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O60925

- PFD1_HUMAN

UniProt

O60925 - PFD1_HUMAN

Protein

Prefoldin subunit 1

Gene

PFDN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    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

    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

    ArrayExpressiO60925.
    BgeeiO60925.
    CleanExiHS_PFDN1.
    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.
    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

    MAAPVDLELK KAFTELQAKV IDTQQKVKLA DIQIEQLNRT KKHAHLTDTE    50
    IMTLVDETNM YEGVGRMFIL QSKEAIHSQL LEKQKIAEEK IKELEQKKSY 100
    LERSVKEAED NIREMLMARR AQ 122
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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.
    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

    ArrayExpressi O60925.
    Bgeei O60925.
    CleanExi HS_PFDN1.
    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

    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 1, 2014
    This is version 119 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