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Q86YN6 (PRGC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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):
PGC-1-related estrogen receptor alpha coactivator
Gene names
Name:PPARGC1B
Synonyms:PERC, PGC1, PGC1B, PPARGC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1023 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 involved in fat oxidation and non-oxidative glucose metabolism and in the regulation of energy expenditure. Induces the expression of PERM1 in the skeletal muscle in an ESRRA-dependent manner. Ref.1 Ref.2 Ref.8 Ref.12

Subunit structure

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 By similarity. Interacts with estrogen receptor alpha/ESR1. Ref.1

Subcellular location

Nucleus Ref.1.

Tissue specificity

Ubiquitous with higher expression in heart, brain and skeletal muscle. Ref.1 Ref.2

Induction

Repressed by saturated fatty acids such as palmitate and stearate in skeletal muscle cells. Induced by insulin and reduced by aging in skeletal muscle biopsies. Down-regulated in type 2 diabetes mellitus subjects as well as in pre-diabetics. Ref.7 Ref.8 Ref.10

Domain

Contains 2 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motif, which are usually required for the association with nuclear receptors By similarity.

Polymorphism

Variation of PPARGC1B may contribute to the pathogenesis of obesity, with a widespread Ala-203 allele being a risk factor for the development of this common disorders.

Sequence similarities

Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandRNA-binding
   Molecular functionActivator
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament organization

Inferred from electronic annotation. Source: Ensembl

bone trabecula formation

Inferred from electronic annotation. Source: Ensembl

cellular lipid metabolic process

Traceable author statement. Source: Reactome

cellular response to reactive oxygen species

Inferred from electronic annotation. Source: Ensembl

intracellular estrogen receptor signaling pathway

Inferred from direct assay Ref.1. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

ossification

Inferred from electronic annotation. Source: Ensembl

positive regulation of alkaline phosphatase activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of bone resorption

Inferred from electronic annotation. Source: Ensembl

positive regulation of osteoclast differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of receptor activity

Inferred from direct assay Ref.1. Source: GOC

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.1. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from direct assay Ref.12. Source: UniProtKB

response to cAMP

Inferred from electronic annotation. Source: Ensembl

response to glucocorticoid

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

transcription from RNA polymerase II promoter

Inferred from direct assay Ref.1. Source: GOC

transcription from mitochondrial promoter

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentmediator complex

Inferred from direct assay Ref.1. Source: UniProtKB

mitochondrion

Inferred from electronic annotation. Source: GOC

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionAF-2 domain binding

Inferred from physical interaction Ref.1. Source: UniProtKB

RNA binding

Non-traceable author statement Ref.1. Source: UniProtKB

RNA polymerase II transcription cofactor activity

Inferred from direct assay Ref.1. Source: UniProtKB

estrogen receptor binding

Inferred from direct assay Ref.1. Source: UniProtKB

ligand-dependent nuclear receptor transcription coactivator activity

Inferred from direct assay Ref.1. Source: UniProtKB

nucleotide binding

Inferred from electronic annotation. Source: InterPro

receptor activator activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q86YN6-1)

Also known as: PGC1beta-1a;

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: Q86YN6-2)

Also known as: PGC1beta-2a;

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MAGNDCGALLDEELSSFFLNYLADTQ → MGVYK
Isoform 3 (identifier: Q86YN6-3)

Also known as: PGC1beta-1b;

The sequence of this isoform differs from the canonical sequence as follows:
     991-1023: DSNSEEALPASGKSKYEAMDFDSLLKEAQQSLH → GKPLKPSHSLVRLKAWEAVPSLNKTQS
Isoform 4 (identifier: Q86YN6-4)

Also known as: PGC1beta-2b;

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MAGNDCGALLDEELSSFFLNYLADTQ → MGVYK
     991-1023: DSNSEEALPASGKSKYEAMDFDSLLKEAQQSLH → GKPLKPSHSLVRLKAWEAVPSLNKTQS
Isoform 5 (identifier: Q86YN6-5)

Also known as: PERC-s;

The sequence of this isoform differs from the canonical sequence as follows:
     156-194: Missing.
Note: Lacks LXXLL motif 1 and has a reduced ability to enhance the hormone-dependent activity of estrogen receptor alpha.
Isoform 6 (identifier: Q86YN6-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MAGNDCGALLDEELSSFFLNYLADTQ → M
     156-194: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10231023Peroxisome proliferator-activated receptor gamma coactivator 1-beta
PRO_0000240158

Regions

Domain902 – 97675RRM
Region1 – 9191Abolishes DNA transcriptional activity when missing
Motif156 – 1605LXXLL motif 1
Motif343 – 3475LXXLL motif 2
Motif691 – 6944HCFC1-binding-motif (HBM)
Compositional bias430 – 45021Glu-rich
Compositional bias772 – 82352Glu-rich

Amino acid modifications

Modified residue5241Phosphoserine Ref.11

Natural variations

Alternative sequence1 – 2626MAGND…LADTQ → MGVYK in isoform 2 and isoform 4.
VSP_019299
Alternative sequence1 – 2626MAGND…LADTQ → M in isoform 6.
VSP_043374
Alternative sequence156 – 19439Missing in isoform 5 and isoform 6.
VSP_019300
Alternative sequence991 – 102333DSNSE…QQSLH → GKPLKPSHSLVRLKAWEAVP SLNKTQS in isoform 3 and isoform 4.
VSP_019301
Natural variant2031A → P. Ref.9
Corresponds to variant rs7732671 [ dbSNP | Ensembl ].
VAR_026698
Natural variant2651R → Q. Ref.2
Corresponds to variant rs45520937 [ dbSNP | Ensembl ].
VAR_026699
Natural variant2791V → I. Ref.9
Corresponds to variant rs17572019 [ dbSNP | Ensembl ].
VAR_026700
Natural variant2921R → S. Ref.6 Ref.9
Corresponds to variant rs11959820 [ dbSNP | Ensembl ].
VAR_026701

Experimental info

Mutagenesis92 – 965LLAEL → AAAEA: Reduces DNA transcriptional activity.
Mutagenesis155 – 1606LLQKLL → AAQKAA: Reduces interaction and activation of ESR1. Loss of interaction and activation of ESR1; when associated with 343-AREAA-347. Ref.1
Mutagenesis343 – 3475LRELL → AREAA: Reduces interaction and activation of ESR1. Loss of interaction and activation of ESR1; when associated with 155-AAQKAA-160. Ref.1
Sequence conflict5581E → G in BAC04541. Ref.3

Secondary structure

... 1023
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (PGC1beta-1a) [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: DC37FCDE4D3CD239

FASTA1,023113,222
        10         20         30         40         50         60 
MAGNDCGALL DEELSSFFLN YLADTQGGGS GEEQLYADFP ELDLSQLDAS DFDSATCFGE 

        70         80         90        100        110        120 
LQWCPENSET EPNQYSPDDS ELFQIDSENE ALLAELTKTL DDIPEDDVGL AAFPALDGGD 

       130        140        150        160        170        180 
ALSCTSASPA PSSAPPSPAP EKPSAPAPEV DELSLLQKLL LATSYPTSSS DTQKEGTAWR 

       190        200        210        220        230        240 
QAGLRSKSQR PCVKADSTQD KKAPMMQSQS RSCTELHKHL TSAQCCLQDR GLQPPCLQSP 

       250        260        270        280        290        300 
RLPAKEDKEP GEDCPSPQPA PASPRDSLAL GRADPGAPVS QEDMQAMVQL IRYMHTYCLP 

       310        320        330        340        350        360 
QRKLPPQTPE PLPKACSNPS QQVRSRPWSR HHSKASWAEF SILRELLAQD VLCDVSKPYR 

       370        380        390        400        410        420 
LATPVYASLT PRSRPRPPKD SQASPGRPSS VEEVRIAASP KSTGPRPSLR PLRLEVKREV 

       430        440        450        460        470        480 
RRPARLQQQE EEDEEEEEEE EEEEKEEEEE WGRKRPGRGL PWTKLGRKLE SSVCPVRRSR 

       490        500        510        520        530        540 
RLNPELGPWL TFADEPLVPS EPQGALPSLC LAPKAYDVER ELGSPTDEDS GQDQQLLRGP 

       550        560        570        580        590        600 
QIPALESPCE SGCGDMDEDP SCPQLPPRDS PRCLMLALSQ SDPTFGKKSF EQTLTVELCG 

       610        620        630        640        650        660 
TAGLTPPTTP PYKPTEEDPF KPDIKHSLGK EIALSLPSPE GLSLKATPGA AHKLPKKHPE 

       670        680        690        700        710        720 
RSELLSHLRH ATAQPASQAG QKRPFSCSFG DHDYCQVLRP EGVLQRKVLR SWEPSGVHLE 

       730        740        750        760        770        780 
DWPQQGAPWA EAQAPGREED RSCDAGAPPK DSTLLRDHEI RASLTKHFGL LETALEEEDL 

       790        800        810        820        830        840 
ASCKSPEYDT VFEDSSSSSG ESSFLPEEEE EEGEEEEEDD EEEDSGVSPT CSDHCPYQSP 

       850        860        870        880        890        900 
PSKANRQLCS RSRSSSGSSP CHSWSPATRR NFRCESRGPC SDRTPSIRHA RKRREKAIGE 

       910        920        930        940        950        960 
GRVVYIQNLS SDMSSRELKR RFEVFGEIEE CEVLTRNRRG EKYGFITYRC SEHAALSLTK 

       970        980        990       1000       1010       1020 
GAALRKRNEP SFQLSYGGLR HFCWPRYTDY DSNSEEALPA SGKSKYEAMD FDSLLKEAQQ 


SLH 

« Hide

Isoform 2 (PGC1beta-2a) [UniParc].

Checksum: 8ACBD368E172B27E
Show »

FASTA1,002110,981
Isoform 3 (PGC1beta-1b) [UniParc].

Checksum: F2229A0A356A2148
Show »

FASTA1,017112,568
Isoform 4 (PGC1beta-2b) [UniParc].

Checksum: 5265F3916B919ECC
Show »

FASTA996110,327
Isoform 5 (PERC-s) [UniParc].

Checksum: 5D91928FD6D6D104
Show »

FASTA984108,919
Isoform 6 [UniParc].

Checksum: D4E5EF57FC0C2459
Show »

FASTA959106,230

References

« Hide 'large scale' references
[1]"The PGC-1-related protein PERC is a selective coactivator of estrogen receptor alpha."
Kressler D., Schreiber S.N., Knutti D., Kralli A.
J. Biol. Chem. 277:13918-13925(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 5), SUBCELLULAR LOCATION, MOTIF, TISSUE SPECIFICITY, MUTAGENESIS OF 92-LEU--LEU-96; 155-LEU--LEU-160 AND 343-LEU--LEU-347, INTERACTION WITH ESR1, FUNCTION.
[2]"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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), TISSUE SPECIFICITY, FUNCTION, VARIANT GLN-265.
[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. expand/collapse author list , 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 6).
Tissue: Tongue.
[4]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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), VARIANT SER-292.
[7]"Coordinated reduction of genes of oxidative metabolism in humans with insulin resistance and diabetes: potential role of PGC1 and NRF1."
Patti M.E., Butte A.J., Crunkhorn S., Cusi K., Berria R., Kashyap S., Miyazaki Y., Kohane I., Costello M., Saccone R., Landaker E.J., Goldfine A.B., Mun E., DeFronzo R., Finlayson J., Kahn C.R., Mandarino L.J.
Proc. Natl. Acad. Sci. U.S.A. 100:8466-8471(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[8]"Multiple environmental and genetic factors influence skeletal muscle PGC-1alpha and PGC-1beta gene expression in twins."
Ling C., Poulsen P., Carlsson E., Ridderstrale M., Almgren P., Wojtaszewski J., Beck-Nielsen H., Groop L., Vaag A.
J. Clin. Invest. 114:1518-1526(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INDUCTION BY INSULIN AND AGING.
[9]"Evidence of an association between genetic variation of the coactivator PGC-1beta and obesity."
Andersen G., Wegner L., Yanagisawa K., Rose C.S., Lin J., Gluemer C., Drivsholm T., Borch-Johnsen K., Jorgensen T., Hansen T., Spiegelman B.M., Pedersen O.
J. Med. Genet. 42:402-407(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: POLYMORPHISM, VARIANTS PRO-203; ILE-279 AND SER-292.
[10]"Fatty acid-induced differential regulation of the genes encoding peroxisome proliferator-activated receptor-gamma coactivator-1alpha and -1beta in human skeletal muscle cells that have been differentiated in vitro."
Staiger H., Staiger K., Haas C., Weisser M., Machicao F., Haering H.-U.
Diabetologia 48:2115-2118(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REGULATION BY FATTY ACIDS.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Peroxisome proliferator-activated receptor gamma coactivator 1 (PGC-1)- and estrogen-related receptor (ERR)-induced regulator in muscle 1 (Perm1) is a tissue-specific regulator of oxidative capacity in skeletal muscle cells."
Cho Y., Hazen B.C., Russell A.P., Kralli A.
J. Biol. Chem. 288:25207-25218(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF468496 mRNA. Translation: AAL78633.1.
AF468497 mRNA. Translation: AAL78634.1.
AY188947 mRNA. Translation: AAO40022.1.
AY188948 mRNA. Translation: AAO40023.1.
AY188949 mRNA. Translation: AAO40024.1.
AY188950 mRNA. Translation: AAO40025.1.
AK095391 mRNA. Translation: BAC04541.1.
AK123614 mRNA. Translation: BAG53922.1.
AC008545 Genomic DNA. No translation available.
AC022100 Genomic DNA. No translation available.
CH471062 Genomic DNA. Translation: EAW61759.1.
BC132971 mRNA. Translation: AAI32972.1.
BC132973 mRNA. Translation: AAI32974.1.
RefSeqNP_001166169.1. NM_001172698.1.
NP_001166170.1. NM_001172699.1.
NP_573570.3. NM_133263.3.
XP_005268429.1. XM_005268372.2.
UniGeneHs.483816.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3SP6X-ray2.21B153-163[»]
ProteinModelPortalQ86YN6.
SMRQ86YN6. Positions 903-964.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid126361. 17 interactions.

PTM databases

PhosphoSiteQ86YN6.

Polymorphism databases

DMDM116242724.

Proteomic databases

PaxDbQ86YN6.
PRIDEQ86YN6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309241; ENSP00000312649; ENSG00000155846. [Q86YN6-1]
ENST00000360453; ENSP00000353638; ENSG00000155846. [Q86YN6-5]
ENST00000394320; ENSP00000377855; ENSG00000155846. [Q86YN6-3]
ENST00000403750; ENSP00000384403; ENSG00000155846. [Q86YN6-6]
GeneID133522.
KEGGhsa:133522.
UCSCuc003lrb.2. human. [Q86YN6-3]
uc003lrc.3. human. [Q86YN6-1]
uc003lrd.3. human. [Q86YN6-5]
uc003lre.1. human. [Q86YN6-4]
uc003lrf.3. human. [Q86YN6-2]
uc021yfr.1. human. [Q86YN6-6]

Organism-specific databases

CTD133522.
GeneCardsGC05P149109.
HGNCHGNC:30022. PPARGC1B.
MIM608886. gene.
neXtProtNX_Q86YN6.
PharmGKBPA134953410.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG87590.
HOGENOMHOG000236356.
HOVERGENHBG080730.
InParanoidQ86YN6.
KOK17962.
OMACESGCGD.
OrthoDBEOG7S4X5H.
PhylomeDBQ86YN6.
TreeFamTF343068.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

BgeeQ86YN6.
CleanExHS_PPARGC1B.
GenevestigatorQ86YN6.

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

EvolutionaryTraceQ86YN6.
GeneWikiPPARGC1B.
GenomeRNAi133522.
NextBio83227.
PROQ86YN6.
SOURCESearch...

Entry information

Entry namePRGC2_HUMAN
AccessionPrimary (citable) accession number: Q86YN6
Secondary accession number(s): A2RUM8 expand/collapse secondary AC list , A2RUN0, B3KVW0, Q86YN3, Q86YN4, Q86YN5, Q8N1N9, Q8TDE4, Q8TDE5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: October 17, 2006
Last modified: April 16, 2014
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM