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O15212 (PFD6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prefoldin subunit 6
Alternative name(s):
Protein Ke2
Gene names
Name:PFDN6
Synonyms:HKE2, PFD6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length129 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3

Subunit structure

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

Sequence similarities

Belongs to the prefoldin subunit beta family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 129128Prefoldin subunit 6
PRO_0000124850

Amino acid modifications

Modified residue21N-acetylalanine Ref.6
Modified residue211N6-acetyllysine Ref.4
Modified residue661N6-acetyllysine Ref.4

Sequences

Sequence LengthMass (Da)Tools
O15212 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 8F138EAAE512A312

FASTA12914,583
        10         20         30         40         50         60 
MAELIQKKLQ GEVEKYQQLQ KDLSKSMSGR QKLEAQLTEN NIVKEELALL DGSNVVFKLL 

        70         80         90        100        110        120 
GPVLVKQELG EARATVGKRL DYITAEIKRY ESQLRDLERQ SEQQRETLAQ LQQEFQRAQA 


AKAGAPGKA 

« Hide

References

« Hide 'large scale' references
[1]"TAPASIN, DAXX, RGL2, HKE2 and four new genes (BING 1, 3 to 5) form a dense cluster at the centromeric end of the MHC."
Herberg J.A., Beck S., Trowsdale J.
J. Mol. Biol. 277:839-857(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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: Mammary gland and Pancreas.
[3]"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.
[4]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21 AND LYS-66, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[5]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[6]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z97184 Genomic DNA. Translation: CAB09993.1.
BC039033 mRNA. Translation: AAH39033.1.
BC059783 mRNA. Translation: AAH59783.1.
CCDSCCDS4773.1.
RefSeqNP_001172110.1. NM_001185181.2.
NP_001252524.1. NM_001265595.1.
NP_001252525.1. NM_001265596.1.
NP_055075.1. NM_014260.3.
UniGeneHs.446374.

3D structure databases

ProteinModelPortalO15212.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115734. 24 interactions.
IntActO15212. 12 interactions.
MINTMINT-1142550.
STRING9606.ENSP00000363734.

PTM databases

PhosphoSiteO15212.

Proteomic databases

MaxQBO15212.
PaxDbO15212.
PeptideAtlasO15212.
PRIDEO15212.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000374606; ENSP00000363734; ENSG00000204220.
ENST00000374607; ENSP00000363735; ENSG00000204220.
ENST00000374610; ENSP00000363738; ENSG00000204220.
ENST00000383207; ENSP00000372694; ENSG00000206283.
ENST00000395131; ENSP00000378563; ENSG00000204220.
ENST00000399383; ENSP00000382314; ENSG00000206283.
ENST00000399385; ENSP00000382316; ENSG00000206283.
ENST00000412289; ENSP00000402212; ENSG00000224782.
ENST00000425878; ENSP00000395462; ENSG00000224782.
ENST00000431830; ENSP00000402553; ENSG00000235692.
ENST00000432391; ENSP00000400152; ENSG00000235692.
ENST00000442285; ENSP00000404773; ENSG00000224782.
ENST00000445559; ENSP00000398171; ENSG00000237335.
ENST00000448594; ENSP00000403771; ENSG00000237335.
ENST00000451970; ENSP00000415678; ENSG00000235692.
ENST00000452658; ENSP00000412319; ENSG00000237335.
ENST00000547641; ENSP00000449925; ENSG00000235692.
ENST00000547952; ENSP00000448784; ENSG00000237335.
ENST00000548040; ENSP00000447540; ENSG00000206283.
ENST00000552711; ENSP00000448607; ENSG00000224782.
GeneID10471.
KEGGhsa:10471.
UCSCuc003odt.2. human.

Organism-specific databases

CTD10471.
GeneCardsGC06P033257.
GC06Pj33178.
GC06Pk33235.
GC06Pm33427.
GC06Pn33185.
HGNCHGNC:4926. PFDN6.
HPAHPA043032.
HPA048123.
MIM605660. gene.
neXtProtNX_O15212.
PharmGKBPA29304.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1382.
HOGENOMHOG000196242.
HOVERGENHBG000199.
InParanoidO15212.
KOK04798.
OMAYINGEIQ.
PhylomeDBO15212.
TreeFamTF315166.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressO15212.
BgeeO15212.
CleanExHS_PFDN6.
GenevestigatorO15212.

Family and domain databases

Gene3D1.10.287.370. 1 hit.
InterProIPR002777. PFD_beta-like.
IPR009053. Prefoldin.
[Graphical view]
PfamPF01920. Prefoldin_2. 1 hit.
[Graphical view]
SUPFAMSSF46579. SSF46579. 1 hit.
ProtoNetSearch...

Other

ChiTaRSPFDN6. human.
GeneWikiPrefoldin_subunit_6.
GenomeRNAi10471.
NextBio39710.
PROO15212.
SOURCESearch...

Entry information

Entry namePFD6_HUMAN
AccessionPrimary (citable) accession number: O15212
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM