SWI5-dependent HO expression protein 3 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P38272 (SHE3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 100. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
SWI5-dependent HO expression protein 3

Gene names

Name:	SHE3
Ordered Locus Names:	YBR130C
ORF Names:	YBR1005

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	425 AA.
Sequence status	Complete.
Protein existence	Evidence 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.14 Ref.15 Ref.17 Ref.22
Subunit structure	Interacts with SHE2 and MYO4. Ref.7 Ref.8 Ref.9 Ref.14 Ref.23
Subcellular location	Endoplasmic reticulum membrane; Peripheral membrane protein Ref.11 Ref.14.
Miscellaneous	Present with 1010 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the SHE3 family.

Ontologies

Keywords
Biological process	Transport mRNA transport
Cellular component	Endoplasmic reticulum Membrane
Domain	Coiled coil
Ligand	RNA-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	endoplasmic reticulum inheritance Inferred from mutant phenotype Ref.11. Source: SGD intracellular mRNA localization Inferred from mutant phenotype Ref.6. Source: SGD mRNA transport Inferred from electronic annotation. Source: UniProtKB-KW mating type switching Inferred from mutant phenotype PubMed 8625407. Source: SGD
Cellular_component	actin cap Traceable author statement PubMed 10652251. Source: SGD cellular bud tip Inferred from direct assay Ref.7. Source: SGD endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	mRNA binding Inferred from direct assay Ref.6. Source: SGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MYO4	P32492	7	EBI-21600,EBI-11681
SHE2	P36068	3	EBI-21600,EBI-26866

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 425

425

SWI5-dependent HO expression protein 3

PRO_0000202490

Regions

Coiled coil

68 – 197

130

Potential

Compositional bias

377 – 381

Poly-Ser

Amino acid modifications

Modified residue

Phosphoserine Ref.19 Ref.21

Modified residue

123

Phosphotyrosine Ref.13

Modified residue

217

Phosphoserine Ref.21

Modified residue

343

Phosphoserine Ref.18 Ref.21

Modified residue

348

Phosphoserine Ref.21

Modified residue

361

Phosphoserine Ref.16 Ref.21

Modified residue

392

Phosphoserine Ref.20

Modified residue

393

Phosphothreonine Ref.21

Modified residue

394

Phosphoserine Ref.16 Ref.20 Ref.21

Experimental info

Mutagenesis

343

S → E: Prevents correct localization of ASH1 mRNA; when associated with E-361. Ref.22

Mutagenesis

348

S → E: Prevents correct localization of ASH1 mRNA. Ref.22

Mutagenesis

361

S → E: Prevents correct localization of ASH1 mRNA; when associated with E-343. Ref.22

Sequences

Sequence

Length

Mass (Da)

Tools

P38272 [UniParc].

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

425

47,417

        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' referencesShow '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. 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]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases 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]	"A proteomics approach to understanding protein ubiquitination." Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., Marsischky G., Roelofs J., Finley D., Gygi S.P. Nat. Biotechnol. 21:921-926(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-123, MASS SPECTROMETRY. Strain: SUB592.
[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, INTERACTION WITH SHE2.
[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]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361 AND SER-394, MASS SPECTROMETRY. Strain: YAL6B.
[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.
[18]	"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, MASS SPECTROMETRY. Strain: ADR376.
[19]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28, MASS SPECTROMETRY.
[20]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392 AND SER-394, MASS SPECTROMETRY.
[21]	"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-28; SER-217; SER-343; SER-348; SER-361; THR-393 AND SER-394, MASS SPECTROMETRY.
[22]	"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.
[23]	"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.
PIR	S45999.
RefSeq	NP_009688.3. NM_001178478.3.
3D structure databases
ProteinModelPortal	P38272.
SMR	P38272. Positions 182-217.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-2037N.
IntAct	P38272. 20 interactions.
MINT	MINT-572712.
STRING	4932.YBR130C.
Proteomic databases
PaxDb	P38272.
PeptideAtlas	P38272.
PRIDE	P38272.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YBR130C; YBR130C; YBR130C.
GeneID	852427.
KEGG	sce:YBR130C.
Organism-specific databases
CYGD	YBR130c.
SGD	S000000334. SHE3.
Phylogenomic databases
eggNOG	NOG130615.
OMA	MANLESS.
OrthoDB	EOG476P87.
Enzyme and pathway databases
BioCyc	YEAST:G3O-29085-MONOMER.
Gene expression databases
Genevestigator	P38272.
GermOnline	YBR130C. Saccharomyces cerevisiae.
Family and domain databases
ProtoNet	Search...
Other
NextBio	971303.

Entry information

Entry name

SHE3_YEAST

Accession

Primary (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:	May 29, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

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

Yeast chromosome II

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents