PFD3_HUMAN
ID PFD3_HUMAN Reviewed; 197 AA.
AC P61758; B2R8L5; B4DWR3; F5H2A7; O55228; Q15765; Q5JT81; Q86X96;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-APR-2019, sequence version 4.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Prefoldin subunit 3;
DE AltName: Full=HIBBJ46;
DE AltName: Full=von Hippel-Lindau-binding protein 1;
DE Short=VBP-1;
DE Short=VHL-binding protein 1;
GN Name=VBP1; Synonyms=PFDN3;
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] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9339366; DOI=10.1006/geno.1997.4902;
RA Brinke A., Green P.M., Giannelli F.;
RT "Characterization of the gene (VBP1) and transcript for the von Hippel-
RT Lindau binding protein and isolation of the highly conserved murine
RT homologue.";
RL Genomics 45:105-112(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cerebellum, and Esophagus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT MET-123.
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-197 (ISOFORMS 1/2).
RX PubMed=8674032;
RA Tsuchiya H., Iseda T., Hino O.;
RT "Identification of a novel protein (VBP-1) binding to the von Hippel-Lindau
RT (VHL) tumor suppressor gene product.";
RL Cancer Res. 56:2881-2885(1996).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-59, AND IDENTIFICATION BY MASS
RP 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 [9]
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 [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).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
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. Binds to the C-terminal part of VHL.
CC -!- INTERACTION:
CC P61758; Q14457: BECN1; NbExp=3; IntAct=EBI-357430, EBI-949378;
CC P61758; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-357430, EBI-8643161;
CC P61758; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-357430, EBI-742054;
CC P61758; Q5JVL4: EFHC1; NbExp=3; IntAct=EBI-357430, EBI-743105;
CC P61758; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-357430, EBI-744099;
CC P61758; P05230: FGF1; NbExp=3; IntAct=EBI-357430, EBI-698068;
CC P61758; Q06547-2: GABPB1; NbExp=3; IntAct=EBI-357430, EBI-618189;
CC P61758; Q9BZE0: GLIS2; NbExp=3; IntAct=EBI-357430, EBI-7251368;
CC P61758; O95872: GPANK1; NbExp=3; IntAct=EBI-357430, EBI-751540;
CC P61758; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-357430, EBI-747204;
CC P61758; Q96JM7-2: L3MBTL3; NbExp=3; IntAct=EBI-357430, EBI-11985629;
CC P61758; P25800: LMO1; NbExp=3; IntAct=EBI-357430, EBI-8639312;
CC P61758; P25791-3: LMO2; NbExp=3; IntAct=EBI-357430, EBI-11959475;
CC P61758; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-357430, EBI-11742507;
CC P61758; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-357430, EBI-16439278;
CC P61758; Q8IVT2: MISP; NbExp=3; IntAct=EBI-357430, EBI-2555085;
CC P61758; Q9NP98: MYOZ1; NbExp=3; IntAct=EBI-357430, EBI-744402;
CC P61758; Q9UHV9: PFDN2; NbExp=7; IntAct=EBI-357430, EBI-359873;
CC P61758; Q9NQP4: PFDN4; NbExp=7; IntAct=EBI-357430, EBI-357021;
CC P61758; Q99471: PFDN5; NbExp=7; IntAct=EBI-357430, EBI-357275;
CC P61758; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-357430, EBI-302345;
CC P61758; O43741: PRKAB2; NbExp=3; IntAct=EBI-357430, EBI-1053424;
CC P61758; O43704: SULT1B1; NbExp=3; IntAct=EBI-357430, EBI-10179062;
CC P61758; P51687: SUOX; NbExp=3; IntAct=EBI-357430, EBI-3921347;
CC P61758; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-357430, EBI-11955057;
CC P61758; Q8WTV1: THAP3; NbExp=3; IntAct=EBI-357430, EBI-17438286;
CC P61758; Q9Y3Q8: TSC22D4; NbExp=3; IntAct=EBI-357430, EBI-739485;
CC P61758; Q96S82: UBL7; NbExp=7; IntAct=EBI-357430, EBI-348604;
CC P61758; Q14119: VEZF1; NbExp=3; IntAct=EBI-357430, EBI-11980193;
CC P61758; Q9UNY5: ZNF232; NbExp=3; IntAct=EBI-357430, EBI-749023;
CC P61758; Q86VK4-3: ZNF410; NbExp=3; IntAct=EBI-357430, EBI-11741890;
CC P61758; Q96MN9-2: ZNF488; NbExp=3; IntAct=EBI-357430, EBI-25831733;
CC P61758; Q9H609: ZNF576; NbExp=3; IntAct=EBI-357430, EBI-3921014;
CC P61758; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-357430, EBI-745520;
CC P61758; P35963: gag-pol; Xeno; NbExp=3; IntAct=EBI-357430, EBI-911612;
CC P61758; Q9Q2G4: ORF; Xeno; NbExp=3; IntAct=EBI-357430, EBI-6248094;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=In complex with VHL can
CC translocate to the nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P61758-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P61758-2; Sequence=VSP_060081;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the prefoldin subunit alpha family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC23907.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U96759; AAC23907.1; ALT_INIT; mRNA.
DR EMBL; Y17394; CAA76761.1; -; mRNA.
DR EMBL; AK301646; BAG63125.1; -; mRNA.
DR EMBL; AK313420; BAG36212.1; -; mRNA.
DR EMBL; BT019604; AAV38411.1; -; mRNA.
DR EMBL; AL356738; CAI41469.1; -; Genomic_DNA.
DR EMBL; BX682237; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC046094; AAH46094.1; -; mRNA.
DR EMBL; U56833; AAC50617.1; -; mRNA.
DR CCDS; CCDS14765.1; -. [P61758-1]
DR CCDS; CCDS78525.1; -. [P61758-2]
DR RefSeq; NP_001290472.1; NM_001303543.1.
DR RefSeq; NP_001290473.1; NM_001303544.1. [P61758-2]
DR RefSeq; NP_001290474.1; NM_001303545.1.
DR RefSeq; NP_003363.1; NM_003372.6. [P61758-1]
DR PDB; 6NR8; EM; 7.80 A; 3=49-180.
DR PDB; 6NR9; EM; 8.50 A; 3=49-180.
DR PDB; 6NRB; EM; 8.70 A; 3=49-180.
DR PDB; 6NRC; EM; 8.30 A; 3=49-180.
DR PDB; 6NRD; EM; 8.20 A; 3=49-180.
DR PDBsum; 6NR8; -.
DR PDBsum; 6NR9; -.
DR PDBsum; 6NRB; -.
DR PDBsum; 6NRC; -.
DR PDBsum; 6NRD; -.
DR AlphaFoldDB; P61758; -.
DR SMR; P61758; -.
DR BioGRID; 113254; 162.
DR ComplexPortal; CPX-6149; Prefoldin co-chaperone complex.
DR CORUM; P61758; -.
DR DIP; DIP-46479N; -.
DR IntAct; P61758; 79.
DR MINT; P61758; -.
DR STRING; 9606.ENSP00000286428; -.
DR GlyGen; P61758; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P61758; -.
DR MetOSite; P61758; -.
DR PhosphoSitePlus; P61758; -.
DR BioMuta; VBP1; -.
DR DMDM; 125987848; -.
DR OGP; P61758; -.
DR EPD; P61758; -.
DR jPOST; P61758; -.
DR MassIVE; P61758; -.
DR MaxQB; P61758; -.
DR PaxDb; P61758; -.
DR PeptideAtlas; P61758; -.
DR PRIDE; P61758; -.
DR ProteomicsDB; 25914; -.
DR ProteomicsDB; 57330; -.
DR Antibodypedia; 3341; 385 antibodies from 29 providers.
DR DNASU; 7411; -.
DR Ensembl; ENST00000286428.7; ENSP00000286428.5; ENSG00000155959.12. [P61758-1]
DR Ensembl; ENST00000535916.5; ENSP00000438694.1; ENSG00000155959.12. [P61758-2]
DR Ensembl; ENST00000625964.2; ENSP00000486053.1; ENSG00000155959.12. [P61758-2]
DR GeneID; 7411; -.
DR KEGG; hsa:7411; -.
DR MANE-Select; ENST00000286428.7; ENSP00000286428.5; NM_003372.7; NP_003363.1.
DR UCSC; uc004fnc.4; human. [P61758-1]
DR UCSC; uc065cjx.1; human.
DR CTD; 7411; -.
DR DisGeNET; 7411; -.
DR GeneCards; VBP1; -.
DR HGNC; HGNC:12662; VBP1.
DR HPA; ENSG00000155959; Low tissue specificity.
DR MIM; 300133; gene.
DR neXtProt; NX_P61758; -.
DR OpenTargets; ENSG00000155959; -.
DR PharmGKB; PA37285; -.
DR VEuPathDB; HostDB:ENSG00000155959; -.
DR eggNOG; KOG3313; Eukaryota.
DR GeneTree; ENSGT00390000018904; -.
DR HOGENOM; CLU_083737_1_0_1; -.
DR InParanoid; P61758; -.
DR OMA; DEQHSKY; -.
DR OrthoDB; 1567796at2759; -.
DR PhylomeDB; P61758; -.
DR TreeFam; TF313706; -.
DR PathwayCommons; P61758; -.
DR Reactome; R-HSA-389957; Prefoldin mediated transfer of substrate to CCT/TriC.
DR SignaLink; P61758; -.
DR BioGRID-ORCS; 7411; 134 hits in 711 CRISPR screens.
DR ChiTaRS; VBP1; human.
DR GenomeRNAi; 7411; -.
DR Pharos; P61758; Tbio.
DR PRO; PR:P61758; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P61758; protein.
DR Bgee; ENSG00000155959; Expressed in biceps brachii and 212 other tissues.
DR Genevisible; P61758; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005844; C:polysome; 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:0015631; F:tubulin binding; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IDA:FlyBase.
DR GO; GO:0007017; P:microtubule-based process; IBA:GO_Central.
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 GO; GO:0007021; P:tubulin complex assembly; IBA:GO_Central.
DR Gene3D; 1.10.287.370; -; 1.
DR InterPro; IPR016655; PFD3.
DR InterPro; IPR009053; Prefoldin.
DR InterPro; IPR004127; Prefoldin_subunit_alpha.
DR PANTHER; PTHR12409; PTHR12409; 1.
DR Pfam; PF02996; Prefoldin; 1.
DR PIRSF; PIRSF016396; Prefoldin_subunit_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Chaperone; Cytoplasm;
KW Nucleus; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..197
FT /note="Prefoldin subunit 3"
FT /id="PRO_0000153652"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 59
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..31
FT /note="MAAVKDSCGKGEMATGNGRRLHLGIPEAVFV -> MAPQPMIHTQQGLRTSS
FT PSTPSPEHQ (in isoform 2)"
FT /id="VSP_060081"
FT VARIANT 123
FT /note="V -> M (in dbSNP:rs572013)"
FT /evidence="ECO:0000269|PubMed:15772651"
FT /id="VAR_023371"
SQ SEQUENCE 197 AA; 22626 MW; 973BA048048D948E CRC64;
MAAVKDSCGK GEMATGNGRR LHLGIPEAVF VEDVDSFMKQ PGNETADTVL KKLDEQYQKY
KFMELNLAQK KRRLKGQIPE IKQTLEILKY MQKKKESTNS METRFLLADN LYCKASVPPT
DKVCLWLGAN VMLEYDIDEA QALLEKNLST ATKNLDSLEE DLDFLRDQFT TTEVNMARVY
NWDVKRRNKD DSTKNKA
