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Protein

26S proteasome complex subunit SEM1

Gene

SEM1

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

Versatile protein that might stabilize multiple protein complexes involved in diverse pathways. Subunit of the 26S proteasome which plays a role in ubiquitin-dependent proteolysis. Associates also with the TREX-2 complex that is required for transcription-coupled mRNA export, and the COP9 signalosome, which is involved in deneddylation.2 Publications

GO - Biological processi

  • exocytosis Source: SGD
  • filamentous growth Source: SGD
  • histone deubiquitination Source: SGD
  • maintenance of DNA trinucleotide repeats Source: SGD
  • mRNA export from nucleus Source: SGD
  • proteasome assembly Source: SGD
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: SGD
  • regulation of cell cycle Source: SGD
  • SAGA complex localization to transcription regulatory region Source: SGD
  • transcription, DNA-templated Source: UniProtKB-KW
  • ubiquitin-dependent protein catabolic process Source: SGD
Complete GO annotation...

Keywords - Biological processi

Transcription

Enzyme and pathway databases

BioCyciYEAST:G3O-30088-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
26S proteasome complex subunit SEM1
Gene namesi
Name:SEM1
Synonyms:DSH1
Ordered Locus Names:YDR363W-A
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR363W-A.
SGDiS000007235. SEM1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
  • nucleus Source: SGD
  • proteasome regulatory particle, lid subcomplex Source: SGD
  • proteasome storage granule Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Proteasome

Pathology & Biotechi

Disruption phenotypei

Impairs mRNA export and transcription elongation, and induces strong transcription-associated hyperrecombination phenotypes.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 898826S proteasome complex subunit SEM1PRO_0000122970Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei12 – 121PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO94742.
PeptideAtlasiO94742.

PTM databases

iPTMnetiO94742.

Interactioni

Subunit structurei

Part of the 26S proteasome. Associates with the nuclear pore complex (NPC)-associated TREX-2 complex and the COP9 signalosome. Interacts with CSN12 and THP3.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HSM3P383482EBI-31337,EBI-21152

Protein-protein interaction databases

BioGridi32420. 349 interactions.
DIPiDIP-8754N.
IntActiO94742. 15 interactions.
MINTiMINT-2779426.

Structurei

Secondary structure

1
89
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni62 – 665Combined sources
Helixi72 – 8716Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JCKelectron microscopy3.50I1-89[»]
3T5VX-ray2.90C/F1-89[»]
4CR2electron microscopy7.70Y1-89[»]
4CR3electron microscopy9.30Y1-89[»]
4CR4electron microscopy8.80Y1-89[»]
4TRQX-ray3.10C/F30-89[»]
5A5Belectron microscopy9.50Y1-89[»]
ProteinModelPortaliO94742.
SMRiO94742. Positions 23-89.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the DSS1/SEM1 family.Curated

Phylogenomic databases

InParanoidiO94742.
KOiK10881.
OMAiWANGETI.

Family and domain databases

InterProiIPR007834. DSS1_SEM1.
[Graphical view]
PfamiPF05160. DSS1_SEM1. 1 hit.
[Graphical view]
SMARTiSM01385. DSS1_SEM1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O94742-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTDVAAAQA QSKIDLTKKK NEEINKKSLE EDDEFEDFPI DTWANGETIK
60 70 80
SNAVTQTNIW EENWDDVEVD DDFTNELKAE LDRYKRENQ
Length:89
Mass (Da):10,386
Last modified:May 1, 1999 - v1
Checksum:iB66B578ABB01E672
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF059310 mRNA. Translation: AAD08804.1.
AF065136 Genomic DNA. Translation: AAC96096.1.
U28372 Genomic DNA. No translation available.
AY557719 Genomic DNA. Translation: AAS56045.1.
BK006938 Genomic DNA. Translation: DAA12202.1.
PIRiS78744.
RefSeqiNP_010651.3. NM_001184328.3.

Genome annotation databases

EnsemblFungiiYDR363W-A; YDR363W-A; YDR363W-A.
GeneIDi851967.
KEGGisce:YDR363W-A.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF059310 mRNA. Translation: AAD08804.1.
AF065136 Genomic DNA. Translation: AAC96096.1.
U28372 Genomic DNA. No translation available.
AY557719 Genomic DNA. Translation: AAS56045.1.
BK006938 Genomic DNA. Translation: DAA12202.1.
PIRiS78744.
RefSeqiNP_010651.3. NM_001184328.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JCKelectron microscopy3.50I1-89[»]
3T5VX-ray2.90C/F1-89[»]
4CR2electron microscopy7.70Y1-89[»]
4CR3electron microscopy9.30Y1-89[»]
4CR4electron microscopy8.80Y1-89[»]
4TRQX-ray3.10C/F30-89[»]
5A5Belectron microscopy9.50Y1-89[»]
ProteinModelPortaliO94742.
SMRiO94742. Positions 23-89.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32420. 349 interactions.
DIPiDIP-8754N.
IntActiO94742. 15 interactions.
MINTiMINT-2779426.

PTM databases

iPTMnetiO94742.

Proteomic databases

MaxQBiO94742.
PeptideAtlasiO94742.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR363W-A; YDR363W-A; YDR363W-A.
GeneIDi851967.
KEGGisce:YDR363W-A.

Organism-specific databases

EuPathDBiFungiDB:YDR363W-A.
SGDiS000007235. SEM1.

Phylogenomic databases

InParanoidiO94742.
KOiK10881.
OMAiWANGETI.

Enzyme and pathway databases

BioCyciYEAST:G3O-30088-MONOMER.

Miscellaneous databases

NextBioi970085.
PROiO94742.

Family and domain databases

InterProiIPR007834. DSS1_SEM1.
[Graphical view]
PfamiPF05160. DSS1_SEM1. 1 hit.
[Graphical view]
SMARTiSM01385. DSS1_SEM1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "SEM1, a homologue of the split hand/split foot malformation candidate gene Dss1, regulates exocytosis and pseudohyphal differentiation in yeast."
    Jantti J., Lahdenranta J., Olkkonen V.M., Soderlund H., Keranen S.
    Proc. Natl. Acad. Sci. U.S.A. 96:909-914(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. DeHoratius C., Green M.R.
    Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 90840 / EAY235 / FY23.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  6. "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
    Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
    Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: YAL6B.
  7. "A genetic interaction map of RNA-processing factors reveals links between Sem1/Dss1-containing complexes and mRNA export and splicing."
    Wilmes G.M., Bergkessel M., Bandyopadhyay S., Shales M., Braberg H., Cagney G., Collins S.R., Whitworth G.B., Kress T.L., Weissman J.S., Ideker T., Guthrie C., Krogan N.J.
    Mol. Cell 32:735-746(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CSN12 AND THP3.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Sem1 is a functional component of the nuclear pore complex-associated messenger RNA export machinery."
    Faza M.B., Kemmler S., Jimeno S., Gonzalez-Aguilera C., Aguilera A., Hurt E., Panse V.G.
    J. Cell Biol. 184:833-846(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION, SUBUNIT, INTERACTION WITH CSN12 AND THP3.
  10. "Sem1p is a novel subunit of the 26S proteasome from Saccharomyces cerevisiae."
    Sone T., Saeki Y., Toh-e A., Yokosawa H.
    J. Biol. Chem. 279:28807-28816(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiSEM1_YEAST
AccessioniPrimary (citable) accession number: O94742
Secondary accession number(s): D6VSZ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: May 1, 1999
Last modified: May 11, 2016
This is version 126 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 5590 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.