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Protein

SWI5-dependent HO expression protein 2

Gene

SHE2

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

RNA-binding protein that binds specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease. Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Recruits the MYO4-SHE3 complex to the ASH1 mRNA. Recruits also LOC1 and PUF6 to ASH1 mRNA, which are required for translational repression of this mRNA.16 Publications

GO - Molecular functioni

  • lipid binding Source: SGD
  • mRNA binding Source: SGD

GO - Biological processi

  • intracellular mRNA localization Source: SGD
  • mating type switching Source: SGD
  • mRNA transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

mRNA transport, Transport

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31911-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
SWI5-dependent HO expression protein 2
Gene namesi
Name:SHE2
Ordered Locus Names:YKL130C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKL130C.
SGDiS000001613. SHE2.

Subcellular locationi

GO - Cellular componenti

  • cellular bud tip Source: SGD
  • cytoplasm Source: SGD
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi36 – 361N → S: Prevents association with ASH1 and IST2 mRNAs and leads to their mislocalization. 1 Publication
Mutagenesisi43 – 431R → A: Prevents association with ASH1 and mRNA and leads to its mislocalization. 1 Publication
Mutagenesisi44 – 441R → A: Prevents association with ASH1 and mRNA and leads to its mislocalization. 1 Publication
Mutagenesisi49 – 491R → K: Prevents association with ASH1 and mRNA and leads to its mislocalization. 1 Publication
Mutagenesisi52 – 521R → A or K: Prevents association with ASH1 and mRNA and leads to its mislocalization. 1 Publication
Mutagenesisi63 – 631R → A or K: Prevents association with ASH1 and IST2 mRNAs and leads to their mislocalization. 1 Publication
Mutagenesisi68 – 681C → Y: Prevents dimerization and RNA-binding. 1 Publication
Mutagenesisi120 – 1201S → Y: Prevents dimerization and RNA-binding. 1 Publication
Mutagenesisi130 – 1301L → Y: Prevents tetramerization. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 246246SWI5-dependent HO expression protein 2PRO_0000203151Add
BLAST

Proteomic databases

MaxQBiP36068.
PeptideAtlasiP36068.

PTM databases

iPTMnetiP36068.

Interactioni

Subunit structurei

Homodimer and homotetramer. Interacts with LOC1, MYO4, PUF6, SHE3 and with RNA pol II subunits RPO21, SPT4 and SPT5.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MYO4P324924EBI-26866,EBI-11681
SHE3P382723EBI-26866,EBI-21600

Protein-protein interaction databases

BioGridi34005. 89 interactions.
DIPiDIP-1206N.
IntActiP36068. 19 interactions.
MINTiMINT-400410.

Structurei

Secondary structure

1
246
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 4230Combined sources
Helixi46 – 483Combined sources
Helixi49 – 7123Combined sources
Helixi74 – 774Combined sources
Turni86 – 883Combined sources
Helixi92 – 11827Combined sources
Helixi120 – 12910Combined sources
Helixi132 – 1343Combined sources
Helixi138 – 16124Combined sources
Helixi167 – 1693Combined sources
Helixi172 – 1798Combined sources
Helixi194 – 1963Combined sources
Beta strandi197 – 1993Combined sources
Helixi205 – 23531Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XLYX-ray1.95A/B6-239[»]
4WNLX-ray2.80A/B/C/D6-239[»]
ProteinModelPortaliP36068.
SMRiP36068. Positions 6-239.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36068.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi15 – 239Nuclear localization signal

Sequence similaritiesi

Belongs to the SHE2 family.Curated

Phylogenomic databases

InParanoidiP36068.
KOiK18736.
OMAiLNKYINY.
OrthoDBiEOG72NS20.

Family and domain databases

Gene3Di1.20.200.20. 1 hit.
InterProiIPR024261. RNA-bd_She2.
[Graphical view]
PfamiPF11435. She2p. 1 hit.
[Graphical view]
SUPFAMiSSF116942. SSF116942. 1 hit.

Sequencei

Sequence statusi: Complete.

P36068-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKDKDIKVT PGTCELVEQI LALLSRYLSS YIHVLNKFIS HLRRVATLRF
60 70 80 90 100
ERTTLIKFVK KLRFYNDCVL SYNASEFINE GKNELDPEAD SFDKVILPIA
110 120 130 140 150
SMFVKCVETF DLLNYYLTQS LQKEILSKTL NEDLTLTAES ILAIDDTYNH
160 170 180 190 200
FVKFSQWMIE SLRIGSNLLD LEVVQFAIKC ADEDGTNIGE TDNIFLQEIL
210 220 230 240
PVNSEEEFQT LSAAWHSILD GKLSALDEEF DVVATKWHDK FGKLKN
Length:246
Mass (Da):28,251
Last modified:June 1, 1994 - v1
Checksum:i5514B374655EFDBB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z28130 Genomic DNA. Translation: CAA81971.1.
AY557902 Genomic DNA. Translation: AAS56228.1.
BK006944 Genomic DNA. Translation: DAA09031.1.
PIRiS37959.
RefSeqiNP_012792.1. NM_001179696.1.

Genome annotation databases

EnsemblFungiiYKL130C; YKL130C; YKL130C.
GeneIDi853728.
KEGGisce:YKL130C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z28130 Genomic DNA. Translation: CAA81971.1.
AY557902 Genomic DNA. Translation: AAS56228.1.
BK006944 Genomic DNA. Translation: DAA09031.1.
PIRiS37959.
RefSeqiNP_012792.1. NM_001179696.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XLYX-ray1.95A/B6-239[»]
4WNLX-ray2.80A/B/C/D6-239[»]
ProteinModelPortaliP36068.
SMRiP36068. Positions 6-239.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34005. 89 interactions.
DIPiDIP-1206N.
IntActiP36068. 19 interactions.
MINTiMINT-400410.

PTM databases

iPTMnetiP36068.

Proteomic databases

MaxQBiP36068.
PeptideAtlasiP36068.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKL130C; YKL130C; YKL130C.
GeneIDi853728.
KEGGisce:YKL130C.

Organism-specific databases

EuPathDBiFungiDB:YKL130C.
SGDiS000001613. SHE2.

Phylogenomic databases

InParanoidiP36068.
KOiK18736.
OMAiLNKYINY.
OrthoDBiEOG72NS20.

Enzyme and pathway databases

BioCyciYEAST:G3O-31911-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP36068.
PROiP36068.

Family and domain databases

Gene3Di1.20.200.20. 1 hit.
InterProiIPR024261. RNA-bd_She2.
[Graphical view]
PfamiPF11435. She2p. 1 hit.
[Graphical view]
SUPFAMiSSF116942. SSF116942. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete DNA sequence of yeast chromosome XI."
    Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
    , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
    Nature 369:371-378(1994) [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. Cited for: FUNCTION.
  5. "Localization and anchoring of mRNA in budding yeast."
    Beach D.L., Salmon E.D., Bloom K.
    Curr. Biol. 9:569-578(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Association of the class V myosin Myo4p with a localised messenger RNA in budding yeast depends on She proteins."
    Munchow S., Sauter C., Jansen R.P.
    J. Cell Sci. 112:1511-1518(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "She2p, a novel RNA-binding protein tethers ASH1 mRNA to the Myo4p myosin motor via She3p."
    Bohl F., Kruse C., Frank A., Ferring D., Jansen R.P.
    EMBO J. 19:5514-5524(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING, INTERACTION WITH SHE3 AND MYO4.
  8. "She2p is a novel RNA-binding protein that recruits the Myo4p-She3p complex to ASH1 mRNA."
    Long R.M., Gu W., Lorimer E., Singer R.H., Chartrand P.
    EMBO J. 19:6592-6601(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING, INTERACTION WITH SHE3.
  9. "The myosin motor, Myo4p, binds Ash1 mRNA via the adapter protein, She3p."
    Takizawa P.A., Vale R.D.
    Proc. Natl. Acad. Sci. U.S.A. 97:5273-5278(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA-BINDING, INTERACTION WITH MYO4.
  10. "Ribonucleoprotein-dependent localization of the yeast class V myosin Myo4p."
    Kruse C., Jaedicke A., Beaudouin J., Bohl F., Ferring D., Guttler T., Ellenberg J., Jansen R.P.
    J. Cell Biol. 159:971-982(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  11. "Myo4p and She3p are required for cortical ER inheritance in Saccharomyces cerevisiae."
    Estrada P., Kim J., Coleman J., Walker L., Dunn B., Takizawa P., Novick P., Ferro-Novick S.
    J. Cell Biol. 163:1255-1266(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  13. "Widespread cytoplasmic mRNA transport in yeast: identification of 22 bud-localized transcripts using DNA microarray analysis."
    Shepard K.A., Gerber A.P., Jambhekar A., Takizawa P.A., Brown P.O., Herschlag D., DeRisi J.L., Vale R.D.
    Proc. Natl. Acad. Sci. U.S.A. 100:11429-11434(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "RNA-protein interactions promote asymmetric sorting of the ASH1 mRNA ribonucleoprotein complex."
    Gonsalvez G.B., Lehmann K.A., Ho D.K., Stanitsa E.S., Williamson J.R., Long R.M.
    RNA 9:1383-1399(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, RNA-BINDING, INTERACTION WITH SHE3, MUTAGENESIS OF ASN-36; ARG-43; ARG-44; ARG-49; ARG-52 AND ARG-63.
  15. "ASH1 mRNA anchoring requires reorganization of the Myo4p-She3p-She2p transport complex."
    Gonsalvez G.B., Little J.L., Long R.M.
    J. Biol. Chem. 279:46286-46294(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "Identification of a conserved RNA motif essential for She2p recognition and mRNA localization to the yeast bud."
    Olivier C., Poirier G., Gendron P., Boisgontier A., Major F., Chartrand P.
    Mol. Cell. Biol. 25:4752-4766(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING.
  17. "Coordination of endoplasmic reticulum and mRNA localization to the yeast bud."
    Schmid M., Jaedicke A., Du T.G., Jansen R.P.
    Curr. Biol. 16:1538-1543(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  18. "Nuclear transit of the RNA-binding protein She2 is required for translational control of localized ASH1 mRNA."
    Du T.G., Jellbauer S., Muller M., Schmid M., Niessing D., Jansen R.P.
    EMBO Rep. 9:781-787(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  19. "Nuclear shuttling of She2p couples ASH1 mRNA localization to its translational repression by recruiting Loc1p and Puf6p."
    Shen Z., Paquin N., Forget A., Chartrand P.
    Mol. Biol. Cell 20:2265-2275(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH LOC1; PUF6 AND SRP1, NUCLEUS LOCALIZATION SIGNAL, SUBCELLULAR LOCATION.
  20. "Formation of She2p tetramers is required for mRNA binding, mRNP assembly, and localization."
    Muller M., Richter K., Heuck A., Kremmer E., Buchner J., Jansen R.P., Niessing D.
    RNA 15:2002-2012(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, MUTAGENESIS OF LEU-130.
  21. "Cotranscriptional recruitment of She2p by RNA pol II elongation factor Spt4-Spt5/DSIF promotes mRNA localization to the yeast bud."
    Shen Z., St-Denis A., Chartrand P.
    Genes Dev. 24:1914-1926(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RPO21; SPT4 AND SPT5.
  22. "She2p is a novel RNA binding protein with a basic helical hairpin motif."
    Niessing D., Huttelmaier S., Zenklusen D., Singer R.H., Burley S.K.
    Cell 119:491-502(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 6-239, SUBUNIT, FUNCTION, RNA-BINDING, MUTAGENESIS OF CYS-68 AND SER-120.

Entry informationi

Entry nameiSHE2_YEAST
AccessioniPrimary (citable) accession number: P36068
Secondary accession number(s): D6VX65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
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 4070 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 XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: 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.