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P38272 (SHE3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
SWI5-dependent HO expression protein 3
Gene names
Name:SHE3
Ordered Locus Names:YBR130C
ORF Names:YBR1005
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length425 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Required for the delivery of cortical endoplasmic reticulum into the emerging bud. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.19

Subunit structure

Interacts with SHE2 and MYO4. Ref.7 Ref.8 Ref.9 Ref.13 Ref.21

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein Ref.11 Ref.13.

Miscellaneous

Present with 1010 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the SHE3 family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

MYO4P324927EBI-21600,EBI-11681
SHE2P360683EBI-21600,EBI-26866

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 425425SWI5-dependent HO expression protein 3
PRO_0000202490

Regions

Coiled coil68 – 197130 Potential
Compositional bias377 – 3815Poly-Ser

Amino acid modifications

Modified residue3431Phosphoserine Ref.16
Modified residue3941Phosphoserine Ref.18 Ref.20

Experimental info

Mutagenesis3431S → E: Prevents correct localization of ASH1 mRNA; when associated with E-361. Ref.19
Mutagenesis3481S → E: Prevents correct localization of ASH1 mRNA. Ref.19
Mutagenesis3611S → E: Prevents correct localization of ASH1 mRNA; when associated with E-343. Ref.19

Secondary structure

..... 425
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P38272 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 590404D2E140BB7A

FASTA42547,417
        10         20         30         40         50         60 
MSDQDNTQTS SSKLAPHHNI FMANLESSPT KDRNTSSQNA SSSRVIESLH DQIDMLTKTN 

        70         80         90        100        110        120 
LQLTTQSQNL LSKLELAQSK ESKLLENLNL LKNENENLNS IFERKNKKLK ELEKDYSELS 

       130        140        150        160        170        180 
NRYNEQKEKM DQLSKLAKNS SAIEQSCSEK LQNMEVNYNS LLESQNLYRD HYSDEISKLN 

       190        200        210        220        230        240 
EKIGLLELEL SNQNLNYGSD TSSNSDIELN LNKFNDSVKD LKSLETEKDS KLSKIITHSL 

       250        260        270        280        290        300 
DELNLQSWLN LYQTNENLIS TFAEKMDLKD VLKRNDEKIS NKGAVVQTLK KNVQTQVESN 

       310        320        330        340        350        360 
NADALSSNNA QDMLPIKMVK LRKTPNTNDS SSNGNSSNNK RRSFYTASPL LSSGSIPKSA 

       370        380        390        400        410        420 
SPVLPGVKRT ASVRKPSSSS SKTNVTHNND PSTSPTISVP PGVTRTVSST HKKKGNSMVV 


HGAQS 

« Hide

References

« Hide 'large scale' references
[1]"The sequence of 29.7 kb from the right arm of chromosome II reveals 13 complete open reading frames, of which ten correspond to new genes."
Becam A.-M., Cullin C., Grzybowska E., Lacroute F., Nasr F., Ozier-Kalogeropoulos O., Palucha A., Slonimski P.P., Zagulski M., Herbert C.J.
Yeast 10:S1-S11(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"Complete DNA sequence of yeast chromosome II."
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. expand/collapse author list , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Localization of ASH1 mRNA particles in living yeast."
Bertrand E., Chartrand P., Schaefer M., Shenoy S.M., Singer R.H., Long R.M.
Mol. Cell 2:437-445(1998) [PubMed] [Europe PMC] [Abstract]
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, INTERACTION WITH SHE2 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 SHE2.
[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.
[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, SUBCELLULAR LOCATION.
[12]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[13]"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, INTERACTION WITH SHE2.
[14]"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.
[15]"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.
[16]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[17]"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"She3p possesses a novel activity required for ASH1 mRNA localization in Saccharomyces cerevisiae."
Landers S.M., Gallas M.R., Little J., Long R.M.
Eukaryot. Cell 8:1072-1083(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, MUTAGENESIS OF SER-343; SER-348 AND SER-361.
[20]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"The structure of the Myo4p globular tail and its function in ASH1 mRNA localization."
Heuck A., Fetka I., Brewer D.N., Huls D., Munson M., Jansen R.P., Niessing D.
J. Cell Biol. 189:497-510(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MYO4.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X75891 Genomic DNA. Translation: CAA53489.1.
Z35999 Genomic DNA. Translation: CAA85087.1.
BK006936 Genomic DNA. Translation: DAA07247.1.
PIRS45999.
RefSeqNP_009688.3. NM_001178478.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4LL7X-ray2.31A/B/C/D/E/F/G/H42-137[»]
4LL8X-ray3.58B/E81-311[»]
ProteinModelPortalP38272.
SMRP38272. Positions 43-196.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32831. 63 interactions.
DIPDIP-2037N.
IntActP38272. 17 interactions.
MINTMINT-572712.
STRING4932.YBR130C.

Proteomic databases

MaxQBP38272.
PaxDbP38272.
PeptideAtlasP38272.
PRIDEP38272.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR130C; YBR130C; YBR130C.
GeneID852427.
KEGGsce:YBR130C.

Organism-specific databases

CYGDYBR130c.
SGDS000000334. SHE3.

Phylogenomic databases

eggNOGNOG130615.
OMAFMANLES.
OrthoDBEOG7J44J8.

Enzyme and pathway databases

BioCycYEAST:G3O-29085-MONOMER.

Gene expression databases

GenevestigatorP38272.

Family and domain databases

ProtoNetSearch...

Other

NextBio971303.

Entry information

Entry nameSHE3_YEAST
AccessionPrimary (citable) accession number: P38272
Secondary accession number(s): D6VQC7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: June 11, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references