NCOA2_MOUSE - dbPTM
NCOA2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NCOA2_MOUSE
UniProt AC Q61026
Protein Name Nuclear receptor coactivator 2
Gene Name Ncoa2
Organism Mus musculus (Mouse).
Sequence Length 1462
Subcellular Localization Nucleus.
Protein Description Transcriptional coactivator for steroid receptors and nuclear receptors. Coactivator of the steroid binding domain (AF-2) but not of the modulating N-terminal domain (AF-1). Required with NCOA1 to control energy balance between white and brown adipose tissues. Critical regulator of glucose metabolism regulation, acts as RORA coactivator to specifically modulate G6PC expression. Involved in the positive regulation of the transcriptional activity of the glucocorticoid receptor NR3C1 by sumoylation enhancer RWDD3. Positively regulates the circadian clock by acting as a transcriptional coactivator for the CLOCK-ARNTL/BMAL1 heterodimer. [PubMed: 24529706]
Protein Sequence MSGMGENTSDPSRAETRKRKECPDQLGPSPKRSTEKRNREQENKYIEELAELIFANFNDIDNFNFKPDKCAILKETVKQIRQIKEQEKAAAANIDEVQKSDVSSTGQGVIDKDALGPMMLEALDGFFFVVNLEGSVVFVSENVTQYLRYNQEELMNKSVYSILHVGDHTEFVKNLLPKSMVNGGSWSGEPPRRSSHTFNCRMLVKPLPDSEEEGHDSQEAHQKYEAMQCFAVSQPKSIKEEGEDLQSCLICVARRVPMKERPTLPSSESFTTRQDLQGKITSLDTSTMRAAMKPGWEDLVRRCIQKFHTQHEGESLSYAKRHHHEVLRQGLAFSQIYRFSLSDGTLVAAQTKSKLIRSQTTNEPQLVISLHMLHREQNVCVMNPDLTGQAMGKPLNPISSSSPAHQALCSGNPGQDMTLGSNINFPMNGPKEQMGMPMGRFGGSGGMNHVSGMQATTPQGSNYALKMNSPSQSSPGMNPGQASSVLSPRQRMSPGVAGSPRIPPSQFSPAGSLHSPVGVCSSTGNSHSYTNSSLNALQALSEGHGVSLGSSLASPDLKMGNLQNSPVNMNPPPLSKMGSLDSKDCFGLYGEPSEGTTGQAEASCHPEEQKGPNDSSMPQAASGDRAEGHSRLHDSKGQTKLLQLLTTKSDQMEPSPLPSSLSDTNKDSTGSLPGPGSTHGTSLKEKHKILHRLLQDSSSPVDLAKLTAEATGKELSQESSSTAPGSEVTVKQEPASPKKKENALLRYLLDKDDTKDIGLPEITPKLERLDSKTDPASNTKLIAMKTVKEEVSFEPSDQPGSELDNLEEILDDLQNSQLPQLFPDTRPGAPTGSVDKQAIINDLMQLTADSSPVPPAGAQKAALRMSQSTFNNPRPGQLGRLLPNQNLPLDITLQSPTGAGPFPPIRNSSPYSVIPQPGMMGNQGMLGSQGNLGNNSTGMIGSSTSRPSMPSGEWAPQSPAVRVTCAATTGAMNRPVQGGMIRNPTASIPMRANSQPGQRQMLQSQVMNIGPSELEMNMGGPQYNQQQAPPNQTAPWPESILPIDQASFASQNRQPFGSSPDDLLCPHPAAESPSDEGALLDQLYLALRNFDGLEEIDRALGIPELVSQSQAVDAEQFSSQESSIMLEQKPPVFPQQYASQAQMAQGGYNPMQDPNFHTMGQRPNYTTLRMQPRPGLRPTGIVQNQPNQLRLQLQHRLQAQQNRQPLMNQISSVSNVNLTLRPGVPTQAPINAQMLAQRQREILNQHLRQRQMQQQVQQRTLMMRGQGLNVTPSMVAPAGLPAAMSNPRIPQANAQQFPFPPNYGISQQPDPGFTGATTPQSPLMSPRMAHTQSPMMQQSQANPAYQPTSDMNGWAQGSMGGNSMFSQQSPPHFGQQANTSMYSNNMNISVSMATNTGGLSSMNQMTGQMSMTSVTSVPTSGLPSMGPEQVNDPALRGGNLFPNQLPGMDMIKQEGDASRKYC
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
2Phosphorylation------MSGMGENTS
------CCCCCCCCC		49.1127087446
2Acetylation------MSGMGENTS
------CCCCCCCCC		49.11-
29PhosphorylationCPDQLGPSPKRSTEK
CCCCCCCCCCCCHHH		41.0525521595
31AcetylationDQLGPSPKRSTEKRN
CCCCCCCCCCHHHHC		64.42133285
185PhosphorylationKSMVNGGSWSGEPPR
HHHCCCCCCCCCCCC		21.3324759943
185O-linked_GlycosylationKSMVNGGSWSGEPPR
HHHCCCCCCCCCCCC		21.3355412805
210PhosphorylationLVKPLPDSEEEGHDS
EEEECCCCCCCCCCH		44.9919144319
217PhosphorylationSEEEGHDSQEAHQKY
CCCCCCCHHHHHHHH		25.0127841257
266PhosphorylationKERPTLPSSESFTTR
CCCCCCCCCCCCCCH		50.2622871156
279UbiquitinationTRQDLQGKITSLDTS
CHHHHCCCEEECCHH		29.8322790023
285PhosphorylationGKITSLDTSTMRAAM
CCEEECCHHHHHHHH		31.2429176673
286PhosphorylationKITSLDTSTMRAAMK
CEEECCHHHHHHHHC		21.6329176673
287PhosphorylationITSLDTSTMRAAMKP
EEECCHHHHHHHHCC		16.8729176673
318PhosphorylationHEGESLSYAKRHHHE
CCCCCCCHHHHHHHH		22.80-
338MethylationLAFSQIYRFSLSDGT
CHHHEEEEEECCCCC		19.1224129315
338Asymmetric dimethylarginineLAFSQIYRFSLSDGT
CHHHEEEEEECCCCC		19.12-
457PhosphorylationVSGMQATTPQGSNYA
CCCCCCCCCCCCCEE		19.34-
469PhosphorylationNYALKMNSPSQSSPG
CEEEECCCCCCCCCC		23.5621082442
471PhosphorylationALKMNSPSQSSPGMN
EEECCCCCCCCCCCC		42.3823527152
473PhosphorylationKMNSPSQSSPGMNPG
ECCCCCCCCCCCCCC		42.7226643407
474PhosphorylationMNSPSQSSPGMNPGQ
CCCCCCCCCCCCCCH		20.1723527152
483PhosphorylationGMNPGQASSVLSPRQ
CCCCCHHHHCCCHHH		17.0626643407
484PhosphorylationMNPGQASSVLSPRQR
CCCCHHHHCCCHHHC		30.0526643407
487PhosphorylationGQASSVLSPRQRMSP
CHHHHCCCHHHCCCC		18.8421082442
492OxidationVLSPRQRMSPGVAGS
CCCHHHCCCCCCCCC		4.2517242355
493PhosphorylationLSPRQRMSPGVAGSP
CCHHHCCCCCCCCCC		22.2325521595
499PhosphorylationMSPGVAGSPRIPPSQ
CCCCCCCCCCCCHHH		10.9825521595
554PhosphorylationSLGSSLASPDLKMGN
CCCCCCCCCCCCCCC		25.00-
565PhosphorylationKMGNLQNSPVNMNPP
CCCCCCCCCCCCCCC		19.7725521595
575PhosphorylationNMNPPPLSKMGSLDS
CCCCCCHHHCCCCCC		26.7728833060
579PhosphorylationPPLSKMGSLDSKDCF
CCHHHCCCCCCCCCC		26.0422817900
635PhosphorylationGHSRLHDSKGQTKLL
CCCCCCCCCCHHHHH		28.1221454597
636AcetylationHSRLHDSKGQTKLLQ
CCCCCCCCCHHHHHH		62.1823806337
640AcetylationHDSKGQTKLLQLLTT
CCCCCHHHHHHHHHC		39.0323806337
640UbiquitinationHDSKGQTKLLQLLTT
CCCCCHHHHHHHHHC		39.0322790023
646PhosphorylationTKLLQLLTTKSDQME
HHHHHHHHCCHHCCC		40.5521454597
648AcetylationLLQLLTTKSDQMEPS
HHHHHHCCHHCCCCC		46.9623236377
649PhosphorylationLQLLTTKSDQMEPSP
HHHHHCCHHCCCCCC		30.8629550500
655PhosphorylationKSDQMEPSPLPSSLS
CHHCCCCCCCCCCCC		26.2626643407
659PhosphorylationMEPSPLPSSLSDTNK
CCCCCCCCCCCCCCC		52.1526643407
682PhosphorylationPGSTHGTSLKEKHKI
CCCCCCCCHHHHHHH		41.87-
697PhosphorylationLHRLLQDSSSPVDLA
HHHHHCCCCCCCHHH		21.5421082442
698PhosphorylationHRLLQDSSSPVDLAK
HHHHCCCCCCCHHHH		47.1225521595
699PhosphorylationRLLQDSSSPVDLAKL
HHHCCCCCCCHHHHH		32.6625521595
705AcetylationSSPVDLAKLTAEATG
CCCCHHHHHHHHHHC		54.3823236377
713AcetylationLTAEATGKELSQESS
HHHHHHCCHHHHHCC		51.6423236377
716PhosphorylationEATGKELSQESSSTA
HHHCCHHHHHCCCCC		32.7517525332
719PhosphorylationGKELSQESSSTAPGS
CCHHHHHCCCCCCCC		23.1923984901
720PhosphorylationKELSQESSSTAPGSE
CHHHHHCCCCCCCCE		30.8423984901
721PhosphorylationELSQESSSTAPGSEV
HHHHHCCCCCCCCEE		37.5623984901
722PhosphorylationLSQESSSTAPGSEVT
HHHHCCCCCCCCEEE		38.5323984901
726PhosphorylationSSSTAPGSEVTVKQE
CCCCCCCCEEEEEEC		28.0326160508
729PhosphorylationTAPGSEVTVKQEPAS
CCCCCEEEEEECCCC		20.2425266776
736PhosphorylationTVKQEPASPKKKENA
EEEECCCCCCHHHHH		48.2225521595
765AcetylationGLPEITPKLERLDSK
CCCCCCCCHHHHCCC		55.0923806337
771PhosphorylationPKLERLDSKTDPASN
CCHHHHCCCCCCCCC		41.8926824392
772AcetylationKLERLDSKTDPASNT
CHHHHCCCCCCCCCC		57.5223806337
773PhosphorylationLERLDSKTDPASNTK
HHHHCCCCCCCCCCE		51.6825266776
780AcetylationTDPASNTKLIAMKTV
CCCCCCCEEEEEEEE		41.9923806337
785AcetylationNTKLIAMKTVKEEVS
CCEEEEEEEEECCCC		40.9423806337
847PhosphorylationINDLMQLTADSSPVP
HHHHHHHHCCCCCCC		16.1330482847
850PhosphorylationLMQLTADSSPVPPAG
HHHHHCCCCCCCCHH		33.7926745281
851PhosphorylationMQLTADSSPVPPAGA
HHHHCCCCCCCCHHH		30.3929514104
864Asymmetric dimethylarginineGAQKAALRMSQSTFN
HHHHHHHHHHHHCCC		20.27-
864MethylationGAQKAALRMSQSTFN
HHHHHHHHHHHHCCC		20.2724129315
874Asymmetric dimethylarginineQSTFNNPRPGQLGRL
HHCCCCCCCCCCCCC		50.53-
874MethylationQSTFNNPRPGQLGRL
HHCCCCCCCCCCCCC		50.5324129315
895PhosphorylationPLDITLQSPTGAGPF
CEEEEEECCCCCCCC		27.7830352176
951PhosphorylationTSRPSMPSGEWAPQS
CCCCCCCCCCCCCCC		40.4828066266
958PhosphorylationSGEWAPQSPAVRVTC
CCCCCCCCCCEEEEE		17.4828066266
964O-linked_GlycosylationQSPAVRVTCAATTGA
CCCCEEEEEEHHCCC		5.9555412813
1173Asymmetric dimethylarginineTTLRMQPRPGLRPTG
CEEECCCCCCCCCCC		22.49-
1173MethylationTTLRMQPRPGLRPTG
CEEECCCCCCCCCCC		22.4924129315
1177MethylationMQPRPGLRPTGIVQN
CCCCCCCCCCCCCCC		32.4224129315
1177Asymmetric dimethylarginineMQPRPGLRPTGIVQN
CCCCCCCCCCCCCCC		32.42-
1190MethylationQNQPNQLRLQLQHRL
CCCCCHHHHHHHHHH		15.6024129315
1190Asymmetric dimethylarginineQNQPNQLRLQLQHRL
CCCCCHHHHHHHHHH		15.60-
1196Asymmetric dimethylarginineLRLQLQHRLQAQQNR
HHHHHHHHHHHHHHC		18.61-
1196MethylationLRLQLQHRLQAQQNR
HHHHHHHHHHHHHHC		18.61-
1203MethylationRLQAQQNRQPLMNQI
HHHHHHHCCCHHHHH		34.8524129315
1203Asymmetric dimethylarginineRLQAQQNRQPLMNQI
HHHHHHHCCCHHHHH		34.85-
1221Asymmetric dimethylarginineSNVNLTLRPGVPTQA
CEECEEECCCCCCCC		22.23-
1221MethylationSNVNLTLRPGVPTQA
CEECEEECCCCCCCC		22.2324129315
1240Asymmetric dimethylarginineQMLAQRQREILNQHL
HHHHHHHHHHHHHHH		34.80-
1240MethylationQMLAQRQREILNQHL
HHHHHHHHHHHHHHH		34.8024129315
1259MethylationMQQQVQQRTLMMRGQ
HHHHHHHHHHHHHCC		16.85-
1264MethylationQQRTLMMRGQGLNVT
HHHHHHHHCCCCCCC		21.96-
1264Asymmetric dimethylarginineQQRTLMMRGQGLNVT
HHHHHHHHCCCCCCC		21.96-
1271PhosphorylationRGQGLNVTPSMVAPA
HCCCCCCCHHHHCCC		14.4725777480
1273PhosphorylationQGLNVTPSMVAPAGL
CCCCCCHHHHCCCCC		19.2725777480
1285PhosphorylationAGLPAAMSNPRIPQA
CCCCHHHCCCCCCCC		38.6725777480
1303PhosphorylationQFPFPPNYGISQQPD
CCCCCCCCCCCCCCC		22.9322802335
1306PhosphorylationFPPNYGISQQPDPGF
CCCCCCCCCCCCCCC		20.5722802335
1314PhosphorylationQQPDPGFTGATTPQS
CCCCCCCCCCCCCCC		31.6422802335
1317PhosphorylationDPGFTGATTPQSPLM
CCCCCCCCCCCCCCC		40.1122802335
1318PhosphorylationPGFTGATTPQSPLMS
CCCCCCCCCCCCCCC		20.8522802335
1321PhosphorylationTGATTPQSPLMSPRM
CCCCCCCCCCCCCCC		22.6222802335
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
736SPhosphorylationKinaseMAPK14Q16539
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NCOA2_MOUSE !!
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 NCOA2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
VDR_HUMANVDRphysical
11514567
NCOA2_HUMANNCOA2physical
11514567
SNW1_HUMANSNW1genetic
11514567
PRGR_HUMANPGRphysical
10757795
MYOD1_MOUSEMyod1physical
15563453
NRIP1_MOUSENrip1physical
15331759
CARM1_MOUSECarm1physical
10381882
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NCOA2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493, AND MASSSPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-716, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-699, AND MASSSPECTROMETRY.

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