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Protein

Pre-mRNA leakage protein 1

Gene

PML1

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

Required for efficient splicing and pre-mRNA nuclear retention.1 Publication

GO - Biological processi

  • maintenance of RNA location Source: SGD
  • mRNA export from nucleus Source: SGD
  • mRNA splicing, via spliceosome Source: SGD
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Enzyme and pathway databases

BioCyciYEAST:G3O-32177-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-mRNA leakage protein 1
Gene namesi
Name:PML1
Ordered Locus Names:YLR016C
ORF Names:L1591
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR016C.
SGDiS000004006. PML1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • RES complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 204204Pre-mRNA leakage protein 1PRO_0000058466Add
BLAST

Proteomic databases

MaxQBiQ07930.

Interactioni

Subunit structurei

Belongs to the pre-mRNA retention and splicing (RES) complex composed of at least BUD13, IST3 and PML1.

Protein-protein interaction databases

BioGridi31290. 50 interactions.
DIPiDIP-2149N.
IntActiQ07930. 2 interactions.
MINTiMINT-556104.

Structurei

Secondary structure

1
204
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi38 – 414Combined sources
Helixi61 – 677Combined sources
Helixi72 – 743Combined sources
Beta strandi78 – 847Combined sources
Helixi85 – 906Combined sources
Beta strandi93 – 975Combined sources
Beta strandi102 – 1087Combined sources
Beta strandi128 – 1314Combined sources
Beta strandi141 – 1488Combined sources
Beta strandi151 – 1588Combined sources
Beta strandi178 – 1803Combined sources
Beta strandi184 – 1907Combined sources
Helixi192 – 1943Combined sources
Beta strandi197 – 2037Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JKDX-ray2.50A/B25-204[»]
2MKCNMR-B22-42[»]
2MY3NMR-B22-42[»]
3ELSX-ray1.80A51-204[»]
3ELVX-ray2.40A/B1-204[»]
ProteinModelPortaliQ07930.
SMRiQ07930. Positions 51-204.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07930.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini104 – 17269FHAPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 FHA domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000001108.
InParanoidiQ07930.
KOiK13108.
OMAiLESKSAY.
OrthoDBiEOG7TQVC5.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
InterProiIPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PfamiPF00498. FHA. 1 hit.
[Graphical view]
SMARTiSM00240. FHA. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q07930-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFHRRKRPYN TRNYGHDDKK FKSQYIDIMP DFSPSGLLEL ESNNKEGIAL
60 70 80 90 100
KHVEPQDAIS PDNYMDMLGL EARDRTMYEL VIYRKNDKDK GPWKRYDLNG
110 120 130 140 150
RSCYLVGREL GHSLDTDLDD RTEIVVADIG IPEETSSKQH CVIQFRNVRG
160 170 180 190 200
ILKCYVMDLD SSNGTCLNNV VIPGARYIEL RSGDVLTLSE FEEDNDYELI

FMNV
Length:204
Mass (Da):23,654
Last modified:November 1, 1996 - v1
Checksum:iDA39B4465EFFD378
GO

Sequence cautioni

The sequence CAA62157.1 differs from that shown. Reason: Frameshift at position 180. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti15 – 151G → A in CAA62157 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X90564 Genomic DNA. Translation: CAA62157.1. Frameshift.
Z73188 Genomic DNA. Translation: CAA97538.1.
AY557934 Genomic DNA. Translation: AAS56260.1.
BK006945 Genomic DNA. Translation: DAA09334.1.
PIRiS64838.
RefSeqiNP_013116.1. NM_001181903.1.

Genome annotation databases

EnsemblFungiiYLR016C; YLR016C; YLR016C.
GeneIDi850703.
KEGGisce:YLR016C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X90564 Genomic DNA. Translation: CAA62157.1. Frameshift.
Z73188 Genomic DNA. Translation: CAA97538.1.
AY557934 Genomic DNA. Translation: AAS56260.1.
BK006945 Genomic DNA. Translation: DAA09334.1.
PIRiS64838.
RefSeqiNP_013116.1. NM_001181903.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JKDX-ray2.50A/B25-204[»]
2MKCNMR-B22-42[»]
2MY3NMR-B22-42[»]
3ELSX-ray1.80A51-204[»]
3ELVX-ray2.40A/B1-204[»]
ProteinModelPortaliQ07930.
SMRiQ07930. Positions 51-204.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31290. 50 interactions.
DIPiDIP-2149N.
IntActiQ07930. 2 interactions.
MINTiMINT-556104.

Proteomic databases

MaxQBiQ07930.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR016C; YLR016C; YLR016C.
GeneIDi850703.
KEGGisce:YLR016C.

Organism-specific databases

EuPathDBiFungiDB:YLR016C.
SGDiS000004006. PML1.

Phylogenomic databases

HOGENOMiHOG000001108.
InParanoidiQ07930.
KOiK13108.
OMAiLESKSAY.
OrthoDBiEOG7TQVC5.

Enzyme and pathway databases

BioCyciYEAST:G3O-32177-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ07930.
PROiQ07930.

Family and domain databases

Gene3Di2.60.200.20. 1 hit.
InterProiIPR000253. FHA_dom.
IPR008984. SMAD_FHA_domain.
[Graphical view]
PfamiPF00498. FHA. 1 hit.
[Graphical view]
SMARTiSM00240. FHA. 1 hit.
[Graphical view]
SUPFAMiSSF49879. SSF49879. 1 hit.
PROSITEiPS50006. FHA_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A 7.8kb fragment from chromosome XII of Saccharomyces cerevisiae does not harbour PKC2."
    Saville S.P., Atkinson S., Jamieson L., Pocklington M.J., Orr E.
    Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "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 BY MASS SPECTROMETRY, INTERACTION WITH IST3 AND BUD13.

Entry informationi

Entry nameiPML1_YEAST
AccessioniPrimary (citable) accession number: Q07930
Secondary accession number(s): D6VY18, Q06901
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1996
Last modified: June 8, 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 1470 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 XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: 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.