Q86YN6 (PRGC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	PPARGC1B
Synonyms:	PERC, PGC1, PGC1B, PPARGC1

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	1023 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.1 Ref.2 Ref.8
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 process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	RNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin filament organization Inferred from electronic annotation. Source: Compara bone trabecula formation Inferred from electronic annotation. Source: Compara cellular response to reactive oxygen species Inferred from electronic annotation. Source: Compara intracellular estrogen receptor signaling pathway Inferred from direct assay Ref.1. Source: UniProtKB negative regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: Compara ossification Inferred from electronic annotation. Source: Compara positive regulation of alkaline phosphatase activity Inferred from electronic annotation. Source: Compara positive regulation of bone resorption Inferred from electronic annotation. Source: Compara positive regulation of osteoclast differentiation Inferred from electronic annotation. Source: Compara positive regulation of phosphorylation Inferred from electronic annotation. Source: Compara positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.1. Source: UniProtKB response to cAMP Inferred from electronic annotation. Source: Compara response to glucocorticoid stimulus Inferred from electronic annotation. Source: Compara transcription from mitochondrial promoter Inferred from electronic annotation. Source: Compara
Cellular_component	mediator complex Inferred from direct assay Ref.1. Source: UniProtKB mitochondrion Inferred from electronic annotation. Source: Compara
Molecular_function	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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1023

1023

Peroxisome proliferator-activated receptor gamma coactivator 1-beta

PRO_0000240158

Regions

Domain

902 – 976

75

RRM

Region

1 – 91

91

Abolishes DNA transcriptional activity when missing

Motif

156 – 160

5

LXXLL motif 1

Motif

343 – 347

5

LXXLL motif 2

Motif

691 – 694

4

HCFC1-binding-motif (HBM)

Compositional bias

430 – 450

21

Glu-rich

Compositional bias

772 – 823

52

Glu-rich

Amino acid modifications

Modified residue

524

1

Phosphoserine Ref.11

Natural variations

Alternative sequence

1 – 26

26

MAGND…LADTQ → MGVYK in isoform 2 and isoform 4.

VSP_019299

Alternative sequence

1 – 26

26

MAGND…LADTQ → M in isoform 6.

VSP_043374

Alternative sequence

156 – 194

39

Missing in isoform 5 and isoform 6.

VSP_019300

Alternative sequence

991 – 1023

33

DSNSE…QQSLH → GKPLKPSHSLVRLKAWEAVP SLNKTQS in isoform 3 and isoform 4.

VSP_019301

Natural variant

203

1

A → P. Ref.9
Corresponds to variant rs7732671 [ dbSNP | Ensembl ].

VAR_026698

Natural variant

265

1

R → Q. Ref.2
Corresponds to variant rs45520937 [ dbSNP | Ensembl ].

VAR_026699

Natural variant

279

1

V → I. Ref.9
Corresponds to variant rs17572019 [ dbSNP | Ensembl ].

VAR_026700

Natural variant

292

1

R → S. Ref.6 Ref.9
Corresponds to variant rs11959820 [ dbSNP | Ensembl ].

VAR_026701

Experimental info

Mutagenesis

92 – 96

5

LLAEL → AAAEA: Reduces DNA transcriptional activity.

Mutagenesis

155 – 160

6

LLQKLL → AAQKAA: Reduces interaction and activation of ESR1. Loss of interaction and activation of ESR1; when associated with 343-AREAA-347. Ref.1

Mutagenesis

343 – 347

5

LRELL → AREAA: Reduces interaction and activation of ESR1. Loss of interaction and activation of ESR1; when associated with 155-AAQKAA-160. Ref.1

Sequence conflict

558

1

E → G in BAC04541. Ref.3

Secondary structure

1

.

.

.

1023

Helix Strand Turn

Details...

Helix

155 – 162

8

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (PGC1beta-1a) [UniParc]. Last modified October 17, 2006. Version 2. Checksum: DC37FCDE4D3CD239	FASTA	1,023	113,222
	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
	Isoform 2 (PGC1beta-2a) [UniParc]. Checksum: 8ACBD368E172B27E	FASTA	1,002	110,981
	10 20 30 40 50 60 MGVYKGGGSG EEQLYADFPE LDLSQLDASD FDSATCFGEL QWCPENSETE PNQYSPDDSE 70 80 90 100 110 120 LFQIDSENEA LLAELTKTLD DIPEDDVGLA AFPALDGGDA LSCTSASPAP SSAPPSPAPE 130 140 150 160 170 180 KPSAPAPEVD ELSLLQKLLL ATSYPTSSSD TQKEGTAWRQ AGLRSKSQRP CVKADSTQDK 190 200 210 220 230 240 KAPMMQSQSR SCTELHKHLT SAQCCLQDRG LQPPCLQSPR LPAKEDKEPG EDCPSPQPAP 250 260 270 280 290 300 ASPRDSLALG RADPGAPVSQ EDMQAMVQLI RYMHTYCLPQ RKLPPQTPEP LPKACSNPSQ 310 320 330 340 350 360 QVRSRPWSRH HSKASWAEFS ILRELLAQDV LCDVSKPYRL ATPVYASLTP RSRPRPPKDS 370 380 390 400 410 420 QASPGRPSSV EEVRIAASPK STGPRPSLRP LRLEVKREVR RPARLQQQEE EDEEEEEEEE 430 440 450 460 470 480 EEEKEEEEEW GRKRPGRGLP WTKLGRKLES SVCPVRRSRR LNPELGPWLT FADEPLVPSE 490 500 510 520 530 540 PQGALPSLCL APKAYDVERE LGSPTDEDSG QDQQLLRGPQ IPALESPCES GCGDMDEDPS 550 560 570 580 590 600 CPQLPPRDSP RCLMLALSQS DPTFGKKSFE QTLTVELCGT AGLTPPTTPP YKPTEEDPFK 610 620 630 640 650 660 PDIKHSLGKE IALSLPSPEG LSLKATPGAA HKLPKKHPER SELLSHLRHA TAQPASQAGQ 670 680 690 700 710 720 KRPFSCSFGD HDYCQVLRPE GVLQRKVLRS WEPSGVHLED WPQQGAPWAE AQAPGREEDR 730 740 750 760 770 780 SCDAGAPPKD STLLRDHEIR ASLTKHFGLL ETALEEEDLA SCKSPEYDTV FEDSSSSSGE 790 800 810 820 830 840 SSFLPEEEEE EGEEEEEDDE EEDSGVSPTC SDHCPYQSPP SKANRQLCSR SRSSSGSSPC 850 860 870 880 890 900 HSWSPATRRN FRCESRGPCS DRTPSIRHAR KRREKAIGEG RVVYIQNLSS DMSSRELKRR 910 920 930 940 950 960 FEVFGEIEEC EVLTRNRRGE KYGFITYRCS EHAALSLTKG AALRKRNEPS FQLSYGGLRH 970 980 990 1000 FCWPRYTDYD SNSEEALPAS GKSKYEAMDF DSLLKEAQQS LH
	Isoform 3 (PGC1beta-1b) [UniParc]. Checksum: F2229A0A356A2148	FASTA	1,017	112,568
	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 GAALRKRNEP SFQLSYGGLR HFCWPRYTDY GKPLKPSHSL VRLKAWEAVP SLNKTQS
	Isoform 4 (PGC1beta-2b) [UniParc]. Checksum: 5265F3916B919ECC	FASTA	996	110,327
	10 20 30 40 50 60 MGVYKGGGSG EEQLYADFPE LDLSQLDASD FDSATCFGEL QWCPENSETE PNQYSPDDSE 70 80 90 100 110 120 LFQIDSENEA LLAELTKTLD DIPEDDVGLA AFPALDGGDA LSCTSASPAP SSAPPSPAPE 130 140 150 160 170 180 KPSAPAPEVD ELSLLQKLLL ATSYPTSSSD TQKEGTAWRQ AGLRSKSQRP CVKADSTQDK 190 200 210 220 230 240 KAPMMQSQSR SCTELHKHLT SAQCCLQDRG LQPPCLQSPR LPAKEDKEPG EDCPSPQPAP 250 260 270 280 290 300 ASPRDSLALG RADPGAPVSQ EDMQAMVQLI RYMHTYCLPQ RKLPPQTPEP LPKACSNPSQ 310 320 330 340 350 360 QVRSRPWSRH HSKASWAEFS ILRELLAQDV LCDVSKPYRL ATPVYASLTP RSRPRPPKDS 370 380 390 400 410 420 QASPGRPSSV EEVRIAASPK STGPRPSLRP LRLEVKREVR RPARLQQQEE EDEEEEEEEE 430 440 450 460 470 480 EEEKEEEEEW GRKRPGRGLP WTKLGRKLES SVCPVRRSRR LNPELGPWLT FADEPLVPSE 490 500 510 520 530 540 PQGALPSLCL APKAYDVERE LGSPTDEDSG QDQQLLRGPQ IPALESPCES GCGDMDEDPS 550 560 570 580 590 600 CPQLPPRDSP RCLMLALSQS DPTFGKKSFE QTLTVELCGT AGLTPPTTPP YKPTEEDPFK 610 620 630 640 650 660 PDIKHSLGKE IALSLPSPEG LSLKATPGAA HKLPKKHPER SELLSHLRHA TAQPASQAGQ 670 680 690 700 710 720 KRPFSCSFGD HDYCQVLRPE GVLQRKVLRS WEPSGVHLED WPQQGAPWAE AQAPGREEDR 730 740 750 760 770 780 SCDAGAPPKD STLLRDHEIR ASLTKHFGLL ETALEEEDLA SCKSPEYDTV FEDSSSSSGE 790 800 810 820 830 840 SSFLPEEEEE EGEEEEEDDE EEDSGVSPTC SDHCPYQSPP SKANRQLCSR SRSSSGSSPC 850 860 870 880 890 900 HSWSPATRRN FRCESRGPCS DRTPSIRHAR KRREKAIGEG RVVYIQNLSS DMSSRELKRR 910 920 930 940 950 960 FEVFGEIEEC EVLTRNRRGE KYGFITYRCS EHAALSLTKG AALRKRNEPS FQLSYGGLRH 970 980 990 FCWPRYTDYG KPLKPSHSLV RLKAWEAVPS LNKTQS
	Isoform 5 (PERC-s) [UniParc]. Checksum: 5D91928FD6D6D104	FASTA	984	108,919
	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 DELSLADSTQ DKKAPMMQSQ SRSCTELHKH 190 200 210 220 230 240 LTSAQCCLQD RGLQPPCLQS PRLPAKEDKE PGEDCPSPQP APASPRDSLA LGRADPGAPV 250 260 270 280 290 300 SQEDMQAMVQ LIRYMHTYCL PQRKLPPQTP EPLPKACSNP SQQVRSRPWS RHHSKASWAE 310 320 330 340 350 360 FSILRELLAQ DVLCDVSKPY RLATPVYASL TPRSRPRPPK DSQASPGRPS SVEEVRIAAS 370 380 390 400 410 420 PKSTGPRPSL RPLRLEVKRE VRRPARLQQQ EEEDEEEEEE EEEEEKEEEE EWGRKRPGRG 430 440 450 460 470 480 LPWTKLGRKL ESSVCPVRRS RRLNPELGPW LTFADEPLVP SEPQGALPSL CLAPKAYDVE 490 500 510 520 530 540 RELGSPTDED SGQDQQLLRG PQIPALESPC ESGCGDMDED PSCPQLPPRD SPRCLMLALS 550 560 570 580 590 600 QSDPTFGKKS FEQTLTVELC GTAGLTPPTT PPYKPTEEDP FKPDIKHSLG KEIALSLPSP 610 620 630 640 650 660 EGLSLKATPG AAHKLPKKHP ERSELLSHLR HATAQPASQA GQKRPFSCSF GDHDYCQVLR 670 680 690 700 710 720 PEGVLQRKVL RSWEPSGVHL EDWPQQGAPW AEAQAPGREE DRSCDAGAPP KDSTLLRDHE 730 740 750 760 770 780 IRASLTKHFG LLETALEEED LASCKSPEYD TVFEDSSSSS GESSFLPEEE EEEGEEEEED 790 800 810 820 830 840 DEEEDSGVSP TCSDHCPYQS PPSKANRQLC SRSRSSSGSS PCHSWSPATR RNFRCESRGP 850 860 870 880 890 900 CSDRTPSIRH ARKRREKAIG EGRVVYIQNL SSDMSSRELK RRFEVFGEIE ECEVLTRNRR 910 920 930 940 950 960 GEKYGFITYR CSEHAALSLT KGAALRKRNE PSFQLSYGGL RHFCWPRYTD YDSNSEEALP 970 980 ASGKSKYEAM DFDSLLKEAQ QSLH
	Isoform 6 [UniParc]. Checksum: D4E5EF57FC0C2459	FASTA	959	106,230
	10 20 30 40 50 60 MGGGSGEEQL YADFPELDLS QLDASDFDSA TCFGELQWCP ENSETEPNQY SPDDSELFQI 70 80 90 100 110 120 DSENEALLAE LTKTLDDIPE DDVGLAAFPA LDGGDALSCT SASPAPSSAP PSPAPEKPSA 130 140 150 160 170 180 PAPEVDELSL ADSTQDKKAP MMQSQSRSCT ELHKHLTSAQ CCLQDRGLQP PCLQSPRLPA 190 200 210 220 230 240 KEDKEPGEDC PSPQPAPASP RDSLALGRAD PGAPVSQEDM QAMVQLIRYM HTYCLPQRKL 250 260 270 280 290 300 PPQTPEPLPK ACSNPSQQVR SRPWSRHHSK ASWAEFSILR ELLAQDVLCD VSKPYRLATP 310 320 330 340 350 360 VYASLTPRSR PRPPKDSQAS PGRPSSVEEV RIAASPKSTG PRPSLRPLRL EVKREVRRPA 370 380 390 400 410 420 RLQQQEEEDE EEEEEEEEEE KEEEEEWGRK RPGRGLPWTK LGRKLESSVC PVRRSRRLNP 430 440 450 460 470 480 ELGPWLTFAD EPLVPSEPQG ALPSLCLAPK AYDVERELGS PTDEDSGQDQ QLLRGPQIPA 490 500 510 520 530 540 LESPCESGCG DMDEDPSCPQ LPPRDSPRCL MLALSQSDPT FGKKSFEQTL TVELCGTAGL 550 560 570 580 590 600 TPPTTPPYKP TEEDPFKPDI KHSLGKEIAL SLPSPEGLSL KATPGAAHKL PKKHPERSEL 610 620 630 640 650 660 LSHLRHATAQ PASQAGQKRP FSCSFGDHDY CQVLRPEGVL QRKVLRSWEP SGVHLEDWPQ 670 680 690 700 710 720 QGAPWAEAQA PGREEDRSCD AGAPPKDSTL LRDHEIRASL TKHFGLLETA LEEEDLASCK 730 740 750 760 770 780 SPEYDTVFED SSSSSGESSF LPEEEEEEGE EEEEDDEEED SGVSPTCSDH CPYQSPPSKA 790 800 810 820 830 840 NRQLCSRSRS SSGSSPCHSW SPATRRNFRC ESRGPCSDRT PSIRHARKRR EKAIGEGRVV 850 860 870 880 890 900 YIQNLSSDMS SRELKRRFEV FGEIEECEVL TRNRRGEKYG FITYRCSEHA ALSLTKGAAL 910 920 930 940 950 RKRNEPSFQL SYGGLRHFCW PRYTDYDSNS EEALPASGKS KYEAMDFDSL LKEAQQSLH

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
+	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.

IPI

IPI00152517.
IPI00163514.
IPI00759533.
IPI00759561.
IPI00759685.
IPI00883834.

RefSeq

NP_001166169.1. NM_001172698.1.
NP_001166170.1. NM_001172699.1.
NP_573570.3. NM_133263.3.

UniGene

Hs.483816.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3SP6	X-ray	2.21	B	153-163	[»]

ProteinModelPortal

Q86YN6.

ModBase

Search...

PTM databases

PhosphoSite

Q86YN6.

Polymorphism databases

DMDM

116242724.

Proteomic databases

PaxDb

Q86YN6.

PRIDE

Q86YN6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000309241; ENSP00000312649; ENSG00000155846.
ENST00000360453; ENSP00000353638; ENSG00000155846.
ENST00000394320; ENSP00000377855; ENSG00000155846.
ENST00000403750; ENSP00000384403; ENSG00000155846.

GeneID

133522.

KEGG

hsa:133522.

UCSC

uc003lrb.2. human.
uc003lrc.3. human.
uc003lrd.3. human.
uc003lre.1. human.
uc003lrf.3. human.

Organism-specific databases

CTD

133522.

GeneCards

GC05P149109.

HGNC

HGNC:30022. PPARGC1B.

MIM

608886. gene.

neXtProt

NX_Q86YN6.

PharmGKB

PA134953410.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG87590.

HOGENOM

HOG000236356.

HOVERGEN

HBG080730.

InParanoid

Q86YN6.

OMA

EDPFKPD.

PhylomeDB

Q86YN6.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.

Gene expression databases

Bgee

Q86YN6.

CleanEx

HS_PPARGC1B.

Genevestigator

Q86YN6.

Family and domain databases

Gene3D

3.30.70.330. 1 hit.

InterPro

IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]

Pfam

PF00076. RRM_1. 1 hit.
[Graphical view]

SMART

SM00360. RRM. 1 hit.
[Graphical view]

PROSITE

PS50102. RRM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q86YN6.

GenomeRNAi

133522.

NextBio

83227.

SOURCE

Search...

Entry information

Entry name

PRGC2_HUMAN

Accession

Primary (citable) accession number: Q86YN6
Secondary accession number(s): A2RUM8 , 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:	May 1, 2013
This is version 91 of the entry and version 2 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.