UniProtKB - P40340 (ATAD2_YEAST)
ATPase histone chaperone YTA7
YTA7
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 PublicationsMiscellaneous
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 454 – 461 | ATPSequence analysis | 8 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- ATP-dependent chromatin remodeler activity Source: UniProtKB
- ATP-dependent histone loader activity Source: UniProtKB
- ATP hydrolysis activity Source: SGD
- chromatin binding Source: SGD
- histone binding Source: SGD
GO - Biological processi
- CENP-A containing chromatin assembly Source: UniProtKB
- chromatin organization Source: UniProtKB
- chromatin remodeling Source: UniProtKB
- negative regulation of transcription by RNA polymerase II Source: SGD
- positive regulation of invasive growth in response to glucose limitation Source: SGD
- positive regulation of transcription by RNA polymerase II Source: UniProtKB
Keywordsi
Molecular function | Hydrolase |
Ligand | ATP-binding, Nucleotide-binding |
Names & Taxonomyi
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 |
Gene namesi | Name:YTA71 Publication Ordered Locus Names:YGR270WImported |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
SGDi | S000003502, YTA7 |
VEuPathDBi | FungiDB:YGR270W |
Subcellular locationi
Nucleus
- Nucleus 1 Publication
Other locations
- centromere 1 Publication
- Chromosome 3 Publications
Note: Binds near the 5'-end within protein-coding genes (PubMed:25406467, PubMed:19683497). Localizes to the negative regulatory element NEG and promoter of the HTA1 gene during G2 and M-phase, and its open reading frame during G1/S (PubMed:22156209, PubMed:19683497).3 Publications
Cytosol
- cytosol Source: SGD
Endoplasmic reticulum
Nucleus
- nucleus Source: SGD
Other locations
- chromatin Source: UniProtKB
- chromosome Source: UniProtKB
- chromosome, centromeric region Source: UniProtKB
Keywords - Cellular componenti
Centromere, Chromosome, NucleusPathology & Biotechi
Disruption phenotypei
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 11 | S → 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 Publication | 1 | |
Mutagenesisi | 67 | T → 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 Publication | 1 | |
Mutagenesisi | 94 | S → 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 Publication | 1 | |
Mutagenesisi | 212 | T → 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 Publication | 1 | |
Mutagenesisi | 230 | S → 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 Publication | 1 | |
Mutagenesisi | 241 | S → 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 Publication | 1 | |
Mutagenesisi | 259 | S → 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 Publication | 1 | |
Mutagenesisi | 285 | S → 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 Publication | 1 | |
Mutagenesisi | 304 | S → 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 Publication | 1 | |
Mutagenesisi | 369 | S → 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 Publication | 1 | |
Mutagenesisi | 370 | S → 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 Publication | 1 | |
Mutagenesisi | 380 | T → 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 Publication | 1 | |
Mutagenesisi | 445 | T → 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 Publication | 1 | |
Mutagenesisi | 460 | K → 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 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedCombined sources | |||
ChainiPRO_0000084771 | 2 – 1379 | ATPase histone chaperone YTA7Add BLAST | 1378 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylalanineCombined sources | 1 | |
Modified residuei | 11 | PhosphoserineCombined sources | 1 | |
Modified residuei | 17 | PhosphoserineCombined sources | 1 | |
Modified residuei | 94 | PhosphoserineCombined sources | 1 | |
Modified residuei | 212 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 229 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 241 | PhosphoserineCombined sources | 1 | |
Modified residuei | 259 | PhosphoserineCombined sources | 1 | |
Modified residuei | 285 | PhosphoserineCombined sources | 1 | |
Modified residuei | 367 | PhosphoserineCombined sources | 1 | |
Modified residuei | 369 | PhosphoserineCombined sources | 1 | |
Modified residuei | 370 | PhosphoserineCombined sources | 1 | |
Modified residuei | 735 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1142 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1256 | PhosphoserineCombined sources | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, PhosphoproteinProteomic databases
MaxQBi | P40340 |
PaxDbi | P40340 |
PRIDEi | P40340 |
PTM databases
iPTMneti | P40340 |
Interactioni
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 PublicationsGO - Molecular functioni
- histone binding Source: SGD
Protein-protein interaction databases
BioGRIDi | 33519, 595 interactors |
DIPi | DIP-6557N |
IntActi | P40340, 88 interactors |
MINTi | P40340 |
STRINGi | 4932.YGR270W |
Miscellaneous databases
RNActi | P40340, protein |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 1044 – 1086 | BromoPROSITE-ProRule annotationAdd BLAST | 43 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 39 | DisorderedSequence analysisAdd BLAST | 39 | |
Regioni | 54 – 243 | DisorderedSequence analysisAdd BLAST | 190 | |
Regioni | 302 – 330 | DisorderedSequence analysisAdd BLAST | 29 | |
Regioni | 375 – 396 | DisorderedSequence analysisAdd BLAST | 22 | |
Regioni | 450 – 578 | AAA-ATPase; required for its chromatin boundary function1 PublicationAdd BLAST | 129 | |
Regioni | 1233 – 1274 | DisorderedSequence analysisAdd BLAST | 42 | |
Regioni | 1291 – 1316 | DisorderedSequence analysisAdd BLAST | 26 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 1 – 15 | Basic and acidic residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 65 – 84 | Basic and acidic residuesSequence analysisAdd BLAST | 20 | |
Compositional biasi | 93 – 122 | Basic and acidic residuesSequence analysisAdd BLAST | 30 | |
Compositional biasi | 123 – 149 | Acidic residuesSequence analysisAdd BLAST | 27 | |
Compositional biasi | 150 – 171 | Basic and acidic residuesSequence analysisAdd BLAST | 22 | |
Compositional biasi | 225 – 243 | Basic and acidic residuesSequence analysisAdd BLAST | 19 | |
Compositional biasi | 1238 – 1258 | Basic and acidic residuesSequence analysisAdd BLAST | 21 | |
Compositional biasi | 1259 – 1274 | Polar residuesSequence analysisAdd BLAST | 16 |
Sequence similaritiesi
Keywords - Domaini
BromodomainPhylogenomic databases
eggNOGi | KOG0732, Eukaryota |
GeneTreei | ENSGT00550000074694 |
HOGENOMi | CLU_000536_6_1_1 |
InParanoidi | P40340 |
OMAi | NAQMGIE |
Family and domain databases
Gene3Di | 1.20.920.10, 1 hit 3.40.50.300, 2 hits |
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 |
PANTHERi | PTHR23069, PTHR23069, 1 hit |
Pfami | View protein in Pfam PF00004, AAA, 2 hits PF17862, AAA_lid_3, 1 hit |
SMARTi | View protein in SMART SM00382, AAA, 1 hit |
SUPFAMi | SSF47370, SSF47370, 1 hit SSF52540, SSF52540, 2 hits |
PROSITEi | View protein in PROSITE PS00674, AAA, 1 hit PS50014, BROMODOMAIN_2, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
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
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 70 | D → E in CAA56963 (PubMed:7754704).Curated | 1 | |
Sequence conflicti | 241 | S → N in CAA56963 (PubMed:7754704).Curated | 1 | |
Sequence conflicti | 1016 | S → N in CAA56963 (PubMed:7754704).Curated | 1 | |
Sequence conflicti | 1142 | S → N in CAA56963 (PubMed:7754704).Curated | 1 | |
Sequence conflicti | 1153 | K → E in CAA56963 (PubMed:7754704).Curated | 1 | |
Sequence conflicti | 1250 | P → L in CAA56963 (PubMed:7754704).Curated | 1 | |
Sequence conflicti | 1276 | I → R in CAA56963 (PubMed:7754704).Curated | 1 | |
Sequence conflicti | 1283 | Q → P in CAA56963 (PubMed:7754704).Curated | 1 |
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 |
PIRi | S64603 |
RefSeqi | NP_011786.1, NM_001181399.1 |
Genome annotation databases
EnsemblFungii | YGR270W_mRNA; YGR270W; YGR270W |
GeneIDi | 853186 |
KEGGi | sce:YGR270W |
Similar proteinsi
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 |
PIRi | S64603 |
RefSeqi | NP_011786.1, NM_001181399.1 |
3D structure databases
AlphaFoldDBi | P40340 |
SMRi | P40340 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 33519, 595 interactors |
DIPi | DIP-6557N |
IntActi | P40340, 88 interactors |
MINTi | P40340 |
STRINGi | 4932.YGR270W |
PTM databases
iPTMneti | P40340 |
Proteomic databases
MaxQBi | P40340 |
PaxDbi | P40340 |
PRIDEi | P40340 |
Genome annotation databases
EnsemblFungii | YGR270W_mRNA; YGR270W; YGR270W |
GeneIDi | 853186 |
KEGGi | sce:YGR270W |
Organism-specific databases
SGDi | S000003502, YTA7 |
VEuPathDBi | FungiDB:YGR270W |
Phylogenomic databases
eggNOGi | KOG0732, Eukaryota |
GeneTreei | ENSGT00550000074694 |
HOGENOMi | CLU_000536_6_1_1 |
InParanoidi | P40340 |
OMAi | NAQMGIE |
Miscellaneous databases
PROi | PR:P40340 |
RNActi | P40340, protein |
Family and domain databases
Gene3Di | 1.20.920.10, 1 hit 3.40.50.300, 2 hits |
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 |
PANTHERi | PTHR23069, PTHR23069, 1 hit |
Pfami | View protein in Pfam PF00004, AAA, 2 hits PF17862, AAA_lid_3, 1 hit |
SMARTi | View protein in SMART SM00382, AAA, 1 hit |
SUPFAMi | SSF47370, SSF47370, 1 hit SSF52540, SSF52540, 2 hits |
PROSITEi | View protein in PROSITE PS00674, AAA, 1 hit PS50014, BROMODOMAIN_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | ATAD2_YEAST | |
Accessioni | P40340Primary (citable) accession number: P40340 Secondary accession number(s): D6VV47 | |
Entry historyi | Integrated 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. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD - Yeast chromosome VII
Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names - SIMILARITY comments
Index of protein domains and families