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O60925

- PFD1_HUMAN

UniProt

O60925 - PFD1_HUMAN

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Protein

Prefoldin subunit 1

Gene

PFDN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. sequence-specific DNA binding transcription factor activity Source: ProtInc

GO - Biological processi

  1. 'de novo' posttranslational protein folding Source: Reactome
  2. actin cytoskeleton organization Source: Ensembl
  3. B cell activation Source: Ensembl
  4. cell cycle Source: ProtInc
  5. cellular protein metabolic process Source: Reactome
  6. cerebellum development Source: Ensembl
  7. protein folding Source: Reactome
  8. regulation of transcription, DNA-templated Source: GOC
  9. telencephalon development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Enzyme and pathway databases

ReactomeiREACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.

Names & Taxonomyi

Protein namesi
Recommended name:
Prefoldin subunit 1
Gene namesi
Name:PFDN1
Synonyms:PFD1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:8866. PFDN1.

Subcellular locationi

GO - Cellular componenti

  1. prefoldin complex Source: InterPro
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33207.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 122121Prefoldin subunit 1PRO_0000124830Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO60925.
PaxDbiO60925.
PeptideAtlasiO60925.
PRIDEiO60925.

2D gel databases

OGPiO60925.

PTM databases

PhosphoSiteiO60925.

Expressioni

Gene expression databases

BgeeiO60925.
CleanExiHS_PFDN1.
ExpressionAtlasiO60925. baseline and differential.
GenevestigatoriO60925.

Organism-specific databases

HPAiHPA006499.

Interactioni

Subunit structurei

Heterohexamer of two PFD-alpha type and four PFD-beta type subunits.

Protein-protein interaction databases

BioGridi111223. 80 interactions.
IntActiO60925. 50 interactions.
MINTiMINT-1143999.
STRINGi9606.ENSP00000261813.

Structurei

3D structure databases

ProteinModelPortaliO60925.
SMRiO60925. Positions 16-114.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the prefoldin subunit beta family.Curated

Phylogenomic databases

eggNOGiNOG261468.
GeneTreeiENSGT00390000009786.
HOGENOMiHOG000005946.
HOVERGENiHBG031813.
InParanoidiO60925.
KOiK09548.
OMAiFTEMQIN.
PhylomeDBiO60925.
TreeFamiTF106490.

Family and domain databases

Gene3Di1.10.287.370. 1 hit.
InterProiIPR002777. PFD_beta-like.
IPR009053. Prefoldin.
[Graphical view]
PfamiPF01920. Prefoldin_2. 1 hit.
[Graphical view]
SUPFAMiSSF46579. SSF46579. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O60925-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAPVDLELK KAFTELQAKV IDTQQKVKLA DIQIEQLNRT KKHAHLTDTE
60 70 80 90 100
IMTLVDETNM YEGVGRMFIL QSKEAIHSQL LEKQKIAEEK IKELEQKKSY
110 120
LERSVKEAED NIREMLMARR AQ
Length:122
Mass (Da):14,210
Last modified:August 13, 2002 - v2
Checksum:i4C88216612864F87
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti86 – 861I → V in BAD97114. 1 PublicationCurated
Sequence conflicti104 – 1052SV → RL in CAA76759. (PubMed:9630229)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti67 – 671M → R.
Corresponds to variant rs1064061 [ dbSNP | Ensembl ].
VAR_014529

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y17392 mRNA. Translation: CAA76759.1.
AK223394 mRNA. Translation: BAD97114.1.
AK315353 mRNA. Translation: BAG37749.1.
CH471062 Genomic DNA. Translation: EAW62071.1.
BC003620 mRNA. Translation: AAH03620.1.
BC006202 mRNA. Translation: AAH06202.1.
BC011869 mRNA. Translation: AAH11869.1.
CCDSiCCDS4222.1.
RefSeqiNP_002613.2. NM_002622.4.
UniGeneiHs.483564.

Genome annotation databases

EnsembliENST00000261813; ENSP00000261813; ENSG00000113068.
GeneIDi5201.
KEGGihsa:5201.
UCSCiuc003lff.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y17392 mRNA. Translation: CAA76759.1 .
AK223394 mRNA. Translation: BAD97114.1 .
AK315353 mRNA. Translation: BAG37749.1 .
CH471062 Genomic DNA. Translation: EAW62071.1 .
BC003620 mRNA. Translation: AAH03620.1 .
BC006202 mRNA. Translation: AAH06202.1 .
BC011869 mRNA. Translation: AAH11869.1 .
CCDSi CCDS4222.1.
RefSeqi NP_002613.2. NM_002622.4.
UniGenei Hs.483564.

3D structure databases

ProteinModelPortali O60925.
SMRi O60925. Positions 16-114.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111223. 80 interactions.
IntActi O60925. 50 interactions.
MINTi MINT-1143999.
STRINGi 9606.ENSP00000261813.

PTM databases

PhosphoSitei O60925.

2D gel databases

OGPi O60925.

Proteomic databases

MaxQBi O60925.
PaxDbi O60925.
PeptideAtlasi O60925.
PRIDEi O60925.

Protocols and materials databases

DNASUi 5201.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000261813 ; ENSP00000261813 ; ENSG00000113068 .
GeneIDi 5201.
KEGGi hsa:5201.
UCSCi uc003lff.1. human.

Organism-specific databases

CTDi 5201.
GeneCardsi GC05M139604.
HGNCi HGNC:8866. PFDN1.
HPAi HPA006499.
MIMi 604897. gene.
neXtProti NX_O60925.
PharmGKBi PA33207.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG261468.
GeneTreei ENSGT00390000009786.
HOGENOMi HOG000005946.
HOVERGENi HBG031813.
InParanoidi O60925.
KOi K09548.
OMAi FTEMQIN.
PhylomeDBi O60925.
TreeFami TF106490.

Enzyme and pathway databases

Reactomei REACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.

Miscellaneous databases

GeneWikii PFDN1.
GenomeRNAii 5201.
NextBioi 20114.
PROi O60925.
SOURCEi Search...

Gene expression databases

Bgeei O60925.
CleanExi HS_PFDN1.
ExpressionAtlasi O60925. baseline and differential.
Genevestigatori O60925.

Family and domain databases

Gene3Di 1.10.287.370. 1 hit.
InterProi IPR002777. PFD_beta-like.
IPR009053. Prefoldin.
[Graphical view ]
Pfami PF01920. Prefoldin_2. 1 hit.
[Graphical view ]
SUPFAMi SSF46579. SSF46579. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Thymus.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Colon.
  6. "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].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPFD1_HUMAN
AccessioniPrimary (citable) accession number: O60925
Secondary accession number(s): B2RD02, Q53F95, Q96EX6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 13, 2002
Last modified: October 29, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3