PFD4_HUMAN
ID PFD4_HUMAN Reviewed; 134 AA.
AC Q9NQP4; Q5TD11; Q92779;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Prefoldin subunit 4;
DE AltName: Full=Protein C-1;
GN Name=PFDN4; Synonyms=PFD4;
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 [MRNA].
RX PubMed=8744932; DOI=10.18926/amo/30489;
RA Iijima M., Kano Y., Nohno T., Namba M.;
RT "Cloning of cDNA with possible transcription factor activity at the G1-S
RT phase transition in human fibroblast cell lines.";
RL Acta Med. Okayama 50:73-77(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [4]
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 [5]
RP INTERACTION WITH URI1, AND SUBCELLULAR LOCATION.
RX PubMed=17936702; DOI=10.1016/j.molcel.2007.08.010;
RA Djouder N., Metzler S.C., Schmidt A., Wirbelauer C., Gstaiger M.,
RA Aebersold R., Hess D., Krek W.;
RT "S6K1-mediated disassembly of mitochondrial URI/PP1gamma complexes
RT activates a negative feedback program that counters S6K1 survival
RT signaling.";
RL Mol. Cell 28:28-40(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
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).
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. Interacts with URI1; the interaction is phosphorylation-
CC dependent and occurs in a growth-dependent manner.
CC {ECO:0000269|PubMed:17936702}.
CC -!- INTERACTION:
CC Q9NQP4; O75679: RFPL3; NbExp=3; IntAct=EBI-357021, EBI-10188956;
CC Q9NQP4; P61758: VBP1; NbExp=7; IntAct=EBI-357021, EBI-357430;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17936702}. Cytoplasm
CC {ECO:0000269|PubMed:17936702}. Mitochondrion
CC {ECO:0000269|PubMed:17936702}.
CC -!- SIMILARITY: Belongs to the prefoldin subunit beta family.
CC {ECO:0000305}.
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DR EMBL; U41816; AAB17063.1; -; mRNA.
DR EMBL; AL133335; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010953; AAH10953.1; -; mRNA.
DR CCDS; CCDS13445.1; -.
DR RefSeq; NP_002614.2; NM_002623.3.
DR PDB; 6NR8; EM; 7.80 A; 4=19-122.
DR PDB; 6NR9; EM; 8.50 A; 4=19-122.
DR PDB; 6NRB; EM; 8.70 A; 4=19-122.
DR PDB; 6NRC; EM; 8.30 A; 4=19-122.
DR PDB; 6NRD; EM; 8.20 A; 4=19-122.
DR PDBsum; 6NR8; -.
DR PDBsum; 6NR9; -.
DR PDBsum; 6NRB; -.
DR PDBsum; 6NRC; -.
DR PDBsum; 6NRD; -.
DR AlphaFoldDB; Q9NQP4; -.
DR SMR; Q9NQP4; -.
DR BioGRID; 111225; 116.
DR ComplexPortal; CPX-6149; Prefoldin co-chaperone complex.
DR CORUM; Q9NQP4; -.
DR IntAct; Q9NQP4; 62.
DR MINT; Q9NQP4; -.
DR STRING; 9606.ENSP00000360473; -.
DR GlyGen; Q9NQP4; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NQP4; -.
DR PhosphoSitePlus; Q9NQP4; -.
DR BioMuta; PFDN4; -.
DR DMDM; 12643815; -.
DR EPD; Q9NQP4; -.
DR jPOST; Q9NQP4; -.
DR MassIVE; Q9NQP4; -.
DR MaxQB; Q9NQP4; -.
DR PaxDb; Q9NQP4; -.
DR PeptideAtlas; Q9NQP4; -.
DR PRIDE; Q9NQP4; -.
DR ProteomicsDB; 82167; -.
DR TopDownProteomics; Q9NQP4; -.
DR Antibodypedia; 13961; 163 antibodies from 23 providers.
DR DNASU; 5203; -.
DR Ensembl; ENST00000371419.7; ENSP00000360473.2; ENSG00000101132.10.
DR GeneID; 5203; -.
DR KEGG; hsa:5203; -.
DR MANE-Select; ENST00000371419.7; ENSP00000360473.2; NM_002623.4; NP_002614.2.
DR UCSC; uc002xwx.4; human.
DR CTD; 5203; -.
DR DisGeNET; 5203; -.
DR GeneCards; PFDN4; -.
DR HGNC; HGNC:8868; PFDN4.
DR HPA; ENSG00000101132; Low tissue specificity.
DR MIM; 604898; gene.
DR neXtProt; NX_Q9NQP4; -.
DR OpenTargets; ENSG00000101132; -.
DR PharmGKB; PA33209; -.
DR VEuPathDB; HostDB:ENSG00000101132; -.
DR eggNOG; KOG1760; Eukaryota.
DR GeneTree; ENSGT00390000006696; -.
DR HOGENOM; CLU_130032_0_1_1; -.
DR InParanoid; Q9NQP4; -.
DR OMA; NARMDEF; -.
DR OrthoDB; 1459797at2759; -.
DR PhylomeDB; Q9NQP4; -.
DR TreeFam; TF106491; -.
DR PathwayCommons; Q9NQP4; -.
DR Reactome; R-HSA-389957; Prefoldin mediated transfer of substrate to CCT/TriC.
DR SignaLink; Q9NQP4; -.
DR SIGNOR; Q9NQP4; -.
DR BioGRID-ORCS; 5203; 194 hits in 1066 CRISPR screens.
DR ChiTaRS; PFDN4; human.
DR GeneWiki; PFDN4; -.
DR GenomeRNAi; 5203; -.
DR Pharos; Q9NQP4; Tbio.
DR PRO; PR:Q9NQP4; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9NQP4; protein.
DR Bgee; ENSG00000101132; Expressed in oocyte and 211 other tissues.
DR ExpressionAtlas; Q9NQP4; baseline and differential.
DR Genevisible; Q9NQP4; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; NAS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016272; C:prefoldin complex; IDA:FlyBase.
DR GO; GO:0001540; F:amyloid-beta binding; IDA:FlyBase.
DR GO; GO:0051087; F:chaperone binding; TAS:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; IDA:FlyBase.
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; IPR016661; PFDN4.
DR InterPro; IPR009053; Prefoldin.
DR PANTHER; PTHR21100; PTHR21100; 1.
DR Pfam; PF01920; Prefoldin_2; 1.
DR PIRSF; PIRSF016477; Prefoldin_subunit_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chaperone; Cytoplasm; Mitochondrion; Nucleus;
KW Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..134
FT /note="Prefoldin subunit 4"
FT /id="PRO_0000124842"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
SQ SEQUENCE 134 AA; 15314 MW; C727F0FCB9343DC3 CRC64;
MAATMKKAAA EDVNVTFEDQ QKINKFARNT SRITELKEEI EVKKKQLQNL EDACDDIMLA
DDDCLMIPYQ IGDVFISHSQ EETQEMLEEA KKNLQEEIDA LESRVESIQR VLADLKVQLY
AKFGSNINLE ADES
