NCOA1_MOUSE - dbPTM
NCOA1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NCOA1_MOUSE
UniProt AC P70365
Protein Name Nuclear receptor coactivator 1
Gene Name Ncoa1
Organism Mus musculus (Mouse).
Sequence Length 1447
Subcellular Localization Nucleus .
Protein Description Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Involved in the coactivation of different nuclear receptors, such as for steroids (PGR, GR and ER), retinoids (RXRs), thyroid hormone (TRs) and prostanoids (PPARs). Also involved in coactivation mediated by STAT3, STAT5A, STAT5B and STAT6 transcription factors. Displays histone acetyltransferase activity toward H3 and H4; the relevance of such activity remains however unclear. Plays a central role in creating multisubunit coactivator complexes that act via remodeling of chromatin, and possibly acts by participating in both chromatin remodeling and recruitment of general transcription factors. Required with NCOA2 to control energy balance between white and brown adipose tissues. Required for mediating steroid hormone response. Isoform 2 has a higher thyroid hormone-dependent transactivation activity than isoform 1 and isoform 3..
Protein Sequence MSGLGDSSSDPANPDSHKRKGSPCDTLASSTEKRRREQENKYLEELAELLSANISDIDSLSVKPDKCKILKKTVDQIQLMKRMEQEKSTTDDDVQKSDISSSSQGVIEKESLGPLLLEALDGFFFVVNCEGRIVFVSENVTSYLGYNQEELMNTSVYSILHVGDHAEFVKNLLPKSLVNGVPWPQEATRRNSHTFNCRMLIHPPEDPGTENQEACQRYEVMQCFTVSQPKSIQEDGEDFQSCLICIARRLPRPPAITGVESFMTKQDTTGKIISIDTSSLRAAGRTGWEDLVRKCIYAFFQPQGREPSYARQLFQEVMTRGTASSPSYRFILNDGTMLSAHTKCKLCYPQSPDMQPFIMGIHIIDREHSGLSPQDDSNSGMSIPRINPSVNPGISPAHGVTRSSTLPPSNNNMVSARVNRQQSSDLNSSSSHTNSSNNQGNFGCSPGNQIVANVALNQGQAGSQSSNPSLNLNNSPMEGTGIALSQFMSPRRQANSGLATRARMSNNSFPPNIPTLSSPVGITSGACNNNNRSYSNIPVTSLQGMNEGPNNSVGFSAGSPVLRQMSSQNSPSRLSMQPAKAESKDSKEIASILNEMIQSDNSDNSANEGKPLDSGLLHNNDRLSEGDSKYSQTSHKLVQLLTTTAEQQLRHADIDTSCKDVLSCTGTSSSASSNPSGGTCPSSHSSLTERHKILHRLLQEGSPSDITTLSVEPEKKDSVPASTAVSVSGQSQGSASIKLELDAAKKKESKDHQLLRYLLDKDEKDLRSTPNLCLDDVKVKVEKKEQMDPCNTNPTPMTKPAPEEVKLESQSQFTADLDQFDQLLPTLEKAAQLPSLCETDRMDGAVTGVSIKAEVLPASLQPTTARAAPRLSRLPELELEAIDNQFGQPGAGDQIPWANNTLTTINQNKPEDQCISSQLDELLCPPTTVEGRNDEKALLEQLVSFLSGKDETELAELDRALGIDKLVQGGGLDVLSERFPPQQATPPLMMEDRPTLYSQPYSSPSPTAGLSGPFQGMVRQKPSLGAMPVQVTPPRGTFSPNMGMQPRQTLNRPPAAPNQLRLQLQQRLQGQQQLMHQNRQAILNQFAANAPVGMNMRSGMQQQITPQPPLNAQMLAQRQRELYSQQHRQRQIIQQQRAMLMRHQSFGNNIPPSSGLPVQMGTPRLPQGAPQQFPYPPNYGTNPGTPPASTSPFSQLAANPEASLATRSSMVNRGMAGNMGGQFGAGISPQMQQNVFQYPGPGLVPQGEATFAPSLSPGSSMVPMPVPPPQSSLLQQTPPTSGYQSPDMKAWQQGTMGNNNVFSQAVQSQPAPAQPGVYNNMSITVSMAGGNANIQNMNPMMGQMQMSSLQMPGMNTVCSEQMNDPALRHTGLYCNQLSSTDLLKTDADGNQQVQQVQVFADVQCTVNLVGGDPYLNQPGPLGTQKPTSGPQTPQAQQKSLLQQLLTE
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
2Acetylation------MSGLGDSSS
------CCCCCCCCC		54.77-
22 (in isoform 3)Phosphorylation-25.9519144319
22PhosphorylationDSHKRKGSPCDTLAS
CCCCCCCCCCHHHCH		25.9525521595
26PhosphorylationRKGSPCDTLASSTEK
CCCCCCHHHCHHHHH		30.8228833060
29PhosphorylationSPCDTLASSTEKRRR
CCCHHHCHHHHHHHH		40.6926643407
30PhosphorylationPCDTLASSTEKRRRE
CCHHHCHHHHHHHHH		34.6726643407
31PhosphorylationCDTLASSTEKRRREQ
CHHHCHHHHHHHHHH		42.9326643407
192PhosphorylationQEATRRNSHTFNCRM
HHHHHCCCCEEEEEE		23.3025338131
369PhosphorylationHIIDREHSGLSPQDD
EEECCCCCCCCCCCC		36.3527742792
372 (in isoform 3)Phosphorylation-24.8419144319
372PhosphorylationDREHSGLSPQDDSNS
CCCCCCCCCCCCCCC		24.8425521595
389PhosphorylationSIPRINPSVNPGISP
CCCCCCCCCCCCCCC		30.0028833060
395PhosphorylationPSVNPGISPAHGVTR
CCCCCCCCCCCCCCC		23.1928833060
401O-linked_GlycosylationISPAHGVTRSSTLPP
CCCCCCCCCCCCCCC		29.4422517741
401PhosphorylationISPAHGVTRSSTLPP
CCCCCCCCCCCCCCC		29.4428833060
475PhosphorylationPSLNLNNSPMEGTGI
CCCCCCCCCCCCCCC		25.26-
518PhosphorylationPNIPTLSSPVGITSG
CCCCCCCCCCCCCCC		27.07-
559PhosphorylationSVGFSAGSPVLRQMS
CCCCCCCCHHHHHHH		16.1419060867
566PhosphorylationSPVLRQMSSQNSPSR
CHHHHHHHCCCCCCC		22.0429899451
567PhosphorylationPVLRQMSSQNSPSRL
HHHHHHHCCCCCCCC		28.2121149613
570PhosphorylationRQMSSQNSPSRLSMQ
HHHHCCCCCCCCCCC		19.3325521595
572PhosphorylationMSSQNSPSRLSMQPA
HHCCCCCCCCCCCCH		45.7529899451
575PhosphorylationQNSPSRLSMQPAKAE
CCCCCCCCCCCHHCC		17.7921149613
702PhosphorylationHRLLQEGSPSDITTL
HHHHHHCCCCCCEEE		22.0725521595
702 (in isoform 3)Phosphorylation-22.0719144319
704PhosphorylationLLQEGSPSDITTLSV
HHHHCCCCCCEEEEC		43.2628833060
707PhosphorylationEGSPSDITTLSVEPE
HCCCCCCEEEECCCC		27.0328833060
708PhosphorylationGSPSDITTLSVEPEK
CCCCCCEEEECCCCC		19.8528833060
710PhosphorylationPSDITTLSVEPEKKD
CCCCEEEECCCCCCC		23.4928833060
718PhosphorylationVEPEKKDSVPASTAV
CCCCCCCCCCCCEEE		38.5930165576
722PhosphorylationKKDSVPASTAVSVSG
CCCCCCCCEEEEECC		15.7230165576
723PhosphorylationKDSVPASTAVSVSGQ
CCCCCCCEEEEECCC		32.9330165576
726PhosphorylationVPASTAVSVSGQSQG
CCCCEEEEECCCCCC		14.2230165576
728PhosphorylationASTAVSVSGQSQGSA
CCEEEEECCCCCCCE		24.4930165576
731PhosphorylationAVSVSGQSQGSASIK
EEEECCCCCCCEEEE		39.7830165576
734PhosphorylationVSGQSQGSASIKLEL
ECCCCCCCEEEEEEE		15.9430165576
736PhosphorylationGQSQGSASIKLELDA
CCCCCCEEEEEEEHH		23.1930165576
768PhosphorylationKDEKDLRSTPNLCLD
CCHHHHHCCCCCCHH		56.3626643407
769PhosphorylationDEKDLRSTPNLCLDD
CHHHHHCCCCCCHHH		15.1225521595
1039PhosphorylationTPPRGTFSPNMGMQP
CCCCCCCCCCCCCCC		18.40-
1052MethylationQPRQTLNRPPAAPNQ
CCCCCCCCCCCCCCH		41.5154541557
1052DimethylationQPRQTLNRPPAAPNQ
CCCCCCCCCCCCCCH		41.51-
1061DimethylationPAAPNQLRLQLQQRL
CCCCCHHHHHHHHHH		15.60-
1061MethylationPAAPNQLRLQLQQRL
CCCCCHHHHHHHHHH		15.6018964457
1067DimethylationLRLQLQQRLQGQQQL
HHHHHHHHHHHHHHH		18.93-
1067MethylationLRLQLQQRLQGQQQL
HHHHHHHHHHHHHHH		18.9354541569
1079Asymmetric dimethylarginineQQLMHQNRQAILNQF
HHHHHHHHHHHHHHH		22.27-
1079MethylationQQLMHQNRQAILNQF
HHHHHHHHHHHHHHH		22.2724129315
1097Asymmetric dimethylarginineAPVGMNMRSGMQQQI
CCCCCCCCCCCCCCC		25.67-
1097MethylationAPVGMNMRSGMQQQI
CCCCCCCCCCCCCCC		25.6724129315
1130Asymmetric dimethylarginineYSQQHRQRQIIQQQR
HHHHHHHHHHHHHHH		29.62-
1130MethylationYSQQHRQRQIIQQQR
HHHHHHHHHHHHHHH		29.6224129315
1137MethylationRQIIQQQRAMLMRHQ
HHHHHHHHHHHHHHH		20.0224129315
1137Asymmetric dimethylarginineRQIIQQQRAMLMRHQ
HHHHHHHHHHHHHHH		20.02-
1185PhosphorylationNYGTNPGTPPASTSP
CCCCCCCCCCCCCCC		27.62-
1191PhosphorylationGTPPASTSPFSQLAA
CCCCCCCCCHHHHHC		22.81-
1271PhosphorylationMPVPPPQSSLLQQTP
CCCCCCCCHHHCCCC		28.82-
1272PhosphorylationPVPPPQSSLLQQTPP
CCCCCCCHHHCCCCC		28.05-
1280PhosphorylationLLQQTPPTSGYQSPD
HHCCCCCCCCCCCCC		35.67-
1370PhosphorylationNDPALRHTGLYCNQL
CCHHHHHHCEECCCC		23.5821149613
1373PhosphorylationALRHTGLYCNQLSST
HHHHHCEECCCCCCC		7.2421149613
1378PhosphorylationGLYCNQLSSTDLLKT
CEECCCCCCCCCCCC		22.7923984901
1379PhosphorylationLYCNQLSSTDLLKTD
EECCCCCCCCCCCCC		34.2423984901
1380PhosphorylationYCNQLSSTDLLKTDA
ECCCCCCCCCCCCCC		27.5623984901
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
1271SPhosphorylationKinasePRKCQQ02111
GPS
1272SPhosphorylationKinasePRKCQQ02111
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NCOA1_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 NCOA1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EP300_MOUSEEp300physical
8855229
MYOD1_MOUSEMyod1physical
15563453
NRIP1_MOUSENrip1physical
15331759
STF1_MOUSENr5a1physical
9482669
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NCOA1_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-22, AND MASSSPECTROMETRY.

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