Q9NPJ4 (PNRC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proline-rich nuclear receptor coactivator 2

Gene names

Name:	PNRC2
ORF Names:	HSPC208

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	139 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 Ref.7
Subunit structure	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. Ref.1 Ref.6 Ref.7
Subcellular location	Nucleus. Cytoplasm › P-body Ref.7.
Tissue specificity	Expressed in heart, lung, muscle and brain. Ref.1
Domain	The interaction between PNRC2 and nuclear receptors is dependent on the SH3 binding motif. Ref.1
Sequence similarities	Belongs to the PNRC family. PNRC2 subfamily.

Ontologies

Keywords
Biological process	Nonsense-mediated mRNA decay Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Molecular function	Activator
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	deadenylation-independent decapping of nuclear-transcribed mRNA Traceable author statement Ref.7. Source: UniProtKB nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Inferred from direct assay Ref.7. Source: UniProtKB regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasmic mRNA processing body Inferred from direct assay Ref.7. Source: UniProtKB nucleus Inferred from direct assay Ref.7. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
UPF1	Q92900	9	EBI-726549,EBI-373471

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9NPJ4-1)

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: Q9NPJ4-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 139	139	Proline-rich nuclear receptor coactivator 2		PRO_0000058485
Regions
	Motif	99 – 105	7	SH3-binding
Natural variations
	Alternative sequence	1 – 54	54	MGGGE…NSSAA → MLASAPRLNSADRPMKTSVL RQRKGSVRKQHLLSW in isoform 2.		VSP_037463
Experimental info
	Mutagenesis	101	1	P → A: Abolishes the interaction with the nuclear receptors; when associated with A-104. Ref.1
	Mutagenesis	104	1	P → A: Abolishes the interaction with the nuclear receptors; when associated with A-101. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 072039CB52551F90	FASTA	139	15,591
	10 20 30 40 50 60 MGGGERYNIP APQSRNVSKN QQQLNRQKTK EQNSQMKIVH KKKERGHGYN SSAAAWQAMQ 70 80 90 100 110 120 NGGKNKNFPN NQSWNSSLSG PRLLFKSQAN QNYAGAKFSE PPSPSVLPKP PSHWVPVSFN 130 PSDKEIMTFQ LKTLLKVQV
	Isoform 2 [UniParc]. Checksum: 185AC9A23E50218B	FASTA	120	13,471
	10 20 30 40 50 60 MLASAPRLNS ADRPMKTSVL RQRKGSVRKQ HLLSWAWQAM QNGGKNKNFP NNQSWNSSLS 70 80 90 100 110 120 GPRLLFKSQA NQNYAGAKFS EPPSPSVLPK PPSHWVPVSF NPSDKEIMTF QLKTLLKVQV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00015681.
IPI00910406.

RefSeq

NP_060231.1. NM_017761.3.
XP_003846464.1. XM_003846416.1.
XP_003846465.1. XM_003846417.1.
XP_003846466.1. XM_003846418.1.
XP_003846467.1. XM_003846419.1.
XP_003846468.1. XM_003846420.1.
XP_003846469.1. XM_003846421.1.
XP_003846470.1. XM_003846422.2.
XP_003846471.1. XM_003846423.1.

UniGene

Hs.512636.
Hs.644217.
Hs.716935.
Hs.7862.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4B6H	X-ray	2.60	C/D	1-121	[»]

ProteinModelPortal

Q9NPJ4.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9NPJ4. 4 interactions.

MINT

MINT-215468.

STRING

9606.ENSP00000334840.

PTM databases

PhosphoSite

Q9NPJ4.

Proteomic databases

PaxDb

Q9NPJ4.

PRIDE

Q9NPJ4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000334351; ENSP00000334840; ENSG00000189266.
ENST00000374468; ENSP00000363592; ENSG00000189266.

GeneID

100996626.
55629.

KEGG

hsa:100996626.
hsa:55629.

UCSC

uc001big.3. human.

Organism-specific databases

CTD

55629.

GeneCards

GC01P024285.

H-InvDB

HIX0028821.

HGNC

HGNC:23158. PNRC2.

HPA

HPA027820.

MIM

611882. gene.

neXtProt

NX_Q9NPJ4.

PharmGKB

PA134931421.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG45103.

HOGENOM

HOG000115593.

HOVERGEN

HBG053627.

InParanoid

Q9NPJ4.

OMA

ERGHTYN.

OrthoDB

EOG4T4CWV.

PhylomeDB

Q9NPJ4.

Gene expression databases

Bgee

Q9NPJ4.

CleanEx

HS_PNRC2.

Genevestigator

Q9NPJ4.

GermOnline

ENSG00000189266. Homo sapiens.

Family and domain databases

InterPro

IPR026781. PNRC2.
[Graphical view]

PANTHER

PTHR32216. PTHR32216. 1 hit.

ProtoNet

Search...

Other

NextBio

60261.

SOURCE

Search...

Entry information

Entry name

PNRC2_HUMAN

Accession

Primary (citable) accession number: Q9NPJ4
Secondary accession number(s): B4DU72

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 29, 2005
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.