PFD6_HUMAN
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 03-AUG-2022, entry version 175.
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}.
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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 PDBsum; 6NR8; -.
DR PDBsum; 6NR9; -.
DR PDBsum; 6NRB; -.
DR PDBsum; 6NRC; -.
DR PDBsum; 6NRD; -.
DR AlphaFoldDB; O15212; -.
DR SMR; O15212; -.
DR BioGRID; 115734; 118.
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; 61.
DR MINT; O15212; -.
DR STRING; 9606.ENSP00000378563; -.
DR iPTMnet; O15212; -.
DR PhosphoSitePlus; O15212; -.
DR BioMuta; PFDN6; -.
DR EPD; O15212; -.
DR jPOST; O15212; -.
DR MassIVE; O15212; -.
DR PaxDb; O15212; -.
DR PeptideAtlas; O15212; -.
DR PRIDE; O15212; -.
DR ProteomicsDB; 48512; -.
DR TopDownProteomics; O15212; -.
DR Antibodypedia; 29059; 126 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 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; 1559044at2759; -.
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 BioGRID-ORCS; 10471; 731 hits in 1081 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 95 other tissues.
DR ExpressionAtlas; O15212; baseline and differential.
DR Genevisible; O15212; HS.
DR GO; GO:0101031; C:chaperone complex; IC:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016272; C:prefoldin complex; IDA:UniProtKB.
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: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: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; IC:ComplexPortal.
DR Gene3D; 1.10.287.370; -; 1.
DR InterPro; IPR002777; PFD_beta-like.
DR InterPro; IPR009053; Prefoldin.
DR Pfam; PF01920; Prefoldin_2; 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
