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Protein

Cold sensitive U2 snRNA suppressor 2

Gene

CUS2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

U2 snRNP protein which helps to refold U2 into a structure favorable for its binding to SF3b and SF3a prior to spliceosome assembly. Mediates functional interactions between U2 RNA and PRP5. Enforces ATP dependence during formation of the prespliceosome by brokering an interaction between PRP5 and the U2 snRNP that depends on correct U2 RNA structure.3 Publications

GO - Molecular functioni

  • nucleotide binding Source: InterPro
  • U2 snRNA binding Source: GO_Central

GO - Biological processi

  • mRNA splicing, via spliceosome Source: SGD
  • U2-type prespliceosome assembly Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33276-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Cold sensitive U2 snRNA suppressor 2
Gene namesi
Name:CUS2
Ordered Locus Names:YNL286W
ORF Names:N0549
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL286W.
SGDiS000005230. CUS2.

Subcellular locationi

GO - Cellular componenti

  • spliceosomal complex Source: UniProtKB-KW
  • U2 snRNP Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 285285Cold sensitive U2 snRNA suppressor 2PRO_0000082037Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei163 – 1631PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53830.

PTM databases

iPTMnetiP53830.

Interactioni

Subunit structurei

Interacts with PRP11. Associates with the U2 snRNA.2 Publications

Protein-protein interaction databases

BioGridi35551. 26 interactions.
DIPiDIP-2316N.
IntActiP53830. 6 interactions.
MINTiMINT-2787174.

Structurei

3D structure databases

ProteinModelPortaliP53830.
SMRiP53830. Positions 42-129.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 13086RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini183 – 26583RRM 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the HTATSF1 family.Curated
Contains 2 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00390000009902.
InParanoidiP53830.
KOiK13093.
OMAiISSIHIF.
OrthoDBiEOG786HDZ.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 2 hits.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53830-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDADELELKG HLKKLKKEEL LRRKQLKESN LQKRELEYNN ASKNTSIYIS
60 70 80 90 100
GLPTDKTTKE GLTEQFCKYG MIRTNRDGEP LCKLYVNDKG AFKGDALITY
110 120 130 140 150
SKEESVTLAI EMMNESIFLG KQIRVERAQF QNKEGDNMHG KENDLKEFNG
160 170 180 190 200
PEPPIKRLKK AKSEGEGEVI DYNDDESLAK ADRTVIFANV FNIYKSYTND
210 220 230 240 250
DINDIQEDLL EGCEEIGQVD SISVSPNKGE ATVVFKNNKV ALQCCKIMTG
260 270 280
RYFDGQKLLA FISGDENTSS TSDKNEDSEV EDDLI
Length:285
Mass (Da):32,284
Last modified:October 1, 1996 - v1
Checksum:i69A926BF0DB2C6FE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti235 – 2351F → L in AAS56342 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71562 Genomic DNA. Translation: CAA96203.1.
AY558016 Genomic DNA. Translation: AAS56342.1.
BK006947 Genomic DNA. Translation: DAA10273.1.
PIRiS63260.
RefSeqiNP_014113.1. NM_001183124.1.

Genome annotation databases

EnsemblFungiiYNL286W; YNL286W; YNL286W.
GeneIDi855430.
KEGGisce:YNL286W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z71562 Genomic DNA. Translation: CAA96203.1.
AY558016 Genomic DNA. Translation: AAS56342.1.
BK006947 Genomic DNA. Translation: DAA10273.1.
PIRiS63260.
RefSeqiNP_014113.1. NM_001183124.1.

3D structure databases

ProteinModelPortaliP53830.
SMRiP53830. Positions 42-129.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35551. 26 interactions.
DIPiDIP-2316N.
IntActiP53830. 6 interactions.
MINTiMINT-2787174.

PTM databases

iPTMnetiP53830.

Proteomic databases

MaxQBiP53830.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL286W; YNL286W; YNL286W.
GeneIDi855430.
KEGGisce:YNL286W.

Organism-specific databases

EuPathDBiFungiDB:YNL286W.
SGDiS000005230. CUS2.

Phylogenomic databases

GeneTreeiENSGT00390000009902.
InParanoidiP53830.
KOiK13093.
OMAiISSIHIF.
OrthoDBiEOG786HDZ.

Enzyme and pathway databases

BioCyciYEAST:G3O-33276-MONOMER.

Miscellaneous databases

NextBioi979307.
PROiP53830.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 2 hits.
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "CUS2, a yeast homolog of human Tat-SF1, rescues function of misfolded U2 through an unusual RNA recognition motif."
    Yan D., Perriman R., Igel H., Howe K.J., Neville M., Ares M. Jr.
    Mol. Cell. Biol. 18:5000-5009(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PRP11, ASSOCIATION WITH U2.
  5. "ATP can be dispensable for prespliceosome formation in yeast."
    Perriman R., Ares M. Jr.
    Genes Dev. 14:97-107(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Composition and functional characterization of the yeast spliceosomal penta-snRNP."
    Stevens S.W., Ryan D.E., Ge H.Y., Moore R.E., Young M.K., Lee T.D., Abelson J.
    Mol. Cell 9:31-44(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE U2 SNRNP, IDENTIFICATION BY MASS SPECTROMETRY.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  9. "Competition between the ATPase Prp5 and branch region-U2 snRNA pairing modulates the fidelity of spliceosome assembly."
    Xu Y.Z., Query C.C.
    Mol. Cell 28:838-849(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiCUS2_YEAST
AccessioniPrimary (citable) accession number: P53830
Secondary accession number(s): D6W0Q7, E9P8U4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 121 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 1360 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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

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.