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Protein

Transcriptional adapter 2

Gene

ada2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and ADA. SAGA is involved in RNA polymerase II-dependent transcriptional regulation. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction and promoter selectivity, interaction with transcription activators, and chromatin modification through histone acetylation (gcn5) and deubiquitination (ubp8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3. ADA preferentially acetylates nucleosomal histones H3 (to form H3K14ac and H3K18ac) and H2B (By similarity). Required for full activation of chromatin alteration and meiotic recombination at meiotic recombination hot spot ade6-M26. Also required for the regulation of transcription and chromatin structure around ade6-M26 in response to osmotic stress. Needed for hyperacetylation of histone H3 around ade6-M26.By similarity1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri2 – 49ZZ-typePROSITE-ProRule annotationAdd BLAST48

GO - Molecular functioni

GO - Biological processi

  • cellular response to osmotic stress Source: UniProtKB
  • chromatin organization Source: UniProtKB
  • chromatin remodeling Source: GO_Central
  • DNA recombination Source: UniProtKB-KW
  • histone acetylation Source: UniProtKB
  • meiotic cell cycle Source: UniProtKB-KW
  • positive regulation of histone acetylation Source: GO_Central
  • regulation of reciprocal meiotic recombination Source: UniProtKB
  • regulation of transcription by RNA polymerase II Source: PomBase
  • transcription by RNA polymerase II Source: PomBase

Keywordsi

Molecular functionChromatin regulator
Biological processDNA recombination, Meiosis, Stress response, Transcription, Transcription regulation
LigandMetal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Transcriptional adapter 2
Gene namesi
Name:ada2By similarity
ORF Names:SPCC24B10.08c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC24B10.08c
PomBaseiSPCC24B10.08c ada2

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; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

Cells are sensitive to replication stress hydroxyurea (HU) and also exhibits weak sensitivity to ultraviolet (UV) and methylmethane sulfonate (MMS).1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003246631 – 437Transcriptional adapter 2Add BLAST437

Proteomic databases

MaxQBiQ9P7J7
PaxDbiQ9P7J7
PRIDEiQ9P7J7

Interactioni

Subunit structurei

Component of the SAGA, SALSA, SLIK and ADA complexes.By similarity

Protein-protein interaction databases

BioGridi275745, 9 interactors
IntActiQ9P7J7, 2 interactors
MINTiQ9P7J7
STRINGi4896.SPCC24B10.08c.1

Structurei

Secondary structure

1437
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi68 – 80Combined sources13
Turni81 – 84Combined sources4
Helixi86 – 93Combined sources8
Helixi99 – 109Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2ELKNMR-A62-112[»]
ProteinModelPortaliQ9P7J7
SMRiQ9P7J7
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9P7J7

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini61 – 114SANTPROSITE-ProRule annotationAdd BLAST54
Domaini347 – 437SWIRMPROSITE-ProRule annotationAdd BLAST91

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri2 – 49ZZ-typePROSITE-ProRule annotationAdd BLAST48

Keywords - Domaini

Zinc-finger

Phylogenomic databases

HOGENOMiHOG000163455
InParanoidiQ9P7J7
KOiK11314
OMAiCHEYDLC
OrthoDBiEOG092C1EX3
PhylomeDBiQ9P7J7

Family and domain databases

CDDicd00167 SANT, 1 hit
InterProiView protein in InterPro
IPR016827 Ada2/TADA2
IPR009057 Homeobox-like_sf
IPR001005 SANT/Myb
IPR017884 SANT_dom
IPR007526 SWIRM
IPR000433 Znf_ZZ
PfamiView protein in Pfam
PF00249 Myb_DNA-binding, 1 hit
PF00569 ZZ, 1 hit
PIRSFiPIRSF025024 Transcriptional_adaptor_2, 1 hit
SMARTiView protein in SMART
SM00717 SANT, 1 hit
SM00291 ZnF_ZZ, 1 hit
SUPFAMiSSF46689 SSF46689, 2 hits
PROSITEiView protein in PROSITE
PS51293 SANT, 1 hit
PS50934 SWIRM, 1 hit
PS01357 ZF_ZZ_1, 1 hit
PS50135 ZF_ZZ_2, 1 hit

Sequencei

Sequence statusi: Complete.

Q9P7J7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPPQKYHCNV CAQDITRSIH IRCVECVDFD LCIPCFTSGA SLGTHHPSHP
60 70 80 90 100
YRIIETNSYP IFDENWGADE ELLLIDACET LGLGNWADIA DYVGNARTKE
110 120 130 140 150
ECRDHYLKTY IESDCYPLAS VELPGPVDRI AFAARKRARI EAFQPPPIIP
160 170 180 190 200
QKPLASTPQC HEIQGYMPGR LEFDQEYMNE AELPIKDMNF DDDLHESAKH
210 220 230 240 250
EMQLKLTMLN IYNSRLTRRA VRKQTIFNHN LLDYRRLQAN EKRMSKEERN
260 270 280 290 300
LLNKTKAFAR LLTGPDYQKF VNSYHEQITL KKQISDLQEW RQMGLTTLEQ
310 320 330 340 350
GHKYERDKTQ KFLLSKASAS YDKQLRHVKS FNQTTSAPFQ VRDIQKIVPR
360 370 380 390 400
KPATPTMFSA SADRQLLSED EQALCSKLQI FPKPFLALKF ALISASLTSK
410 420 430
KPFQKTDAVN LFKHLDANKV EQVYDFFHNA RWIGAPT
Length:437
Mass (Da):50,478
Last modified:October 1, 2000 - v1
Checksum:i1FD6F81E6E6A0B9B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329672 Genomic DNA Translation: CAB76217.1
PIRiT50415
RefSeqiNP_588011.1, NM_001023002.2

Genome annotation databases

EnsemblFungiiSPCC24B10.08c.1; SPCC24B10.08c.1:pep; SPCC24B10.08c
GeneIDi2539174
KEGGispo:SPCC24B10.08c

Similar proteinsi

Entry informationi

Entry nameiADA2_SCHPO
AccessioniPrimary (citable) accession number: Q9P7J7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: October 1, 2000
Last modified: May 23, 2018
This is version 139 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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