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P53297

- PBP1_YEAST

UniProt

P53297 - PBP1_YEAST

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Protein
PAB1-binding protein 1
Gene
PBP1, MRS16, YGR178C
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Appears to promote proper polyadenylation. In the absence of PBP1, the 3'termini of pre-mRNAs are properly cleaved but lack full-length poly(A) tails. May act to repress the ability of PAB1 to negatively regulate polyadenylation. Negative regulator of poly(A) nuclease (PAN) activity.2 Publications

GO - Molecular functioni

  1. protein binding Source: IntAct

GO - Biological processi

  1. mRNA polyadenylation Source: SGD
  2. positive regulation of translation Source: SGD
  3. stress granule assembly Source: SGD
Complete GO annotation...

Enzyme and pathway databases

BioCyciYEAST:G3O-30871-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
PAB1-binding protein 1
Gene namesi
Name:PBP1
Synonyms:MRS16
Ordered Locus Names:YGR178C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome VII

Organism-specific databases

CYGDiYGR178c.
SGDiS000003410. PBP1.

Subcellular locationi

Cytoplasm. Nucleus. Mitochondrion 2 Publications

GO - Cellular componenti

  1. cytoplasmic stress granule Source: SGD
  2. mitochondrion Source: UniProtKB-SubCell
  3. nucleus Source: UniProtKB-SubCell
  4. polysome Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 722722PAB1-binding protein 1
PRO_0000058244Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei106 – 1061Phosphoserine3 Publications
Modified residuei193 – 1931Phosphothreonine1 Publication
Modified residuei215 – 2151Phosphoserine1 Publication
Modified residuei436 – 4361Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53297.
PaxDbiP53297.
PeptideAtlasiP53297.

Expressioni

Gene expression databases

GenevestigatoriP53297.

Interactioni

Subunit structurei

Interacts with FIR1, IGO1, LSM12, PBP4 and PAB1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
LSM12P388286EBI-12961,EBI-24700

Protein-protein interaction databases

BioGridi33430. 126 interactions.
DIPiDIP-2464N.
IntActiP53297. 23 interactions.
MINTiMINT-488669.
STRINGi4932.YGR178C.

Structurei

3D structure databases

ProteinModelPortaliP53297.

Family & Domainsi

Sequence similaritiesi

Belongs to the ataxin-2 family.

Phylogenomic databases

eggNOGiCOG5180.
GeneTreeiENSGT00530000063565.
HOGENOMiHOG000093792.
OMAiIEKPYFT.
OrthoDBiEOG7TF7K9.

Family and domain databases

InterProiIPR009604. LsmAD_domain.
IPR025852. SM_dom_ATX.
[Graphical view]
PfamiPF06741. LsmAD. 1 hit.
PF14438. SM-ATX. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P53297-1 [UniParc]FASTAAdd to Basket

« Hide

MKGNFRKRDS STNSRKGGNS DSNYTNGGVP NQNNSSMFYE NPEITRNFDD    50
RQDYLLANSI GSDVTVTVTS GVKYTGLLVS CNLESTNGID VVLRFPRVAD 100
SGVSDSVDDL AKTLGETLLI HGEDVAELEL KNIDLSLDEK WENSKAQETT 150
PARTNIEKER VNGESNEVTK FRTDVDISGS GREIKERKLE KWTPEEGAEH 200
FDINKGKALE DDSASWDQFA VNEKKFGVKS TFDEHLYTTK INKDDPNYSK 250
RLQEAERIAK EIESQGTSGN IHIAEDRGII IDDSGLDEED LYSGVDRRGD 300
ELLAALKSNS KPNSNKGNRY VPPTLRQQPH HMDPAIISSS NSNKNENAVS 350
TDTSTPAAAG APEGKPPQKT SKNKKSLSSK EAQIEELKKF SEKFKVPYDI 400
PKDMLEVLKR SSSTLKSNSS LPPKPISKTP SAKTVSPTTQ ISAGKSESRR 450
SGSNISQGQS STGHTTRSST SLRRRNHGSF FGAKNPHTND AKRVLFGKSF 500
NMFIKSKEAH DEKKKGDDAS ENMEPFFIEK PYFTAPTWLN TIEESYKTFF 550
PDEDTAIQEA QTRFQQRQLN SMGNAVPGMN PAMGMNMGGM MGFPMGGPSA 600
SPNPMMNGFA AGSMGMYMPF QPQPMFYHPS MPQMMPVMGS NGAEEGGGNI 650
SPHVPAGFMA AGPGAPMGAF GYPGGIPFQG MMGSGPSGMP ANGSAMHSHG 700
HSRNYHQTSH HGHHNSSTSG HK 722
Length:722
Mass (Da):78,781
Last modified:October 1, 1996 - v1
Checksum:i92005F3A2346193E
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U46931 Genomic DNA. Translation: AAB94294.1.
Z72963 Genomic DNA. Translation: CAA97204.1.
BK006941 Genomic DNA. Translation: DAA08273.1.
PIRiS64492.
RefSeqiNP_011694.3. NM_001181307.3.

Genome annotation databases

EnsemblFungiiYGR178C; YGR178C; YGR178C.
GeneIDi853089.
KEGGisce:YGR178C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U46931 Genomic DNA. Translation: AAB94294.1 .
Z72963 Genomic DNA. Translation: CAA97204.1 .
BK006941 Genomic DNA. Translation: DAA08273.1 .
PIRi S64492.
RefSeqi NP_011694.3. NM_001181307.3.

3D structure databases

ProteinModelPortali P53297.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33430. 126 interactions.
DIPi DIP-2464N.
IntActi P53297. 23 interactions.
MINTi MINT-488669.
STRINGi 4932.YGR178C.

Proteomic databases

MaxQBi P53297.
PaxDbi P53297.
PeptideAtlasi P53297.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YGR178C ; YGR178C ; YGR178C .
GeneIDi 853089.
KEGGi sce:YGR178C.

Organism-specific databases

CYGDi YGR178c.
SGDi S000003410. PBP1.

Phylogenomic databases

eggNOGi COG5180.
GeneTreei ENSGT00530000063565.
HOGENOMi HOG000093792.
OMAi IEKPYFT.
OrthoDBi EOG7TF7K9.

Enzyme and pathway databases

BioCyci YEAST:G3O-30871-MONOMER.

Miscellaneous databases

NextBioi 973070.

Gene expression databases

Genevestigatori P53297.

Family and domain databases

InterProi IPR009604. LsmAD_domain.
IPR025852. SM_dom_ATX.
[Graphical view ]
Pfami PF06741. LsmAD. 1 hit.
PF14438. SM-ATX. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequencing and characterization of a suppressor of the pet- phenotype in a Saccharomyces cerevisiae strain without mitochondrial group II introns."
    Mecklenbrauker I.
    Thesis (1996), Vienna Biocentre, Austria
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 44774 / DBY747.
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "Pbp1p, a factor interacting with Saccharomyces cerevisiae poly(A)-binding protein, regulates polyadenylation."
    Mangus D.A., Amrani N., Jacobson A.
    Mol. Cell. Biol. 18:7383-7396(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PAB1.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. "Systematic identification and functional screens of uncharacterized proteins associated with eukaryotic ribosomal complexes."
    Fleischer T.C., Weaver C.M., McAfee K.J., Jennings J.L., Link A.J.
    Genes Dev. 20:1294-1307(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LSM12 AND PBP4, IDENTIFICATION BY MASS SPECTROMETRY.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Strain: ATCC 76625 / YPH499.
  9. "Identification of factors regulating poly(A) tail synthesis and maturation."
    Mangus D.A., Smith M.M., McSweeney J.M., Jacobson A.
    Mol. Cell. Biol. 24:4196-4206(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH FIR1 AND PBP4.
  10. "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-106 AND SER-436, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  11. "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-106; SER-215 AND SER-436, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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-106 AND THR-193, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Initiation of the TORC1-regulated G0 program requires Igo1/2, which license specific mRNAs to evade degradation via the 5'-3' mRNA decay pathway."
    Talarek N., Cameroni E., Jaquenoud M., Luo X., Bontron S., Lippman S., Devgan G., Snyder M., Broach J.R., De Virgilio C.
    Mol. Cell 38:345-355(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IGO1.
  14. "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 nameiPBP1_YEAST
AccessioniPrimary (citable) accession number: P53297
Secondary accession number(s): D6VUW2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 11, 2014
This is version 118 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 2870 molecules/cell in log phase SD medium.

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

External Data

Dasty 3

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