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Protein

Proline-rich nuclear receptor coactivator 2

Gene

PNRC2

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

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 - Biological processi

Complete GO annotation...

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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:23158. PNRC2.

Subcellular locationi

  • Nucleus 1 Publication
  • CytoplasmP-body 1 Publication

GO - Cellular componenti

  • cytoplasmic mRNA processing body Source: UniProtKB
  • nucleus Source: UniProtKB
Complete GO annotation...

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.

Polymorphism and mutation databases

BioMutaiPNRC2.

PTM / Processingi

Molecule processing

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

Proteomic databases

MaxQBiQ9NPJ4.
PaxDbiQ9NPJ4.
PRIDEiQ9NPJ4.

PTM databases

PhosphoSiteiQ9NPJ4.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ9NPJ4.
CleanExiHS_PNRC2.
ExpressionAtlasiQ9NPJ4. baseline and differential.
GenevisibleiQ9NPJ4. HS.

Organism-specific databases

HPAiHPA027820.
HPA045837.

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
DCP1AQ9NPI66EBI-726549,EBI-374238
UPF1Q929009EBI-726549,EBI-373471

Protein-protein interaction databases

BioGridi120768. 15 interactions.
DIPiDIP-41328N.
IntActiQ9NPJ4. 13 interactions.
MINTiMINT-215468.
STRINGi9606.ENSP00000383587.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00530000063881.
HOGENOMiHOG000115593.
HOVERGENiHBG053627.
InParanoidiQ9NPJ4.
KOiK18751.
OMAiERGHTYN.
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. AlignAdd to basket

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

        10         20         30         40         50
MGGGERYNIP APQSRNVSKN QQQLNRQKTK EQNSQMKIVH KKKERGHGYN
60 70 80 90 100
SSAAAWQAMQ NGGKNKNFPN NQSWNSSLSG PRLLFKSQAN QNYAGAKFSE
110 120 130
PPSPSVLPKP PSHWVPVSFN PSDKEIMTFQ LKTLLKVQV
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi120768. 15 interactions.
DIPiDIP-41328N.
IntActiQ9NPJ4. 13 interactions.
MINTiMINT-215468.
STRINGi9606.ENSP00000383587.

PTM databases

PhosphoSiteiQ9NPJ4.

Polymorphism and mutation databases

BioMutaiPNRC2.

Proteomic databases

MaxQBiQ9NPJ4.
PaxDbiQ9NPJ4.
PRIDEiQ9NPJ4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi55629.
GeneCardsiGC01P024285.
H-InvDBHIX0028821.
HGNCiHGNC:23158. PNRC2.
HPAiHPA027820.
HPA045837.
MIMi611882. gene.
neXtProtiNX_Q9NPJ4.
PharmGKBiPA134931421.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG45103.
GeneTreeiENSGT00530000063881.
HOGENOMiHOG000115593.
HOVERGENiHBG053627.
InParanoidiQ9NPJ4.
KOiK18751.
OMAiERGHTYN.
PhylomeDBiQ9NPJ4.
TreeFamiTF333211.

Miscellaneous databases

ChiTaRSiPNRC2. human.
GeneWikiiPNRC2.
GenomeRNAii55629.
NextBioi60261.
PROiQ9NPJ4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NPJ4.
CleanExiHS_PNRC2.
ExpressionAtlasiQ9NPJ4. baseline and differential.
GenevisibleiQ9NPJ4. HS.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 121 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.