PFD1_HUMAN
ID PFD1_HUMAN Reviewed; 122 AA.
AC O60925; B2RD02; Q53F95; Q96EX6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Prefoldin subunit 1;
GN Name=PFDN1; Synonyms=PFD1;
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=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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 [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=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
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).
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.
CC -!- SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta type
CC subunits.
CC -!- INTERACTION:
CC O60925; Q9NPF5: DMAP1; NbExp=3; IntAct=EBI-356919, EBI-399105;
CC O60925; Q9UHV9: PFDN2; NbExp=3; IntAct=EBI-356919, EBI-359873;
CC -!- SIMILARITY: Belongs to the prefoldin subunit beta family.
CC {ECO:0000305}.
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DR EMBL; Y17392; CAA76759.1; -; mRNA.
DR EMBL; AK223394; BAD97114.1; -; mRNA.
DR EMBL; AK315353; BAG37749.1; -; mRNA.
DR EMBL; CH471062; EAW62071.1; -; Genomic_DNA.
DR EMBL; BC003620; AAH03620.1; -; mRNA.
DR EMBL; BC006202; AAH06202.1; -; mRNA.
DR EMBL; BC011869; AAH11869.1; -; mRNA.
DR CCDS; CCDS4222.1; -.
DR RefSeq; NP_002613.2; NM_002622.4.
DR PDB; 6NR8; EM; 7.80 A; 1=12-118.
DR PDB; 6NR9; EM; 8.50 A; 1=12-118.
DR PDB; 6NRB; EM; 8.70 A; 1=12-118.
DR PDB; 6NRC; EM; 8.30 A; 1=12-118.
DR PDB; 6NRD; EM; 8.20 A; 1=12-118.
DR PDBsum; 6NR8; -.
DR PDBsum; 6NR9; -.
DR PDBsum; 6NRB; -.
DR PDBsum; 6NRC; -.
DR PDBsum; 6NRD; -.
DR AlphaFoldDB; O60925; -.
DR SMR; O60925; -.
DR BioGRID; 111223; 166.
DR ComplexPortal; CPX-6149; Prefoldin co-chaperone complex.
DR CORUM; O60925; -.
DR IntAct; O60925; 74.
DR MINT; O60925; -.
DR STRING; 9606.ENSP00000261813; -.
DR iPTMnet; O60925; -.
DR PhosphoSitePlus; O60925; -.
DR BioMuta; PFDN1; -.
DR OGP; O60925; -.
DR EPD; O60925; -.
DR jPOST; O60925; -.
DR MassIVE; O60925; -.
DR MaxQB; O60925; -.
DR PaxDb; O60925; -.
DR PeptideAtlas; O60925; -.
DR PRIDE; O60925; -.
DR ProteomicsDB; 49671; -.
DR TopDownProteomics; O60925; -.
DR Antibodypedia; 1773; 311 antibodies from 35 providers.
DR DNASU; 5201; -.
DR Ensembl; ENST00000261813.9; ENSP00000261813.4; ENSG00000113068.10.
DR GeneID; 5201; -.
DR KEGG; hsa:5201; -.
DR MANE-Select; ENST00000261813.9; ENSP00000261813.4; NM_002622.5; NP_002613.2.
DR UCSC; uc003lff.2; human.
DR CTD; 5201; -.
DR DisGeNET; 5201; -.
DR GeneCards; PFDN1; -.
DR HGNC; HGNC:8866; PFDN1.
DR HPA; ENSG00000113068; Low tissue specificity.
DR MIM; 604897; gene.
DR neXtProt; NX_O60925; -.
DR OpenTargets; ENSG00000113068; -.
DR PharmGKB; PA33207; -.
DR VEuPathDB; HostDB:ENSG00000113068; -.
DR eggNOG; KOG3501; Eukaryota.
DR GeneTree; ENSGT00390000009786; -.
DR HOGENOM; CLU_122140_2_0_1; -.
DR InParanoid; O60925; -.
DR OMA; HKNSREH; -.
DR OrthoDB; 1492856at2759; -.
DR PhylomeDB; O60925; -.
DR TreeFam; TF106490; -.
DR PathwayCommons; O60925; -.
DR Reactome; R-HSA-389957; Prefoldin mediated transfer of substrate to CCT/TriC.
DR SignaLink; O60925; -.
DR BioGRID-ORCS; 5201; 509 hits in 1079 CRISPR screens.
DR ChiTaRS; PFDN1; human.
DR GeneWiki; PFDN1; -.
DR GenomeRNAi; 5201; -.
DR Pharos; O60925; Tbio.
DR PRO; PR:O60925; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O60925; protein.
DR Bgee; ENSG00000113068; Expressed in calcaneal tendon and 203 other tissues.
DR ExpressionAtlas; O60925; baseline and differential.
DR Genevisible; O60925; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016272; C:prefoldin complex; IDA:FlyBase.
DR GO; GO:0001540; F:amyloid-beta binding; IDA:FlyBase.
DR GO; GO:0044183; F:protein folding chaperone; IPI:AgBase.
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; IPR009053; Prefoldin.
DR Pfam; PF01920; Prefoldin_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chaperone; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..122
FT /note="Prefoldin subunit 1"
FT /id="PRO_0000124830"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CONFLICT 86
FT /note="I -> V (in Ref. 3; BAD97114)"
FT /evidence="ECO:0000305"
FT CONFLICT 104..105
FT /note="SV -> RL (in Ref. 1; CAA76759)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 122 AA; 14210 MW; 4C88216612864F87 CRC64;
MAAPVDLELK KAFTELQAKV IDTQQKVKLA DIQIEQLNRT KKHAHLTDTE IMTLVDETNM
YEGVGRMFIL QSKEAIHSQL LEKQKIAEEK IKELEQKKSY LERSVKEAED NIREMLMARR
AQ
