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Protein

Pre-mRNA-splicing factor PRP21

Gene

PRP21

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

mRNA splicing factors, PRP9, PRP11, and PRP21, are necessary for binding of the U2 snRNP to the pre-mRNA in an early step of spliceosome assembly.

GO - Molecular functioni

  • RNA binding Source: SGD

GO - Biological processi

  • mRNA splicing, via spliceosome Source: SGD
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Enzyme and pathway databases

BioCyciYEAST:G3O-31631-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-mRNA-splicing factor PRP21
Gene namesi
Name:PRP21
Synonyms:SPP91
Ordered Locus Names:YJL203W
ORF Names:J0322
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJL203W.
SGDiS000003739. PRP21.

Subcellular locationi

GO - Cellular componenti

  • U2 snRNP Source: SGD
  • U2-type prespliceosome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi168 – 1681T → A in SPP91-1; corrects the PRP9-1 growth defect through partial restoration of splicing and by a complete reversion of the pre-mRNA escape phenotype.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 280280Pre-mRNA-splicing factor PRP21PRO_0000174322Add
BLAST

Proteomic databases

MaxQBiP32524.
PRIDEiP32524.

PTM databases

iPTMnetiP32524.

Interactioni

Subunit structurei

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 YJU2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PRP11Q073506EBI-603,EBI-688

Protein-protein interaction databases

BioGridi33555. 101 interactions.
DIPiDIP-33054N.
DIP-689N.
IntActiP32524. 25 interactions.
MINTiMINT-383990.

Structurei

Secondary structure

1
280
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi90 – 10314Combined sources
Helixi109 – 1168Combined sources
Helixi123 – 1253Combined sources
Helixi132 – 14514Combined sources
Helixi157 – 19337Combined sources
Turni222 – 2243Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DGWX-ray3.11B87-237[»]
ProteinModelPortaliP32524.
SMRiP32524. Positions 89-228.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati11 – 4939SURP motif 1Add
BLAST
Repeati95 – 13541SURP motif 2Add
BLAST

Sequence similaritiesi

Contains 2 SURP motif repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00730000111077.
InParanoidiP32524.
OrthoDBiEOG7034T9.

Family and domain databases

InterProiIPR022030. SF3A1.
IPR000061. Surp.
[Graphical view]
PfamiPF12230. PRP21_like_P. 1 hit.
PF01805. Surp. 2 hits.
[Graphical view]
SMARTiSM00648. SWAP. 2 hits.
[Graphical view]
SUPFAMiSSF109905. SSF109905. 2 hits.
PROSITEiPS50128. SURP. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P32524-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPEDTQLKE DIKTTVNYIK QHGVEFENKL LEDERFSFIK KDDPLHEYYT
60 70 80 90 100
KLMNEPTDTV SGEDNDRKSE REIARPPDFL FSQYDTGISR RDMEVIKLTA
110 120 130 140 150
RYYAKDKSIV EQMISKDGEA RLNFMNSSHP LHKTFTDFVA QYKRVYSFTG
160 170 180 190 200
QEIKKSKRTI LDNCFERTQY WEFEKDKDRE HDKLVELCKI QFAAIPWDKF
210 220 230 240 250
TQVAKFSIPE DTEIFEGSLD LEQMRLRRVQ TGIKLFDSIK PTNEEEKIVS
260 270 280
DQGKQKGGDS KGKKRKIRAV GETRLKKSKK
Length:280
Mass (Da):33,052
Last modified:October 1, 1993 - v1
Checksum:i2E9DBA6F06759B3F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti205 – 2051K → N in AAS56405 (PubMed:17322287).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67564 Genomic DNA. Translation: CAA47860.1.
L07744 Genomic DNA. Translation: AAB09601.1.
X77688 Genomic DNA. Translation: CAA54754.1.
Z49478 Genomic DNA. Translation: CAA89497.1.
AY558079 Genomic DNA. Translation: AAS56405.1.
BK006943 Genomic DNA. Translation: DAA08607.1.
PIRiS23553.
RefSeqiNP_012332.1. NM_001181636.1.

Genome annotation databases

EnsemblFungiiYJL203W; YJL203W; YJL203W.
GeneIDi853227.
KEGGisce:YJL203W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67564 Genomic DNA. Translation: CAA47860.1.
L07744 Genomic DNA. Translation: AAB09601.1.
X77688 Genomic DNA. Translation: CAA54754.1.
Z49478 Genomic DNA. Translation: CAA89497.1.
AY558079 Genomic DNA. Translation: AAS56405.1.
BK006943 Genomic DNA. Translation: DAA08607.1.
PIRiS23553.
RefSeqiNP_012332.1. NM_001181636.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DGWX-ray3.11B87-237[»]
ProteinModelPortaliP32524.
SMRiP32524. Positions 89-228.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33555. 101 interactions.
DIPiDIP-33054N.
DIP-689N.
IntActiP32524. 25 interactions.
MINTiMINT-383990.

PTM databases

iPTMnetiP32524.

Proteomic databases

MaxQBiP32524.
PRIDEiP32524.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYJL203W; YJL203W; YJL203W.
GeneIDi853227.
KEGGisce:YJL203W.

Organism-specific databases

EuPathDBiFungiDB:YJL203W.
SGDiS000003739. PRP21.

Phylogenomic databases

GeneTreeiENSGT00730000111077.
InParanoidiP32524.
OrthoDBiEOG7034T9.

Enzyme and pathway databases

BioCyciYEAST:G3O-31631-MONOMER.

Miscellaneous databases

NextBioi973437.
PROiP32524.

Family and domain databases

InterProiIPR022030. SF3A1.
IPR000061. Surp.
[Graphical view]
PfamiPF12230. PRP21_like_P. 1 hit.
PF01805. Surp. 2 hits.
[Graphical view]
SMARTiSM00648. SWAP. 2 hits.
[Graphical view]
SUPFAMiSSF109905. SSF109905. 2 hits.
PROSITEiPS50128. SURP. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel gene, spp91-1, suppresses the splicing defect and the pre-mRNA nuclear export in the prp9-1 mutant."
    Chapon C., Legrain P.
    EMBO J. 11:3279-3288(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTANT SPP91-1.
    Strain: CY183.
  2. "The Saccharomyces cerevisiae PRP21 gene product is an integral component of the prespliceosome."
    Arenas J.E., Abelson J.N.
    Proc. Natl. Acad. Sci. U.S.A. 90:6771-6775(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The sequence of a 36 kb segment on the left arm of yeast chromosome X identifies 24 open reading frames including NUC1, PRP21 (SPP91), CDC6, CRY2, the gene for S24, a homologue to the aconitase gene ACO1 and two homologues to chromosome III genes."
    Purnelle B., Coster F., Goffeau A.
    Yeast 10:1235-1249(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
    Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
    , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
    EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  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: IDENTIFICATION IN THE CWC COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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].

Entry informationi

Entry nameiPRP21_YEAST
AccessioniPrimary (citable) accession number: P32524
Secondary accession number(s): D6VVZ1, Q6Q5G7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: May 11, 2016
This is version 128 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 2490 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 X
    Yeast (Saccharomyces cerevisiae) chromosome X: 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.