P61758 (PFD3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Prefoldin subunit 3

Alternative name(s):
HIBBJ46
Von Hippel-Lindau-binding protein 1
Short name=VBP-1
Short name=VHL-binding protein 1

Gene names

Name:	VBP1
Synonyms:	PFDN3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	197 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. Ref.2
Subunit structure	Heterohexamer of two PFD-alpha type and four PFD-beta type subunits. Binds to the C-terminal part of VHL.
Subcellular location	Cytoplasm. Nucleus. Note: In complex with VHL can translocate to the nucleus.
Tissue specificity	Ubiquitous.
Sequence similarities	Belongs to the prefoldin subunit alpha family.
Sequence caution	The sequence AAC23907.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Molecular function	Chaperone
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	'de novo' posttranslational protein folding Traceable author statement. Source: Reactome
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell prefoldin complex Inferred from electronic annotation. Source: InterPro
Molecular function	unfolded protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 197	197	Prefoldin subunit 3		PRO_0000153652
Amino acid modifications
	Modified residue	59	1	N6-acetyllysine Ref.8
Natural variations
	Natural variant	123	1	M → V. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6 Ref.7 Corresponds to variant rs572013 [ dbSNP | Ensembl ].		VAR_023371

Sequences

	Sequence		Length	Mass (Da)
	P61758 [UniParc]. Last modified February 6, 2007. Version 3. Checksum: 973BBDE2B3903E39	FASTA	197	22,658
	10 20 30 40 50 60 MAAVKDSCGK GEMATGNGRR LHLGIPEAVF VEDVDSFMKQ PGNETADTVL KKLDEQYQKY 70 80 90 100 110 120 KFMELNLAQK KRRLKGQIPE IKQTLEILKY MQKKKESTNS METRFLLADN LYCKASVPPT 130 140 150 160 170 180 DKMCLWLGAN VMLEYDIDEA QALLEKNLST ATKNLDSLEE DLDFLRDQFT TTEVNMARVY 190 NWDVKRRNKD DSTKNKA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of the gene (VBP1) and transcript for the von Hippel-Lindau binding protein and isolation of the highly conserved murine homologue." Brinke A., Green P.M., Giannelli F. Genomics 45:105-112(1997) [PubMed: 9339366] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-123. Tissue: Brain.
[2]	"Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin." Vainberg I.E., Lewis S.A., Rommelaere H., Ampe C., Vandekerckhove J., Klein H.L., Cowan N.J. Cell 93:863-873(1998) [PubMed: 9630229] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-123, FUNCTION.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-123. Tissue: Cerebellum.
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-123.
[5]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT VAL-123. Tissue: Lung.
[7]	"Identification of a novel protein (VBP-1) binding to the von Hippel-Lindau (VHL) tumor suppressor gene product." Tsuchiya H., Iseda T., Hino O. Cancer Res. 56:2881-2885(1996) [PubMed: 8674032] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-197, VARIANT VAL-123.
[8]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-59, MASS SPECTROMETRY.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U96759 mRNA. Translation: AAC23907.1. Different initiation. Y17394 mRNA. Translation: CAA76761.1. AK313420 mRNA. Translation: BAG36212.1. BT019604 mRNA. Translation: AAV38411.1. AL356738 Genomic DNA. Translation: CAI41469.1. BC046094 mRNA. Translation: AAH46094.1. U56833 mRNA. Translation: AAC50617.1.
IPI	IPI00334159.
RefSeq	NP_003363.1. NM_003372.5.
UniGene	Hs.436803.
3D structure databases
ProteinModelPortal	P61758.
SMR	P61758. Positions 47-178.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-46479N.
IntAct	P61758. 5 interactions.
MINT	MINT-1148501.
STRING	P61758.
PTM databases
PhosphoSite	P61758.
Polymorphism databases
DMDM	125987848.
2D gel databases
OGP	P61758.
Proteomic databases
PRIDE	P61758.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000286428; ENSP00000286428; ENSG00000155959.
GeneID	7411.
KEGG	hsa:7411.
NMPDR	fig|9606.3.peg.33684.
UCSC	uc004fnc.1. human.
Organism-specific databases
CTD	7411.
GeneCards	GC0XP154444.
HGNC	HGNC:12662. VBP1.
HPA	CAB006260. HPA023230.
MIM	300133. gene.
neXtProt	NX_P61758.
PharmGKB	PA37285.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG04614.
HOGENOM	HBG631514.
HOVERGEN	HBG053576.
InParanoid	P61758.
OMA	QITTTEV.
OrthoDB	EOG4DBTFP.
PhylomeDB	P61758.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
Gene expression databases
ArrayExpress	P61758.
Bgee	P61758.
CleanEx	HS_VBP1.
Genevestigator	P61758.
GermOnline	ENSG00000155959. Homo sapiens.
Family and domain databases
InterPro	IPR009053. Prefoldin. IPR016655. Prefoldin_su-3. IPR004127. Prefoldin_subunit. [Graphical view]
PANTHER	PTHR12409. PTHR12409. 1 hit.
Pfam	PF02996. Prefoldin. 1 hit. [Graphical view]
PIRSF	PIRSF016396. Prefoldin_subunit_3. 1 hit.
SUPFAM	SSF46579. Prefoldin. 1 hit.
ProtoNet	Search...
Other
NextBio	29016.
SOURCE	Search...

Entry information

Entry name

PFD3_HUMAN

Accession

Primary (citable) accession number: P61758
Secondary accession number(s): B2R8L5 , O55228, Q15765, Q5JT81, Q86X96

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2004
Last sequence update:	February 6, 2007
Last modified:	January 25, 2012
This is version 72 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.