PRGC2_HUMAN - dbPTM
PRGC2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PRGC2_HUMAN
UniProt AC Q86YN6
Protein Name Peroxisome proliferator-activated receptor gamma coactivator 1-beta
Gene Name PPARGC1B
Organism Homo sapiens (Human).
Sequence Length 1023
Subcellular Localization Nucleus .
Protein Description Plays a role of stimulator of transcription factors and nuclear receptors activities. Activates transcriptional 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..
Protein Sequence MAGNDCGALLDEELSSFFLNYLADTQGGGSGEEQLYADFPELDLSQLDASDFDSATCFGELQWCPENSETEPNQYSPDDSELFQIDSENEALLAELTKTLDDIPEDDVGLAAFPALDGGDALSCTSASPAPSSAPPSPAPEKPSAPAPEVDELSLLQKLLLATSYPTSSSDTQKEGTAWRQAGLRSKSQRPCVKADSTQDKKAPMMQSQSRSCTELHKHLTSAQCCLQDRGLQPPCLQSPRLPAKEDKEPGEDCPSPQPAPASPRDSLALGRADPGAPVSQEDMQAMVQLIRYMHTYCLPQRKLPPQTPEPLPKACSNPSQQVRSRPWSRHHSKASWAEFSILRELLAQDVLCDVSKPYRLATPVYASLTPRSRPRPPKDSQASPGRPSSVEEVRIAASPKSTGPRPSLRPLRLEVKREVRRPARLQQQEEEDEEEEEEEEEEEKEEEEEWGRKRPGRGLPWTKLGRKLESSVCPVRRSRRLNPELGPWLTFADEPLVPSEPQGALPSLCLAPKAYDVERELGSPTDEDSGQDQQLLRGPQIPALESPCESGCGDMDEDPSCPQLPPRDSPRCLMLALSQSDPTFGKKSFEQTLTVELCGTAGLTPPTTPPYKPTEEDPFKPDIKHSLGKEIALSLPSPEGLSLKATPGAAHKLPKKHPERSELLSHLRHATAQPASQAGQKRPFSCSFGDHDYCQVLRPEGVLQRKVLRSWEPSGVHLEDWPQQGAPWAEAQAPGREEDRSCDAGAPPKDSTLLRDHEIRASLTKHFGLLETALEEEDLASCKSPEYDTVFEDSSSSSGESSFLPEEEEEEGEEEEEDDEEEDSGVSPTCSDHCPYQSPPSKANRQLCSRSRSSSGSSPCHSWSPATRRNFRCESRGPCSDRTPSIRHARKRREKAIGEGRVVYIQNLSSDMSSRELKRRFEVFGEIEECEVLTRNRRGEKYGFITYRCSEHAALSLTKGAALRKRNEPSFQLSYGGLRHFCWPRYTDYDSNSEEALPASGKSKYEAMDFDSLLKEAQQSLH
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
197O-linked_GlycosylationRPCVKADSTQDKKAP
CCCCCCCCCCCCCCH		32.5930379171
198O-linked_GlycosylationPCVKADSTQDKKAPM
CCCCCCCCCCCCCHH		41.1430379171
208PhosphorylationKKAPMMQSQSRSCTE
CCCHHHHHCCCHHHH		16.5425072903
210PhosphorylationAPMMQSQSRSCTELH
CHHHHHCCCHHHHHH		31.2625072903
212PhosphorylationMMQSQSRSCTELHKH
HHHHCCCHHHHHHHH		30.5525072903
214PhosphorylationQSQSRSCTELHKHLT
HHCCCHHHHHHHHHH		42.7125072903
239PhosphorylationLQPPCLQSPRLPAKE
CCCCCCCCCCCCCCC		10.0725159151
245AcetylationQSPRLPAKEDKEPGE
CCCCCCCCCCCCCCC		65.5926051181
256PhosphorylationEPGEDCPSPQPAPAS
CCCCCCCCCCCCCCC		42.3628450419
263PhosphorylationSPQPAPASPRDSLAL
CCCCCCCCHHHHHHC		21.2928450419
267PhosphorylationAPASPRDSLALGRAD
CCCCHHHHHHCCCCC		19.4730576142
303UbiquitinationTYCLPQRKLPPQTPE
HHHCCCCCCCCCCCC		61.16-
308PhosphorylationQRKLPPQTPEPLPKA
CCCCCCCCCCCCCHH		35.0822985185
314UbiquitinationQTPEPLPKACSNPSQ
CCCCCCCHHCCCHHH		70.48-
317PhosphorylationEPLPKACSNPSQQVR
CCCCHHCCCHHHHHH		57.5528842319
320PhosphorylationPKACSNPSQQVRSRP
CHHCCCHHHHHHHCC		37.1828842319
357UbiquitinationDVLCDVSKPYRLATP
CCCCCCCCCCCCCCC		46.01-
357AcetylationDVLCDVSKPYRLATP
CCCCCCCCCCCCCCC		46.0126051181
363PhosphorylationSKPYRLATPVYASLT
CCCCCCCCCEEECCC		20.2028555341
366PhosphorylationYRLATPVYASLTPRS
CCCCCCEEECCCCCC		7.5327642862
370PhosphorylationTPVYASLTPRSRPRP
CCEEECCCCCCCCCC		17.7328555341
381PhosphorylationRPRPPKDSQASPGRP
CCCCCCCCCCCCCCC		33.5030266825
384PhosphorylationPPKDSQASPGRPSSV
CCCCCCCCCCCCCCH		21.9130266825
389PhosphorylationQASPGRPSSVEEVRI
CCCCCCCCCHHEEEE		45.7330266825
390PhosphorylationASPGRPSSVEEVRIA
CCCCCCCCHHEEEEE		35.9130266825
399PhosphorylationEEVRIAASPKSTGPR
HEEEEECCCCCCCCC		24.6824719451
464AcetylationGRGLPWTKLGRKLES
CCCCCHHHHHHHHHH		45.1126051181
516PhosphorylationLCLAPKAYDVERELG
CEECCCCCCHHHHHC		27.0128450419
524PhosphorylationDVERELGSPTDEDSG
CHHHHHCCCCCCCCC		36.9325159151
526PhosphorylationERELGSPTDEDSGQD
HHHHCCCCCCCCCHH		54.4325262027
530PhosphorylationGSPTDEDSGQDQQLL
CCCCCCCCCHHHHHH		35.9828450419
570PhosphorylationPQLPPRDSPRCLMLA
CCCCCCCCCCCEEHH		18.6117554339
587AcetylationQSDPTFGKKSFEQTL
CCCCCCCCCCHHEEE		40.8426051181
630AcetylationDIKHSLGKEIALSLP
CCCHHCCCCCEECCC		51.7626051181
635PhosphorylationLGKEIALSLPSPEGL
CCCCCEECCCCCCCC		29.2528634298
638PhosphorylationEIALSLPSPEGLSLK
CCEECCCCCCCCCCC		40.6621712546
643PhosphorylationLPSPEGLSLKATPGA
CCCCCCCCCCCCCCC		38.3929978859
647PhosphorylationEGLSLKATPGAAHKL
CCCCCCCCCCCHHCC		22.2221712546
711PhosphorylationLQRKVLRSWEPSGVH
HHHHHHHHCCCCCCC		31.4622817900
763PhosphorylationRDHEIRASLTKHFGL
CHHHHHHHHHHHHCH		27.0725627689
854PhosphorylationQLCSRSRSSSGSSPC
HHHHCCCCCCCCCCC		30.06-
856PhosphorylationCSRSRSSSGSSPCHS
HHCCCCCCCCCCCCC		43.8924719451
859PhosphorylationSRSSSGSSPCHSWSP
CCCCCCCCCCCCCCH		34.7624719451
865PhosphorylationSSPCHSWSPATRRNF
CCCCCCCCHHHCCCC		13.99-
886PhosphorylationPCSDRTPSIRHARKR
CCCCCCHHHHHHHHH		31.4824719451
943PhosphorylationRNRRGEKYGFITYRC
ECCCCCEEEEEEEEC		16.99-
947PhosphorylationGEKYGFITYRCSEHA
CCEEEEEEEECCHHH		11.58-
948PhosphorylationEKYGFITYRCSEHAA
CEEEEEEEECCHHHH		12.57-
957PhosphorylationCSEHAALSLTKGAAL
CCHHHHHHHHCCHHH		29.3024719451
971PhosphorylationLRKRNEPSFQLSYGG
HHHCCCCCEEEEECC		21.3228555341
987PhosphorylationRHFCWPRYTDYDSNS
HHCCCCCCCCCCCCC		10.4122817900
988PhosphorylationHFCWPRYTDYDSNSE
HCCCCCCCCCCCCCC		29.3925599653
990PhosphorylationCWPRYTDYDSNSEEA
CCCCCCCCCCCCCCC		17.3025884760
992PhosphorylationPRYTDYDSNSEEALP
CCCCCCCCCCCCCCC		35.7128450419
994PhosphorylationYTDYDSNSEEALPAS
CCCCCCCCCCCCCCC		40.5422210691
1001PhosphorylationSEEALPASGKSKYEA
CCCCCCCCCCCHHHH		44.8325599653
1013PhosphorylationYEAMDFDSLLKEAQQ
HHHCCHHHHHHHHHH		35.2824719451
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of PRGC2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PRGC2_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of PRGC2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ESR1_HUMANESR1physical
11854298
HNF4A_HUMANHNF4Aphysical
11733490
THB_HUMANTHRBphysical
11733490
PPARA_HUMANPPARAphysical
11733490
ERR3_MOUSEEsrrggenetic
12470660
ZBTB9_HUMANZBTB9physical
20211142
FOXA2_HUMANFOXA2physical
16459311
SRC_HUMANSRCphysical
17631495
PIAS1_HUMANPIAS1physical
22969086
PPARG_HUMANPPARGphysical
25985799
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PRGC2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524, AND MASSSPECTROMETRY.

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