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Q8VHJ7 (PRGC2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxisome proliferator-activated receptor gamma coactivator 1-beta

Short name=PGC-1-beta
Short name=PPAR-gamma coactivator 1-beta
Short name=PPARGC-1-beta
Alternative name(s):
ERR ligand 1
Gene names
Name:Ppargc1b
Synonyms:Errl1, Pgc1, Pgc1b, Ppargc1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1014 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role of stimulator of transcription factors and nuclear receptors activities. Activates transcritional activity of estrogen receptor alpha, nuclear respiratory factor 1 (NRF1) and glucocorticoid receptor in the presence of glucocorticoids. May play a role in constitutive non-adrenergic-mediated mitochondrial biogenesis as suggested by increased basal oxygen consumption and mitochondrial number when overexpressed. May be part of the pathways regulating the elevation of gluconeogenesis, beta-oxidation of fatty acids and ketogenesis during fasting. Stimulates SREBP-mediated lipogenic gene expression in the liver. Induces energy expenditure and antagonizes obesity when overexpressed. Induces also the expression of mitochondrial genes involved in oxidative metabolism. Induces the expression of PERM1 in the skeletal muscle in an ESRRA-dependent manner. Ref.1 Ref.2 Ref.5 Ref.6

Subunit structure

Interacts with estrogen receptor alpha/ESR1 By similarity. Interacts with hepatocyte nuclear factor 4-alpha/HNF4A, Sterol regulatory binding transcription factor 1/SREBF1, PPAR-alpha/PPARA, thyroid hormone receptor beta/THRB and host cell factor/HCFC1. Interacts with estrogen-related receptor gamma/ESRRG and alpha/ESRRA. Interacts with PRDM16. Ref.1 Ref.2 Ref.4 Ref.6 Ref.7 Ref.8

Subcellular location

Nucleus By similarity.

Tissue specificity

Ubiquitous with higher expression in heart, brown adipose tissue, brain and skeletal muscle. Ref.1 Ref.5

Induction

Induced by fasting in the liver, but not by cold exposure in brown adipose tissue. Induced also by saturated fatty acids in primary hepatocytes. Ref.1 Ref.6

Domain

Contains 3 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motif, which are usually required for the association with nuclear receptors By similarity.

Miscellaneous

Transgenic mice overexpressing PPARGC1B exhibits increased expression of medium-chain acyl CoA dehydrogenase. They are hyperphagic but lean, with increased energy expenditure and resistance to obesity.

Sequence similarities

Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
   LigandRNA-binding
   Molecular functionActivator
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament organization

Inferred from mutant phenotype PubMed 19252502. Source: DFLAT

bone trabecula formation

Inferred from mutant phenotype PubMed 19252502. Source: DFLAT

cellular response to reactive oxygen species

Inferred from direct assay PubMed 19252502. Source: DFLAT

intracellular estrogen receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 19252502. Source: DFLAT

ossification

Inferred from mutant phenotype PubMed 19252502. Source: DFLAT

positive regulation of alkaline phosphatase activity

Inferred from mutant phenotype PubMed 19252502. Source: DFLAT

positive regulation of bone resorption

Inferred from mutant phenotype PubMed 19252502. Source: DFLAT

positive regulation of osteoclast differentiation

Inferred from mutant phenotype PubMed 19252502. Source: DFLAT

positive regulation of phosphorylation

Inferred from mutant phenotype PubMed 19252502. Source: DFLAT

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 19252502. Source: DFLAT

regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

response to cAMP

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

transcription from mitochondrial promoter

Inferred from mutant phenotype PubMed 19252502. Source: DFLAT

   Cellular_componentmediator complex

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from mutant phenotype PubMed 19252502. Source: GOC

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionAF-2 domain binding

Inferred from sequence or structural similarity. Source: UniProtKB

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA polymerase II transcription cofactor activity

Inferred from electronic annotation. Source: Ensembl

ligand-dependent nuclear receptor transcription coactivator activity

Inferred from sequence or structural similarity. Source: UniProtKB

nucleotide binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction Ref.7Ref.8. Source: UniProtKB

receptor activator activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8VHJ7-1)

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: Q8VHJ7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MAGNDCGALLDEELSSFFLNYLSDTQ → MKSSRPSSSTISLTRRSAEGLEEVDHEALDRDGCGRRRLADM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10141014Peroxisome proliferator-activated receptor gamma coactivator 1-beta
PRO_0000240159

Regions

Domain893 – 96775RRM
Region1 – 9191Abolishes DNA transcriptional activity when missing By similarity
Motif140 – 1445LXXLL motif 1
Motif156 – 1605LXXLL motif 2
Motif343 – 3475LXXLL motif 3
Motif683 – 6864HCFC1-binding-motif (HBM)
Compositional bias246 – 2505Poly-Glu
Compositional bias429 – 45123Glu-rich
Compositional bias786 – 85671Ser-rich

Amino acid modifications

Modified residue5191Phosphoserine By similarity

Natural variations

Alternative sequence1 – 2626MAGND…LSDTQ → MKSSRPSSSTISLTRRSAEG LEEVDHEALDRDGCGRRRLA DM in isoform 2.
VSP_019302

Experimental info

Sequence conflict551A → P in BAC25964. Ref.3
Sequence conflict5791K → R in BAC25964. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 004BCB7797EAFD1F

FASTA1,014112,075
        10         20         30         40         50         60 
MAGNDCGALL DEELSSFFLN YLSDTQGGDS GEEQLCADLP ELDLSQLDAS DFDSATCFGE 

        70         80         90        100        110        120 
LQWCPETSET EPSQYSPDDS ELFQIDSENE ALLAALTKTL DDIPEDDVGL AAFPELDEGD 

       130        140        150        160        170        180 
TPSCTPASPA PLSAPPSPTL ERLLSPASDV DELSLLQKLL LATSSPTASS DALKDGATWS 

       190        200        210        220        230        240 
QTSLSSRSQR PCVKVDGTQD KKTPTLRAQS RPCTELHKHL TSVLPCPRVK ACSPTPHPSP 

       250        260        270        280        290        300 
RLLSKEEEEE VGEDCPSPWP TPASPQDSLA QDTASPDSAQ PPEEDVRAMV QLIRYMHTYC 

       310        320        330        340        350        360 
LPQRKLPQRA PEPIPQACSS LSRQVQPRSR HPPKAFWTEF SILRELLAQD ILCDVSKPYR 

       370        380        390        400        410        420 
LAIPVYASLT PQSRPRPPKD SQASPAHSAM AEEVRITASP KSTGPRPSLR PLRLEVKRDV 

       430        440        450        460        470        480 
NKPTRQKREE DEEEEEEEEE EEEEKEEEEE EWGRKRPGRG LPWTKLGRKM DSSVCPVRRS 

       490        500        510        520        530        540 
RRLNPELGPW LTFTDEPLGA LPSMCLDTET HNLEEDLGSL TDSSQGRQLP QGSQIPALES 

       550        560        570        580        590        600 
PCESGCGDTD EDPSCPQPTS RDSSRCLMLA LSQSDSLGKK SFEESLTVEL CGTAGLTPPT 

       610        620        630        640        650        660 
TPPYKPMEED PFKPDTKLSP GQDTAPSLPS PEALPLTATP GASHKLPKRH PERSELLSHL 

       670        680        690        700        710        720 
QHATTQPVSQ AGQKRPFSCS FGDHDYCQVL RPEAALQRKV LRSWEPIGVH LEDLAQQGAP 

       730        740        750        760        770        780 
LPTETKAPRR EANQNCDPTH KDSMQLRDHE IRASLTKHFG LLETALEGED LASCKSPEYD 

       790        800        810        820        830        840 
TVFEDSSSSS GESSFLLEEE EEEEEGGEED DEGEDSGVSP PCSDHCPYQS PPSKASRQLC 

       850        860        870        880        890        900 
SRSRSSSGSS SCSSWSPATR KNFRRESRGP CSDGTPSVRH ARKRREKAIG EGRVVYIRNL 

       910        920        930        940        950        960 
SSDMSSRELK KRFEVFGEIV ECQVLTRSKR GQKHGFITFR CSEHAALSVR NGATLRKRNE 

       970        980        990       1000       1010 
PSFHLSYGGL RHFRWPRYTD YDPTSEESLP SSGKSKYEAM DFDSLLKEAQ QSLH 

« Hide

Isoform 2 [UniParc].

Checksum: 4F2B27E32E91C84C
Show »

FASTA1,030113,898

References

« Hide 'large scale' references
[1]"Peroxisome proliferator-activated receptor gamma coactivator 1beta (PGC-1beta), a novel PGC-1-related transcription coactivator associated with host cell factor."
Lin J., Puigserver P., Donovan J., Tarr P., Spiegelman B.M.
J. Biol. Chem. 277:1645-1648(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, MOTIFS, FUNCTION, INDUCTION, SUBUNIT.
Strain: C57BL/6.
[2]"PPARgamma coactivator 1beta/ERR ligand 1 is an ERR protein ligand, whose expression induces a high-energy expenditure and antagonizes obesity."
Kamei Y., Ohizumi H., Fujitani Y., Nemoto T., Tanaka T., Takahashi N., Kawada T., Miyoshi M., Ezaki O., Kakizuka A.
Proc. Natl. Acad. Sci. U.S.A. 100:12378-12383(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH ESRRA AND ESRRG.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Skin.
[4]"PGC-1 and PERC, coactivators of the estrogen receptor-related receptor gamma."
Hentschke M., Suesens U., Borgmeyer U.
Biochem. Biophys. Res. Commun. 299:872-879(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ESRRG.
[5]"Characterization of the human, mouse and rat PGC1 beta (peroxisome-proliferator-activated receptor-gamma co-activator 1 beta) gene in vitro and in vivo."
Meirhaeghe A., Crowley V., Lenaghan C., Lelliott C., Green K., Stewart A., Hart K., Schinner S., Sethi J.K., Yeo G., Brand M.D., Cortright R.N., O'Rahilly S., Montague C., Vidal-Puig A.J.
Biochem. J. 373:155-165(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, FUNCTION.
[6]"Hyperlipidemic effects of dietary saturated fats mediated through PGC-1beta coactivation of SREBP."
Lin J., Yang R., Tarr P.T., Wu P.-H., Handschin C., Li S., Yang W., Pei L., Uldry M., Tontonoz P., Newgard C.B., Spiegelman B.M.
Cell 120:261-273(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH SREBF1, INDUCTION.
[7]"Transcriptional control of brown fat determination by PRDM16."
Seale P., Kajimura S., Yang W., Chin S., Rohas L.M., Uldry M., Tavernier G., Langin D., Spiegelman B.M.
Cell Metab. 6:38-54(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRDM16.
[8]"Regulation of the brown and white fat gene programs through a PRDM16/CtBP transcriptional complex."
Kajimura S., Seale P., Tomaru T., Erdjument-Bromage H., Cooper M.P., Ruas J.L., Chin S., Tempst P., Lazar M.A., Spiegelman B.M.
Genes Dev. 22:1397-1409(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PRDM16.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF453324 mRNA. Translation: AAL47054.1.
AK028464 mRNA. Translation: BAC25964.1.
CCDSCCDS29284.1. [Q8VHJ7-1]
RefSeqNP_573512.1. NM_133249.2. [Q8VHJ7-1]
UniGeneMm.415302.

3D structure databases

ProteinModelPortalQ8VHJ7.
SMRQ8VHJ7. Positions 892-955.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid228460. 3 interactions.
IntActQ8VHJ7. 1 interaction.

PTM databases

PhosphoSiteQ8VHJ7.

Proteomic databases

PRIDEQ8VHJ7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000063307; ENSMUSP00000069431; ENSMUSG00000033871. [Q8VHJ7-2]
ENSMUST00000075299; ENSMUSP00000074771; ENSMUSG00000033871. [Q8VHJ7-1]
GeneID170826.
KEGGmmu:170826.
UCSCuc008fbx.1. mouse. [Q8VHJ7-1]
uc012bdq.1. mouse. [Q8VHJ7-2]

Organism-specific databases

CTD133522.
MGIMGI:2444934. Ppargc1b.

Phylogenomic databases

eggNOGNOG87590.
GeneTreeENSGT00530000063196.
HOGENOMHOG000236356.
HOVERGENHBG080730.
KOK17962.
OMACESGCGD.
OrthoDBEOG7S4X5H.
PhylomeDBQ8VHJ7.
TreeFamTF343068.

Enzyme and pathway databases

ReactomeREACT_224594. Organelle biogenesis and maintenance.

Gene expression databases

BgeeQ8VHJ7.
GenevestigatorQ8VHJ7.

Family and domain databases

Gene3D3.30.70.330. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPARGC1B. mouse.
NextBio370487.
PROQ8VHJ7.
SOURCESearch...

Entry information

Entry namePRGC2_MOUSE
AccessionPrimary (citable) accession number: Q8VHJ7
Secondary accession number(s): Q8C1C0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: March 1, 2002
Last modified: July 9, 2014
This is version 91 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot