U2 snRNP component IST3 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P40565 (IST3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 119. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
U2 snRNP component IST3

Alternative name(s):
Increased sodium tolerance protein 3
U2 snRNP protein SNU17

Gene names

Name:	IST3
Synonyms:	SNU17
Ordered Locus Names:	YIR005W
ORF Names:	YIB5W

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	148 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for pre-mRNA splicing and spliceosome assembly. As part of the pre-mRNA retention and splicing (RES) complex, required for nuclear pre-mRNA retention and efficient splicing. Required for MER1-activated splicing. Ref.5 Ref.11 Ref.12
Subunit structure	Component of the 45S U1.U2.U4/U6.U5 penta-snRNP particle, a subcomplex of the spliceosome. Belongs to the CWC complex (or CEF1-associated complex), a spliceosome sub-complex reminiscent of a late-stage spliceosome composed of the U2, U5 and U6 snRNAs and at least BUD13, BUD31, BRR2, CDC40, CEF1, CLF1, CUS1, CWC2, CWC15, CWC21, CWC22, CWC23, CWC24, CWC25, CWC27, ECM2, HSH155, IST3, ISY1, LEA1, MSL1, NTC20, PRP8, PRP9, PRP11, PRP19, PRP21, PRP22, PRP45, PRP46, SLU7, SMB1, SMD1, SMD2, SMD3, SMX2, SMX3, SNT309, SNU114, SPP2, SYF1, SYF2, RSE1 and YJU2. Belongs to the pre-mRNA retention and splicing (RES) complex composed of at least BUD13, IST3 and PML1. Subunit of the U2 snRNP. Interacts with RDS3. Ref.5 Ref.6 Ref.7 Ref.8 Ref.11
Subcellular location	Cytoplasm. Nucleus Ref.5 Ref.9.
Disruption phenotype	Cells have a slow growth phenotype that is exacerbated at 37 degrees Celsius. Deletion mutants have a significant pre-mRNA leakage at 25 degrees Celsius. Ref.11
Miscellaneous	Present with 922 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the IST3 family. Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus Spliceosome
Ligand	RNA-binding
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	generation of catalytic spliceosome for first transesterification step Inferred from mutant phenotype Ref.5. Source: SGD mRNA export from nucleus Inferred from mutant phenotype Ref.11. Source: SGD spliceosomal complex assembly Inferred from mutant phenotype Ref.5. Source: SGD
Cellular_component	RES complex Inferred from direct assay Ref.11. Source: SGD U2 snRNP Inferred from direct assay PubMed 16314500. Source: SGD cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell spliceosomal complex Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BUD13	P46947	7	EBI-25387,EBI-24073

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 148

148

U2 snRNP component IST3

PRO_0000081621

Regions

Domain

31 – 109

RRM

Sequences

Sequence

Length

Mass (Da)

Tools

P40565 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 9D51C3043AB823D2
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FASTA

148

17,098

        10         20         30         40         50         60 
MNKIQQINDK ELQSGILSPH QSWHNEYKDN AYIYIGNLNR ELTEGDILTV FSEYGVPVDV 

        70         80         90        100        110        120 
ILSRDENTGE SQGFAYLKYE DQRSTILAVD NLNGFKIGGR ALKIDHTFYR PKRSLQKYYE 

       130        140 
AVKEELDRDI VSKNNAEKLI LAKKDQPN

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence and analysis of the centromeric region of yeast chromosome IX." Voss H., Tamames J., Teodoru C., Valencia A., Sensen C., Wiemann S., Schwager C., Zimmermann J., Sander C., Ansorge W. Yeast 11:61-78(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX." Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D., Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C. Barrell B.G. Nature 387:84-87(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[3]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[4]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"A novel yeast U2 snRNP protein, Snu17p, is required for the first catalytic step of splicing and for progression of spliceosome assembly." Gottschalk A., Bartels C., Neubauer G., Luehrmann R., Fabrizio P. Mol. Cell. Biol. 21:3037-3046(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
[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 U1.U2.U4/U6.U5 PENTA-SNRNP COMPLEX BY MASS SPECTROMETRY.
[7]	"Proteomics analysis reveals stable multiprotein complexes in both fission and budding yeasts containing Myb-related Cdc5p/Cef1p, novel pre-mRNA splicing factors, and snRNAs." Ohi M.D., Link A.J., Ren L., Jennings J.L., McDonald W.H., Gould K.L. Mol. Cell. Biol. 22:2011-2024(2002) [PubMed] [Europe PMC] [Abstract] Cited for: MASS SPECTROMETRY, IDENTIFICATION IN THE CWC COMPLEX.
[8]	"Rds3p is required for stable U2 snRNP recruitment to the splicing apparatus." Wang Q., Rymond B.C. Mol. Cell. Biol. 23:7339-7349(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RDS3.
[9]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[10]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[11]	"Proteomic analysis identifies a new complex required for nuclear pre-mRNA retention and splicing." Dziembowski A., Ventura A.-P., Rutz B., Caspary F., Faux C., Halgand F., Laprevote O., Seraphin B. EMBO J. 23:4847-4856(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE RES COMPLEX BY MASS SPECTROMETRY, DISRUPTION PHENOTYPE.
[12]	"Mer1p is a modular splicing factor whose function depends on the conserved U2 snRNP protein Snu17p." Spingola M., Armisen J., Ares M. Jr. Nucleic Acids Res. 32:1242-1250(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X79743 Genomic DNA. No translation available. Z38062 Genomic DNA. Translation: CAA86207.1. AY558081 Genomic DNA. Translation: AAS56407.1. BK006942 Genomic DNA. Translation: DAA08551.1.
PIR	S48439.
RefSeq	NP_012270.1. NM_001179527.1.
3D structure databases
ProteinModelPortal	P40565.
SMR	P40565. Positions 33-106.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2076N.
IntAct	P40565. 21 interactions.
MINT	MINT-389778.
STRING	4932.YIR005W.
Proteomic databases
PaxDb	P40565.
PeptideAtlas	P40565.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YIR005W; YIR005W; YIR005W.
GeneID	854821.
KEGG	sce:YIR005W.
Organism-specific databases
CYGD	YIR005w.
SGD	S000001444. IST3.
Phylogenomic databases
eggNOG	COG0724.
GeneTree	ENSGT00600000084414.
HOGENOM	HOG000174091.
KO	K13107.
OMA	YGVPVDV.
OrthoDB	EOG441TN4.
Gene expression databases
Genevestigator	P40565.
GermOnline	YIR005W. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.30.70.330. 1 hit.
InterPro	IPR012677. Nucleotide-bd_a/b_plait. IPR000504. RRM_dom. [Graphical view]
Pfam	PF00076. RRM_1. 1 hit. [Graphical view]
SMART	SM00360. RRM. 1 hit. [Graphical view]
PROSITE	PS50102. RRM. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	977669.

Entry information

Entry name

IST3_YEAST

Accession

Primary (citable) accession number: P40565
Secondary accession number(s): D6VVT5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 119 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome IX

Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents