Full text data of PFDN4
PFDN4
(PFD4)
[Confidence: low (only semi-automatic identification from reviews)]
Prefoldin subunit 4 (Protein C-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Prefoldin subunit 4 (Protein C-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9NQP4
ID PFD4_HUMAN Reviewed; 134 AA.
AC Q9NQP4; Q5TD11; Q92779;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 102.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8744932;
RA Iijima M., Kano Y., Nohno T., Namba M.;
RT "Cloning of cDNA with possible transcription factor activity at the
RT G1-S 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.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA 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.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA 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
RT project: 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 MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal 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
CC chain and promotes folding in an environment in which there are
CC many competing pathways for nonnative proteins.
CC -!- SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta
CC type subunits. Interacts with URI1; the interaction is
CC phosphorylation-dependent and occurs in a growth-dependent manner.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Mitochondrion.
CC -!- SIMILARITY: Belongs to the prefoldin subunit beta family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U41816; AAB17063.1; -; mRNA.
DR EMBL; AL133335; CAI19316.1; -; Genomic_DNA.
DR EMBL; BC010953; AAH10953.1; -; mRNA.
DR RefSeq; NP_002614.2; NM_002623.3.
DR UniGene; Hs.91161; -.
DR ProteinModelPortal; Q9NQP4; -.
DR IntAct; Q9NQP4; 4.
DR MINT; MINT-1131938; -.
DR STRING; 9606.ENSP00000360473; -.
DR PhosphoSite; Q9NQP4; -.
DR DMDM; 12643815; -.
DR PaxDb; Q9NQP4; -.
DR PeptideAtlas; Q9NQP4; -.
DR PRIDE; Q9NQP4; -.
DR DNASU; 5203; -.
DR Ensembl; ENST00000371419; ENSP00000360473; ENSG00000101132.
DR GeneID; 5203; -.
DR KEGG; hsa:5203; -.
DR UCSC; uc002xwx.3; human.
DR CTD; 5203; -.
DR GeneCards; GC20P052824; -.
DR HGNC; HGNC:8868; PFDN4.
DR HPA; HPA024055; -.
DR MIM; 604898; gene.
DR neXtProt; NX_Q9NQP4; -.
DR PharmGKB; PA33209; -.
DR eggNOG; COG1382; -.
DR HOGENOM; HOG000204477; -.
DR HOVERGEN; HBG005034; -.
DR InParanoid; Q9NQP4; -.
DR KO; K09550; -.
DR OrthoDB; EOG77M8QW; -.
DR PhylomeDB; Q9NQP4; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR GeneWiki; PFDN4; -.
DR GenomeRNAi; 5203; -.
DR NextBio; 20122; -.
DR PRO; PR:Q9NQP4; -.
DR ArrayExpress; Q9NQP4; -.
DR Bgee; Q9NQP4; -.
DR CleanEx; HS_PFDN4; -.
DR Genevestigator; Q9NQP4; -.
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; IEA:InterPro.
DR GO; GO:0051087; F:chaperone binding; TAS:UniProtKB.
DR GO; GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
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.
DR SUPFAM; SSF46579; SSF46579; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Complete proteome; Cytoplasm; Mitochondrion;
KW Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 134 Prefoldin subunit 4.
FT /FTId=PRO_0000124842.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 125 125 Phosphoserine.
SQ SEQUENCE 134 AA; 15314 MW; C727F0FCB9343DC3 CRC64;
MAATMKKAAA EDVNVTFEDQ QKINKFARNT SRITELKEEI EVKKKQLQNL EDACDDIMLA
DDDCLMIPYQ IGDVFISHSQ EETQEMLEEA KKNLQEEIDA LESRVESIQR VLADLKVQLY
AKFGSNINLE ADES
//
ID PFD4_HUMAN Reviewed; 134 AA.
AC Q9NQP4; Q5TD11; Q92779;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 102.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8744932;
RA Iijima M., Kano Y., Nohno T., Namba M.;
RT "Cloning of cDNA with possible transcription factor activity at the
RT G1-S 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.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA 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.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA 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
RT project: 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 MASS
RP SPECTROMETRY.
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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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 MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal 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
CC chain and promotes folding in an environment in which there are
CC many competing pathways for nonnative proteins.
CC -!- SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta
CC type subunits. Interacts with URI1; the interaction is
CC phosphorylation-dependent and occurs in a growth-dependent manner.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Mitochondrion.
CC -!- SIMILARITY: Belongs to the prefoldin subunit beta family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U41816; AAB17063.1; -; mRNA.
DR EMBL; AL133335; CAI19316.1; -; Genomic_DNA.
DR EMBL; BC010953; AAH10953.1; -; mRNA.
DR RefSeq; NP_002614.2; NM_002623.3.
DR UniGene; Hs.91161; -.
DR ProteinModelPortal; Q9NQP4; -.
DR IntAct; Q9NQP4; 4.
DR MINT; MINT-1131938; -.
DR STRING; 9606.ENSP00000360473; -.
DR PhosphoSite; Q9NQP4; -.
DR DMDM; 12643815; -.
DR PaxDb; Q9NQP4; -.
DR PeptideAtlas; Q9NQP4; -.
DR PRIDE; Q9NQP4; -.
DR DNASU; 5203; -.
DR Ensembl; ENST00000371419; ENSP00000360473; ENSG00000101132.
DR GeneID; 5203; -.
DR KEGG; hsa:5203; -.
DR UCSC; uc002xwx.3; human.
DR CTD; 5203; -.
DR GeneCards; GC20P052824; -.
DR HGNC; HGNC:8868; PFDN4.
DR HPA; HPA024055; -.
DR MIM; 604898; gene.
DR neXtProt; NX_Q9NQP4; -.
DR PharmGKB; PA33209; -.
DR eggNOG; COG1382; -.
DR HOGENOM; HOG000204477; -.
DR HOVERGEN; HBG005034; -.
DR InParanoid; Q9NQP4; -.
DR KO; K09550; -.
DR OrthoDB; EOG77M8QW; -.
DR PhylomeDB; Q9NQP4; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR GeneWiki; PFDN4; -.
DR GenomeRNAi; 5203; -.
DR NextBio; 20122; -.
DR PRO; PR:Q9NQP4; -.
DR ArrayExpress; Q9NQP4; -.
DR Bgee; Q9NQP4; -.
DR CleanEx; HS_PFDN4; -.
DR Genevestigator; Q9NQP4; -.
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; IEA:InterPro.
DR GO; GO:0051087; F:chaperone binding; TAS:UniProtKB.
DR GO; GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
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.
DR SUPFAM; SSF46579; SSF46579; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Complete proteome; Cytoplasm; Mitochondrion;
KW Nucleus; Phosphoprotein; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 134 Prefoldin subunit 4.
FT /FTId=PRO_0000124842.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 125 125 Phosphoserine.
SQ SEQUENCE 134 AA; 15314 MW; C727F0FCB9343DC3 CRC64;
MAATMKKAAA EDVNVTFEDQ QKINKFARNT SRITELKEEI EVKKKQLQNL EDACDDIMLA
DDDCLMIPYQ IGDVFISHSQ EETQEMLEEA KKNLQEEIDA LESRVESIQR VLADLKVQLY
AKFGSNINLE ADES
//
MIM
604898
*RECORD*
*FIELD* NO
604898
*FIELD* TI
*604898 PREFOLDIN 4; PFDN4
;;C1
*FIELD* TX
Molecular chaperones are proteins that assist in the correct folding of
read moreother proteins in the crowded molecular environment that exists in
living cells. Within this class of proteins, a key role is played by
chaperonins, multisubunit toroidal assemblies that undergo major
ATP-dependent conformational changes as part of the mechanism of
facilitated folding (see 118190).
By differential hybridization of SV40T-introduced crisis cells and young
Wilms tumor patient fibroblasts, Iijima et al. (1996) cloned a cDNA,
which they termed C1, that is highly expressed in 11p-negative cells at
the time of crisis. Sequence analysis of the C1 cDNA predicted a
130-amino acid protein with a helix-loop-helix domain, indicating that
it might be a transcription factor. Northern blot analysis revealed
expression of 0.6- and 0.8-kb transcripts which peaked in the early G1
phase in normal and SV40T-immortalized fibroblast cell lines.
Vainberg et al. (1998) described the biochemical purification of a
heterohexameric chaperone protein, which they called prefoldin. One of
its subunits, prefoldin-4, is identical to C1.
The International Radiation Hybrid Mapping Consortium mapped the PFDN4
gene to chromosome 20 (TMAP RH93494).
*FIELD* RF
1. Iijima, M.; Kano, Y.; Nohno, T.; Namba, M.: Cloning of cDNA with
possible transcription factor activity at the G1-S phase transition
in human fibroblast cell lines. Acta Med. Okayama 50: 73-77, 1996.
2. Vainberg, I. E.; Lewis, S. A.; Rommelaere, H.; Ampe, C.; Vandekerckhove,
J.; Klein, H. L.; Cowan, N. J.: Prefoldin, a chaperone that delivers
unfolded proteins to cytosolic chaperonin. Cell 93: 863-873, 1998.
*FIELD* CD
Paul J. Converse: 5/1/2000
*FIELD* ED
joanna: 07/10/2006
cwells: 9/17/2003
carol: 5/1/2000
*RECORD*
*FIELD* NO
604898
*FIELD* TI
*604898 PREFOLDIN 4; PFDN4
;;C1
*FIELD* TX
Molecular chaperones are proteins that assist in the correct folding of
read moreother proteins in the crowded molecular environment that exists in
living cells. Within this class of proteins, a key role is played by
chaperonins, multisubunit toroidal assemblies that undergo major
ATP-dependent conformational changes as part of the mechanism of
facilitated folding (see 118190).
By differential hybridization of SV40T-introduced crisis cells and young
Wilms tumor patient fibroblasts, Iijima et al. (1996) cloned a cDNA,
which they termed C1, that is highly expressed in 11p-negative cells at
the time of crisis. Sequence analysis of the C1 cDNA predicted a
130-amino acid protein with a helix-loop-helix domain, indicating that
it might be a transcription factor. Northern blot analysis revealed
expression of 0.6- and 0.8-kb transcripts which peaked in the early G1
phase in normal and SV40T-immortalized fibroblast cell lines.
Vainberg et al. (1998) described the biochemical purification of a
heterohexameric chaperone protein, which they called prefoldin. One of
its subunits, prefoldin-4, is identical to C1.
The International Radiation Hybrid Mapping Consortium mapped the PFDN4
gene to chromosome 20 (TMAP RH93494).
*FIELD* RF
1. Iijima, M.; Kano, Y.; Nohno, T.; Namba, M.: Cloning of cDNA with
possible transcription factor activity at the G1-S phase transition
in human fibroblast cell lines. Acta Med. Okayama 50: 73-77, 1996.
2. Vainberg, I. E.; Lewis, S. A.; Rommelaere, H.; Ampe, C.; Vandekerckhove,
J.; Klein, H. L.; Cowan, N. J.: Prefoldin, a chaperone that delivers
unfolded proteins to cytosolic chaperonin. Cell 93: 863-873, 1998.
*FIELD* CD
Paul J. Converse: 5/1/2000
*FIELD* ED
joanna: 07/10/2006
cwells: 9/17/2003
carol: 5/1/2000