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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: -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

Miscellaneous

Present with 4070 molecules/cell in log phase SD medium.1 Publication

GO - Molecular functioni

  • lipid binding Source: SGD
  • mRNA binding Source: SGD
  • sequence-specific mRNA binding Source: SGD

GO - Biological processi

  • intracellular mRNA localization Source: SGD
  • mating type switching Source: SGD
  • mRNA transport Source: UniProtKB-KW

Keywordsi

Molecular functionRNA-binding
Biological processmRNA transport, Transport

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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi36N → S: Prevents association with ASH1 and IST2 mRNAs and leads to their mislocalization. 1 Publication1
Mutagenesisi43R → A: Prevents association with ASH1 and mRNA and leads to its mislocalization. 1 Publication1
Mutagenesisi44R → A: Prevents association with ASH1 and mRNA and leads to its mislocalization. 1 Publication1
Mutagenesisi49R → K: Prevents association with ASH1 and mRNA and leads to its mislocalization. 1 Publication1
Mutagenesisi52R → A or K: Prevents association with ASH1 and mRNA and leads to its mislocalization. 1 Publication1
Mutagenesisi63R → A or K: Prevents association with ASH1 and IST2 mRNAs and leads to their mislocalization. 1 Publication1
Mutagenesisi68C → Y: Prevents dimerization and RNA-binding. 1 Publication1
Mutagenesisi120S → Y: Prevents dimerization and RNA-binding. 1 Publication1
Mutagenesisi130L → Y: Prevents tetramerization. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002031511 – 246SWI5-dependent HO expression protein 2Add BLAST246

Proteomic databases

MaxQBiP36068
PaxDbiP36068
PRIDEiP36068

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

Show more details

Protein-protein interaction databases

BioGridi34005, 111 interactors
DIPiDIP-1206N
IntActiP36068, 30 interactors
MINTiP36068
STRINGi4932.YKL130C

Structurei

Secondary structure

1246
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi13 – 42Combined sources30
Helixi46 – 48Combined sources3
Helixi49 – 71Combined sources23
Helixi74 – 77Combined sources4
Turni86 – 88Combined sources3
Helixi92 – 118Combined sources27
Helixi120 – 129Combined sources10
Helixi132 – 134Combined sources3
Helixi138 – 161Combined sources24
Helixi167 – 169Combined sources3
Helixi172 – 179Combined sources8
Helixi194 – 196Combined sources3
Beta strandi197 – 199Combined sources3
Helixi205 – 235Combined sources31

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XLYX-ray1.95A/B6-239[»]
4WNLX-ray2.80A/B/C/D6-239[»]
5M0IX-ray2.41A/B/C/D6-246[»]
5M0JX-ray2.80A/B/C/D/G/H/I/J6-246[»]
ProteinModelPortaliP36068
SMRiP36068
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36068

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi15 – 23Nuclear localization signal9

Sequence similaritiesi

Belongs to the SHE2 family.Curated

Phylogenomic databases

InParanoidiP36068
KOiK18736
OMAiDTYNHFV
OrthoDBiEOG092C5B2J

Family and domain databases

Gene3Di1.20.200.20, 1 hit
InterProiView protein in InterPro
IPR024261 RNA-bd_She2
IPR036827 She2_dom_sf
PfamiView protein in Pfam
PF11435 She2p, 1 hit
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

Similar proteinsi

Entry informationi

Entry nameiSHE2_YEAST
AccessioniPrimary (citable) accession number: P36068
Secondary accession number(s): D6VX65
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: March 28, 2018
This is version 134 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome
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Main funding by: National Institutes of Health