ID PFD5_HUMAN Reviewed; 154 AA. AC Q99471; A8K9A8; Q54AA8; Q9C083; Q9C084; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2001, sequence version 2. DT 27-MAR-2024, entry version 200. DE RecName: Full=Prefoldin subunit 5; DE AltName: Full=Myc modulator 1; DE AltName: Full=c-Myc-binding protein Mm-1; GN Name=PFDN5; Synonyms=MM1, PFD5; 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=9792694; DOI=10.1074/jbc.273.45.29794; RA Mori K., Maeda Y., Kitaura H., Taira T., Iguchi-Ariga S.M., Ariga H.; RT "MM-1, a novel c-Myc-associating protein that represses transcriptional RT activity of c-Myc."; RL J. Biol. Chem. 273:29794-29800(1998). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1). RC TISSUE=Blood, and Fibroblast; RX PubMed=11567024; DOI=10.1074/jbc.m106127200; RA Fujioka Y., Taira T., Maeda Y., Tanaka S., Nishihara H., RA Iguchi-Ariga S.M.M., Nagashima K., Ariga H.; RT "MM-1, a c-Myc-binding protein, is a candidate for a tumor suppressor in RT leukemia/lymphoma and tongue cancer."; RL J. Biol. Chem. 276:45137-45144(2001). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION, AND RP ALTERNATIVE SPLICING. RC TISSUE=B-cell, and Placenta; RX PubMed=16173081; DOI=10.1002/jcb.20619; RA Hagio Y., Kimura Y., Taira T., Fujioka Y., Iguchi-Ariga S.M.M., Ariga H.; RT "Distinct localizations and repression activities of MM-1 isoforms toward RT c-Myc."; RL J. Cell. Biochem. 97:145-155(2006). 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 (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Thymus; 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [7] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Placenta; 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 [9] 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 [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=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 [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42, 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 [12] 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 [13] 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=22223895; DOI=10.1074/mcp.m111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., RA Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). 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. Represses the transcriptional activity CC of MYC. {ECO:0000269|PubMed:9630229}. CC -!- SUBUNIT: Heterohexamer of two PFD-alpha type and four PFD-beta type CC subunits. Binds to MYC; interacts with its N-terminal domain. CC -!- INTERACTION: CC Q99471; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-357275, EBI-11096309; CC Q99471; Q3KP44: ANKRD55; NbExp=3; IntAct=EBI-357275, EBI-14493093; CC Q99471; Q7L5A3: ATOSB; NbExp=3; IntAct=EBI-357275, EBI-745689; CC Q99471; O75934: BCAS2; NbExp=3; IntAct=EBI-357275, EBI-1050106; CC Q99471; P41182: BCL6; NbExp=3; IntAct=EBI-357275, EBI-765407; CC Q99471; O14503: BHLHE40; NbExp=3; IntAct=EBI-357275, EBI-711810; CC Q99471; Q5SWW7: C10orf55; NbExp=3; IntAct=EBI-357275, EBI-12809220; CC Q99471; Q5T681: C10orf62; NbExp=3; IntAct=EBI-357275, EBI-744052; CC Q99471; Q6P5X5: C22orf39; NbExp=3; IntAct=EBI-357275, EBI-7317823; CC Q99471; Q13137: CALCOCO2; NbExp=4; IntAct=EBI-357275, EBI-739580; CC Q99471; E9PSE9: CCDC198; NbExp=3; IntAct=EBI-357275, EBI-11748295; CC Q99471; Q9H1P6: CIMIP1; NbExp=3; IntAct=EBI-357275, EBI-12155483; CC Q99471; Q1MSJ5-1: CSPP1; NbExp=3; IntAct=EBI-357275, EBI-10239122; CC Q99471; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-357275, EBI-9679045; CC Q99471; Q8TEW6: DOK4; NbExp=3; IntAct=EBI-357275, EBI-6918542; CC Q99471; Q9P104-2: DOK5; NbExp=3; IntAct=EBI-357275, EBI-10692909; CC Q99471; Q5T9C2-3: EEIG1; NbExp=3; IntAct=EBI-357275, EBI-11980989; CC Q99471; P41970: ELK3; NbExp=3; IntAct=EBI-357275, EBI-1758534; CC Q99471; Q6ZVH7: ESPNL; NbExp=3; IntAct=EBI-357275, EBI-12831272; CC Q99471; Q6NZ36-4: FAAP20; NbExp=3; IntAct=EBI-357275, EBI-12013806; CC Q99471; Q9BQ89: FAM110A; NbExp=3; IntAct=EBI-357275, EBI-1752811; CC Q99471; A4D161: FAM221A; NbExp=3; IntAct=EBI-357275, EBI-11960181; CC Q99471; Q8WU58: FAM222B; NbExp=3; IntAct=EBI-357275, EBI-2807642; CC Q99471; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-357275, EBI-6658203; CC Q99471; O76003: GLRX3; NbExp=3; IntAct=EBI-357275, EBI-374781; CC Q99471; Q8IVS8: GLYCTK; NbExp=3; IntAct=EBI-357275, EBI-748515; CC Q99471; O95872: GPANK1; NbExp=3; IntAct=EBI-357275, EBI-751540; CC Q99471; Q9H4Y5: GSTO2; NbExp=3; IntAct=EBI-357275, EBI-10194609; CC Q99471; Q96NT3-2: GUCD1; NbExp=3; IntAct=EBI-357275, EBI-11978177; CC Q99471; Q9GZV7: HAPLN2; NbExp=3; IntAct=EBI-357275, EBI-11956675; CC Q99471; Q03014: HHEX; NbExp=3; IntAct=EBI-357275, EBI-747421; CC Q99471; P17482: HOXB9; NbExp=3; IntAct=EBI-357275, EBI-745290; CC Q99471; P31273: HOXC8; NbExp=3; IntAct=EBI-357275, EBI-1752118; CC Q99471; P42858: HTT; NbExp=3; IntAct=EBI-357275, EBI-466029; CC Q99471; Q9UKT9: IKZF3; NbExp=7; IntAct=EBI-357275, EBI-747204; CC Q99471; Q14005-2: IL16; NbExp=3; IntAct=EBI-357275, EBI-17178971; CC Q99471; Q0VD86: INCA1; NbExp=3; IntAct=EBI-357275, EBI-6509505; CC Q99471; Q9BZI1: IRX2; NbExp=3; IntAct=EBI-357275, EBI-12166369; CC Q99471; P78412: IRX6; NbExp=3; IntAct=EBI-357275, EBI-12100506; CC Q99471; Q7L273: KCTD9; NbExp=3; IntAct=EBI-357275, EBI-4397613; CC Q99471; O60341: KDM1A; NbExp=3; IntAct=EBI-357275, EBI-710124; CC Q99471; O14901: KLF11; NbExp=3; IntAct=EBI-357275, EBI-948266; CC Q99471; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-357275, EBI-6426443; CC Q99471; Q9P2K6: KLHL42; NbExp=3; IntAct=EBI-357275, EBI-739890; CC Q99471; Q6P4E2: LARP4; NbExp=3; IntAct=EBI-357275, EBI-12079790; CC Q99471; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-357275, EBI-739832; CC Q99471; Q13163: MAP2K5; NbExp=3; IntAct=EBI-357275, EBI-307294; CC Q99471; Q8WXB1: METTL21A; NbExp=3; IntAct=EBI-357275, EBI-8652459; CC Q99471; Q8IVT2: MISP; NbExp=3; IntAct=EBI-357275, EBI-2555085; CC Q99471; Q9BRJ2: MRPL45; NbExp=3; IntAct=EBI-357275, EBI-2514313; CC Q99471; Q9UBF9: MYOT; NbExp=3; IntAct=EBI-357275, EBI-296701; CC Q99471; Q9NP98: MYOZ1; NbExp=3; IntAct=EBI-357275, EBI-744402; CC Q99471; Q9H2A3: NEUROG2; NbExp=3; IntAct=EBI-357275, EBI-7969348; CC Q99471; Q86UR1-2: NOXA1; NbExp=3; IntAct=EBI-357275, EBI-12025760; CC Q99471; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-357275, EBI-741158; CC Q99471; Q9HBE1-4: PATZ1; NbExp=3; IntAct=EBI-357275, EBI-11022007; CC Q99471; P55771: PAX9; NbExp=3; IntAct=EBI-357275, EBI-12111000; CC Q99471; Q7Z412: PEX26; NbExp=3; IntAct=EBI-357275, EBI-752057; CC Q99471; Q9UHV9: PFDN2; NbExp=5; IntAct=EBI-357275, EBI-359873; CC Q99471; O43189: PHF1; NbExp=3; IntAct=EBI-357275, EBI-530034; CC Q99471; Q9UPV7: PHF24; NbExp=3; IntAct=EBI-357275, EBI-17717171; CC Q99471; C9JJ79: PILRA; NbExp=3; IntAct=EBI-357275, EBI-12117156; CC Q99471; P78337: PITX1; NbExp=3; IntAct=EBI-357275, EBI-748265; CC Q99471; Q99697-2: PITX2; NbExp=3; IntAct=EBI-357275, EBI-12138495; CC Q99471; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-357275, EBI-1389308; CC Q99471; O43741: PRKAB2; NbExp=3; IntAct=EBI-357275, EBI-1053424; CC Q99471; Q99633: PRPF18; NbExp=3; IntAct=EBI-357275, EBI-2798416; CC Q99471; P0CG20: PRR35; NbExp=3; IntAct=EBI-357275, EBI-11986293; CC Q99471; P28070: PSMB4; NbExp=3; IntAct=EBI-357275, EBI-603350; CC Q99471; P28062-2: PSMB8; NbExp=3; IntAct=EBI-357275, EBI-372312; CC Q99471; P61289: PSME3; NbExp=6; IntAct=EBI-357275, EBI-355546; CC Q99471; Q8N443: RIBC1; NbExp=3; IntAct=EBI-357275, EBI-10265323; CC Q99471; Q0D2K3: RIPPLY1; NbExp=3; IntAct=EBI-357275, EBI-10226430; CC Q99471; Q7L4I2: RSRC2; NbExp=3; IntAct=EBI-357275, EBI-953753; CC Q99471; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-357275, EBI-6257312; CC Q99471; Q8IYX7: SAXO1; NbExp=3; IntAct=EBI-357275, EBI-3957636; CC Q99471; Q7Z5V6-2: SAXO4; NbExp=3; IntAct=EBI-357275, EBI-12000762; CC Q99471; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-357275, EBI-748391; CC Q99471; O00560: SDCBP; NbExp=3; IntAct=EBI-357275, EBI-727004; CC Q99471; Q6ZSJ9: SHISA6; NbExp=3; IntAct=EBI-357275, EBI-12037847; CC Q99471; Q8ND83: SLAIN1; NbExp=3; IntAct=EBI-357275, EBI-10269374; CC Q99471; Q8IYB5-2: SMAP1; NbExp=3; IntAct=EBI-357275, EBI-12061577; CC Q99471; Q9H0W8: SMG9; NbExp=3; IntAct=EBI-357275, EBI-2872322; CC Q99471; O95863: SNAI1; NbExp=3; IntAct=EBI-357275, EBI-1045459; CC Q99471; Q9BV90: SNRNP25; NbExp=3; IntAct=EBI-357275, EBI-9675976; CC Q99471; P14678-2: SNRPB; NbExp=3; IntAct=EBI-357275, EBI-372475; CC Q99471; Q5JUK2: SOHLH1; NbExp=3; IntAct=EBI-357275, EBI-12288855; CC Q99471; Q99932-2: SPAG8; NbExp=3; IntAct=EBI-357275, EBI-11959123; CC Q99471; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-357275, EBI-742688; CC Q99471; Q96LM5: SPMIP2; NbExp=3; IntAct=EBI-357275, EBI-12020542; CC Q99471; Q8N865: SPMIP4; NbExp=3; IntAct=EBI-357275, EBI-10174456; CC Q99471; B7ZLI8: STK19; NbExp=3; IntAct=EBI-357275, EBI-10176124; CC Q99471; Q9BSW7: SYT17; NbExp=3; IntAct=EBI-357275, EBI-745392; CC Q99471; Q9Y6J9: TAF6L; NbExp=3; IntAct=EBI-357275, EBI-743984; CC Q99471; O15119: TBX3; NbExp=3; IntAct=EBI-357275, EBI-3452216; CC Q99471; Q9Y242: TCF19; NbExp=3; IntAct=EBI-357275, EBI-7413767; CC Q99471; Q92734: TFG; NbExp=3; IntAct=EBI-357275, EBI-357061; CC Q99471; Q08117-2: TLE5; NbExp=3; IntAct=EBI-357275, EBI-11741437; CC Q99471; O75865-2: TRAPPC6A; NbExp=3; IntAct=EBI-357275, EBI-8451480; CC Q99471; Q9UIW0: VAX2; NbExp=3; IntAct=EBI-357275, EBI-12090999; CC Q99471; P61758: VBP1; NbExp=7; IntAct=EBI-357275, EBI-357430; CC Q99471; Q14119: VEZF1; NbExp=3; IntAct=EBI-357275, EBI-11980193; CC Q99471; Q99990: VGLL1; NbExp=3; IntAct=EBI-357275, EBI-11983165; CC Q99471; Q64LD2-2: WDR25; NbExp=3; IntAct=EBI-357275, EBI-12032042; CC Q99471; P62699: YPEL5; NbExp=3; IntAct=EBI-357275, EBI-11721624; CC Q99471; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-357275, EBI-14104088; CC Q99471; Q9UQR1-2: ZNF148; NbExp=3; IntAct=EBI-357275, EBI-11742222; CC Q99471; Q9DUN1: vIRF-3; Xeno; NbExp=8; IntAct=EBI-357275, EBI-1647907; CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus. CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Comment=Additional isoforms seem to exist.; CC Name=1; Synonyms=MM1-alpha; CC IsoId=Q99471-1; Sequence=Displayed; CC Name=2; Synonyms=MM1-beta; CC IsoId=Q99471-2; Sequence=VSP_043104; CC Name=3; Synonyms=MM1-gamma; CC IsoId=Q99471-3; Sequence=VSP_043103; CC -!- TISSUE SPECIFICITY: Highly expressed in pancreas and skeletal muscle CC and moderately in other tissues. CC -!- MISCELLANEOUS: [Isoform 2]: Does not repress transcription activity of CC MYC. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the prefoldin subunit alpha family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA14006.1; Type=Erroneous initiation; Evidence={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; D89667; BAA14006.1; ALT_INIT; mRNA. DR EMBL; AB055802; BAB32643.1; -; Genomic_DNA. DR EMBL; AB055803; BAB32644.1; -; mRNA. DR EMBL; AB055804; BAB32645.1; -; mRNA. DR EMBL; AB055805; BAB32646.1; -; mRNA. DR EMBL; BT007195; AAP35859.1; -; mRNA. DR EMBL; AK292623; BAF85312.1; -; mRNA. DR EMBL; AC073611; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471054; EAW96683.1; -; Genomic_DNA. DR EMBL; CH471054; EAW96685.1; -; Genomic_DNA. DR EMBL; BC003373; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC062671; AAH62671.1; -; mRNA. DR CCDS; CCDS8853.1; -. [Q99471-1] DR CCDS; CCDS8854.1; -. [Q99471-3] DR RefSeq; NP_002615.2; NM_002624.3. [Q99471-1] DR RefSeq; NP_665904.1; NM_145897.2. [Q99471-3] DR PDB; 6NR8; EM; 7.80 A; 5=11-137. DR PDB; 6NR9; EM; 8.50 A; 5=11-137. DR PDB; 6NRB; EM; 8.70 A; 5=11-137. DR PDB; 6NRC; EM; 8.30 A; 5=11-137. DR PDB; 6NRD; EM; 8.20 A; 5=11-137. DR PDB; 7WU7; EM; 3.85 A; 5=1-140. DR PDBsum; 6NR8; -. DR PDBsum; 6NR9; -. DR PDBsum; 6NRB; -. DR PDBsum; 6NRC; -. DR PDBsum; 6NRD; -. DR PDBsum; 7WU7; -. DR AlphaFoldDB; Q99471; -. DR EMDB; EMD-0490; -. DR EMDB; EMD-0491; -. DR EMDB; EMD-0493; -. DR EMDB; EMD-0494; -. DR EMDB; EMD-0495; -. DR EMDB; EMD-32823; -. DR SMR; Q99471; -. DR BioGRID; 111226; 308. DR ComplexPortal; CPX-6149; Prefoldin co-chaperone complex. DR CORUM; Q99471; -. DR DIP; DIP-28155N; -. DR IntAct; Q99471; 165. DR MINT; Q99471; -. DR STRING; 9606.ENSP00000447942; -. DR GlyGen; Q99471; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q99471; -. DR PhosphoSitePlus; Q99471; -. DR SwissPalm; Q99471; -. DR BioMuta; PFDN5; -. DR DMDM; 12231038; -. DR OGP; Q99471; -. DR EPD; Q99471; -. DR jPOST; Q99471; -. DR MassIVE; Q99471; -. DR MaxQB; Q99471; -. DR PaxDb; 9606-ENSP00000447942; -. DR PeptideAtlas; Q99471; -. DR ProteomicsDB; 78287; -. [Q99471-1] DR ProteomicsDB; 78288; -. [Q99471-2] DR ProteomicsDB; 78289; -. [Q99471-3] DR Pumba; Q99471; -. DR TopDownProteomics; Q99471-1; -. [Q99471-1] DR TopDownProteomics; Q99471-3; -. [Q99471-3] DR Antibodypedia; 1782; 291 antibodies from 28 providers. DR DNASU; 5204; -. DR Ensembl; ENST00000243040.10; ENSP00000243040.6; ENSG00000123349.15. [Q99471-2] DR Ensembl; ENST00000334478.9; ENSP00000334188.4; ENSG00000123349.15. [Q99471-1] DR Ensembl; ENST00000351500.7; ENSP00000266964.4; ENSG00000123349.15. [Q99471-3] DR Ensembl; ENST00000551018.5; ENSP00000447942.1; ENSG00000123349.15. [Q99471-1] DR Ensembl; ENST00000708922.1; ENSP00000517421.1; ENSG00000291834.1. [Q99471-1] DR Ensembl; ENST00000708930.1; ENSP00000517425.1; ENSG00000291834.1. [Q99471-3] DR Ensembl; ENST00000708936.1; ENSP00000517428.1; ENSG00000291834.1. [Q99471-2] DR Ensembl; ENST00000708937.1; ENSP00000517429.1; ENSG00000291834.1. [Q99471-1] DR GeneID; 5204; -. DR KEGG; hsa:5204; -. DR MANE-Select; ENST00000334478.9; ENSP00000334188.4; NM_002624.4; NP_002615.2. DR UCSC; uc001scl.5; human. [Q99471-1] DR AGR; HGNC:8869; -. DR CTD; 5204; -. DR DisGeNET; 5204; -. DR GeneCards; PFDN5; -. DR HGNC; HGNC:8869; PFDN5. DR HPA; ENSG00000123349; Low tissue specificity. DR MIM; 604899; gene. DR neXtProt; NX_Q99471; -. DR OpenTargets; ENSG00000123349; -. DR PharmGKB; PA33210; -. DR VEuPathDB; HostDB:ENSG00000123349; -. DR eggNOG; KOG3048; Eukaryota. DR GeneTree; ENSGT00390000008783; -. DR HOGENOM; CLU_091867_0_1_1; -. DR InParanoid; Q99471; -. DR OMA; TGYYVEN; -. DR OrthoDB; 241387at2759; -. DR PhylomeDB; Q99471; -. DR TreeFam; TF106509; -. DR PathwayCommons; Q99471; -. DR Reactome; R-HSA-389957; Prefoldin mediated transfer of substrate to CCT/TriC. DR SignaLink; Q99471; -. DR SIGNOR; Q99471; -. DR BioGRID-ORCS; 5204; 494 hits in 1171 CRISPR screens. DR ChiTaRS; PFDN5; human. DR GeneWiki; PFDN5; -. DR GenomeRNAi; 5204; -. DR Pharos; Q99471; Tbio. DR PRO; PR:Q99471; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q99471; Protein. DR Bgee; ENSG00000123349; Expressed in pituitary gland and 99 other cell types or tissues. DR ExpressionAtlas; Q99471; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA. DR GO; GO:0005634; C:nucleus; TAS:ProtInc. DR GO; GO:0016272; C:prefoldin complex; IDA:FlyBase. DR GO; GO:0001540; F:amyloid-beta binding; IDA:FlyBase. DR GO; GO:0003714; F:transcription corepressor activity; TAS:ProtInc. 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:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:BHF-UCL. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IMP:BHF-UCL. DR GO; GO:0006457; P:protein folding; IDA:FlyBase. DR GO; GO:0006355; P:regulation of DNA-templated transcription; TAS:ProtInc. DR GO; GO:0060041; P:retina development in camera-type eye; IEA:Ensembl. DR GO; GO:1990113; P:RNA polymerase I assembly; IBA:GO_Central. DR GO; GO:1990114; P:RNA polymerase II core complex assembly; IBA:GO_Central. DR GO; GO:1990115; P:RNA polymerase III assembly; IBA:GO_Central. DR CDD; cd00584; Prefoldin_alpha; 1. DR Gene3D; 1.10.287.370; -; 1. DR HAMAP; MF_00308; PfdA; 1. DR InterPro; IPR011599; PFD_alpha_archaea. DR InterPro; IPR009053; Prefoldin. DR InterPro; IPR004127; Prefoldin_subunit_alpha. DR NCBIfam; TIGR00293; prefoldin subunit alpha; 1. DR PANTHER; PTHR12674; PREFOLDIN SUBUNIT 5; 1. DR PANTHER; PTHR12674:SF2; PREFOLDIN SUBUNIT 5; 1. DR Pfam; PF02996; Prefoldin; 1. DR SUPFAM; SSF46579; Prefoldin; 1. DR Genevisible; Q99471; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Chaperone; Cytoplasm; KW Nucleus; Phosphoprotein; Reference proteome. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895" FT CHAIN 2..154 FT /note="Prefoldin subunit 5" FT /id="PRO_0000153661" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:22223895" FT MOD_RES 42 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 56 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 25..69 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:16173081" FT /id="VSP_043103" FT VAR_SEQ 59..154 FT /note="GKELLVPLTSSMYVPGKLHDVEHVLIDVGTGYYVEKTAEDAKDFFKRKIDFL FT TKQMEKIQPALQEKHAMKQAVMEMMSQKIQQLTALGAAQATAKA -> DVCPWEAA FT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16173081" FT /id="VSP_043104" SQ SEQUENCE 154 AA; 17328 MW; 0DA1F3644548CB14 CRC64; MAQSINITEL NLPQLEMLKN QLDQEVEFLS TSIAQLKVVQ TKYVEAKDCL NVLNKSNEGK ELLVPLTSSM YVPGKLHDVE HVLIDVGTGY YVEKTAEDAK DFFKRKIDFL TKQMEKIQPA LQEKHAMKQA VMEMMSQKIQ QLTALGAAQA TAKA //