Suppressor protein STM1 - Saccharomyces cerevisiae (Baker's yeast)

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Names and origin

Protein names

Recommended name:
    Suppressor protein STM1
Alternative name(s):
    GU4 nucleic-binding protein 2
      Short name=G4p2 protein
    Triplex-binding protein 1
    3BP1
    Ribosomal subunits association factor
      Short name=AF
    POP2 multicopy suppressor protein 4
    TOM1 suppressor protein 1

Gene names

Name:	STM1
Synonyms:	MPT4, STO1
Ordered Locus Names:	YLR150W
ORF Names:	L9634.1

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	273 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Binds specifically G4 quadruplex (these are four-stranded right-handed helices, stabilized by guanine base quartets) and purine motif triplex (characterized by a third, antiparallel purine-rich DNA strand located within the major groove of a homopurine stretch of duplex DNA) nucleic acid structures. These structures may be present at telomeres or in rRNAs. Acts with CDC13 to control telomere length homeostasis. Involved in the control of the apoptosis-like cell death. Ref.12
Subunit structure	Interacts with CDC13. Associates with mature 80S ribosomes. Associates with the telomere-proximal Y' element. Ref.12 Ref.10
Subcellular location	Cytoplasm. Nucleus. Cytoplasm › perinuclear region. Note: Concentrated in the perinuclear region. Ref.12 Ref.9
Miscellaneous	Present with 46842 molecules/cell in log phase SD medium. Ref.11

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Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Ligand	DNA-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	TOR signaling pathway Inferred from mutant phenotype. Source: SGD anti-apoptosis Ref.9 Inferred from direct assay. Source: SGD regulation of translational initiation in response to stress Inferred from mutant phenotype. Source: SGD telomere maintenance Ref.10 Inferred from genetic interaction. Source: SGD
Cellular component	cytosolic ribosome Ref.12 Inferred from direct assay. Source: SGD nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell polysome Ref.12 Inferred from direct assay. Source: SGD
Molecular function	protein binding Inferred from physical interaction. Source: IntAct telomeric DNA binding Ref.12 Inferred from direct assay. Source: SGD triplex DNA binding Inferred from direct assay. Source: SGD
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
	P43582	1	EBI-11238,EBI-22766
ESS1	P22696	1	EBI-11238,EBI-6679
PRP40	P33203	1	EBI-11238,EBI-701
RSP5	P39940	1	EBI-11238,EBI-16219
SET2	P46995	1	EBI-11238,EBI-16985
SSM4	P40318	1	EBI-11238,EBI-18208
URN1	Q06525	1	EBI-11238,EBI-35138

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.6

Chain

2 – 273

272

Suppressor protein STM1

PRO_0000072278

Regions

Compositional bias

38 – 54

Pro-rich

Compositional bias

77 – 102

Ser/Thr-rich

Compositional bias

119 – 141

Ala-rich

Compositional bias

147 – 164

Asn/Gln-rich

Compositional bias

225 – 250

Arg/Asn/Gly-rich

Amino acid modifications

Modified residue

N-acetylserine Ref.6

Modified residue

Phosphoserine Ref.14

Modified residue

Phosphoserine Ref.15 Ref.16

Modified residue

118

Phosphoserine Ref.15 Ref.16 Ref.13

Modified residue

181

Phosphothreonine Ref.14

Modified residue

229

Phosphoserine Ref.14

Experimental info

Sequence conflict

133

E → Q AA sequence Ref.8

Sequence conflict

171

K → E in AAA70169. Ref.3

Sequence conflict

177

E → G in AAA70169. Ref.3

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Sequences

Sequence

Length

Mass (Da)

Tools

P39015-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: CD01C5C047F99523
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FASTA

273

29,995

        10         20         30         40         50         60 
MSNPFDLLGN DVEDADVVVL PPKEIVKSNT SSKKADVPPP SADPSKARKN RPRPSGNEGA 

        70         80         90        100        110        120 
IRDKTAGRRN NRSKDVTDSA TTKKSNTRRA TDRHSRTGKT DTKKKVNQGW GDDKKELSAE 

       130        140        150        160        170        180 
KEAQADAAAE IAEDAAEAED AGKPKTAQLS LQDYLNQQAN NQFNKVPEAK KVELDAERIE 

       190        200        210        220        230        240 
TAEKEAYVPA TKVKNVKSKQ LKTKEYLEFD ATFVESNTRK NFGDRNNNSR NNFNNRRGGR 

       250        260        270 
GARKGNNTAN ATNSANTVQK NRNIDVSNLP SLA

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Dhh1p, a putative RNA helicase, associates with the general transcription factors Pop2p and Ccr4p from Saccharomyces cerevisiae." Hata H., Mitsui H., Liu H., Bai Y., Denis C.L., Shimizu Y., Sakai A. Genetics 148:571-579(1998) [PubMed: 9504907] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[2]	"A high dose of the STM1 gene suppresses the temperature sensitivity of the tom1 and htr1 mutants in Saccharomyces cerevisiae." Utsugi T., Toh-e A., Kikuchi Y. Biochim. Biophys. Acta 1263:285-288(1995) [PubMed: 7548221] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"A yeast gene product, G4p2, with a specific affinity for quadruplex nucleic acids." Frantz J.D., Gilbert W. J. Biol. Chem. 270:9413-9419(1995) [PubMed: 7721866] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 122-145 AND 146-170, DNA-BINDING.
[4]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII." Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H. Hoheisel J.D. Nature 387:87-90(1997) [PubMed: 9169871] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[5]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed: 17322287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	Bienvenut W.V., Peters C. Submitted (JUN-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-27; 34-46 AND 263-273, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, MASS SPECTROMETRY.
[7]	"The yeast STM1 gene encodes a purine motif triple helical DNA-binding protein." Nelson L.D., Musso M., Van Dyke M.W. J. Biol. Chem. 275:5573-5581(2000) [PubMed: 10681538] [Abstract] Cited for: PROTEIN SEQUENCE OF 106-114 AND 265-273, DNA-BINDING.
[8]	"Similarity between the association factor of ribosomal subunits and the protein Stm1p from Saccharomyces cerevisiae." Correia H., Medina R., Hernandez A., Bustamante E., Chakraburtty K., Herrera F. Mem. Inst. Oswaldo Cruz 99:733-737(2004) [PubMed: 15654430] [Abstract] Cited for: PROTEIN SEQUENCE OF 110-137.
[9]	"The proteasomal substrate Stm1 participates in apoptosis-like cell death in yeast." Ligr M., Velten I., Froehlich E., Madeo F., Ledig M., Froehlich K.-U., Wolf D.H., Hilt W. Mol. Biol. Cell 12:2422-2432(2001) [PubMed: 11514626] [Abstract] Cited for: SUBCELLULAR LOCATION.
[10]	"STM1, a gene which encodes a guanine quadruplex binding protein, interacts with CDC13 in Saccharomyces cerevisiae." Hayashi N., Murakami S. Mol. Genet. Genomics 267:806-813(2002) [PubMed: 12207228] [Abstract] Cited for: INTERACTION WITH CDC13.
[11]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[12]	"Stm1p, a G4 quadruplex and purine motif triplex nucleic acid-binding protein, interacts with ribosomes and subtelomeric Y' DNA in Saccharomyces cerevisiae." Van Dyke M.W., Nelson L.D., Weilbaecher R.G., Mehta D.V. J. Biol. Chem. 279:24323-24333(2004) [PubMed: 15044472] [Abstract] Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
[13]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118, MASS SPECTROMETRY.
[14]	"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: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; THR-181 AND SER-229, MASS SPECTROMETRY.
[15]	"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: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73 AND SER-118, MASS SPECTROMETRY.
[16]	"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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73 AND SER-118, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	D26183 Genomic DNA. Translation: BAA05171.1. D32208 Genomic DNA. Translation: BAA06907.1. U20616 Genomic DNA. Translation: AAA70169.1. Z73322 Genomic DNA. Translation: CAA97722.1. U53879 Genomic DNA. Translation: AAB82384.1. AY557944 Genomic DNA. Translation: AAS56270.1.
PIR	S48511.
RefSeq	NP_013251.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:1675N.
IntAct	P39015. 27 interactions.
Proteomic databases
PeptideAtlas	P39015.
PRIDE	P39015.
Genome annotation databases
Ensembl	YLR150W. Saccharomyces cerevisiae. [Contig view]
GeneID	850843.
GenomeReviews	Gene locus YLR150W in contig Y13138_GR.
KEGG	sce:YLR150W.
NMPDR	fig\|4932.3.peg.4245.
Organism-specific databases
CYGD	YLR150w.
SGD	S000004140. STM1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	P39015.
OMA	P39015. KKPFDRH.
Gene expression databases
ArrayExpress	P39015.
GermOnline	YLR150W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR019084. Stm1_N-terminal. [Graphical view]
Pfam	PF09598. Stm1_N. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	967129.

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Entry information

Entry name

STM1_YEAST

Accession

Primary (citable) accession number: P39015

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 84 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)

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Relevant documents

Yeast

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

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

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents