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 24-JAN-2024, entry version 183. 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}. 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; 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 PDB; 7WU7; EM; 3.85 A; 1=1-122. DR PDBsum; 6NR8; -. DR PDBsum; 6NR9; -. DR PDBsum; 6NRB; -. DR PDBsum; 6NRC; -. DR PDBsum; 6NRD; -. DR PDBsum; 7WU7; -. DR AlphaFoldDB; O60925; -. DR EMDB; EMD-32823; -. DR SMR; O60925; -. DR BioGRID; 111223; 190. DR ComplexPortal; CPX-6149; Prefoldin co-chaperone complex. DR CORUM; O60925; -. DR IntAct; O60925; 80. DR MINT; O60925; -. DR STRING; 9606.ENSP00000261813; -. DR GlyGen; O60925; 1 site, 1 O-linked glycan (1 site). 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; 9606-ENSP00000261813; -. DR PeptideAtlas; O60925; -. DR ProteomicsDB; 49671; -. DR Pumba; O60925; -. DR TopDownProteomics; O60925; -. DR Antibodypedia; 1773; 339 antibodies from 36 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 AGR; HGNC:8866; -. 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; MFVAVPM; -. DR OrthoDB; 26461at2759; -. 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 SIGNOR; O60925; -. DR BioGRID-ORCS; 5201; 530 hits in 1157 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 205 other cell types or tissues. DR ExpressionAtlas; O60925; baseline and differential. 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: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 Gene3D; 1.10.287.370; -; 1. DR InterPro; IPR002777; PFD_beta-like. DR InterPro; IPR009053; Prefoldin. DR PANTHER; PTHR20903:SF1; PREFOLDIN SUBUNIT 1; 1. DR PANTHER; PTHR20903; PREFOLDIN SUBUNIT 1-RELATED; 1. DR Pfam; PF01920; Prefoldin_2; 1. DR SUPFAM; SSF46579; Prefoldin; 1. DR Genevisible; O60925; HS. 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 //