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Protein

Prefoldin subunit 4

Gene

GIM3

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

Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins.

GO - Molecular functioni

  1. tubulin binding Source: SGD

GO - Biological processi

  1. positive regulation of transcription elongation from RNA polymerase II promoter Source: SGD
  2. protein folding Source: InterPro
  3. tubulin complex assembly Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Enzyme and pathway databases

BioCyciYEAST:G3O-33170-MONOMER.
ReactomeiREACT_306488. Prefoldin mediated transfer of substrate to CCT/TriC.

Names & Taxonomyi

Protein namesi
Recommended name:
Prefoldin subunit 4
Alternative name(s):
Genes involved in microtubule biogenesis protein 3
Gim complex subunit 3
Short name:
GimC subunit 3
Gene namesi
Name:GIM3
Synonyms:PFD4
Ordered Locus Names:YNL153C
ORF Names:N1761
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311 Componenti: Chromosome XIV

Organism-specific databases

CYGDiYNL153c.
EuPathDBiFungiDB:YNL153C.
SGDiS000005097. GIM3.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: SGD
  2. prefoldin complex Source: SGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 129129Prefoldin subunit 4PRO_0000124848Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP53900.
PaxDbiP53900.

Expressioni

Gene expression databases

GenevestigatoriP53900.

Interactioni

Subunit structurei

Heterohexamer of two PFD-alpha type and four PFD-beta type subunits.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PAC10P483634EBI-13246,EBI-13239

Protein-protein interaction databases

BioGridi35676. 411 interactions.
DIPiDIP-3000N.
IntActiP53900. 11 interactions.
MINTiMINT-434964.
STRINGi4932.YNL153C.

Structurei

3D structure databases

ProteinModelPortaliP53900.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the prefoldin subunit beta family.Curated

Phylogenomic databases

eggNOGiCOG1382.
GeneTreeiENSGT00390000006696.
HOGENOMiHOG000204477.
InParanoidiP53900.
KOiK09550.
OMAiEDEKIQY.
OrthoDBiEOG735492.

Family and domain databases

Gene3Di1.10.287.370. 1 hit.
InterProiIPR002777. PFD_beta-like.
IPR016661. PFDN4.
IPR009053. Prefoldin.
[Graphical view]
PANTHERiPTHR21100:SF9. PTHR21100:SF9. 1 hit.
PfamiPF01920. Prefoldin_2. 1 hit.
[Graphical view]
PIRSFiPIRSF016477. Prefoldin_subunit_4. 1 hit.
SUPFAMiSSF46579. SSF46579. 1 hit.

Sequencei

Sequence statusi: Complete.

P53900-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELLPQGQRN NTQVTFEDQQ KINEFSKLIM RKDAIAQELS LQREEKEYLD
60 70 80 90 100
DVSLEIELID EDEPVQYKVG DLFIFMKQSK VTAQLEKDAE RLDNKIETLE
110 120
DKQRDIDSRL DALKAILYAK FGDNINLER
Length:129
Mass (Da):15,180
Last modified:October 1, 1996 - v1
Checksum:i4738F9EA813E04A9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92517 Genomic DNA. Translation: CAA63286.1.
Z71429 Genomic DNA. Translation: CAA96040.1.
AY692812 Genomic DNA. Translation: AAT92831.1.
BK006947 Genomic DNA. Translation: DAA10396.1.
PIRiS60974.
RefSeqiNP_014246.1. NM_001182991.1.

Genome annotation databases

EnsemblFungiiYNL153C; YNL153C; YNL153C.
GeneIDi855569.
KEGGisce:YNL153C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92517 Genomic DNA. Translation: CAA63286.1.
Z71429 Genomic DNA. Translation: CAA96040.1.
AY692812 Genomic DNA. Translation: AAT92831.1.
BK006947 Genomic DNA. Translation: DAA10396.1.
PIRiS60974.
RefSeqiNP_014246.1. NM_001182991.1.

3D structure databases

ProteinModelPortaliP53900.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi35676. 411 interactions.
DIPiDIP-3000N.
IntActiP53900. 11 interactions.
MINTiMINT-434964.
STRINGi4932.YNL153C.

Proteomic databases

MaxQBiP53900.
PaxDbiP53900.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYNL153C; YNL153C; YNL153C.
GeneIDi855569.
KEGGisce:YNL153C.

Organism-specific databases

CYGDiYNL153c.
EuPathDBiFungiDB:YNL153C.
SGDiS000005097. GIM3.

Phylogenomic databases

eggNOGiCOG1382.
GeneTreeiENSGT00390000006696.
HOGENOMiHOG000204477.
InParanoidiP53900.
KOiK09550.
OMAiEDEKIQY.
OrthoDBiEOG735492.

Enzyme and pathway databases

BioCyciYEAST:G3O-33170-MONOMER.
ReactomeiREACT_306488. Prefoldin mediated transfer of substrate to CCT/TriC.

Miscellaneous databases

NextBioi979679.
PROiP53900.

Gene expression databases

GenevestigatoriP53900.

Family and domain databases

Gene3Di1.10.287.370. 1 hit.
InterProiIPR002777. PFD_beta-like.
IPR016661. PFDN4.
IPR009053. Prefoldin.
[Graphical view]
PANTHERiPTHR21100:SF9. PTHR21100:SF9. 1 hit.
PfamiPF01920. Prefoldin_2. 1 hit.
[Graphical view]
PIRSFiPIRSF016477. Prefoldin_subunit_4. 1 hit.
SUPFAMiSSF46579. SSF46579. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The sequence of 36.8 kb from the left arm of chromosome XIV reveals 24 complete open reading frames: 18 correspond to new genes, one of which encodes a protein similar to the human myotonic dystrophy kinase."
    Nasr F., Becam A.-M., Herbert C.J.
    Yeast 12:169-175(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  2. "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.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. "A novel protein complex promoting formation of functional alpha- and gamma-tubulin."
    Geissler S., Siegers K., Schiebel E.
    EMBO J. 17:952-966(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. "Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system."
    Siegers K., Waldmann T., Leroux M.R., Grein K., Shevchenko A., Schiebel E., Hartl F.U.
    EMBO J. 18:75-84(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE PREFOLDIN COMPLEX.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPFD4_YEAST
AccessioniPrimary (citable) accession number: P53900
Secondary accession number(s): D6W130
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 29, 2015
This is version 111 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 7470 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 XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: 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.