Q99471 (PFD5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Prefoldin subunit 5

Alternative name(s):
C-Myc-binding protein Mm-1
Myc modulator 1

Gene names

Name:	PFDN5
Synonyms:	MM1, PFD5

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	154 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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.7
Subunit structure	Heterohexamer of two PFD-alpha type and four PFD-beta type subunits. Binds to MYC; interacts with its N-terminal domain. Represses the transcriptional activity of MYC.
Tissue specificity	Highly expressed in pancreas and skeletal muscle and moderately in other tissues.
Sequence similarities	Belongs to the prefoldin subunit alpha family.
Sequence caution	The sequence BAA14006.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
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 negative regulation of canonical Wnt receptor signaling pathway Inferred from mutant phenotype. Source: BHF-UCL negative regulation of transcription, DNA-dependent Inferred from mutant phenotype. Source: BHF-UCL
Cellular component	nucleus Traceable author statement. Source: ProtInc prefoldin complex Inferred from electronic annotation. Source: InterPro
Molecular function	transcription corepressor activity Traceable author statement. Source: ProtInc unfolded protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
vIRF-3	Q9DUN1	8	EBI-1047551,EBI-1647907	From a different organism.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 154	153	Prefoldin subunit 5		PRO_0000153661
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.8
	Modified residue	42	1	N6-acetyllysine Ref.9
	Modified residue	112	1	N6-acetyllysine Ref.9

Sequences

	Sequence		Length	Mass (Da)
	Q99471 [UniParc]. Last modified January 11, 2001. Version 2. Checksum: 0DA1F3644548CB14	FASTA	154	17,328
	10 20 30 40 50 60 MAQSINITEL NLPQLEMLKN QLDQEVEFLS TSIAQLKVVQ TKYVEAKDCL NVLNKSNEGK 70 80 90 100 110 120 ELLVPLTSSM YVPGKLHDVE HVLIDVGTGY YVEKTAEDAK DFFKRKIDFL TKQMEKIQPA 130 140 150 LQEKHAMKQA VMEMMSQKIQ QLTALGAAQA TAKA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"MM-1, a novel c-Myc-associating protein that represses transcriptional activity of c-Myc." Mori K., Maeda Y., Kitaura H., Taira T., Iguchi-Ariga S.M., Ariga H. J. Biol. Chem. 273:29794-29800(1998) [PubMed: 9792694] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Brain.
[2]	"MM-1, a c-Myc-binding protein, is a candidate for a tumor suppressor in leukemia/lymphoma and tongue cancer." Fujioka Y., Taira T., Maeda Y., Tanaka S., Nishihara H., Iguchi-Ariga S.M.M., Nagashima K., Ariga H. J. Biol. Chem. 276:45137-45144(2001) [PubMed: 11567024] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Blood and Fibroblast.
[3]	"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 (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"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]. Tissue: Thymus.
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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]. Tissue: Placenta.
[7]	"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: FUNCTION.
[8]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[9]	"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-42 AND LYS-112, MASS SPECTROMETRY.
[10]	"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].

Cross-references

Sequence databases
EMBL GenBank DDBJ	D89667 mRNA. Translation: BAA14006.1. Different initiation. AB055802 Genomic DNA. Translation: BAB32643.1. AB055803 mRNA. Translation: BAB32644.1. BT007195 mRNA. Translation: AAP35859.1. AK292623 mRNA. Translation: BAF85312.1. CH471054 Genomic DNA. Translation: EAW96683.1. BC003373 mRNA. No translation available. BC062671 mRNA. Translation: AAH62671.1.
IPI	IPI00015361.
RefSeq	NP_002615.2. NM_002624.3.
UniGene	Hs.655327.
3D structure databases
ProteinModelPortal	Q99471.
SMR	Q99471. Positions 11-144.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-28155N.
IntAct	Q99471. 9 interactions.
STRING	Q99471.
PTM databases
PhosphoSite	Q99471.
Polymorphism databases
DMDM	12231038.
2D gel databases
OGP	Q99471.
Proteomic databases
PeptideAtlas	Q99471.
PRIDE	Q99471.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000334478; ENSP00000334188; ENSG00000123349.
GeneID	5204.
KEGG	hsa:5204.
UCSC	uc001scl.1. human.
Organism-specific databases
CTD	5204.
GeneCards	GC12P053689.
H-InvDB	HIX0010679.
HGNC	HGNC:8869. PFDN5.
HPA	HPA008587.
MIM	604899. gene.
neXtProt	NX_Q99471.
PharmGKB	PA33210.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG18523.
GeneTree	ENSGT00390000008783.
HOGENOM	HBG522331.
HOVERGEN	HBG004539.
InParanoid	Q99471.
OMA	KDYFKRR.
OrthoDB	EOG415GFQ.
PhylomeDB	Q99471.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
Gene expression databases
ArrayExpress	Q99471.
Bgee	Q99471.
CleanEx	HS_PFDN5.
Genevestigator	Q99471.
GermOnline	ENSG00000123349. Homo sapiens.
Family and domain databases
InterPro	IPR011599. PFD_alpha. IPR009053. Prefoldin. IPR004127. Prefoldin_subunit. [Graphical view]
KO	K04797.
Pfam	PF02996. Prefoldin. 1 hit. [Graphical view]
SUPFAM	SSF46579. Prefoldin. 1 hit.
TIGRFAMs	TIGR00293. TIGR00293. 1 hit.
ProtoNet	Search...
Other
NextBio	20126.
SOURCE	Search...

Entry information

Entry name

PFD5_HUMAN

Accession

Primary (citable) accession number: Q99471
Secondary accession number(s): A8K9A8, Q54AA8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 11, 2001
Last modified:	January 25, 2012
This is version 102 of the entry and version 2 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.