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Protein

RNA-binding protein SRO9

Gene

SRO9

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May overlap in function with tropomyosin and may be involved in organization of actin filaments. Acts as a multicopy suppressor of RHO3 mutation. RNA-binding protein which may modulate mRNA translation. Involved in heme regulation of HAP1, as a component of the high-molecular-weight complex (HMC).2 Publications

GO - Molecular functioni

  • RNA binding Source: SGD

GO - Biological processi

  • cytoplasmic translation Source: SGD
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29296-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
RNA-binding protein SRO9
Alternative name(s):
Suppressor of RHO3 protein 9
Gene namesi
Name:SRO9
Ordered Locus Names:YCL037C
ORF Names:YCL37C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:YCL037C.
SGDiS000000542. SRO9.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic stress granule Source: SGD
  • polysome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 434434RNA-binding protein SRO9PRO_0000207615Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei55 – 551PhosphoserineCombined sources
Modified residuei148 – 1481PhosphoserineCombined sources
Modified residuei422 – 4221PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP25567.
PeptideAtlasiP25567.

PTM databases

iPTMnetiP25567.

Interactioni

Subunit structurei

Interacts with HAP1. Component of the HMC including HAP1, SRO9 and YDJ1.1 Publication

Protein-protein interaction databases

BioGridi30946. 937 interactions.
DIPiDIP-6638N.
IntActiP25567. 36 interactions.
MINTiMINT-8285517.

Structurei

3D structure databases

ProteinModelPortaliP25567.
SMRiP25567. Positions 261-339.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini255 – 35197HTH La-type RNA-bindingPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi168 – 1714Poly-Gln
Compositional biasi174 – 18411His-richAdd
BLAST
Compositional biasi222 – 2265Poly-Asn

Sequence similaritiesi

Contains 1 HTH La-type RNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00530000067375.
HOGENOMiHOG000057093.
InParanoidiP25567.
KOiK18757.
OMAiSSANTKW.
OrthoDBiEOG7QNVZG.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR006630. Lupus_La_RNA-bd.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF05383. La. 1 hit.
[Graphical view]
SMARTiSM00715. LA. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS50961. HTH_LA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P25567-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAETAAANT ATAPVPEVQE QESSKSKQVN LTPAPLPTSS PWKLAPTEIP
60 70 80 90 100
VSTISIEDLD ATRKKKNRTP TPKSSTATKW VPIKASITVS GTKRSGSKNG
110 120 130 140 150
ASNGNSNKSK NNKTAASSTS SSNANRKKKH HQHNAKKQQQ MKKDGFESAV
160 170 180 190 200
GEEDSKDATS QENGQSTQQQ QPPHHRNHHH SHHHNSNGPQ RRKFHNSNNA
210 220 230 240 250
GMPQNQGFPP QFKPYQGRNA RNNNNNRSKY HNHFHHNQQH PQQPMVKLQQ
260 270 280 290 300
QFYPVQPVLM AINNIARQIE YYFSEENLTV DNYLRSKLSK DGFAPLSLIS
310 320 330 340 350
KFYRVVNMSF GGDTNLILAA LREIVANEAA TVNVAEGTLA AKEGDNVTGE
360 370 380 390 400
AKEPSPLDKY FVRSKSWSNW LPETFETEIN IEKELVGDAL DQFMISLPPV
410 420 430
PQQEEESSTE LASQEQETKE DSAPVAAGES ESSL
Length:434
Mass (Da):48,060
Last modified:March 7, 2006 - v2
Checksum:iB1B720D40C7B9914
GO

Sequence cautioni

The sequence CAA42379.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAA42379.1. Different initiation.
BK006937 Genomic DNA. Translation: DAA07447.1.
PIRiS19365.
RefSeqiNP_009893.2. NM_001178682.1.

Genome annotation databases

EnsemblFungiiCAA42379; CAA42379; CAA42379.
YCL037C; YCL037C; YCL037C.
GeneIDi850320.
KEGGisce:YCL037C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59720 Genomic DNA. Translation: CAA42379.1. Different initiation.
BK006937 Genomic DNA. Translation: DAA07447.1.
PIRiS19365.
RefSeqiNP_009893.2. NM_001178682.1.

3D structure databases

ProteinModelPortaliP25567.
SMRiP25567. Positions 261-339.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi30946. 937 interactions.
DIPiDIP-6638N.
IntActiP25567. 36 interactions.
MINTiMINT-8285517.

PTM databases

iPTMnetiP25567.

Proteomic databases

MaxQBiP25567.
PeptideAtlasiP25567.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCAA42379; CAA42379; CAA42379.
YCL037C; YCL037C; YCL037C.
GeneIDi850320.
KEGGisce:YCL037C.

Organism-specific databases

EuPathDBiFungiDB:YCL037C.
SGDiS000000542. SRO9.

Phylogenomic databases

GeneTreeiENSGT00530000067375.
HOGENOMiHOG000057093.
InParanoidiP25567.
KOiK18757.
OMAiSSANTKW.
OrthoDBiEOG7QNVZG.

Enzyme and pathway databases

BioCyciYEAST:G3O-29296-MONOMER.

Miscellaneous databases

NextBioi965730.
PROiP25567.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR006630. Lupus_La_RNA-bd.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF05383. La. 1 hit.
[Graphical view]
SMARTiSM00715. LA. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS50961. HTH_LA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The complete DNA sequence of yeast chromosome III."
    Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M.
    , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
    Nature 357:38-46(1992) [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. "The Hsp70-Ydj1 molecular chaperone represses the activity of the heme activator protein Hap1 in the absence of heme."
    Hon T., Lee H.C., Hach A., Johnson J.L., Craig E.A., Erdjument-Bromage H., Tempst P., Zhang L.
    Mol. Cell. Biol. 21:7923-7932(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 24-44; 43-65; 137-157; 192-219; 227-248 AND 342-364, FUNCTION, IDENTIFICATION IN HMC COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  4. "SRO9, a multicopy suppressor of the bud growth defect in the Saccharomyces cerevisiae RHO3-deficient cells, shows strong genetic interactions with tropomyosin genes, suggesting its role in organization of the actin cytoskeleton."
    Kagami M., Toh-e A., Matsui Y.
    Genetics 147:1003-1016(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  5. "Two yeast La motif-containing proteins are RNA-binding proteins that associate with polyribosomes."
    Sobel S.G., Wolin S.L.
    Mol. Biol. Cell 10:3849-3862(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  6. "Sequencing and comparison of yeast species to identify genes and regulatory elements."
    Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.
    Nature 423:241-254(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF PROBABLE INITIATION SITE.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "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-55 AND SER-422, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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-148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Sites of ubiquitin attachment in Saccharomyces cerevisiae."
    Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.
    Proteomics 12:236-240(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSRO9_YEAST
AccessioniPrimary (citable) accession number: P25567
Secondary accession number(s): D6VQX8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: March 7, 2006
Last modified: May 11, 2016
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 8430 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome III
    Yeast (Saccharomyces cerevisiae) chromosome III: 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.