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Protein

Pumilio homology domain family member 6

Gene

PUF6

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

Functioni

RNA-binding protein involved in post-transcriptional regulation. Component of the ASH1 mRNP which transports the ASH1 mRNA to the distal tip of the bud, where the ASH1 protein is translated and targeted to the daughter cell nucleus. Binds to the ASH1 3'-UTR containing the PUF consensus UUGU segment and represses its translation. This silencing of ASH1 mRNA is critical for asymmetric seggregation of ASH1 to the daughter cell nucleus.3 Publications

GO - Molecular functioni

  • mRNA 3'-UTR binding Source: SGD
  • translation repressor activity, nucleic acid binding Source: SGD

GO - Biological processi

  • negative regulation of translation Source: SGD
  • ribosomal large subunit biogenesis Source: SGD
  • transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

Translation regulation, Transport

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-30019-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Pumilio homology domain family member 6
Gene namesi
Name:PUF6
Ordered Locus Names:YDR496C
ORF Names:D9719.2
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR496C.
SGDiS000002904. PUF6.

Subcellular locationi

GO - Cellular componenti

  • cellular bud tip Source: UniProtKB-SubCell
  • large ribosomal subunit Source: SGD
  • nucleolus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi31 – 311S → A: Increases translation repression of ASH1 mRNA. 1 Publication
Mutagenesisi34 – 341S → A: Increases translation repression of ASH1 mRNA. 1 Publication
Mutagenesisi35 – 351S → A: Increases translation repression of ASH1 mRNA. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 656656Pumilio homology domain family member 6PRO_0000075926Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei31 – 311Phosphoserine; by CK21 Publication
Modified residuei34 – 341PhosphoserineCombined sources1 Publication
Modified residuei34 – 341Phosphoserine; by CK21 Publication
Modified residuei35 – 351PhosphoserineCombined sources1 Publication
Modified residuei35 – 351Phosphoserine; by CK21 Publication

Post-translational modificationi

phosphorylation by CK2 relieves translational repression activity.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ04373.
PeptideAtlasiQ04373.

PTM databases

iPTMnetiQ04373.

Interactioni

Subunit structurei

Component of the ASH1 mRNP composed of at least PUF6, SHE2, SHE3, SHE1 and the ASH1 mRNA. Interacts with SHE2 and FUN12.3 Publications

Protein-protein interaction databases

BioGridi32547. 142 interactions.
DIPiDIP-6579N.
IntActiQ04373. 60 interactions.
MINTiMINT-637951.

Structurei

3D structure databases

ProteinModelPortaliQ04373.
SMRiQ04373. Positions 73-508.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini133 – 483351PUM-HDPROSITE-ProRule annotationAdd
BLAST
Repeati155 – 19137Pumilio 1Add
BLAST
Repeati192 – 22736Pumilio 2Add
BLAST
Repeati228 – 26437Pumilio 3Add
BLAST
Repeati340 – 37637Pumilio 4Add
BLAST
Repeati377 – 41337Pumilio 5Add
BLAST
Repeati415 – 45036Pumilio 6Add
BLAST

Sequence similaritiesi

Belongs to the PUF6 family.Curated
Contains 1 PUM-HD domain.PROSITE-ProRule annotation
Contains 6 pumilio repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00390000015757.
HOGENOMiHOG000246618.
InParanoidiQ04373.
KOiK14844.
OMAiKRGPIMK.
OrthoDBiEOG7NW6JR.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR012959. CPL_dom.
IPR033133. PUM-HD.
IPR001313. Pumilio_RNA-bd_rpt.
[Graphical view]
PfamiPF08144. CPL. 1 hit.
[Graphical view]
SMARTiSM00025. Pumilio. 6 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50302. PUM. 5 hits.
PS50303. PUM_HD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q04373-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPLTKKTNG KRSAKEVSHS EKKLAKKPRI SIDSSDEESE LSKKEDAVSS
60 70 80 90 100
SSDDDDLDDL STSDSEAEEE ADELDISDDS EEHENENEEK EGKDKSEGGE
110 120 130 140 150
NGNHTEQRKL LKERKMQRKS GTQVQQIKSV WERLRVKTPP LPKQIREKLS
160 170 180 190 200
NEIWELSKDC ISDLVLKHDA SRIVQTLVKY SSKDRREQIV DALKGKFYVL
210 220 230 240 250
ATSAYGKYLL VKLLHYGSRS SRQTIINELH GSLRKLMRHR EGAYVVEDLF
260 270 280 290 300
VLYATHEQRQ QMIKEFWGSE YAVFRETHKD LTIEKVCESS IEKRNIIARN
310 320 330 340 350
LIGTITASVE KGSTGFQILH AAMREYVKIA NEKEISEMIE LLHEQFAELV
360 370 380 390 400
HTPEGSDVAC TLVARANAKE RKLILKALKN HAEKLIKNEY GNIVFITILN
410 420 430 440 450
CVDDTVLVFK TFSPTVKEHL QEFIIDKFGR RPWLYILLGL DGKYFSPIVK
460 470 480 490 500
NELLRYIELS KATSKKDPLQ RRHELLSKFA PMFLSTISKD YSSILTENLG
510 520 530 540 550
CQFIAEVLIN DELYAQLNEK DQEKYQQVLN NILTTFKGDI TEEEHPIHRA
560 570 580 590 600
FSTRLLKALI QGGKWNNKEK KVIPLKNVQG LGVPFAEKLY DEIIDSSNLL
610 620 630 640 650
EWINNADSSF TIVALYETLK DQKEGKPFLK DLRGVQSKIT TDESNKGSQL

LAKLLK
Length:656
Mass (Da):75,106
Last modified:November 1, 1996 - v1
Checksum:i4D172E8854326ECF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33057 Genomic DNA. Translation: AAB64938.1.
BK006938 Genomic DNA. Translation: DAA12328.1.
PIRiS69554.
RefSeqiNP_010784.1. NM_001180804.1.

Genome annotation databases

EnsemblFungiiYDR496C; YDR496C; YDR496C.
GeneIDi852107.
KEGGisce:YDR496C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U33057 Genomic DNA. Translation: AAB64938.1.
BK006938 Genomic DNA. Translation: DAA12328.1.
PIRiS69554.
RefSeqiNP_010784.1. NM_001180804.1.

3D structure databases

ProteinModelPortaliQ04373.
SMRiQ04373. Positions 73-508.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32547. 142 interactions.
DIPiDIP-6579N.
IntActiQ04373. 60 interactions.
MINTiMINT-637951.

PTM databases

iPTMnetiQ04373.

Proteomic databases

MaxQBiQ04373.
PeptideAtlasiQ04373.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR496C; YDR496C; YDR496C.
GeneIDi852107.
KEGGisce:YDR496C.

Organism-specific databases

EuPathDBiFungiDB:YDR496C.
SGDiS000002904. PUF6.

Phylogenomic databases

GeneTreeiENSGT00390000015757.
HOGENOMiHOG000246618.
InParanoidiQ04373.
KOiK14844.
OMAiKRGPIMK.
OrthoDBiEOG7NW6JR.

Enzyme and pathway databases

BioCyciYEAST:G3O-30019-MONOMER.

Miscellaneous databases

PROiQ04373.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR012959. CPL_dom.
IPR033133. PUM-HD.
IPR001313. Pumilio_RNA-bd_rpt.
[Graphical view]
PfamiPF08144. CPL. 1 hit.
[Graphical view]
SMARTiSM00025. Pumilio. 6 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50302. PUM. 5 hits.
PS50303. PUM_HD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [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. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  5. "A new yeast PUF family protein, Puf6p, represses ASH1 mRNA translation and is required for its localization."
    Gu W., Deng Y., Zenklusen D., Singer R.H.
    Genes Dev. 18:1452-1465(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, INTERACTION WITH SHE2, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  6. "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-34 AND SER-35, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  7. "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].
  8. "Translation of ASH1 mRNA is repressed by Puf6p-Fun12p/eIF5B interaction and released by CK2 phosphorylation."
    Deng Y., Singer R.H., Gu W.
    Genes Dev. 22:1037-1050(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Nonsense-mediated decay of ash1 nonsense transcripts in Saccharomyces cerevisiae."
    Zheng W., Finkel J.S., Landers S.M., Long R.M., Culbertson M.R.
    Genetics 180:1391-1405(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FUN12, PHOSPHORYLATION AT SER-31; SER-34 AND SER-35, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF SER-31; SER-34 AND SER-35.
  10. "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-34 AND SER-35, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Nuclear shuttling of She2p couples ASH1 mRNA localization to its translational repression by recruiting Loc1p and Puf6p."
    Shen Z., Paquin N., Forget A., Chartrand P.
    Mol. Biol. Cell 20:2265-2275(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SHE2.
  12. "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-34 AND SER-35, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPUF6_YEAST
AccessioniPrimary (citable) accession number: Q04373
Secondary accession number(s): D6VTB8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 21500 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, 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 IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: 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.