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Q9NPJ4

- PNRC2_HUMAN

UniProt

Q9NPJ4 - PNRC2_HUMAN

Protein

Proline-rich nuclear receptor coactivator 2

Gene

PNRC2

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

    Involved in nonsense-mediated mRNA decay (NMD) by acting as a bridge between the mRNA decapping complex and the NMD machinery. May act by targeting the NMD machinery to the P-body and recruiting the decapping machinery to aberrant mRNAs. Required for UPF1/RENT1 localization to the P-body. Also acts as a nuclear receptor coactivator. May play a role in controlling the energy balance between energy storage and energy expenditure.2 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. deadenylation-independent decapping of nuclear-transcribed mRNA Source: UniProtKB
    2. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
    3. regulation of transcription, DNA-templated Source: UniProtKB-KW
    4. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator

    Keywords - Biological processi

    Nonsense-mediated mRNA decay, Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Proline-rich nuclear receptor coactivator 2
    Gene namesi
    Name:PNRC2
    ORF Names:HSPC208
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:23158. PNRC2.

    Subcellular locationi

    Nucleus 1 Publication. CytoplasmP-body 1 Publication

    GO - Cellular componenti

    1. cytoplasmic mRNA processing body Source: UniProtKB
    2. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi101 – 1011P → A: Abolishes the interaction with the nuclear receptors; when associated with A-104. 1 Publication
    Mutagenesisi104 – 1041P → A: Abolishes the interaction with the nuclear receptors; when associated with A-101. 1 Publication

    Organism-specific databases

    PharmGKBiPA134931421.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 139139Proline-rich nuclear receptor coactivator 2PRO_0000058485Add
    BLAST

    Proteomic databases

    PaxDbiQ9NPJ4.
    PRIDEiQ9NPJ4.

    PTM databases

    PhosphoSiteiQ9NPJ4.

    Expressioni

    Tissue specificityi

    Expressed in heart, lung, muscle and brain.1 Publication

    Gene expression databases

    ArrayExpressiQ9NPJ4.
    BgeeiQ9NPJ4.
    CleanExiHS_PNRC2.
    GenevestigatoriQ9NPJ4.

    Organism-specific databases

    HPAiHPA027820.

    Interactioni

    Subunit structurei

    Interacts with UPF1/RENT1; preferentially interacts with hyperphosphorylated form. Interacts with DCP1A. Interacts with many nuclear receptors including ESR1, ESRRA, ESRRG, NR3C1/GR, NR5A1, PGR, TR, RAR and RXR.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    UPF1Q929009EBI-726549,EBI-373471

    Protein-protein interaction databases

    BioGridi120768. 15 interactions.
    DIPiDIP-41328N.
    IntActiQ9NPJ4. 13 interactions.
    MINTiMINT-215468.
    STRINGi9606.ENSP00000334840.

    Structurei

    Secondary structure

    1
    139
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi112 – 1143

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4B6HX-ray2.60C/D1-121[»]
    ProteinModelPortaliQ9NPJ4.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi99 – 1057SH3-binding

    Domaini

    The interaction between PNRC2 and nuclear receptors is dependent on the SH3 binding motif.1 Publication

    Sequence similaritiesi

    Belongs to the PNRC family. PNRC2 subfamily.Curated

    Phylogenomic databases

    eggNOGiNOG45103.
    HOGENOMiHOG000115593.
    HOVERGENiHBG053627.
    InParanoidiQ9NPJ4.
    OMAiERYNIPD.
    PhylomeDBiQ9NPJ4.
    TreeFamiTF333211.

    Family and domain databases

    InterProiIPR026780. PNRC1/2.
    IPR026781. PNRC2.
    [Graphical view]
    PANTHERiPTHR15405. PTHR15405. 1 hit.
    PTHR15405:SF5. PTHR15405:SF5. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NPJ4-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MGGGERYNIP APQSRNVSKN QQQLNRQKTK EQNSQMKIVH KKKERGHGYN    50
    SSAAAWQAMQ NGGKNKNFPN NQSWNSSLSG PRLLFKSQAN QNYAGAKFSE 100
    PPSPSVLPKP PSHWVPVSFN PSDKEIMTFQ LKTLLKVQV 139
    Length:139
    Mass (Da):15,591
    Last modified:October 1, 2000 - v1
    Checksum:i072039CB52551F90
    GO
    Isoform 2 (identifier: Q9NPJ4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-54: MGGGERYNIP...RGHGYNSSAA → MLASAPRLNSADRPMKTSVLRQRKGSVRKQHLLSW

    Note: No experimental confirmation available.

    Show »
    Length:120
    Mass (Da):13,471
    Checksum:i185AC9A23E50218B
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5454MGGGE…NSSAA → MLASAPRLNSADRPMKTSVL RQRKGSVRKQHLLSW in isoform 2. 1 PublicationVSP_037463Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF374386 mRNA. Translation: AAK54613.1.
    AF151042 mRNA. Translation: AAF36128.1.
    AK000319 mRNA. Translation: BAA91082.1.
    AK300522 mRNA. Translation: BAG62234.1.
    AL590609 Genomic DNA. Translation: CAI14802.1.
    BC001959 mRNA. Translation: AAH01959.1.
    BC078177 mRNA. Translation: AAH78177.1.
    BC085018 mRNA. Translation: AAH85018.1.
    CCDSiCCDS246.1. [Q9NPJ4-1]
    RefSeqiNP_060231.1. NM_017761.3. [Q9NPJ4-1]
    UniGeneiHs.512636.
    Hs.644217.
    Hs.716935.
    Hs.7862.

    Genome annotation databases

    EnsembliENST00000334351; ENSP00000334840; ENSG00000189266. [Q9NPJ4-1]
    ENST00000374468; ENSP00000363592; ENSG00000189266. [Q9NPJ4-1]
    GeneIDi55629.
    KEGGihsa:55629.
    UCSCiuc001big.3. human. [Q9NPJ4-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF374386 mRNA. Translation: AAK54613.1 .
    AF151042 mRNA. Translation: AAF36128.1 .
    AK000319 mRNA. Translation: BAA91082.1 .
    AK300522 mRNA. Translation: BAG62234.1 .
    AL590609 Genomic DNA. Translation: CAI14802.1 .
    BC001959 mRNA. Translation: AAH01959.1 .
    BC078177 mRNA. Translation: AAH78177.1 .
    BC085018 mRNA. Translation: AAH85018.1 .
    CCDSi CCDS246.1. [Q9NPJ4-1 ]
    RefSeqi NP_060231.1. NM_017761.3. [Q9NPJ4-1 ]
    UniGenei Hs.512636.
    Hs.644217.
    Hs.716935.
    Hs.7862.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4B6H X-ray 2.60 C/D 1-121 [» ]
    ProteinModelPortali Q9NPJ4.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120768. 15 interactions.
    DIPi DIP-41328N.
    IntActi Q9NPJ4. 13 interactions.
    MINTi MINT-215468.
    STRINGi 9606.ENSP00000334840.

    PTM databases

    PhosphoSitei Q9NPJ4.

    Proteomic databases

    PaxDbi Q9NPJ4.
    PRIDEi Q9NPJ4.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000334351 ; ENSP00000334840 ; ENSG00000189266 . [Q9NPJ4-1 ]
    ENST00000374468 ; ENSP00000363592 ; ENSG00000189266 . [Q9NPJ4-1 ]
    GeneIDi 55629.
    KEGGi hsa:55629.
    UCSCi uc001big.3. human. [Q9NPJ4-1 ]

    Organism-specific databases

    CTDi 55629.
    GeneCardsi GC01P024285.
    H-InvDB HIX0028821.
    HGNCi HGNC:23158. PNRC2.
    HPAi HPA027820.
    MIMi 611882. gene.
    neXtProti NX_Q9NPJ4.
    PharmGKBi PA134931421.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG45103.
    HOGENOMi HOG000115593.
    HOVERGENi HBG053627.
    InParanoidi Q9NPJ4.
    OMAi ERYNIPD.
    PhylomeDBi Q9NPJ4.
    TreeFami TF333211.

    Miscellaneous databases

    GeneWikii PNRC2.
    GenomeRNAii 55629.
    NextBioi 60261.
    PROi Q9NPJ4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NPJ4.
    Bgeei Q9NPJ4.
    CleanExi HS_PNRC2.
    Genevestigatori Q9NPJ4.

    Family and domain databases

    InterProi IPR026780. PNRC1/2.
    IPR026781. PNRC2.
    [Graphical view ]
    PANTHERi PTHR15405. PTHR15405. 1 hit.
    PTHR15405:SF5. PTHR15405:SF5. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "PNRC2 is a 16 kDa coactivator that interacts with nuclear receptors through an SH3-binding motif."
      Zhou D., Chen S.
      Nucleic Acids Res. 29:3939-3948(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, DOMAIN, MUTAGENESIS OF PRO-101 AND PRO-104, INTERACTION WITH ESR1; ESRRA; NR3C1; NR5A1; PGR; TR; RAR AND RXR.
    2. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
      Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
      , Gu J., Chen S.-J., Chen Z.
      Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Umbilical cord blood.
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Prostate.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 1).
      Tissue: Lung, Ovary and Uterus.
    6. "Identification of PNRC2 and TLE1 as activation function-1 cofactors of the orphan nuclear receptor ERRgamma."
      Hentschke M., Borgmeyer U.
      Biochem. Biophys. Res. Commun. 312:975-982(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ESRRG.
    7. "Human proline-rich nuclear receptor coregulatory protein 2 mediates an interaction between mRNA surveillance machinery and decapping complex."
      Cho H., Kim K.M., Kim Y.K.
      Mol. Cell 33:75-86(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH UPF1 AND DCP1A.

    Entry informationi

    Entry nameiPNRC2_HUMAN
    AccessioniPrimary (citable) accession number: Q9NPJ4
    Secondary accession number(s): B4DU72
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 29, 2005
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 114 of the entry and version 1 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3