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Protein

Peroxisome proliferator-activated receptor gamma coactivator 1-beta

Gene

PPARGC1B

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

Functioni

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.4 Publications

GO - Molecular functioni

  1. AF-2 domain binding Source: UniProtKB
  2. estrogen receptor binding Source: UniProtKB
  3. ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
  4. nucleotide binding Source: InterPro
  5. receptor activator activity Source: UniProtKB
  6. RNA binding Source: UniProtKB
  7. RNA polymerase II transcription cofactor activity Source: UniProtKB
  8. transcription factor binding Source: GO_Central

GO - Biological processi

  1. actin filament organization Source: Ensembl
  2. bone trabecula formation Source: Ensembl
  3. cellular lipid metabolic process Source: Reactome
  4. cellular response to reactive oxygen species Source: Ensembl
  5. intracellular estrogen receptor signaling pathway Source: UniProtKB
  6. mitochondrion organization Source: Reactome
  7. negative regulation of transcription, DNA-templated Source: Ensembl
  8. organelle organization Source: Reactome
  9. ossification Source: Ensembl
  10. positive regulation of alkaline phosphatase activity Source: Ensembl
  11. positive regulation of bone resorption Source: Ensembl
  12. positive regulation of osteoclast differentiation Source: Ensembl
  13. positive regulation of phosphorylation Source: Ensembl
  14. positive regulation of receptor activity Source: GOC
  15. positive regulation of sequence-specific DNA binding transcription factor activity Source: GO_Central
  16. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  17. regulation of transcription, DNA-templated Source: UniProtKB
  18. response to cAMP Source: Ensembl
  19. response to glucocorticoid Source: Ensembl
  20. small molecule metabolic process Source: Reactome
  21. transcription from mitochondrial promoter Source: Ensembl
  22. transcription from RNA polymerase II promoter Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_116145. PPARA activates gene expression.
REACT_200608. Transcriptional activation of mitochondrial biogenesis.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:PPARGC1B
Synonyms:PERC, PGC1, PGC1B, PPARGC1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:30022. PPARGC1B.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. mediator complex Source: UniProtKB
  2. mitochondrion Source: Ensembl
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi92 – 965LLAEL → AAAEA: Reduces DNA transcriptional activity. 1 Publication
Mutagenesisi155 – 1606LLQKLL → AAQKAA: Reduces interaction and activation of ESR1. Loss of interaction and activation of ESR1; when associated with 343-AREAA-347. 1 Publication
Mutagenesisi343 – 3475LRELL → AREAA: Reduces interaction and activation of ESR1. Loss of interaction and activation of ESR1; when associated with 155-AAQKAA-160. 1 Publication

Organism-specific databases

PharmGKBiPA134953410.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10231023Peroxisome proliferator-activated receptor gamma coactivator 1-betaPRO_0000240158Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei524 – 5241Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ86YN6.
PaxDbiQ86YN6.
PRIDEiQ86YN6.

PTM databases

PhosphoSiteiQ86YN6.

Expressioni

Tissue specificityi

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

Inductioni

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.2 Publications

Gene expression databases

BgeeiQ86YN6.
CleanExiHS_PPARGC1B.
GenevestigatoriQ86YN6.

Interactioni

Subunit structurei

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.By similarity1 Publication

Protein-protein interaction databases

BioGridi126361. 18 interactions.

Structurei

Secondary structure

1
1023
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi155 – 1628Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SP6X-ray2.21B153-163[»]
ProteinModelPortaliQ86YN6.
SMRiQ86YN6. Positions 900-992.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ86YN6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini902 – 97675RRMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 9191Abolishes DNA transcriptional activity when missingAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi156 – 1605LXXLL motif 1
Motifi343 – 3475LXXLL motif 2
Motifi691 – 6944HCFC1-binding-motif (HBM)

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi430 – 45021Glu-richAdd
BLAST
Compositional biasi772 – 82352Glu-richAdd
BLAST

Domaini

Sequence similaritiesi

Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG87590.
GeneTreeiENSGT00530000063196.
HOGENOMiHOG000236356.
HOVERGENiHBG080730.
InParanoidiQ86YN6.
KOiK17962.
OMAiIPALESP.
OrthoDBiEOG7S4X5H.
PhylomeDBiQ86YN6.
TreeFamiTF343068.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q86YN6-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAGNDCGALL DEELSSFFLN YLADTQGGGS GEEQLYADFP ELDLSQLDAS
60 70 80 90 100
DFDSATCFGE LQWCPENSET EPNQYSPDDS ELFQIDSENE ALLAELTKTL
110 120 130 140 150
DDIPEDDVGL AAFPALDGGD ALSCTSASPA PSSAPPSPAP EKPSAPAPEV
160 170 180 190 200
DELSLLQKLL LATSYPTSSS DTQKEGTAWR QAGLRSKSQR PCVKADSTQD
210 220 230 240 250
KKAPMMQSQS RSCTELHKHL TSAQCCLQDR GLQPPCLQSP RLPAKEDKEP
260 270 280 290 300
GEDCPSPQPA PASPRDSLAL GRADPGAPVS QEDMQAMVQL IRYMHTYCLP
310 320 330 340 350
QRKLPPQTPE PLPKACSNPS QQVRSRPWSR HHSKASWAEF SILRELLAQD
360 370 380 390 400
VLCDVSKPYR LATPVYASLT PRSRPRPPKD SQASPGRPSS VEEVRIAASP
410 420 430 440 450
KSTGPRPSLR PLRLEVKREV RRPARLQQQE EEDEEEEEEE EEEEKEEEEE
460 470 480 490 500
WGRKRPGRGL PWTKLGRKLE SSVCPVRRSR RLNPELGPWL TFADEPLVPS
510 520 530 540 550
EPQGALPSLC LAPKAYDVER ELGSPTDEDS GQDQQLLRGP QIPALESPCE
560 570 580 590 600
SGCGDMDEDP SCPQLPPRDS PRCLMLALSQ SDPTFGKKSF EQTLTVELCG
610 620 630 640 650
TAGLTPPTTP PYKPTEEDPF KPDIKHSLGK EIALSLPSPE GLSLKATPGA
660 670 680 690 700
AHKLPKKHPE RSELLSHLRH ATAQPASQAG QKRPFSCSFG DHDYCQVLRP
710 720 730 740 750
EGVLQRKVLR SWEPSGVHLE DWPQQGAPWA EAQAPGREED RSCDAGAPPK
760 770 780 790 800
DSTLLRDHEI RASLTKHFGL LETALEEEDL ASCKSPEYDT VFEDSSSSSG
810 820 830 840 850
ESSFLPEEEE EEGEEEEEDD EEEDSGVSPT CSDHCPYQSP PSKANRQLCS
860 870 880 890 900
RSRSSSGSSP CHSWSPATRR NFRCESRGPC SDRTPSIRHA RKRREKAIGE
910 920 930 940 950
GRVVYIQNLS SDMSSRELKR RFEVFGEIEE CEVLTRNRRG EKYGFITYRC
960 970 980 990 1000
SEHAALSLTK GAALRKRNEP SFQLSYGGLR HFCWPRYTDY DSNSEEALPA
1010 1020
SGKSKYEAMD FDSLLKEAQQ SLH
Length:1,023
Mass (Da):113,222
Last modified:October 17, 2006 - v2
Checksum:iDC37FCDE4D3CD239
GO
Isoform 2 (identifier: Q86YN6-2) [UniParc]FASTAAdd to basket

Also known as: PGC1beta-2a

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

Show »
Length:1,002
Mass (Da):110,981
Checksum:i8ACBD368E172B27E
GO
Isoform 3 (identifier: Q86YN6-3) [UniParc]FASTAAdd to basket

Also known as: PGC1beta-1b

The sequence of this isoform differs from the canonical sequence as follows:
     991-1023: DSNSEEALPASGKSKYEAMDFDSLLKEAQQSLH → GKPLKPSHSLVRLKAWEAVPSLNKTQS

Show »
Length:1,017
Mass (Da):112,568
Checksum:iF2229A0A356A2148
GO
Isoform 4 (identifier: Q86YN6-4) [UniParc]FASTAAdd to basket

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

Show »
Length:996
Mass (Da):110,327
Checksum:i5265F3916B919ECC
GO
Isoform 5 (identifier: Q86YN6-5) [UniParc]FASTAAdd to basket

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.

Show »
Length:984
Mass (Da):108,919
Checksum:i5D91928FD6D6D104
GO
Isoform 6 (identifier: Q86YN6-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-26: MAGNDCGALLDEELSSFFLNYLADTQ → M
     156-194: Missing.

Note: No experimental confirmation available.

Show »
Length:959
Mass (Da):106,230
Checksum:iD4E5EF57FC0C2459
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti558 – 5581E → G in BAC04541 (PubMed:14702039).Curated

Polymorphismi

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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti203 – 2031A → P.1 Publication
Corresponds to variant rs7732671 [ dbSNP | Ensembl ].
VAR_026698
Natural varianti265 – 2651R → Q.1 Publication
Corresponds to variant rs45520937 [ dbSNP | Ensembl ].
VAR_026699
Natural varianti279 – 2791V → I.1 Publication
Corresponds to variant rs17572019 [ dbSNP | Ensembl ].
VAR_026700
Natural varianti292 – 2921R → S.2 Publications
Corresponds to variant rs11959820 [ dbSNP | Ensembl ].
VAR_026701

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2626MAGND…LADTQ → MGVYK in isoform 2 and isoform 4. 1 PublicationVSP_019299Add
BLAST
Alternative sequencei1 – 2626MAGND…LADTQ → M in isoform 6. 1 PublicationVSP_043374Add
BLAST
Alternative sequencei156 – 19439Missing in isoform 5 and isoform 6. 2 PublicationsVSP_019300Add
BLAST
Alternative sequencei991 – 102333DSNSE…QQSLH → GKPLKPSHSLVRLKAWEAVP SLNKTQS in isoform 3 and isoform 4. 1 PublicationVSP_019301Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4298.1. [Q86YN6-1]
CCDS54933.1. [Q86YN6-5]
CCDS54934.1. [Q86YN6-6]
RefSeqiNP_001166169.1. NM_001172698.1. [Q86YN6-5]
NP_001166170.1. NM_001172699.1. [Q86YN6-6]
NP_573570.3. NM_133263.3. [Q86YN6-1]
XP_005268429.1. XM_005268372.2. [Q86YN6-2]
UniGeneiHs.483816.

Genome annotation databases

EnsembliENST00000309241; ENSP00000312649; ENSG00000155846. [Q86YN6-1]
ENST00000360453; ENSP00000353638; ENSG00000155846. [Q86YN6-5]
ENST00000394320; ENSP00000377855; ENSG00000155846. [Q86YN6-3]
ENST00000403750; ENSP00000384403; ENSG00000155846. [Q86YN6-6]
GeneIDi133522.
KEGGihsa:133522.
UCSCiuc003lrb.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]

Polymorphism databases

DMDMi116242724.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4298.1. [Q86YN6-1]
CCDS54933.1. [Q86YN6-5]
CCDS54934.1. [Q86YN6-6]
RefSeqiNP_001166169.1. NM_001172698.1. [Q86YN6-5]
NP_001166170.1. NM_001172699.1. [Q86YN6-6]
NP_573570.3. NM_133263.3. [Q86YN6-1]
XP_005268429.1. XM_005268372.2. [Q86YN6-2]
UniGeneiHs.483816.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3SP6X-ray2.21B153-163[»]
ProteinModelPortaliQ86YN6.
SMRiQ86YN6. Positions 900-992.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126361. 18 interactions.

PTM databases

PhosphoSiteiQ86YN6.

Polymorphism databases

DMDMi116242724.

Proteomic databases

MaxQBiQ86YN6.
PaxDbiQ86YN6.
PRIDEiQ86YN6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000309241; ENSP00000312649; ENSG00000155846. [Q86YN6-1]
ENST00000360453; ENSP00000353638; ENSG00000155846. [Q86YN6-5]
ENST00000394320; ENSP00000377855; ENSG00000155846. [Q86YN6-3]
ENST00000403750; ENSP00000384403; ENSG00000155846. [Q86YN6-6]
GeneIDi133522.
KEGGihsa:133522.
UCSCiuc003lrb.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

CTDi133522.
GeneCardsiGC05P149109.
HGNCiHGNC:30022. PPARGC1B.
MIMi608886. gene.
neXtProtiNX_Q86YN6.
PharmGKBiPA134953410.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG87590.
GeneTreeiENSGT00530000063196.
HOGENOMiHOG000236356.
HOVERGENiHBG080730.
InParanoidiQ86YN6.
KOiK17962.
OMAiIPALESP.
OrthoDBiEOG7S4X5H.
PhylomeDBiQ86YN6.
TreeFamiTF343068.

Enzyme and pathway databases

ReactomeiREACT_116145. PPARA activates gene expression.
REACT_200608. Transcriptional activation of mitochondrial biogenesis.

Miscellaneous databases

ChiTaRSiPPARGC1B. human.
EvolutionaryTraceiQ86YN6.
GeneWikiiPPARGC1B.
GenomeRNAii133522.
NextBioi83227.
PROiQ86YN6.
SOURCEiSearch...

Gene expression databases

BgeeiQ86YN6.
CleanExiHS_PPARGC1B.
GenevestigatoriQ86YN6.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
PfamiPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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.

Entry informationi

Entry nameiPRGC2_HUMAN
AccessioniPrimary (citable) accession number: Q86YN6
Secondary accession number(s): A2RUM8
, A2RUN0, B3KVW0, Q86YN3, Q86YN4, Q86YN5, Q8N1N9, Q8TDE4, Q8TDE5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: October 17, 2006
Last modified: March 4, 2015
This is version 109 of the entry and version 2 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 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.