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Protein

Prefoldin subunit 4

Gene

PFDN4

Organism
Homo sapiens (Human)
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.1 Publication

GO - Molecular functioni

  • chaperone binding Source: UniProtKB

GO - Biological processi

  • 'de novo' posttranslational protein folding Source: Reactome
  • cellular protein metabolic process Source: Reactome
  • protein folding Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Enzyme and pathway databases

ReactomeiR-HSA-389957. Prefoldin mediated transfer of substrate to CCT/TriC.

Names & Taxonomyi

Protein namesi
Recommended name:
Prefoldin subunit 4
Alternative name(s):
Protein C-1
Gene namesi
Name:PFDN4
Synonyms:PFD4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:8868. PFDN4.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • nucleus Source: UniProtKB
  • prefoldin complex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33209.

Polymorphism and mutation databases

BioMutaiPFDN4.
DMDMi12643815.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 134133Prefoldin subunit 4PRO_0000124842Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei125 – 1251PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9NQP4.
MaxQBiQ9NQP4.
PaxDbiQ9NQP4.
PeptideAtlasiQ9NQP4.
PRIDEiQ9NQP4.
TopDownProteomicsiQ9NQP4.

PTM databases

iPTMnetiQ9NQP4.
PhosphoSiteiQ9NQP4.

Expressioni

Gene expression databases

BgeeiQ9NQP4.
CleanExiHS_PFDN4.
ExpressionAtlasiQ9NQP4. baseline and differential.
GenevisibleiQ9NQP4. HS.

Organism-specific databases

HPAiHPA024055.

Interactioni

Subunit structurei

Heterohexamer of two PFD-alpha type and four PFD-beta type subunits. Interacts with URI1; the interaction is phosphorylation-dependent and occurs in a growth-dependent manner.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
VBP1P617583EBI-357021,EBI-357430

GO - Molecular functioni

  • chaperone binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111225. 60 interactions.
IntActiQ9NQP4. 13 interactions.
MINTiMINT-1131938.
STRINGi9606.ENSP00000360473.

Structurei

3D structure databases

ProteinModelPortaliQ9NQP4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the prefoldin subunit beta family.Curated

Phylogenomic databases

eggNOGiKOG1760. Eukaryota.
COG1382. LUCA.
GeneTreeiENSGT00390000006696.
HOGENOMiHOG000204477.
HOVERGENiHBG005034.
InParanoidiQ9NQP4.
KOiK09550.
OrthoDBiEOG77M8QW.
PhylomeDBiQ9NQP4.
TreeFamiTF106491.

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.

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

Q9NQP4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAATMKKAAA EDVNVTFEDQ QKINKFARNT SRITELKEEI EVKKKQLQNL
60 70 80 90 100
EDACDDIMLA DDDCLMIPYQ IGDVFISHSQ EETQEMLEEA KKNLQEEIDA
110 120 130
LESRVESIQR VLADLKVQLY AKFGSNINLE ADES
Length:134
Mass (Da):15,314
Last modified:October 1, 2000 - v1
Checksum:iC727F0FCB9343DC3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41816 mRNA. Translation: AAB17063.1.
AL133335 Genomic DNA. Translation: CAI19316.1.
BC010953 mRNA. Translation: AAH10953.1.
CCDSiCCDS13445.1.
RefSeqiNP_002614.2. NM_002623.3.
UniGeneiHs.91161.

Genome annotation databases

EnsembliENST00000371419; ENSP00000360473; ENSG00000101132.
GeneIDi5203.
KEGGihsa:5203.
UCSCiuc002xwx.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41816 mRNA. Translation: AAB17063.1.
AL133335 Genomic DNA. Translation: CAI19316.1.
BC010953 mRNA. Translation: AAH10953.1.
CCDSiCCDS13445.1.
RefSeqiNP_002614.2. NM_002623.3.
UniGeneiHs.91161.

3D structure databases

ProteinModelPortaliQ9NQP4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111225. 60 interactions.
IntActiQ9NQP4. 13 interactions.
MINTiMINT-1131938.
STRINGi9606.ENSP00000360473.

PTM databases

iPTMnetiQ9NQP4.
PhosphoSiteiQ9NQP4.

Polymorphism and mutation databases

BioMutaiPFDN4.
DMDMi12643815.

Proteomic databases

EPDiQ9NQP4.
MaxQBiQ9NQP4.
PaxDbiQ9NQP4.
PeptideAtlasiQ9NQP4.
PRIDEiQ9NQP4.
TopDownProteomicsiQ9NQP4.

Protocols and materials databases

DNASUi5203.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371419; ENSP00000360473; ENSG00000101132.
GeneIDi5203.
KEGGihsa:5203.
UCSCiuc002xwx.4. human.

Organism-specific databases

CTDi5203.
GeneCardsiPFDN4.
HGNCiHGNC:8868. PFDN4.
HPAiHPA024055.
MIMi604898. gene.
neXtProtiNX_Q9NQP4.
PharmGKBiPA33209.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1760. Eukaryota.
COG1382. LUCA.
GeneTreeiENSGT00390000006696.
HOGENOMiHOG000204477.
HOVERGENiHBG005034.
InParanoidiQ9NQP4.
KOiK09550.
OrthoDBiEOG77M8QW.
PhylomeDBiQ9NQP4.
TreeFamiTF106491.

Enzyme and pathway databases

ReactomeiR-HSA-389957. Prefoldin mediated transfer of substrate to CCT/TriC.

Miscellaneous databases

ChiTaRSiPFDN4. human.
GeneWikiiPFDN4.
GenomeRNAii5203.
NextBioi20122.
PROiQ9NQP4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NQP4.
CleanExiHS_PFDN4.
ExpressionAtlasiQ9NQP4. baseline and differential.
GenevisibleiQ9NQP4. HS.

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. "Cloning of cDNA with possible transcription factor activity at the G1-S phase transition in human fibroblast cell lines."
    Iijima M., Kano Y., Nohno T., Namba M.
    Acta Med. Okayama 50:73-77(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  4. "Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin."
    Vainberg I.E., Lewis S.A., Rommelaere H., Ampe C., Vandekerckhove J., Klein H.L., Cowan N.J.
    Cell 93:863-873(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "S6K1-mediated disassembly of mitochondrial URI/PP1gamma complexes activates a negative feedback program that counters S6K1 survival signaling."
    Djouder N., Metzler S.C., Schmidt A., Wirbelauer C., Gstaiger M., Aebersold R., Hess D., Krek W.
    Mol. Cell 28:28-40(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH URI1, SUBCELLULAR LOCATION.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPFD4_HUMAN
AccessioniPrimary (citable) accession number: Q9NQP4
Secondary accession number(s): Q5TD11, Q92779
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: October 1, 2000
Last modified: May 11, 2016
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

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.