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Q99471 (PFD5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Prefoldin subunit 5
Alternative name(s):
C-Myc-binding protein Mm-1
Myc modulator 1
Gene names
Name:PFDN5
Synonyms:MM1, PFD5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length154 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Represses the transcriptional activity of MYC. Ref.9

Subunit structure

Heterohexamer of two PFD-alpha type and four PFD-beta type subunits. Binds to MYC; interacts with its N-terminal domain.

Subcellular location

Isoform 1: Nucleus Ref.3.

Isoform 2: Cytoplasm Ref.3.

Isoform 3: Nucleus Ref.3.

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

vIRF-3Q9DUN18EBI-357275,EBI-1647907From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: Q99471-1)

Also known as: MM1-alpha;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q99471-2)

Also known as: MM1-beta;

The sequence of this isoform differs from the canonical sequence as follows:
     59-154: GKELLVPLTS...LGAAQATAKA → DVCPWEAA
Note: Does not repress transcription activity of MYC.
Isoform 3 (identifier: Q99471-3)

Also known as: MM1-gamma;

The sequence of this isoform differs from the canonical sequence as follows:
     25-69: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.10
Chain2 – 154153Prefoldin subunit 5 HAMAP-Rule MF_00308
PRO_0000153661

Amino acid modifications

Modified residue21N-acetylalanine Ref.10 Ref.13
Modified residue421N6-acetyllysine Ref.11

Natural variations

Alternative sequence25 – 6945Missing in isoform 3.
VSP_043103
Alternative sequence59 – 15496GKELL…ATAKA → DVCPWEAA in isoform 2.
VSP_043104

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (MM1-alpha) [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: 0DA1F3644548CB14

FASTA15417,328
        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 

« Hide

Isoform 2 (MM1-beta) [UniParc].

Checksum: C07E3472E5BD2A76
Show »

FASTA667,481
Isoform 3 (MM1-gamma) [UniParc].

Checksum: 899AFF472DCC00D7
Show »

FASTA10912,379

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
Tissue: Blood and Fibroblast.
[3]"Distinct localizations and repression activities of MM-1 isoforms toward c-Myc."
Hagio Y., Kimura Y., Taira T., Fujioka Y., Iguchi-Ariga S.M.M., Ariga H.
J. Cell. Biochem. 97:145-155(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION, ALTERNATIVE SPLICING.
Tissue: B-cell and Placenta.
[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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]"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. expand/collapse author list , 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Thymus.
[6]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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. expand/collapse author list , 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].
[8]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Placenta.
[9]"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] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"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] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[11]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, 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.
AB055804 mRNA. Translation: BAB32645.1.
AB055805 mRNA. Translation: BAB32646.1.
BT007195 mRNA. Translation: AAP35859.1.
AK292623 mRNA. Translation: BAF85312.1.
AC073611 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW96683.1.
CH471054 Genomic DNA. Translation: EAW96685.1.
BC003373 mRNA. No translation available.
BC062671 mRNA. Translation: AAH62671.1.
CCDSCCDS8853.1. [Q99471-1]
CCDS8854.1. [Q99471-3]
RefSeqNP_002615.2. NM_002624.3. [Q99471-1]
NP_665904.1. NM_145897.2. [Q99471-3]
UniGeneHs.655327.

3D structure databases

ProteinModelPortalQ99471.
SMRQ99471. Positions 11-149.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111226. 54 interactions.
DIPDIP-28155N.
IntActQ99471. 14 interactions.
MINTMINT-5003456.
STRING9606.ENSP00000334188.

PTM databases

PhosphoSiteQ99471.

Polymorphism databases

DMDM12231038.

2D gel databases

OGPQ99471.

Proteomic databases

MaxQBQ99471.
PaxDbQ99471.
PeptideAtlasQ99471.
PRIDEQ99471.

Protocols and materials databases

DNASU5204.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000243040; ENSP00000243040; ENSG00000123349. [Q99471-2]
ENST00000334478; ENSP00000334188; ENSG00000123349. [Q99471-1]
ENST00000351500; ENSP00000266964; ENSG00000123349. [Q99471-3]
ENST00000551018; ENSP00000447942; ENSG00000123349. [Q99471-1]
GeneID5204.
KEGGhsa:5204.
UCSCuc001scl.3. human. [Q99471-1]
uc001scm.3. human. [Q99471-3]

Organism-specific databases

CTD5204.
GeneCardsGC12P053689.
HGNCHGNC:8869. PFDN5.
HPAHPA008587.
MIM604899. gene.
neXtProtNX_Q99471.
PharmGKBPA33210.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1730.
HOGENOMHOG000207562.
HOVERGENHBG004539.
InParanoidQ99471.
KOK04797.
OMAFVECECI.
PhylomeDBQ99471.
TreeFamTF106509.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

BgeeQ99471.
CleanExHS_PFDN5.
GenevestigatorQ99471.

Family and domain databases

Gene3D1.10.287.370. 1 hit.
HAMAPMF_00308. PfdA.
InterProIPR011599. PFD_alpha.
IPR009053. Prefoldin.
IPR004127. Prefoldin_subunit_alpha.
[Graphical view]
PfamPF02996. Prefoldin. 1 hit.
[Graphical view]
SUPFAMSSF46579. SSF46579. 1 hit.
TIGRFAMsTIGR00293. TIGR00293. 1 hit.
ProtoNetSearch...

Other

ChiTaRSPFDN5. human.
GeneWikiPFDN5.
GenomeRNAi5204.
NextBio20126.
PROQ99471.
SOURCESearch...

Entry information

Entry namePFD5_HUMAN
AccessionPrimary (citable) accession number: Q99471
Secondary accession number(s): A8K9A8 expand/collapse secondary AC list , Q54AA8, Q9C083, Q9C084
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 11, 2001
Last modified: July 9, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM