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Protein

A1 cistron-splicing factor AAR2

Gene

AAR2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Component of the U5 snRNP complex that is required for spliceosome assembly and for pre-mRNA splicing. Involved in splicing pre-mRNA of the A1 cistron and other genes that are important for cell growth.2 Publications

GO - Biological processi

  • spliceosomal tri-snRNP complex assembly Source: SGD
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Enzyme and pathway databases

BioCyciYEAST:G3O-28966-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
A1 cistron-splicing factor AAR2
Gene namesi
Name:AAR2
Ordered Locus Names:YBL074C
ORF Names:YBL06.06, YBL0611
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome II

Organism-specific databases

CYGDiYBL074c.
EuPathDBiFungiDB:YBL074C.
SGDiS000000170. AAR2.

Subcellular locationi

  • Cytoplasm
  • Nucleus

  • Note: This protein lacks a nuclear localization signal, it may interact in the cytoplasm with a component of spliceosomes via the leucine-zipper and then be transported into the nucleus.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • U5 snRNP Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi253 – 2531S → A: No effect on interaction with PRP8. 1 Publication
Mutagenesisi253 – 2531S → D or E: Disrupts interaction with PRP8. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 355355A1 cistron-splicing factor AAR2PRO_0000209705Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei253 – 2531Phosphoserine1 Publication
Modified residuei274 – 2741Phosphothreonine1 Publication
Modified residuei328 – 3281Phosphotyrosine1 Publication
Modified residuei331 – 3311Phosphoserine1 Publication
Modified residuei345 – 3451Phosphothreonine1 Publication

Post-translational modificationi

Phosphorylated on serine and tyrosine residues.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP32357.
PaxDbiP32357.

Interactioni

Subunit structurei

Heterodimer (Probable). Interacts with PRP8 (via RNase H homology domain and MPN domain), competing with BRR2 for the same binding site. Component of a U5 snRNP complex that contains at least the U5 snRNA, PRP8, SNU114, AAR2, SMB1, SMD1, SMD2, SMD3, SME1, SMX2 and SMX3, but is not a component of the U4/U6-U5 tri-snRNP complex.Curated3 Publications

Protein-protein interaction databases

BioGridi32628. 20 interactions.
DIPiDIP-6642N.
IntActiP32357. 7 interactions.
MINTiMINT-663730.
STRINGi4932.YBL074C.

Structurei

Secondary structure

1
355
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 76Combined sources
Beta strandi13 – 175Combined sources
Beta strandi20 – 245Combined sources
Beta strandi32 – 365Combined sources
Beta strandi38 – 403Combined sources
Beta strandi42 – 487Combined sources
Beta strandi51 – 6010Combined sources
Helixi62 – 643Combined sources
Beta strandi66 – 727Combined sources
Turni73 – 764Combined sources
Beta strandi77 – 837Combined sources
Helixi86 – 9813Combined sources
Beta strandi102 – 1043Combined sources
Helixi113 – 1186Combined sources
Helixi123 – 1297Combined sources
Beta strandi136 – 1416Combined sources
Turni147 – 1493Combined sources
Beta strandi153 – 1553Combined sources
Helixi172 – 1743Combined sources
Beta strandi183 – 1853Combined sources
Turni186 – 1883Combined sources
Helixi194 – 1996Combined sources
Helixi202 – 2065Combined sources
Helixi207 – 2148Combined sources
Helixi217 – 23418Combined sources
Helixi237 – 25115Combined sources
Helixi258 – 27417Combined sources
Helixi277 – 2793Combined sources
Helixi280 – 2834Combined sources
Helixi286 – 2949Combined sources
Turni297 – 3004Combined sources
Helixi303 – 31210Combined sources
Helixi314 – 3163Combined sources
Beta strandi345 – 3539Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SBSX-ray2.10A1-355[»]
3SBTX-ray1.80B1-355[»]
3ZEFX-ray3.10A/D1-355[»]
4I43X-ray2.00A1-355[»]
4ILGX-ray2.10A1-355[»]
4ILHX-ray1.85B1-331[»]
4ILIX-ray3.20A/B1-318[»]
ProteinModelPortaliP32357.
SMRiP32357. Positions 1-355.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni261 – 28222Leucine-zipperAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi332 – 34110Asp/Glu-rich (acidic)

Sequence similaritiesi

Belongs to the AAR2 family.Curated

Phylogenomic databases

eggNOGiNOG331204.
HOGENOMiHOG000033742.
InParanoidiP32357.
KOiK13205.
OMAiYLDKSWY.
OrthoDBiEOG7GTTGG.

Family and domain databases

InterProiIPR007946. AAR2.
[Graphical view]
PANTHERiPTHR12689. PTHR12689. 1 hit.
PfamiPF05282. AAR2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32357-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTVPFTSAP IEVTIGIDQY SFNVKENQPF HGIKDIPIGH VHVIHFQHAD
60 70 80 90 100
NSSMRYGYWF DCRMGNFYIQ YDPKDGLYKM MEERDGAKFE NIVHNFKERQ
110 120 130 140 150
MMVSYPKIDE DDTWYNLTEF VQMDKIRKIV RKDENQFSYV DSSMTTVQEN
160 170 180 190 200
ELLKSSLQKA GSKMEAKNED DPAHSLNYTV INFKSREAIR PGHEMEDFLD
210 220 230 240 250
KSYYLNTVML QGIFKNSSNY FGELQFAFLN AMFFGNYGSS LQWHAMIELI
260 270 280 290 300
CSSATVPKHM LDKLDEILYY QIKTLPEQYS DILLNERVWN ICLYSSFQKN
310 320 330 340 350
SLHNTEKIME NKYPELLGKD NEDDALIYGI SDEERDDEDD EHNPTIVGGL

YYQRP
Length:355
Mass (Da):41,688
Last modified:October 1, 1993 - v1
Checksum:i1F030D821D974131
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90455 Genomic DNA. Translation: BAA14421.1.
Z26879 Genomic DNA. Translation: CAA81524.1.
Z35835 Genomic DNA. Translation: CAA84894.1.
M36115 Genomic DNA. No translation available.
BK006936 Genomic DNA. Translation: DAA07048.1.
PIRiS18510.
RefSeqiNP_009479.1. NM_001178314.1.

Genome annotation databases

EnsemblFungiiYBL074C; YBL074C; YBL074C.
GeneIDi852205.
KEGGisce:YBL074C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D90455 Genomic DNA. Translation: BAA14421.1.
Z26879 Genomic DNA. Translation: CAA81524.1.
Z35835 Genomic DNA. Translation: CAA84894.1.
M36115 Genomic DNA. No translation available.
BK006936 Genomic DNA. Translation: DAA07048.1.
PIRiS18510.
RefSeqiNP_009479.1. NM_001178314.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SBSX-ray2.10A1-355[»]
3SBTX-ray1.80B1-355[»]
3ZEFX-ray3.10A/D1-355[»]
4I43X-ray2.00A1-355[»]
4ILGX-ray2.10A1-355[»]
4ILHX-ray1.85B1-331[»]
4ILIX-ray3.20A/B1-318[»]
ProteinModelPortaliP32357.
SMRiP32357. Positions 1-355.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32628. 20 interactions.
DIPiDIP-6642N.
IntActiP32357. 7 interactions.
MINTiMINT-663730.
STRINGi4932.YBL074C.

Proteomic databases

MaxQBiP32357.
PaxDbiP32357.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYBL074C; YBL074C; YBL074C.
GeneIDi852205.
KEGGisce:YBL074C.

Organism-specific databases

CYGDiYBL074c.
EuPathDBiFungiDB:YBL074C.
SGDiS000000170. AAR2.

Phylogenomic databases

eggNOGiNOG331204.
HOGENOMiHOG000033742.
InParanoidiP32357.
KOiK13205.
OMAiYLDKSWY.
OrthoDBiEOG7GTTGG.

Enzyme and pathway databases

BioCyciYEAST:G3O-28966-MONOMER.

Miscellaneous databases

NextBioi970703.
PROiP32357.

Family and domain databases

InterProiIPR007946. AAR2.
[Graphical view]
PANTHERiPTHR12689. PTHR12689. 1 hit.
PfamiPF05282. AAR2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "AAR2, a gene for splicing pre-mRNA of the MATa1 cistron in cell type control of Saccharomyces cerevisiae."
    Nakazawa N., Harashima S., Oshima Y.
    Mol. Cell. Biol. 11:5693-5700(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
  2. "The two genes encoding yeast ribosomal protein S8 reside on different chromosomes, and are closely linked to the hsp70 stress protein genes SSA3 and SSA4."
    Logghe M., Molemans F., Fiers W., Contreras R.
    Yeast 10:1093-1100(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "Complete DNA sequence of yeast chromosome II."
    Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
    , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
    EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "Transcriptional regulation of SSA3, an HSP70 gene from Saccharomyces cerevisiae."
    Boorstein W.R., Craig E.A.
    Mol. Cell. Biol. 10:3262-3267(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-355.
  6. "The yeast U5 snRNP coisolated with the U1 snRNP has an unexpected protein composition and includes the splicing factor Aar2p."
    Gottschalk A., Kastner B., Luhrmann R., Fabrizio P.
    RNA 7:1554-1565(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), INTERACTION WITH PRP8, PHOSPHORYLATION AT SER-253; THR-274; TYR-328; SER-331 AND THR-345, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF SER-253.
  10. "Crystal structure of Prp8 reveals active site cavity of the spliceosome."
    Galej W.P., Oubridge C., Newman A.J., Nagai K.
    Nature 493:638-643(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH PRP8, INTERACTION WITH PRP8.

Entry informationi

Entry nameiAAR2_YEAST
AccessioniPrimary (citable) accession number: P32357
Secondary accession number(s): D6VPS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 24, 2015
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 7330 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

External Data

Dasty 3

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 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.