Full text data of VBP1
VBP1
(PFDN3)
[Confidence: low (only semi-automatic identification from reviews)]
Prefoldin subunit 3 (HIBBJ46; Von Hippel-Lindau-binding protein 1; VBP-1; VHL-binding protein 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Prefoldin subunit 3 (HIBBJ46; Von Hippel-Lindau-binding protein 1; VBP-1; VHL-binding protein 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P61758
ID PFD3_HUMAN Reviewed; 197 AA.
AC P61758; B2R8L5; O55228; Q15765; Q5JT81; Q86X96;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 06-FEB-2007, sequence version 3.
DT 22-JAN-2014, entry version 90.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-123.
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
RT Hippel-Lindau binding protein and isolation of the highly conserved
RT murine homologue.";
RL Genomics 45:105-112(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-123, 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], AND VARIANT VAL-123.
RC TISSUE=Cerebellum;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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], AND VARIANT VAL-123.
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
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA 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.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA 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.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA 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.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA 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.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., 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], AND VARIANT VAL-123.
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-197, AND VARIANT VAL-123.
RX PubMed=8674032;
RA Tsuchiya H., Iseda T., Hino O.;
RT "Identification of a novel protein (VBP-1) binding to the von Hippel-
RT Lindau (VHL) tumor suppressor gene product.";
RL Cancer Res. 56:2881-2885(1996).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-59, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
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 [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. Binds to the C-terminal part of VHL.
CC -!- INTERACTION:
CC Q9Q2G4:ORF (xeno); NbExp=3; IntAct=EBI-357430, EBI-6248094;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=In complex with VHL
CC can translocate to the nucleus.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the prefoldin subunit alpha family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC23907.1; Type=Erroneous initiation;
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DR EMBL; U96759; AAC23907.1; ALT_INIT; mRNA.
DR EMBL; Y17394; CAA76761.1; -; mRNA.
DR EMBL; AK313420; BAG36212.1; -; mRNA.
DR EMBL; BT019604; AAV38411.1; -; mRNA.
DR EMBL; AL356738; CAI41469.1; -; Genomic_DNA.
DR EMBL; BC046094; AAH46094.1; -; mRNA.
DR EMBL; U56833; AAC50617.1; -; mRNA.
DR RefSeq; NP_003363.1; NM_003372.5.
DR UniGene; Hs.436803; -.
DR ProteinModelPortal; P61758; -.
DR SMR; P61758; 47-178.
DR DIP; DIP-46479N; -.
DR IntAct; P61758; 10.
DR MINT; MINT-1148501; -.
DR STRING; 9606.ENSP00000286428; -.
DR PhosphoSite; P61758; -.
DR DMDM; 125987848; -.
DR OGP; P61758; -.
DR PaxDb; P61758; -.
DR PRIDE; P61758; -.
DR DNASU; 7411; -.
DR Ensembl; ENST00000286428; ENSP00000286428; ENSG00000155959.
DR Ensembl; ENST00000601657; ENSP00000472021; ENSG00000268440.
DR GeneID; 7411; -.
DR KEGG; hsa:7411; -.
DR UCSC; uc004fnd.3; human.
DR CTD; 7411; -.
DR GeneCards; GC0XP154444; -.
DR HGNC; HGNC:12662; VBP1.
DR HPA; CAB006260; -.
DR HPA; HPA023230; -.
DR MIM; 300133; gene.
DR neXtProt; NX_P61758; -.
DR PharmGKB; PA37285; -.
DR eggNOG; NOG237266; -.
DR HOVERGEN; HBG053576; -.
DR InParanoid; P61758; -.
DR OMA; LENCEED; -.
DR PhylomeDB; P61758; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR GenomeRNAi; 7411; -.
DR NextBio; 29016; -.
DR PRO; PR:P61758; -.
DR ArrayExpress; P61758; -.
DR Bgee; P61758; -.
DR CleanEx; HS_VBP1; -.
DR Genevestigator; P61758; -.
DR GO; GO:0005737; C:cytoplasm; 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:0016272; C:prefoldin complex; IEA:InterPro.
DR GO; GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
DR InterPro; IPR009053; Prefoldin.
DR InterPro; IPR016655; Prefoldin_su-3.
DR InterPro; IPR004127; Prefoldin_subunit_alpha.
DR PANTHER; PTHR12409; PTHR12409; 1.
DR Pfam; PF02996; Prefoldin; 1.
DR PIRSF; PIRSF016396; Prefoldin_subunit_3; 1.
DR SUPFAM; SSF46579; SSF46579; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Complete proteome; Cytoplasm; Nucleus;
KW Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 197 Prefoldin subunit 3.
FT /FTId=PRO_0000153652.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 59 59 N6-acetyllysine.
FT VARIANT 123 123 M -> V (in dbSNP:rs572013).
FT /FTId=VAR_023371.
SQ SEQUENCE 197 AA; 22658 MW; 973BBDE2B3903E39 CRC64;
MAAVKDSCGK GEMATGNGRR LHLGIPEAVF VEDVDSFMKQ PGNETADTVL KKLDEQYQKY
KFMELNLAQK KRRLKGQIPE IKQTLEILKY MQKKKESTNS METRFLLADN LYCKASVPPT
DKMCLWLGAN VMLEYDIDEA QALLEKNLST ATKNLDSLEE DLDFLRDQFT TTEVNMARVY
NWDVKRRNKD DSTKNKA
//
ID PFD3_HUMAN Reviewed; 197 AA.
AC P61758; B2R8L5; O55228; Q15765; Q5JT81; Q86X96;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 06-FEB-2007, sequence version 3.
DT 22-JAN-2014, entry version 90.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-123.
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
RT Hippel-Lindau binding protein and isolation of the highly conserved
RT murine homologue.";
RL Genomics 45:105-112(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-123, 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], AND VARIANT VAL-123.
RC TISSUE=Cerebellum;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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], AND VARIANT VAL-123.
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
RT vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.,
RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
RA 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.,
RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
RA 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.,
RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
RA 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.,
RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
RA Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
RA 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.,
RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
RA Gibbs R.A., Beck S., 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], AND VARIANT VAL-123.
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-197, AND VARIANT VAL-123.
RX PubMed=8674032;
RA Tsuchiya H., Iseda T., Hino O.;
RT "Identification of a novel protein (VBP-1) binding to the von Hippel-
RT Lindau (VHL) tumor suppressor gene product.";
RL Cancer Res. 56:2881-2885(1996).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-59, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., 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.,
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 [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. Binds to the C-terminal part of VHL.
CC -!- INTERACTION:
CC Q9Q2G4:ORF (xeno); NbExp=3; IntAct=EBI-357430, EBI-6248094;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=In complex with VHL
CC can translocate to the nucleus.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the prefoldin subunit alpha family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC23907.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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DR EMBL; U96759; AAC23907.1; ALT_INIT; mRNA.
DR EMBL; Y17394; CAA76761.1; -; mRNA.
DR EMBL; AK313420; BAG36212.1; -; mRNA.
DR EMBL; BT019604; AAV38411.1; -; mRNA.
DR EMBL; AL356738; CAI41469.1; -; Genomic_DNA.
DR EMBL; BC046094; AAH46094.1; -; mRNA.
DR EMBL; U56833; AAC50617.1; -; mRNA.
DR RefSeq; NP_003363.1; NM_003372.5.
DR UniGene; Hs.436803; -.
DR ProteinModelPortal; P61758; -.
DR SMR; P61758; 47-178.
DR DIP; DIP-46479N; -.
DR IntAct; P61758; 10.
DR MINT; MINT-1148501; -.
DR STRING; 9606.ENSP00000286428; -.
DR PhosphoSite; P61758; -.
DR DMDM; 125987848; -.
DR OGP; P61758; -.
DR PaxDb; P61758; -.
DR PRIDE; P61758; -.
DR DNASU; 7411; -.
DR Ensembl; ENST00000286428; ENSP00000286428; ENSG00000155959.
DR Ensembl; ENST00000601657; ENSP00000472021; ENSG00000268440.
DR GeneID; 7411; -.
DR KEGG; hsa:7411; -.
DR UCSC; uc004fnd.3; human.
DR CTD; 7411; -.
DR GeneCards; GC0XP154444; -.
DR HGNC; HGNC:12662; VBP1.
DR HPA; CAB006260; -.
DR HPA; HPA023230; -.
DR MIM; 300133; gene.
DR neXtProt; NX_P61758; -.
DR PharmGKB; PA37285; -.
DR eggNOG; NOG237266; -.
DR HOVERGEN; HBG053576; -.
DR InParanoid; P61758; -.
DR OMA; LENCEED; -.
DR PhylomeDB; P61758; -.
DR Reactome; REACT_17015; Metabolism of proteins.
DR GenomeRNAi; 7411; -.
DR NextBio; 29016; -.
DR PRO; PR:P61758; -.
DR ArrayExpress; P61758; -.
DR Bgee; P61758; -.
DR CleanEx; HS_VBP1; -.
DR Genevestigator; P61758; -.
DR GO; GO:0005737; C:cytoplasm; 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:0016272; C:prefoldin complex; IEA:InterPro.
DR GO; GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
DR InterPro; IPR009053; Prefoldin.
DR InterPro; IPR016655; Prefoldin_su-3.
DR InterPro; IPR004127; Prefoldin_subunit_alpha.
DR PANTHER; PTHR12409; PTHR12409; 1.
DR Pfam; PF02996; Prefoldin; 1.
DR PIRSF; PIRSF016396; Prefoldin_subunit_3; 1.
DR SUPFAM; SSF46579; SSF46579; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chaperone; Complete proteome; Cytoplasm; Nucleus;
KW Polymorphism; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 197 Prefoldin subunit 3.
FT /FTId=PRO_0000153652.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 59 59 N6-acetyllysine.
FT VARIANT 123 123 M -> V (in dbSNP:rs572013).
FT /FTId=VAR_023371.
SQ SEQUENCE 197 AA; 22658 MW; 973BBDE2B3903E39 CRC64;
MAAVKDSCGK GEMATGNGRR LHLGIPEAVF VEDVDSFMKQ PGNETADTVL KKLDEQYQKY
KFMELNLAQK KRRLKGQIPE IKQTLEILKY MQKKKESTNS METRFLLADN LYCKASVPPT
DKMCLWLGAN VMLEYDIDEA QALLEKNLST ATKNLDSLEE DLDFLRDQFT TTEVNMARVY
NWDVKRRNKD DSTKNKA
//
MIM
300133
*RECORD*
*FIELD* NO
300133
*FIELD* TI
*300133 VON HIPPEL-LINDAU BINDING PROTEIN 1; VBP1
;;PREFOLDIN 3; PFDN3
*FIELD* TX
read moreCLONING
Von Hippel-Lindau syndrome (193300) is associated with mutations in the
VHL gene (608537), which encodes a tumor suppressor. Using a yeast
2-hybrid assay to screen for proteins that interact with VHL, Tsuchiya
et al. (1996) identified B-cell cDNAs encoding a protein they called
VBP1 (VHL binding protein-1). By immunoprecipitation studies and Western
analysis, the authors demonstrated that VBP1 forms complexes with VHL in
vivo. By immunocytolocalization in mammalian cells expressing one or
both proteins, Tsuchiya et al. (1996) found that VHL acts as a molecular
chaperone that carries VBP1 from perinuclear granules to the nucleus or
cytoplasm.
Brinke et al. (1996) reported the presence of a novel inversion in the
factor VIII (300841) gene in hemophilic monozygotic twins. Brinke et al.
(1996) noted that this novel inversion creates 2 hybrid transcription
units. One of these is formed by the promoter and first exon of factor
VIII and novel sequences. Brinke et al. (1997) determined that these
novel sequences were part of the VBP1 gene. Northern blot analysis
revealed that VBP1 is ubiquitously expressed as a 1.7-kb mRNA and a much
weaker 5.0-kb mRNA. By primer extension analysis, Brinke et al. (1997)
found that there are 2 major and 1 minor transcription start sites.
Brinke et al. (1997) cloned cDNAs of the mouse VBP1 homolog. The
160-amino acid mouse and human VBP1 protein sequences were identical.
Hemberger et al. (1999) used murine Vbp1 cDNA to investigate the
expression of the Vbp1 mRNA in the mouse by in situ hybridization and
Northern blot analysis. In fetal stages between days 9 and 18 of
gestation, Vbp1 was expressed mainly in the central nervous system,
retina, and liver. In addition, at day 12, high expression was observed
in the labyrinthine region of the placenta. In later stage placentas,
Vbp1 expression was, however, considerably reduced. Northern blot
analysis of adult mouse tissues showed that Vbp1 was ubiquitously
expressed. In situ analysis of several adult tissues showed that in most
tissues the transcripts were evenly distributed. In brain, eye, kidney,
and intestine, however, Vbp1 was expressed in specific cell types. In
cerebellum and various tumors of VHL patients, no consistent differences
in VBP1 expression levels could be detected between tumors
characteristic of von Hippel-Lindau disease and normal tissue.
GENE STRUCTURE
Brinke et al. (1997) determined that the VBP1 gene contains 6 exons and
spans at least 30 kb.
MAPPING
By analysis of a YAC contig, Brinke et al. (1997) mapped the VBP1 gene
to Xq28, 100 to 150 kb distal to the factor VIII gene.
Mapping of the murine Vbp1 gene revealed conserved chromosomal
localization between mouse and human in a region homologous to human
Xq28 (Hemberger et al., 1999).
MOLECULAR GENETICS
Clifford et al. (1999) could demonstrate no mutation in VBP1 in 89
sporadic cases of renal cell carcinoma.
*FIELD* RF
1. Brinke, A.; Green, P. M.; Giannelli, F.: Characterization of the
gene (VBP1) and transcript for the von Hippel-Lindau binding protein
and isolation of the highly conserved murine homologue. Genomics 45:
105-112, 1997.
2. Brinke, A.; Tagliavacca, L.; Naylor, J.; Green, P.; Giangrande,
P.; Giannelli, F.: Two chimaeric transcription units result from
an inversion breaking intron 1 of the factor VIII gene and a region
reportedly affected by reciprocal translocations in T-cell leukaemia. Hum.
Molec. Genet. 5: 1945-1951, 1996.
3. Clifford, S. C.; Walsh, S.; Hewson, K.; Green, E. K.; Brinke, A.;
Green, P. M.; Gianelli, F.; Eng, C.; Maher, E. R.: Genomic organization
and chromosomal localization of the human CUL2 gene and the role of
von Hippel-Lindau tumor suppressor-binding protein (CUL2 and VBP1)
mutation and loss in renal-cell carcinoma development. Genes Chromosomes
Cancer 26: 20-28, 1999.
4. Hemberger, M.; Himmelbauer, H.; Neumann, H. P. H.; Plate, K. H.;
Schwarzkopf, G.; Fundele, R.: Expression of the von Hippel-Lindau-binding
protein-1 (Vbp1) in fetal and adult mouse tissues. Hum. Molec. Genet. 8:
229-236, 1999.
5. Tsuchiya, H.; Iseda, T.; Hino, O.: Identification of a novel protein
(VBP-1) binding to the von Hippel-Lindau (VHL) tumor suppressor gene
product. Cancer Res. 56: 2881-2885, 1996.
*FIELD* CN
Victor A. McKusick - updated: 11/1/1999
Victor A. McKusick - updated: 3/8/1999
*FIELD* CD
Rebekah S. Rasooly: 6/22/1998
*FIELD* ED
carol: 04/07/2011
ckniffin: 3/23/2004
joanna: 3/8/2002
carol: 11/9/1999
terry: 11/1/1999
carol: 3/25/1999
terry: 3/8/1999
alopez: 6/22/1998
*RECORD*
*FIELD* NO
300133
*FIELD* TI
*300133 VON HIPPEL-LINDAU BINDING PROTEIN 1; VBP1
;;PREFOLDIN 3; PFDN3
*FIELD* TX
read moreCLONING
Von Hippel-Lindau syndrome (193300) is associated with mutations in the
VHL gene (608537), which encodes a tumor suppressor. Using a yeast
2-hybrid assay to screen for proteins that interact with VHL, Tsuchiya
et al. (1996) identified B-cell cDNAs encoding a protein they called
VBP1 (VHL binding protein-1). By immunoprecipitation studies and Western
analysis, the authors demonstrated that VBP1 forms complexes with VHL in
vivo. By immunocytolocalization in mammalian cells expressing one or
both proteins, Tsuchiya et al. (1996) found that VHL acts as a molecular
chaperone that carries VBP1 from perinuclear granules to the nucleus or
cytoplasm.
Brinke et al. (1996) reported the presence of a novel inversion in the
factor VIII (300841) gene in hemophilic monozygotic twins. Brinke et al.
(1996) noted that this novel inversion creates 2 hybrid transcription
units. One of these is formed by the promoter and first exon of factor
VIII and novel sequences. Brinke et al. (1997) determined that these
novel sequences were part of the VBP1 gene. Northern blot analysis
revealed that VBP1 is ubiquitously expressed as a 1.7-kb mRNA and a much
weaker 5.0-kb mRNA. By primer extension analysis, Brinke et al. (1997)
found that there are 2 major and 1 minor transcription start sites.
Brinke et al. (1997) cloned cDNAs of the mouse VBP1 homolog. The
160-amino acid mouse and human VBP1 protein sequences were identical.
Hemberger et al. (1999) used murine Vbp1 cDNA to investigate the
expression of the Vbp1 mRNA in the mouse by in situ hybridization and
Northern blot analysis. In fetal stages between days 9 and 18 of
gestation, Vbp1 was expressed mainly in the central nervous system,
retina, and liver. In addition, at day 12, high expression was observed
in the labyrinthine region of the placenta. In later stage placentas,
Vbp1 expression was, however, considerably reduced. Northern blot
analysis of adult mouse tissues showed that Vbp1 was ubiquitously
expressed. In situ analysis of several adult tissues showed that in most
tissues the transcripts were evenly distributed. In brain, eye, kidney,
and intestine, however, Vbp1 was expressed in specific cell types. In
cerebellum and various tumors of VHL patients, no consistent differences
in VBP1 expression levels could be detected between tumors
characteristic of von Hippel-Lindau disease and normal tissue.
GENE STRUCTURE
Brinke et al. (1997) determined that the VBP1 gene contains 6 exons and
spans at least 30 kb.
MAPPING
By analysis of a YAC contig, Brinke et al. (1997) mapped the VBP1 gene
to Xq28, 100 to 150 kb distal to the factor VIII gene.
Mapping of the murine Vbp1 gene revealed conserved chromosomal
localization between mouse and human in a region homologous to human
Xq28 (Hemberger et al., 1999).
MOLECULAR GENETICS
Clifford et al. (1999) could demonstrate no mutation in VBP1 in 89
sporadic cases of renal cell carcinoma.
*FIELD* RF
1. Brinke, A.; Green, P. M.; Giannelli, F.: Characterization of the
gene (VBP1) and transcript for the von Hippel-Lindau binding protein
and isolation of the highly conserved murine homologue. Genomics 45:
105-112, 1997.
2. Brinke, A.; Tagliavacca, L.; Naylor, J.; Green, P.; Giangrande,
P.; Giannelli, F.: Two chimaeric transcription units result from
an inversion breaking intron 1 of the factor VIII gene and a region
reportedly affected by reciprocal translocations in T-cell leukaemia. Hum.
Molec. Genet. 5: 1945-1951, 1996.
3. Clifford, S. C.; Walsh, S.; Hewson, K.; Green, E. K.; Brinke, A.;
Green, P. M.; Gianelli, F.; Eng, C.; Maher, E. R.: Genomic organization
and chromosomal localization of the human CUL2 gene and the role of
von Hippel-Lindau tumor suppressor-binding protein (CUL2 and VBP1)
mutation and loss in renal-cell carcinoma development. Genes Chromosomes
Cancer 26: 20-28, 1999.
4. Hemberger, M.; Himmelbauer, H.; Neumann, H. P. H.; Plate, K. H.;
Schwarzkopf, G.; Fundele, R.: Expression of the von Hippel-Lindau-binding
protein-1 (Vbp1) in fetal and adult mouse tissues. Hum. Molec. Genet. 8:
229-236, 1999.
5. Tsuchiya, H.; Iseda, T.; Hino, O.: Identification of a novel protein
(VBP-1) binding to the von Hippel-Lindau (VHL) tumor suppressor gene
product. Cancer Res. 56: 2881-2885, 1996.
*FIELD* CN
Victor A. McKusick - updated: 11/1/1999
Victor A. McKusick - updated: 3/8/1999
*FIELD* CD
Rebekah S. Rasooly: 6/22/1998
*FIELD* ED
carol: 04/07/2011
ckniffin: 3/23/2004
joanna: 3/8/2002
carol: 11/9/1999
terry: 11/1/1999
carol: 3/25/1999
terry: 3/8/1999
alopez: 6/22/1998