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Protein

Protein PBP4

Gene

PBP4

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Enzyme and pathway databases

BioCyciYEAST:G3O-29470-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein PBP4
Alternative name(s):
PBP1-binding protein 4
Gene namesi
Name:PBP4
Ordered Locus Names:YDL053C
ORF Names:D2574
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome IV

Organism-specific databases

CYGDiYDL053c.
SGDiS000002211. PBP4.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 185185Protein PBP4PRO_0000262746Add
BLAST

Proteomic databases

MaxQBiQ07362.
PaxDbiQ07362.
PeptideAtlasiQ07362.

Expressioni

Gene expression databases

GenevestigatoriQ07362.

Interactioni

Subunit structurei

Interacts with IGO1, LSM12 and PBP1.3 Publications

Protein-protein interaction databases

BioGridi32006. 62 interactions.
DIPiDIP-5229N.
IntActiQ07362. 11 interactions.
MINTiMINT-536916.
STRINGi4932.YDL053C.

Structurei

3D structure databases

ProteinModelPortaliQ07362.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi56 – 627Poly-Gln

Phylogenomic databases

eggNOGiNOG87662.
InParanoidiQ07362.
OMAiKLTGWAQ.
OrthoDBiEOG75XGZJ.

Sequencei

Sequence statusi: Complete.

Q07362-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTTSTTSVD GRTSSTLKAT LSASGPNSNG PTPAVLPQKP KLTGWAQAAA
60 70 80 90 100
KALPRQQQQQ QQARKDDSVA VQPANTKTKT IASTAPPANI KGSSTANGSS
110 120 130 140 150
TNKKFKRANK QPYNREEVRS YMHKLFQSYT AGEKSHSMKT YKQVLSETAS
160 170 180
GRVSTATDWG TVSSSKNKNK KYGCLSDIAK VLRNQ
Length:185
Mass (Da):19,881
Last modified:October 31, 1996 - v1
Checksum:i516811BEF07EC37D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74101 Genomic DNA. Translation: CAA98615.1.
BK006938 Genomic DNA. Translation: DAA11803.1.
PIRiS67588.
RefSeqiNP_010230.1. NM_001180112.1.

Genome annotation databases

EnsemblFungiiYDL053C; YDL053C; YDL053C.
GeneIDi851507.
KEGGisce:YDL053C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z74101 Genomic DNA. Translation: CAA98615.1.
BK006938 Genomic DNA. Translation: DAA11803.1.
PIRiS67588.
RefSeqiNP_010230.1. NM_001180112.1.

3D structure databases

ProteinModelPortaliQ07362.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32006. 62 interactions.
DIPiDIP-5229N.
IntActiQ07362. 11 interactions.
MINTiMINT-536916.
STRINGi4932.YDL053C.

Proteomic databases

MaxQBiQ07362.
PaxDbiQ07362.
PeptideAtlasiQ07362.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL053C; YDL053C; YDL053C.
GeneIDi851507.
KEGGisce:YDL053C.

Organism-specific databases

CYGDiYDL053c.
SGDiS000002211. PBP4.

Phylogenomic databases

eggNOGiNOG87662.
InParanoidiQ07362.
OMAiKLTGWAQ.
OrthoDBiEOG75XGZJ.

Enzyme and pathway databases

BioCyciYEAST:G3O-29470-MONOMER.

Miscellaneous databases

NextBioi968863.

Gene expression databases

GenevestigatoriQ07362.

Family and domain databases

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(1996) [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. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PBP1.
  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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LSM12 AND PBP1, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IGO1.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPBP4_YEAST
AccessioniPrimary (citable) accession number: Q07362
Secondary accession number(s): D6VRU3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 27, 2006
Last sequence update: October 31, 1996
Last modified: February 3, 2015
This is version 79 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 1560 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

External Data

Dasty 3

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 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.