310        320        330        340        350
HNPSPARRGR GGWNASQNSG PTRRLFPTGG PFGGNDVTTI FGKNTNFYNQ 
       360        370        380        390        400
VPSAFSDNNN NKLILDSDSS DDEILPLGVT PKTKKENTQK KKKKKPEIAD 
       410        420        430        440        450
LDPLGVDMNV NFDDIGGLDN YIDQLKEMVA LPLLYPELYQ NFNITPPRGV 
       460        470        480        490        500
LFHGPPGTGK TLMARALAAS CSSDERKITF FMRKGADILS KWVGEAERQL 
       510        520        530        540        550
RLLFEEAKKH QPSIIFFDEI DGLAPVRSSK QEQIHASIVS TLLALMDGMD 
       560        570        580        590        600
NRGQVIVIGA TNRPDAVDPA LRRPGRFDRE FYFPLPDVKA RFKILQIQTR 
       610        620        630        640        650
KWSSPLSTNF IDKLAFLTKG YGGADLRSLC TEAALISIQR SFPQIYRSND 
       660        670        680        690        700
KLLVDPSKIK VKVSDFMLAL KKIVPSSARS TGSSPQPLPE LIKPLLADQL 
       710        720        730        740        750
NNLKNKLDYM LNIKDTTFQR NTSLLQNFID YEEYSGEEEE HDKYGGNEDT 
       760        770        780        790        800
SSFRSYEFFE SMAESQICKP RLLINGPKGN GQQYVGAAIL NYLEEFNVQN 
       810        820        830        840        850
LDLASLVSES SRTIEAAVVQ SFMEAKKRQP SVVFIPNLDI WINTIPENVI 
       860        870        880        890        900
LVLSGLFRSL QSNEKILLLC LAENLDISEV KNGILSDFAF DKNIFQLHKP 
       910        920        930        940        950
SKENITRYFS NLIELLKTKP SDIPMKKRRV KPLPELQKVT SNAAPTNFDE 
       960        970        980        990       1000
NGEPLSEKVV LRRKLKSFQH QDMRLKNVLK IKLSGLMDLF KNRYKRFRKP 
      1010       1020       1030       1040       1050
PIDDAFLVHL FEPETSNDPN WQPAYIKDEN MILEVSTGRK FFNMDLDIVE 
      1060       1070       1080       1090       1100
ERLWNGYYSE PKQFLKDIEL IYRDANTIGD RERVIKASEM FANAQMGIEE 
      1110       1120       1130       1140       1150
ISTPDFIQEC KATRQRDLER QELFLEDEEK RAAMELEAKE QSQENILQEP 
      1160       1170       1180       1190       1200
DLKDNKANEF GVAAGNQLQA QLQTTINTAS IVNNSEVPQP IDTNLYKKEI 
      1210       1220       1230       1240       1250
PAAIPSAVDK EKAVIPEDSG ANEEYTTELI QATCTSEITT DDDERARKEP 
      1260       1270       1280       1290       1300
KENEDSLQTQ VTEENFSKID ANTNNINHVK EIQSVNKPNS LHETVEKRER 
      1310       1320       1330       1340       1350
SPIPKEVVEP EQGKKSDKEL ILTPEQIKKV SACLIEHCQN FTVSQLEDVH 
      1360       1370 
SSVAKIIWKS KSAWDKTGTV DEIIKFLSE
Length:1,379
Mass (Da):157,407
Last modified:October 1, 1996 - 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:i31D1F6F87E62E04F
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 conflicti70D → E in CAA56963 (PubMed:7754704).Curated1
Sequence conflicti241S → N in CAA56963 (PubMed:7754704).Curated1
Sequence conflicti1016S → N in CAA56963 (PubMed:7754704).Curated1
Sequence conflicti1142S → N in CAA56963 (PubMed:7754704).Curated1
Sequence conflicti1153K → E in CAA56963 (PubMed:7754704).Curated1
Sequence conflicti1250P → L in CAA56963 (PubMed:7754704).Curated1
Sequence conflicti1276I → R in CAA56963 (PubMed:7754704).Curated1
Sequence conflicti1283Q → P in CAA56963 (PubMed:7754704).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
X81072 Genomic DNA Translation: CAA56963.1
Y07893 Genomic DNA Translation: CAA69201.1
Z73055 Genomic DNA Translation: CAA97300.1
BK006941 Genomic DNA Translation: DAA08358.1

Protein sequence database of the Protein Information Resource

More...PIRi		S64603

NCBI Reference Sequences

More...RefSeqi		NP_011786.1, NM_001181399.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YGR270W_mRNA; YGR270W; YGR270W

Database of genes from NCBI RefSeq genomes

More...GeneIDi		853186

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YGR270W

<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
X81072 Genomic DNA Translation: CAA56963.1
Y07893 Genomic DNA Translation: CAA69201.1
Z73055 Genomic DNA Translation: CAA97300.1
BK006941 Genomic DNA Translation: DAA08358.1
PIRiS64603
RefSeqiNP_011786.1, NM_001181399.1

3D structure databases

AlphaFoldDBiP40340
SMRiP40340
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi33519, 595 interactors
DIPiDIP-6557N
IntActiP40340, 88 interactors
MINTiP40340
STRINGi4932.YGR270W

PTM databases

iPTMnetiP40340

Proteomic databases

MaxQBiP40340
PaxDbiP40340
PRIDEiP40340

Genome annotation databases

EnsemblFungiiYGR270W_mRNA; YGR270W; YGR270W
GeneIDi853186
KEGGisce:YGR270W

Organism-specific databases

SGDiS000003502, YTA7
VEuPathDBiFungiDB:YGR270W

Phylogenomic databases

eggNOGiKOG0732, Eukaryota
GeneTreeiENSGT00550000074694
HOGENOMiCLU_000536_6_1_1
InParanoidiP40340
OMAiNAQMGIE

Miscellaneous databases

Protein Ontology

More...PROi		PR:P40340
RNActiP40340, protein

Family and domain databases

Gene3Di1.20.920.10, 1 hit
3.40.50.300, 2 hits
InterProiView protein in InterPro
IPR003593, AAA+_ATPase
IPR041569, AAA_lid_3
IPR045199, ATAD2-like
IPR003959, ATPase_AAA_core
IPR003960, ATPase_AAA_CS
IPR001487, Bromodomain
IPR036427, Bromodomain-like_sf
IPR027417, P-loop_NTPase
PANTHERiPTHR23069, PTHR23069, 1 hit
PfamiView protein in Pfam
PF00004, AAA, 2 hits
PF17862, AAA_lid_3, 1 hit
SMARTiView protein in SMART
SM00382, AAA, 1 hit
SUPFAMiSSF47370, SSF47370, 1 hit
SSF52540, SSF52540, 2 hits
PROSITEiView protein in PROSITE
PS00674, AAA, 1 hit
PS50014, BROMODOMAIN_2, 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 nameiATAD2_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: P40340
Secondary accession number(s): D6VV47
<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: February 1, 1995
Last sequence update: October 1, 1996
Last modified: May 25, 2022
This is version 173 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

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
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