pfdn6 prefoldin subunit 6 [Danio rerio (zebrafish)] - Gene

Summary

Official Symbol: pfdn6provided by ZNC
Official Full Name: prefoldin subunit 6provided by ZNC
Primary source: ZFIN:ZDB-GENE-040426-1589
See related: Ensembl:ENSDARG00000037108 AllianceGenome:ZFIN:ZDB-GENE-040426-1589
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Danio rerio
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; Danionidae; Danioninae; Danio
Also known as: zgc:66282
Summary: Predicted to enable protein-folding chaperone binding activity. Predicted to be involved in chaperone-mediated protein complex assembly and protein folding. Predicted to be part of prefoldin complex. Predicted to be active in cytoplasm. Orthologous to human PFDN6 (prefoldin subunit 6). [provided by Alliance of Genome Resources, Dec 2024]
Orthologs: human mouse all
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Location:: chromosome: 14

Exon count:: 4

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCz11 (GCF_000002035.6)	14	NC_007125.7 (30551321..30557021, complement)
105	previous assembly	GRCz10 (GCF_000002035.5)	14	NC_007125.6 (30211007..30216707, complement)

Chromosome 14 - NC_007125.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Expression

Go to the top of the page Help

See details

Project title: Sequencing the Zebrafish transcriptome from a range of tissues and developmental stages
Description: Sequencing the Zebrafish transcriptome from a range of tissues and developmental stages
BioProject: PRJEB1986
Analysis date: Fri Dec 8 19:48:10 2017

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Submit: New GeneRIF Correction

General gene information

Go to the top of the page Help

Gene Ontology Provided by ZFIN

Function	Evidence Code	Pubs
enables protein-folding chaperone binding	IBA Inferred from Biological aspect of Ancestor more info
enables unfolded protein binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in chaperone-mediated protein complex assembly	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within protein folding	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
part_of prefoldin complex	IBA Inferred from Biological aspect of Ancestor more info
part_of prefoldin complex	IEA Inferred from Electronic Annotation more info

General protein information

Go to the top of the page Help

Preferred Names: prefoldin subunit 6

NCBI Reference Sequences (RefSeq)

Go to the top of the page Help

NEW Try the new Transcript table

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_200513.1 → NP_956807.1 prefoldin subunit 6

See identical proteins and their annotated locations for NP_956807.1

Status: PROVISIONAL

Source sequence(s)

BC055580

UniProtKB/TrEMBL

B2GQZ7, F6NH43, Q7SX94

Related

ENSDARP00000053935.5, ENSDART00000053936.7

Conserved Domains (1) summary

cd00632
Location:9 → 113

Prefoldin_beta; Prefoldin beta; Prefoldin is a hexameric molecular chaperone complex, composed of two evolutionarily related subunits (alpha and beta), which are found in both eukaryotes and archaea. Prefoldin binds and stabilizes newly synthesized polypeptides ...