ID PFD6_HUMAN Reviewed; 129 AA. AC O15212; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 24-JAN-2024, entry version 183. DE RecName: Full=Prefoldin subunit 6; DE AltName: Full=Protein Ke2; GN Name=PFDN6; Synonyms=HKE2, PFD6; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9545376; DOI=10.1006/jmbi.1998.1637; RA Herberg J.A., Beck S., Trowsdale J.; RT "TAPASIN, DAXX, RGL2, HKE2 and four new genes (BING 1, 3 to 5) form a dense RT cluster at the centromeric end of the MHC."; RL J. Mol. Biol. 277:839-857(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary gland, and Pancreas; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP FUNCTION. RX PubMed=9630229; DOI=10.1016/s0092-8674(00)81446-4; RA Vainberg I.E., Lewis S.A., Rommelaere H., Ampe C., Vandekerckhove J., RA Klein H.L., Cowan N.J.; RT "Prefoldin, a chaperone that delivers unfolded proteins to cytosolic RT chaperonin."; RL Cell 93:863-873(1998). RN [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21 AND LYS-66, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [7] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-66, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; DOI=10.1073/pnas.1413825111; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [8] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-66, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [9] RP IDENTIFICATION IN THE PAQOSOME COMPLEX. RX PubMed=31738558; DOI=10.1021/acs.jproteome.9b00599; RA Cloutier P., Poitras C., Faubert D., Bouchard A., Blanchette M., RA Gauthier M.S., Coulombe B.; RT "Upstream ORF-Encoded ASDURF Is a Novel Prefoldin-like Subunit of the RT PAQosome."; RL J. Proteome Res. 19:18-27(2020). CC -!- FUNCTION: Binds specifically to cytosolic chaperonin (c-CPN) and CC transfers target proteins to it. Binds to nascent polypeptide chain and CC promotes folding in an environment in which there are many competing CC pathways for nonnative proteins. {ECO:0000269|PubMed:9630229}. CC -!- SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta type CC subunits (By similarity). Component of the PAQosome complex which is CC responsible for the biogenesis of several protein complexes and which CC consists of R2TP complex members RUVBL1, RUVBL2, RPAP3 and PIH1D1, URI CC complex members PFDN2, PFDN6, PDRG1, UXT and URI1 as well as ASDURF, CC POLR2E and DNAAF10/WDR92 (PubMed:31738558). CC {ECO:0000250|UniProtKB:P52553, ECO:0000269|PubMed:31738558}. CC -!- INTERACTION: CC O15212; Q13155: AIMP2; NbExp=3; IntAct=EBI-356973, EBI-745226; CC O15212; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-356973, EBI-10175300; CC O15212; P53567: CEBPG; NbExp=3; IntAct=EBI-356973, EBI-740209; CC O15212; Q9UK22: FBXO2; NbExp=3; IntAct=EBI-356973, EBI-4287196; CC O15212; P22607: FGFR3; NbExp=3; IntAct=EBI-356973, EBI-348399; CC O15212; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-356973, EBI-2556193; CC O15212; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-356973, EBI-14069005; CC O15212; O15481: MAGEB4; NbExp=3; IntAct=EBI-356973, EBI-751857; CC O15212; O95983-2: MBD3; NbExp=3; IntAct=EBI-356973, EBI-11978579; CC O15212; Q9NQG5: RPRD1B; NbExp=3; IntAct=EBI-356973, EBI-747925; CC -!- SIMILARITY: Belongs to the prefoldin subunit beta family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; Z97184; CAB09993.1; -; Genomic_DNA. DR EMBL; BC039033; AAH39033.1; -; mRNA. DR EMBL; BC059783; AAH59783.1; -; mRNA. DR CCDS; CCDS4773.1; -. DR RefSeq; NP_001172110.1; NM_001185181.2. DR RefSeq; NP_001252524.1; NM_001265595.1. DR RefSeq; NP_001252525.1; NM_001265596.1. DR RefSeq; NP_055075.1; NM_014260.3. DR PDB; 6NR8; EM; 7.80 A; 6=13-114. DR PDB; 6NR9; EM; 8.50 A; 6=13-114. DR PDB; 6NRB; EM; 8.70 A; 6=13-114. DR PDB; 6NRC; EM; 8.30 A; 6=13-114. DR PDB; 6NRD; EM; 8.20 A; 6=13-114. DR PDB; 7WU7; EM; 3.85 A; 6=1-129. DR PDBsum; 6NR8; -. DR PDBsum; 6NR9; -. DR PDBsum; 6NRB; -. DR PDBsum; 6NRC; -. DR PDBsum; 6NRD; -. DR PDBsum; 7WU7; -. DR AlphaFoldDB; O15212; -. DR EMDB; EMD-0490; -. DR EMDB; EMD-0491; -. DR EMDB; EMD-0493; -. DR EMDB; EMD-0494; -. DR EMDB; EMD-0495; -. DR EMDB; EMD-32823; -. DR SMR; O15212; -. DR BioGRID; 115734; 153. DR ComplexPortal; CPX-6144; URI1 prefoldin co-chaperone complex. DR ComplexPortal; CPX-6149; Prefoldin co-chaperone complex. DR CORUM; O15212; -. DR DIP; DIP-50304N; -. DR IntAct; O15212; 64. DR MINT; O15212; -. DR STRING; 9606.ENSP00000378563; -. DR GlyGen; O15212; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O15212; -. DR PhosphoSitePlus; O15212; -. DR BioMuta; PFDN6; -. DR EPD; O15212; -. DR jPOST; O15212; -. DR MassIVE; O15212; -. DR PaxDb; 9606-ENSP00000378563; -. DR PeptideAtlas; O15212; -. DR ProteomicsDB; 48512; -. DR Pumba; O15212; -. DR TopDownProteomics; O15212; -. DR Antibodypedia; 29059; 141 antibodies from 24 providers. DR DNASU; 10471; -. DR Ensembl; ENST00000374606.10; ENSP00000363734.5; ENSG00000204220.12. DR Ensembl; ENST00000374607.5; ENSP00000363735.1; ENSG00000204220.12. DR Ensembl; ENST00000374610.6; ENSP00000363738.2; ENSG00000204220.12. DR Ensembl; ENST00000383207.6; ENSP00000372694.2; ENSG00000206283.10. DR Ensembl; ENST00000395131.5; ENSP00000378563.1; ENSG00000204220.12. DR Ensembl; ENST00000399383.7; ENSP00000382314.3; ENSG00000206283.10. DR Ensembl; ENST00000399385.5; ENSP00000382316.1; ENSG00000206283.10. DR Ensembl; ENST00000412289.5; ENSP00000402212.1; ENSG00000224782.8. DR Ensembl; ENST00000425878.6; ENSP00000395462.2; ENSG00000224782.8. DR Ensembl; ENST00000431830.5; ENSP00000402553.1; ENSG00000235692.8. DR Ensembl; ENST00000432391.6; ENSP00000400152.2; ENSG00000235692.8. DR Ensembl; ENST00000442285.5; ENSP00000404773.1; ENSG00000224782.8. DR Ensembl; ENST00000445559.5; ENSP00000398171.1; ENSG00000237335.8. DR Ensembl; ENST00000448594.5; ENSP00000403771.1; ENSG00000237335.8. DR Ensembl; ENST00000451970.5; ENSP00000415678.1; ENSG00000235692.8. DR Ensembl; ENST00000452658.6; ENSP00000412319.2; ENSG00000237335.8. DR Ensembl; ENST00000547641.2; ENSP00000449925.1; ENSG00000235692.8. DR Ensembl; ENST00000547952.2; ENSP00000448784.1; ENSG00000237335.8. DR Ensembl; ENST00000548040.2; ENSP00000447540.1; ENSG00000206283.10. DR Ensembl; ENST00000552711.2; ENSP00000448607.1; ENSG00000224782.8. DR GeneID; 10471; -. DR KEGG; hsa:10471; -. DR MANE-Select; ENST00000374606.10; ENSP00000363734.5; NM_001185181.3; NP_001172110.1. DR AGR; HGNC:4926; -. DR CTD; 10471; -. DR DisGeNET; 10471; -. DR GeneCards; PFDN6; -. DR HGNC; HGNC:4926; PFDN6. DR HPA; ENSG00000204220; Low tissue specificity. DR MIM; 605660; gene. DR neXtProt; NX_O15212; -. DR OpenTargets; ENSG00000204220; -. DR PharmGKB; PA29304; -. DR VEuPathDB; HostDB:ENSG00000204220; -. DR eggNOG; KOG3478; Eukaryota. DR GeneTree; ENSGT00390000010512; -. DR HOGENOM; CLU_125172_0_1_1; -. DR InParanoid; O15212; -. DR OMA; VQTEFAQ; -. DR OrthoDB; 125360at2759; -. DR PhylomeDB; O15212; -. DR TreeFam; TF315166; -. DR PathwayCommons; O15212; -. DR Reactome; R-HSA-389957; Prefoldin mediated transfer of substrate to CCT/TriC. DR SignaLink; O15212; -. DR SIGNOR; O15212; -. DR BioGRID-ORCS; 10471; 762 hits in 1165 CRISPR screens. DR ChiTaRS; PFDN6; human. DR GeneWiki; Prefoldin_subunit_6; -. DR GenomeRNAi; 10471; -. DR Pharos; O15212; Tbio. DR PRO; PR:O15212; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; O15212; Protein. DR Bgee; ENSG00000204220; Expressed in left testis and 97 other cell types or tissues. DR ExpressionAtlas; O15212; baseline and differential. DR Genevisible; O15212; HS. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0016272; C:prefoldin complex; IDA:UniProtKB. DR GO; GO:0101031; C:protein folding chaperone complex; NAS:ComplexPortal. DR GO; GO:1990062; C:RPAP3/R2TP/prefoldin-like complex; IPI:ComplexPortal. DR GO; GO:0001540; F:amyloid-beta binding; IDA:FlyBase. DR GO; GO:0051087; F:protein-folding chaperone binding; IDA:UniProtKB. DR GO; GO:0051082; F:unfolded protein binding; IDA:FlyBase. DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IDA:UniProtKB. DR GO; GO:0061077; P:chaperone-mediated protein folding; NAS:ComplexPortal. DR GO; GO:1905907; P:negative regulation of amyloid fibril formation; IDA:FlyBase. DR GO; GO:0006457; P:protein folding; IDA:FlyBase. DR GO; GO:0050821; P:protein stabilization; NAS:ComplexPortal. DR CDD; cd00632; Prefoldin_beta; 1. DR Gene3D; 1.10.287.370; -; 1. DR InterPro; IPR002777; PFD_beta-like. DR InterPro; IPR009053; Prefoldin. DR PANTHER; PTHR21431; PREFOLDIN SUBUNIT 6; 1. DR PANTHER; PTHR21431:SF0; PREFOLDIN SUBUNIT 6; 1. DR Pfam; PF01920; Prefoldin_2; 1. DR SUPFAM; SSF46579; Prefoldin; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Chaperone; Isopeptide bond; Reference proteome; KW Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..129 FT /note="Prefoldin subunit 6" FT /id="PRO_0000124850" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 21 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 66 FT /note="N6-acetyllysine; alternate" FT /evidence="ECO:0007744|PubMed:19608861" FT CROSSLNK 66 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1); alternate" FT /evidence="ECO:0007744|PubMed:25114211" FT CROSSLNK 66 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:28112733" SQ SEQUENCE 129 AA; 14583 MW; 8F138EAAE512A312 CRC64; MAELIQKKLQ GEVEKYQQLQ KDLSKSMSGR QKLEAQLTEN NIVKEELALL DGSNVVFKLL GPVLVKQELG EARATVGKRL DYITAEIKRY ESQLRDLERQ SEQQRETLAQ LQQEFQRAQA AKAGAPGKA //