Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Transcriptional adapter 2

Gene

ada2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri2 – 4948ZZ-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • cellular response to osmotic stress Source: UniProtKB
  • chromatin modification 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 from RNA polymerase II promoter Source: PomBase
  • transcription from RNA polymerase II promoter Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

DNA recombination, Meiosis, Stress response, Transcription, Transcription regulation

Keywords - Ligandi

Metal-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

GO - Cellular componenti

  • nuclear chromatin Source: PomBase
  • nucleus Source: PomBase
  • SAGA complex Source: PomBase
Complete GO annotation...

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 437437Transcriptional adapter 2PRO_0000324663Add
BLAST

Proteomic databases

MaxQBiQ9P7J7.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi275745. 5 interactions.
IntActiQ9P7J7. 2 interactions.
MINTiMINT-8210506.

Structurei

Secondary structure

1
437
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi68 – 8013Combined sources
Turni81 – 844Combined sources
Helixi86 – 938Combined sources
Helixi99 – 10911Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ELKNMR-A62-112[»]
ProteinModelPortaliQ9P7J7.
SMRiQ9P7J7. Positions 62-112.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9P7J7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 11454SANTPROSITE-ProRule annotationAdd
BLAST
Domaini347 – 43791SWIRMPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 SANT domain.PROSITE-ProRule annotation
Contains 1 SWIRM domain.PROSITE-ProRule annotation
Contains 1 ZZ-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri2 – 4948ZZ-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

HOGENOMiHOG000163455.
InParanoidiQ9P7J7.
KOiK11314.
OMAiLRIQPKP.
OrthoDBiEOG7XM380.
PhylomeDBiQ9P7J7.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
InterProiIPR016827. Ada2/TADA2.
IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR007526. SWIRM.
IPR000433. Znf_ZZ.
[Graphical view]
PANTHERiPTHR12374:SF20. PTHR12374:SF20. 1 hit.
PfamiPF00249. Myb_DNA-binding. 1 hit.
PF00569. ZZ. 1 hit.
[Graphical view]
PIRSFiPIRSF025024. Transcriptional_adaptor_2. 1 hit.
SMARTiSM00717. SANT. 1 hit.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 2 hits.
PROSITEiPS51293. SANT. 1 hit.
PS50934. SWIRM. 1 hit.
PS01357. ZF_ZZ_1. 1 hit.
PS50135. ZF_ZZ_2. 1 hit.
[Graphical view]

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.

Cross-referencesi

Sequence databases

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2ELKNMR-A62-112[»]
ProteinModelPortaliQ9P7J7.
SMRiQ9P7J7. Positions 62-112.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275745. 5 interactions.
IntActiQ9P7J7. 2 interactions.
MINTiMINT-8210506.

Proteomic databases

MaxQBiQ9P7J7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EuPathDBiFungiDB:SPCC24B10.08c.
PomBaseiSPCC24B10.08c. ada2.

Phylogenomic databases

HOGENOMiHOG000163455.
InParanoidiQ9P7J7.
KOiK11314.
OMAiLRIQPKP.
OrthoDBiEOG7XM380.
PhylomeDBiQ9P7J7.

Miscellaneous databases

EvolutionaryTraceiQ9P7J7.
PROiQ9P7J7.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
InterProiIPR016827. Ada2/TADA2.
IPR009057. Homeodomain-like.
IPR001005. SANT/Myb.
IPR017884. SANT_dom.
IPR007526. SWIRM.
IPR000433. Znf_ZZ.
[Graphical view]
PANTHERiPTHR12374:SF20. PTHR12374:SF20. 1 hit.
PfamiPF00249. Myb_DNA-binding. 1 hit.
PF00569. ZZ. 1 hit.
[Graphical view]
PIRSFiPIRSF025024. Transcriptional_adaptor_2. 1 hit.
SMARTiSM00717. SANT. 1 hit.
SM00291. ZnF_ZZ. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 2 hits.
PROSITEiPS51293. SANT. 1 hit.
PS50934. SWIRM. 1 hit.
PS01357. ZF_ZZ_1. 1 hit.
PS50135. ZF_ZZ_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  2. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  3. "Distinct chromatin modulators regulate the formation of accessible and repressive chromatin at the fission yeast recombination hotspot ade6-M26."
    Hirota K., Mizuno K.I., Shibata T., Ohta K.
    Mol. Biol. Cell 19:1162-1173(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  4. "Solution structure of the SANT domain of fission yeast SPCC24B10.08c protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 62-112.

Entry informationi

Entry nameiADA2_SCHPO
AccessioniPrimary (citable) accession number: Q9P7J7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: October 1, 2000
Last modified: July 6, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.