Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Nuclear and cytoplasmic polyadenylated RNA-binding protein PUB1

Gene

PUB1

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

May be associated with hnRNA within the nucleus and remains associated during nucleocytoplasmic mRNA transport, once the proteins are in the cytoplasm, disassembly of PUB1-RNA complexes may occur prior to PAB1 binding and formation of a translationally competent RNP complex. Binds to polyadenylated RNA; prefers to bind poly(rU); binds to T-rich single-stranded DNA.

GO - Molecular functioni

  • mRNA binding Source: SGD
  • nucleotide binding Source: InterPro
  • poly(U) RNA binding Source: SGD

GO - Biological processi

  • nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: SGD
  • regulation of mRNA stability Source: SGD
  • stress granule assembly Source: SGD
Complete GO annotation...

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-33055-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear and cytoplasmic polyadenylated RNA-binding protein PUB1
Alternative name(s):
ARS consensus-binding protein ACBP-60
Poly uridylate-binding protein
Short name:
Poly(U)-binding protein
Gene namesi
Name:PUB1
Synonyms:RNP1
Ordered Locus Names:YNL016W
ORF Names:N2842
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XIV

Organism-specific databases

EuPathDBiFungiDB:YNL016W.
SGDiS000004961. PUB1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • cytoplasmic mRNA processing body Source: SGD
  • cytoplasmic stress granule Source: SGD
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 453452Nuclear and cytoplasmic polyadenylated RNA-binding protein PUB1PRO_0000081745Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP32588.
PeptideAtlasiP32588.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
SGN1P405613EBI-14231,EBI-25362
TIF4632P399363EBI-14231,EBI-9006

Protein-protein interaction databases

BioGridi35810. 122 interactions.
DIPiDIP-5480N.
IntActiP32588. 45 interactions.
MINTiMINT-499485.

Structurei

Secondary structure

1
453
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi76 – 838Combined sources
Helixi88 – 958Combined sources
Helixi96 – 983Combined sources
Beta strandi101 – 1077Combined sources
Beta strandi115 – 12410Combined sources
Helixi125 – 13511Combined sources
Beta strandi146 – 1494Combined sources
Beta strandi162 – 1676Combined sources
Helixi175 – 1828Combined sources
Beta strandi188 – 1958Combined sources
Turni197 – 1993Combined sources
Beta strandi202 – 21110Combined sources
Helixi213 – 22311Combined sources
Beta strandi234 – 2374Combined sources
Beta strandi322 – 3243Combined sources
Helixi326 – 3338Combined sources
Beta strandi342 – 3476Combined sources
Helixi354 – 3629Combined sources
Beta strandi368 – 3736Combined sources
Turni374 – 3774Combined sources
Beta strandi378 – 3825Combined sources
Helixi386 – 39611Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LA4NMR-A315-414[»]
3MD1X-ray1.60A/B161-240[»]
3MD3X-ray2.70A75-240[»]
ProteinModelPortaliP32588.
SMRiP32588. Positions 75-271, 315-414.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP32588.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini75 – 15278RRM 1PROSITE-ProRule annotationAdd
BLAST
Domaini162 – 24079RRM 2PROSITE-ProRule annotationAdd
BLAST
Domaini341 – 41373RRM 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni260 – 2645RNA-binding RGG-boxBy similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi8 – 169Gln-rich
Compositional biasi243 – 28846Asn-richAdd
BLAST
Compositional biasi442 – 45312Gln-richAdd
BLAST

Sequence similaritiesi

Contains 3 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00840000129750.
HOGENOMiHOG000206748.
InParanoidiP32588.
KOiK13201.
OMAiCGWGKER.
OrthoDBiEOG706125.

Family and domain databases

Gene3Di3.30.70.330. 3 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR003954. RRM_dom_euk.
[Graphical view]
PfamiPF00076. RRM_1. 3 hits.
[Graphical view]
SMARTiSM00360. RRM. 3 hits.
SM00361. RRM_1. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 2 hits.
PROSITEiPS50102. RRM. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P32588-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSENNEEQHQ QQQQQQPVAV ETPSAVEAPA SADPSSEQSV AVEGNSEQAE
60 70 80 90 100
DNQGENDPSV VPANAITGGR ETSDRVLYVG NLDKAITEDI LKQYFQVGGP
110 120 130 140 150
IANIKIMIDK NNKNVNYAFV EYHQSHDANI ALQTLNGKQI ENNIVKINWA
160 170 180 190 200
FQSQQSSSDD TFNLFVGDLN VNVDDETLRN AFKDFPSYLS GHVMWDMQTG
210 220 230 240 250
SSRGYGFVSF TSQDDAQNAM DSMQGQDLNG RPLRINWAAK RDNNNNNNYQ
260 270 280 290 300
QRRNYGNNNR GGFRQYNSNN NNNMNMGMNM NMNMNMNNSR GMPPSSMGMP
310 320 330 340 350
IGAMPLPSQG QPQQSQTIGL PPQVNPQAVD HIIRSAPPRV TTAYIGNIPH
360 370 380 390 400
FATEADLIPL FQNFGFILDF KHYPEKGCCF IKYDTHEQAA VCIVALANFP
410 420 430 440 450
FQGRNLRTGW GKERSNFMPQ QQQQGGQPLI MNDQQQPVMS EQQQQQQQQQ

QQQ
Length:453
Mass (Da):50,763
Last modified:October 5, 2010 - v4
Checksum:i3B81A7735505D3CA
GO

Sequence cautioni

The sequence AAA02808.1 differs from that shown. Reason: Frameshift at positions 428 and 450. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti268 – 2681S → N in AAC37348 (PubMed:8413212).Curated
Sequence conflicti268 – 2681S → N in AAC37364 (PubMed:8413213).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13725 Unassigned DNA. Translation: AAC37348.1.
L20767 Unassigned DNA. Translation: AAC37364.1.
L01797 Unassigned DNA. Translation: AAA02808.1. Frameshift.
Z71292 Genomic DNA. Translation: CAA95877.1.
BK006947 Genomic DNA. Translation: DAA10528.1.
PIRiS62928.
RefSeqiNP_014382.1. NM_001182855.1.

Genome annotation databases

EnsemblFungiiYNL016W; YNL016W; YNL016W.
GeneIDi855716.
KEGGisce:YNL016W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L13725 Unassigned DNA. Translation: AAC37348.1.
L20767 Unassigned DNA. Translation: AAC37364.1.
L01797 Unassigned DNA. Translation: AAA02808.1. Frameshift.
Z71292 Genomic DNA. Translation: CAA95877.1.
BK006947 Genomic DNA. Translation: DAA10528.1.
PIRiS62928.
RefSeqiNP_014382.1. NM_001182855.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LA4NMR-A315-414[»]
3MD1X-ray1.60A/B161-240[»]
3MD3X-ray2.70A75-240[»]
ProteinModelPortaliP32588.
SMRiP32588. Positions 75-271, 315-414.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35810. 122 interactions.
DIPiDIP-5480N.
IntActiP32588. 45 interactions.
MINTiMINT-499485.

Proteomic databases

MaxQBiP32588.
PeptideAtlasiP32588.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL016W; YNL016W; YNL016W.
GeneIDi855716.
KEGGisce:YNL016W.

Organism-specific databases

EuPathDBiFungiDB:YNL016W.
SGDiS000004961. PUB1.

Phylogenomic databases

GeneTreeiENSGT00840000129750.
HOGENOMiHOG000206748.
InParanoidiP32588.
KOiK13201.
OMAiCGWGKER.
OrthoDBiEOG706125.

Enzyme and pathway databases

BioCyciYEAST:G3O-33055-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP32588.
NextBioi980072.
PROiP32588.

Family and domain databases

Gene3Di3.30.70.330. 3 hits.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR003954. RRM_dom_euk.
[Graphical view]
PfamiPF00076. RRM_1. 3 hits.
[Graphical view]
SMARTiSM00360. RRM. 3 hits.
SM00361. RRM_1. 2 hits.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 2 hits.
PROSITEiPS50102. RRM. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "PUB1 is a major nuclear and cytoplasmic polyadenylated RNA-binding protein in Saccharomyces cerevisiae."
    Anderson J.T., Paddy M.R., Swanson M.S.
    Mol. Cell. Biol. 13:6102-6113(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "PUB1: a major yeast poly(A)+ RNA-binding protein."
    Matunis M.J., Matunis E.L., Dreyfuss G.
    Mol. Cell. Biol. 13:6114-6123(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  3. "A protein containing conserved RNA-recognition motifs is associated with ribosomal subunits in Saccharomyces cerevisiae."
    Ripmaster T.L., Woolford J.L. Jr.
    Nucleic Acids Res. 21:3211-3216(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications."
    Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K., Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K., Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M., Beinhauer J.D., Boskovic J., Buitrago M.J.
    , Bussereau F., Coster F., Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F., Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C., Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A., Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H., Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L., Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R., Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D., Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A., Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C., Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F., Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G., Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M., Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.
    Nature 387:93-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  6. "The yeast protein encoded by PUB1 binds T-rich single stranded DNA."
    Cockell M., Frutiger S., Hughes G.J., Gasser S.M.
    Nucleic Acids Res. 22:32-40(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, PARTIAL PROTEIN SEQUENCE.
  7. "Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins."
    Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I., Kobayashi R., Schwender B., Volpe T., Anderson D.S., Mesquita-Fuentes R., Payne W.E.
    Electrophoresis 18:1347-1360(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT SER-2.
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPUB1_YEAST
AccessioniPrimary (citable) accession number: P32588
Secondary accession number(s): D6W1G2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 5, 2010
Last modified: May 11, 2016
This is version 150 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 49600 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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