NCOA1_HUMAN - dbPTM
NCOA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NCOA1_HUMAN
UniProt AC Q15788
Protein Name Nuclear receptor coactivator 1
Gene Name NCOA1
Organism Homo sapiens (Human).
Sequence Length 1441
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 MSGLGDSSSDPANPDSHKRKGSPCDTLASSTEKRRREQENKYLEELAELLSANISDIDSLSVKPDKCKILKKTVDQIQLMKRMEQEKSTTDDDVQKSDISSSSQGVIEKESLGPLLLEALDGFFFVVNCEGRIVFVSENVTSYLGYNQEELMNTSVYSILHVGDHAEFVKNLLPKSLVNGVPWPQEATRRNSHTFNCRMLIHPPDEPGTENQEACQRYEVMQCFTVSQPKSIQEDGEDFQSCLICIARRLPRPPAITGVESFMTKQDTTGKIISIDTSSLRAAGRTGWEDLVRKCIYAFFQPQGREPSYARQLFQEVMTRGTASSPSYRFILNDGTMLSAHTKCKLCYPQSPDMQPFIMGIHIIDREHSGLSPQDDTNSGMSIPRVNPSVNPSISPAHGVARSSTLPPSNSNMVSTRINRQQSSDLHSSSHSNSSNSQGSFGCSPGSQIVANVALNQGQASSQSSNPSLNLNNSPMEGTGISLAQFMSPRRQVTSGLATRPRMPNNSFPPNISTLSSPVGMTSSACNNNNRSYSNIPVTSLQGMNEGPNNSVGFSASSPVLRQMSSQNSPSRLNIQPAKAESKDNKEIASILNEMIQSDNSSSDGKPLDSGLLHNNDRLSDGDSKYSQTSHKLVQLLTTTAEQQLRHADIDTSCKDVLSCTGTSNSASANSSGGSCPSSHSSLTERHKILHRLLQEGSPSDITTLSVEPDKKDSASTSVSVTGQVQGNSSIKLELDASKKKESKDHQLLRYLLDKDEKDLRSTPNLSLDDVKVKVEKKEQMDPCNTNPTPMTKPTPEEIKLEAQSQFTADLDQFDQLLPTLEKAAQLPGLCETDRMDGAVTSVTIKSEILPASLQSATARPTSRLNRLPELELEAIDNQFGQPGTGDQIPWTNNTVTAINQSKSEDQCISSQLDELLCPPTTVEGRNDEKALLEQLVSFLSGKDETELAELDRALGIDKLVQGGGLDVLSERFPPQQATPPLIMEERPNLYSQPYSSPSPTANLPSPFQGMVRQKPSLGTMPVQVTPPRGAFSPGMGMQPRQTLNRPPAAPNQLRLQLQQRLQGQQQLIHQNRQAILNQFAATAPVGINMRSGMQQQITPQPPLNAQMLAQRQRELYSQQHRQRQLIQQQRAMLMRQQSFGNNLPPSSGLPVQMGNPRLPQGAPQQFPYPPNYGTNPGTPPASTSPFSQLAANPEASLANRNSMVSRGMTGNIGGQFGTGINPQMQQNVFQYPGAGMVPQGEANFAPSLSPGSSMVPMPIPPPQSSLLQQTPPASGYQSPDMKAWQQGAIGNNNVFSQAVQNQPTPAQPGVYNNMSITVSMAGGNTNVQNMNPMMAQMQMSSLQMPGMNTVCPEQINDPALRHTGLYCNQLSSTDLLKTEADGTQQVQQVQVFADVQCTVNLVGGDPYLNQPGPLGTQKPTSGPQTPQAQQKSLLQQLLTE
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
54.7720068231
2Phosphorylation------MSGLGDSSS
------CCCCCCCCC
54.7720068231
7Phosphorylation-MSGLGDSSSDPANP
-CCCCCCCCCCCCCC
29.9125159151
8PhosphorylationMSGLGDSSSDPANPD
CCCCCCCCCCCCCCC
43.4226074081
9PhosphorylationSGLGDSSSDPANPDS
CCCCCCCCCCCCCCC
52.1126074081
16PhosphorylationSDPANPDSHKRKGSP
CCCCCCCCCCCCCCC
31.9726074081
18AcetylationPANPDSHKRKGSPCD
CCCCCCCCCCCCCCH
60.8125953088
22PhosphorylationDSHKRKGSPCDTLAS
CCCCCCCCCCHHHCH
25.9523401153
26PhosphorylationRKGSPCDTLASSTEK
CCCCCCHHHCHHHHH
30.8230266825
29PhosphorylationSPCDTLASSTEKRRR
CCCHHHCHHHHHHHH
40.6923403867
30PhosphorylationPCDTLASSTEKRRRE
CCHHHCHHHHHHHHH
34.6723403867
31PhosphorylationCDTLASSTEKRRREQ
CHHHCHHHHHHHHHH
42.9323403867
59PhosphorylationANISDIDSLSVKPDK
CCCCHHHHCCCCHHH
23.9124719451
88PhosphorylationKRMEQEKSTTDDDVQ
HHHHHHCCCCCHHHH
35.4728450419
89PhosphorylationRMEQEKSTTDDDVQK
HHHHHCCCCCHHHHH
45.3628450419
90PhosphorylationMEQEKSTTDDDVQKS
HHHHCCCCCHHHHHH
44.5128450419
97PhosphorylationTDDDVQKSDISSSSQ
CCHHHHHHHHCCCCC
24.0828450419
102PhosphorylationQKSDISSSSQGVIEK
HHHHHCCCCCCCCCH
21.6427282143
103PhosphorylationKSDISSSSQGVIEKE
HHHHCCCCCCCCCHH
32.6617525332
192PhosphorylationQEATRRNSHTFNCRM
HHHHCCCCCEEEEEE
23.3026091039
209PhosphorylationHPPDEPGTENQEACQ
CCCCCCCCCCHHHHH
42.3420068231
269PhosphorylationFMTKQDTTGKIISID
EECCCCCCCCEEEEE
44.7822210691
274PhosphorylationDTTGKIISIDTSSLR
CCCCCEEEEEHHHHH
20.20-
277PhosphorylationGKIISIDTSSLRAAG
CCEEEEEHHHHHHCC
20.6722210691
278PhosphorylationKIISIDTSSLRAAGR
CEEEEEHHHHHHCCC
24.5122210691
279PhosphorylationIISIDTSSLRAAGRT
EEEEEHHHHHHCCCC
24.7829457462
308PhosphorylationQPQGREPSYARQLFQ
CCCCCCCHHHHHHHH
27.0324719451
325PhosphorylationMTRGTASSPSYRFIL
HHHCCCCCCCEEEEC
18.5321550420
369PhosphorylationHIIDREHSGLSPQDD
EEECCCCCCCCCCCC
36.3523401153
372PhosphorylationDREHSGLSPQDDTNS
CCCCCCCCCCCCCCC
24.8423401153
377PhosphorylationGLSPQDDTNSGMSIP
CCCCCCCCCCCCCCC
39.3030108239
389PhosphorylationSIPRVNPSVNPSISP
CCCCCCCCCCCCCCC
29.3523403867
393PhosphorylationVNPSVNPSISPAHGV
CCCCCCCCCCCCCCC
30.4130266825
395PhosphorylationPSVNPSISPAHGVAR
CCCCCCCCCCCCCCC
22.0029255136
405PhosphorylationHGVARSSTLPPSNSN
CCCCCCCCCCCCCCC
44.5224260401
411PhosphorylationSTLPPSNSNMVSTRI
CCCCCCCCCCCCCEE
30.5524260401
416PhosphorylationSNSNMVSTRINRQQS
CCCCCCCCEECCHHC
24.9424260401
423PhosphorylationTRINRQQSSDLHSSS
CEECCHHCCCCCCCC
19.92-
488PhosphorylationISLAQFMSPRRQVTS
CCHHHHCCCCCCCCC
19.2821550420
517PhosphorylationPNISTLSSPVGMTSS
CCCCCCCCCCCCCCH
27.0722817900
532PhosphorylationACNNNNRSYSNIPVT
HHCCCCCCCCCCCCE
34.7329978859
533PhosphorylationCNNNNRSYSNIPVTS
HCCCCCCCCCCCCEE
11.5129978859
534PhosphorylationNNNNRSYSNIPVTSL
CCCCCCCCCCCCEEE
29.5429978859
539PhosphorylationSYSNIPVTSLQGMNE
CCCCCCCEEECCCCC
20.5429978859
540PhosphorylationYSNIPVTSLQGMNEG
CCCCCCEEECCCCCC
20.9429978859
551PhosphorylationMNEGPNNSVGFSASS
CCCCCCCCCCCCCCH
30.2027080861
555PhosphorylationPNNSVGFSASSPVLR
CCCCCCCCCCHHHHH
22.7027080861
557PhosphorylationNSVGFSASSPVLRQM
CCCCCCCCHHHHHHH
33.7029978859
558PhosphorylationSVGFSASSPVLRQMS
CCCCCCCHHHHHHHH
20.8129978859
565PhosphorylationSPVLRQMSSQNSPSR
HHHHHHHHCCCCCCC
22.0429978859
566PhosphorylationPVLRQMSSQNSPSRL
HHHHHHHCCCCCCCC
28.2129978859
569PhosphorylationRQMSSQNSPSRLNIQ
HHHHCCCCCCCCCCC
19.3321550420
571PhosphorylationMSSQNSPSRLNIQPA
HHCCCCCCCCCCCCC
49.5829978859
579AcetylationRLNIQPAKAESKDNK
CCCCCCCCCCCCCHH
60.4125953088
582PhosphorylationIQPAKAESKDNKEIA
CCCCCCCCCCHHHHH
50.6018077418
590PhosphorylationKDNKEIASILNEMIQ
CCHHHHHHHHHHHHH
33.0227732954
598PhosphorylationILNEMIQSDNSSSDG
HHHHHHHCCCCCCCC
28.0327732954
601PhosphorylationEMIQSDNSSSDGKPL
HHHHCCCCCCCCCCC
35.8927732954
602PhosphorylationMIQSDNSSSDGKPLD
HHHCCCCCCCCCCCC
38.4127732954
603PhosphorylationIQSDNSSSDGKPLDS
HHCCCCCCCCCCCCC
50.6427732954
620PhosphorylationLHNNDRLSDGDSKYS
CCCCCCCCCCCCCCH
40.2025159151
624PhosphorylationDRLSDGDSKYSQTSH
CCCCCCCCCCHHHHH
38.7429449344
632AcetylationKYSQTSHKLVQLLTT
CCHHHHHHHHHHHHH
50.5523954790
639O-linked_GlycosylationKLVQLLTTTAEQQLR
HHHHHHHHCHHHHHH
24.7928657654
640O-linked_GlycosylationLVQLLTTTAEQQLRH
HHHHHHHCHHHHHHH
23.9828657654
659PhosphorylationTSCKDVLSCTGTSNS
CCHHHHHHCCCCCCC
14.9620068231
661PhosphorylationCKDVLSCTGTSNSAS
HHHHHHCCCCCCCCC
39.8720068231
663PhosphorylationDVLSCTGTSNSASAN
HHHHCCCCCCCCCCC
13.4420068231
664PhosphorylationVLSCTGTSNSASANS
HHHCCCCCCCCCCCC
30.0820068231
666PhosphorylationSCTGTSNSASANSSG
HCCCCCCCCCCCCCC
24.3020068231
668PhosphorylationTGTSNSASANSSGGS
CCCCCCCCCCCCCCC
28.0120068231
671PhosphorylationSNSASANSSGGSCPS
CCCCCCCCCCCCCCC
30.0320068231
672PhosphorylationNSASANSSGGSCPSS
CCCCCCCCCCCCCCC
47.1620068231
675PhosphorylationSANSSGGSCPSSHSS
CCCCCCCCCCCCCCH
26.7820068231
678PhosphorylationSSGGSCPSSHSSLTE
CCCCCCCCCCCHHHH
45.0420068231
679PhosphorylationSGGSCPSSHSSLTER
CCCCCCCCCCHHHHH
16.7220068231
681PhosphorylationGSCPSSHSSLTERHK
CCCCCCCCHHHHHHH
29.0520068231
682PhosphorylationSCPSSHSSLTERHKI
CCCCCCCHHHHHHHH
33.6120068231
684PhosphorylationPSSHSSLTERHKILH
CCCCCHHHHHHHHHH
32.6820068231
698PhosphorylationHRLLQEGSPSDITTL
HHHHHCCCCCCCEEE
22.0723401153
700PhosphorylationLLQEGSPSDITTLSV
HHHCCCCCCCEEEEE
43.2630266825
703PhosphorylationEGSPSDITTLSVEPD
CCCCCCCEEEEECCC
27.0330266825
704PhosphorylationGSPSDITTLSVEPDK
CCCCCCEEEEECCCC
19.8530266825
706PhosphorylationPSDITTLSVEPDKKD
CCCCEEEEECCCCCC
23.4930266825
716PhosphorylationPDKKDSASTSVSVTG
CCCCCCCCCEEEEEE
25.7630576142
720PhosphorylationDSASTSVSVTGQVQG
CCCCCEEEEEEEECC
17.4630576142
729PhosphorylationTGQVQGNSSIKLELD
EEEECCCCEEEEEEE
40.0230576142
732SumoylationVQGNSSIKLELDASK
ECCCCEEEEEEECCC
37.55-
732SumoylationVQGNSSIKLELDASK
ECCCCEEEEEEECCC
37.5512529333
758AcetylationYLLDKDEKDLRSTPN
HHHCCCHHHHHCCCC
72.6723236377
762PhosphorylationKDEKDLRSTPNLSLD
CCHHHHHCCCCCCHH
56.3630576142
763PhosphorylationDEKDLRSTPNLSLDD
CHHHHHCCCCCCHHH
15.1230576142
767PhosphorylationLRSTPNLSLDDVKVK
HHCCCCCCHHHCEEE
36.0727732954
774SumoylationSLDDVKVKVEKKEQM
CHHHCEEEEEEHHHC
38.67-
774SumoylationSLDDVKVKVEKKEQM
CHHHCEEEEEEHHHC
38.6712529333
789PhosphorylationDPCNTNPTPMTKPTP
CCCCCCCCCCCCCCH
27.9721550420
793AcetylationTNPTPMTKPTPEEIK
CCCCCCCCCCHHHHH
40.4126051181
820PhosphorylationQFDQLLPTLEKAAQL
HHHHHHHHHHHHHCC
47.7424173317
841O-linked_GlycosylationDRMDGAVTSVTIKSE
CCCCCCEEEEEEECC
19.5628657654
844O-linked_GlycosylationDGAVTSVTIKSEILP
CCCEEEEEEECCCCC
23.5828657654
846SumoylationAVTSVTIKSEILPAS
CEEEEEEECCCCCHH
32.4428112733
853PhosphorylationKSEILPASLQSATAR
ECCCCCHHHHHCCCC
25.6323312004
856PhosphorylationILPASLQSATARPTS
CCCHHHHHCCCCCCC
32.6428348404
858PhosphorylationPASLQSATARPTSRL
CHHHHHCCCCCCCHH
28.5728348404
862PhosphorylationQSATARPTSRLNRLP
HHCCCCCCCHHHCCC
22.4128348404
863PhosphorylationSATARPTSRLNRLPE
HCCCCCCCHHHCCCH
37.1428348404
959UbiquitinationDRALGIDKLVQGGGL
HHHHCHHHHHCCCCC
48.9529967540
979PhosphorylationRFPPQQATPPLIMEE
CCCCHHCCCCCEECC
22.5421550420
996PhosphorylationNLYSQPYSSPSPTAN
CCCCCCCCCCCCCCC
42.3226074081
997PhosphorylationLYSQPYSSPSPTANL
CCCCCCCCCCCCCCC
24.4526074081
999PhosphorylationSQPYSSPSPTANLPS
CCCCCCCCCCCCCCC
36.5126074081
1001PhosphorylationPYSSPSPTANLPSPF
CCCCCCCCCCCCCCC
32.3026074081
1006PhosphorylationSPTANLPSPFQGMVR
CCCCCCCCCCCCCCC
41.3221550420
1026PhosphorylationGTMPVQVTPPRGAFS
CCCCCEECCCCCCCC
15.5221550420
1029DimethylationPVQVTPPRGAFSPGM
CCEECCCCCCCCCCC
50.72-
1029MethylationPVQVTPPRGAFSPGM
CCEECCCCCCCCCCC
50.7230763205
1033PhosphorylationTPPRGAFSPGMGMQP
CCCCCCCCCCCCCCC
21.7322817900
1041DimethylationPGMGMQPRQTLNRPP
CCCCCCCCCCCCCCC
25.81-
1041MethylationPGMGMQPRQTLNRPP
CCCCCCCCCCCCCCC
25.8130763211
1073Asymmetric dimethylarginineQQLIHQNRQAILNQF
HHHHHHHHHHHHHHH
22.27-
1073MethylationQQLIHQNRQAILNQF
HHHHHHHHHHHHHHH
22.27-
1091Asymmetric dimethylarginineAPVGINMRSGMQQQI
CCCCEECCCCCCCCC
26.10-
1091MethylationAPVGINMRSGMQQQI
CCCCEECCCCCCCCC
26.10-
1092PhosphorylationPVGINMRSGMQQQIT
CCCEECCCCCCCCCC
28.0524043423
1099PhosphorylationSGMQQQITPQPPLNA
CCCCCCCCCCCCCCH
16.1324043423
1114MethylationQMLAQRQRELYSQQH
HHHHHHHHHHHHHHH
37.77115917689
1117PhosphorylationAQRQRELYSQQHRQR
HHHHHHHHHHHHHHH
10.3227174698
1118PhosphorylationQRQRELYSQQHRQRQ
HHHHHHHHHHHHHHH
35.6727174698
1124Asymmetric dimethylarginineYSQQHRQRQLIQQQR
HHHHHHHHHHHHHHH
32.98-
1124MethylationYSQQHRQRQLIQQQR
HHHHHHHHHHHHHHH
32.98-
1131Asymmetric dimethylarginineRQLIQQQRAMLMRQQ
HHHHHHHHHHHHHHH
20.02-
1131MethylationRQLIQQQRAMLMRQQ
HHHHHHHHHHHHHHH
20.0230763217
1179PhosphorylationNYGTNPGTPPASTSP
CCCCCCCCCCCCCCC
27.6222817900
1185PhosphorylationGTPPASTSPFSQLAA
CCCCCCCCCHHHHHC
22.8122817900
1250PhosphorylationANFAPSLSPGSSMVP
CCCCCCCCCCCCCCC
31.3921550420
1271PhosphorylationQSSLLQQTPPASGYQ
CCHHHCCCCCCCCCC
20.4821550420
1279PhosphorylationPPASGYQSPDMKAWQ
CCCCCCCCCCHHHHH
17.8721550420
1364PhosphorylationNDPALRHTGLYCNQL
CCHHHHHCCEECCCC
23.5823186163
1367PhosphorylationALRHTGLYCNQLSST
HHHHCCEECCCCCCC
7.2423186163
1372PhosphorylationGLYCNQLSSTDLLKT
CEECCCCCCCCCCCC
22.797481822
1373PhosphorylationLYCNQLSSTDLLKTE
EECCCCCCCCCCCCC
34.2428450419
1374PhosphorylationYCNQLSSTDLLKTEA
ECCCCCCCCCCCCCC
27.5628450419
1394 (in isoform 2)Phosphorylation-19.7429083192
1397 (in isoform 2)Phosphorylation-20.0829083192
1398 (in isoform 2)Phosphorylation-4.6329083192
1426PhosphorylationKPTSGPQTPQAQQKS
CCCCCCCCHHHHHHH
22.0921550420

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
22SPhosphorylationKinaseCDK2P24941
PSP
325SPhosphorylationKinaseCDK2P24941
PSP
395SPhosphorylationKinaseMAPK1P28482
GPS
395SPhosphorylationKinaseCDK2P24941
PSP
488SPhosphorylationKinaseCDK2P24941
PSP
569SPhosphorylationKinaseCDK2P24941
PSP
789TPhosphorylationKinaseCDK2P24941
PSP
979TPhosphorylationKinaseCDK2P24941
PSP
997SPhosphorylationKinaseCDK2P24941
PSP
1006SPhosphorylationKinaseCDK2P24941
PSP
1026TPhosphorylationKinaseCDK2P24941
PSP
1033SPhosphorylationKinaseCDK2P24941
PSP
1179TPhosphorylationKinaseCDK2P24941
PSP
1179TPhosphorylationKinaseMAPK1P28482
GPS
1179TPhosphorylationKinaseMAPK3P27361
GPS
1185SPhosphorylationKinaseCDK2P24941
PSP
1185SPhosphorylationKinaseMAPK1P28482
GPS
1185SPhosphorylationKinaseMAPK3P27361
GPS
1250SPhosphorylationKinaseCDK2P24941
PSP
1271TPhosphorylationKinaseCDK2P24941
PSP
1279SPhosphorylationKinaseCDK2P24941
PSP
1426TPhosphorylationKinaseCDK1P06493
PSP
1426TPhosphorylationKinaseCDK2P24941
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NCOA1_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 NCOA1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FOS_HUMANFOSphysical
10847592
JUN_HUMANJUNphysical
10567404
JUN_HUMANJUNphysical
10847592
NFKB1_HUMANNFKB1physical
10847592
SMCE1_MOUSESmarce1physical
12145209
SMCE1_HUMANSMARCE1physical
12145209
TRIP4_HUMANTRIP4physical
10454579
CBP_HUMANCREBBPphysical
11113179
KAT2B_HUMANKAT2Bphysical
9296499
FOXA2_HUMANFOXA2physical
11069927
RARB_HUMANRARBphysical
8754792
TF2B_HUMANGTF2Bphysical
8754792
TBP_HUMANTBPphysical
8754792
TEAD2_HUMANTEAD2physical
10934189
TEAD1_HUMANTEAD1physical
10934189
STAT3_HUMANSTAT3physical
11773079
CCND1_HUMANCCND1physical
9832502
ANDR_HUMANARphysical
10567563
ESR2_HUMANESR2physical
10809226
NCOA2_HUMANNCOA2physical
11971985
CBP_HUMANCREBBPphysical
11971985
RO52_HUMANTRIM21physical
11971985
GCR_HUMANNR3C1physical
12118039
PRGC1_HUMANPPARGC1Aphysical
10558993
THB_HUMANTHRBgenetic
9171239
THB_HUMANTHRBphysical
9171239
ESR1_HUMANESR1physical
12574227
NCOA3_HUMANNCOA3physical
18267973
STAT6_HUMANSTAT6physical
18267973
ESR1_HUMANESR1physical
11358671
RARA_HUMANRARAphysical
10760302
GCR_HUMANNR3C1physical
10659697
ESR1_HUMANESR1physical
10598586
RARA_HUMANRARAphysical
10082574
RXRA_HUMANRXRAphysical
10082574
THA_HUMANTHRAphysical
9849963
THA_HUMANTHRAphysical
9804773
NCOA2_HUMANNCOA2physical
9751728
STAT6_HUMANSTAT6physical
14993689
ESR1_HUMANESR1physical
9192902
CBP_HUMANCREBBPphysical
9192892
RARA_HUMANRARAphysical
17475621
STAT3_HUMANSTAT3physical
17471507
EP300_HUMANEP300physical
14722092
ESR1_HUMANESR1physical
14715875
ESR2_HUMANESR2physical
14715875
RBBP6_HUMANRBBP6physical
20184719
PRGR_HUMANPGRphysical
21273440
EP300_HUMANEP300physical
20368990
PPARG_HUMANPPARGphysical
17468099
NCOA1_HUMANNCOA1physical
9774463
NCOA2_HUMANNCOA2physical
9774463
TIF1A_HUMANTRIM24physical
9774463
KANK2_HUMANKANK2physical
17476305
ESR1_HUMANESR1physical
10731636
ESR2_HUMANESR2physical
10731636
ESR2_RATEsr2physical
10731636
ANDR_HUMANARphysical
10731636
GCR_HUMANNR3C1physical
10731636
PPARA_HUMANPPARAphysical
10731636
PPARG_HUMANPPARGphysical
10731636
PPARG_HUMANPPARGphysical
17449869
NR1I2_HUMANNR1I2physical
19171678
PPARG_HUMANPPARGphysical
9744270
PPARG_HUMANPPARGphysical
20717101
PPARG_HUMANPPARGphysical
17312272
CBP_HUMANCREBBPphysical
11003650
ESR1_HUMANESR1physical
17363140
RARA_HUMANRARAphysical
17363140
RARB_HUMANRARBphysical
17363140
RARG_HUMANRARGphysical
17363140
RXRA_HUMANRXRAphysical
17363140
EZH2_HUMANEZH2physical
17502350
NR1H4_HUMANNR1H4physical
20338915
RARA_HUMANRARAphysical
20338915
BRCA1_HUMANBRCA1physical
16860316
KAT2B_HUMANKAT2Bphysical
9223281
RXRA_HUMANRXRAphysical
10517671
HNF1A_HUMANHNF1Aphysical
10777539
FOXO1_HUMANFOXO1physical
10973497
EP300_HUMANEP300physical
10973497
ARNT_HUMANARNTphysical
12024042
AHR_HUMANAHRphysical
12024042
CBP_HUMANCREBBPphysical
15615775
VDR_HUMANVDRphysical
12796488
THA_HUMANTHRAphysical
15140878
RXRA_HUMANRXRAphysical
15140878
ESR1_HUMANESR1physical
15140878
ETS2_HUMANETS2physical
15788656
ETS1_HUMANETS1physical
15788656
NR4A1_HUMANNR4A1physical
16002533
SF01_HUMANSF1physical
16002533
WDHD1_HUMANWDHD1physical
16051665
SYTL2_HUMANSYTL2physical
16051665
HSP72_HUMANHSPA2physical
16051665
GRP78_HUMANHSPA5physical
16051665
KCTD3_HUMANKCTD3physical
16051665
TERA_HUMANVCPphysical
16051665
ITCH_HUMANITCHphysical
16051665
TRIPB_HUMANTRIP11physical
16051665
RBBP6_HUMANRBBP6physical
16051665
UBR5_HUMANUBR5physical
16051665
NR1I2_HUMANNR1I2physical
17429319
NR4A2_HUMANNR4A2physical
21757690
NR1I2_HUMANNR1I2physical
15331348
NKX21_HUMANNKX2-1physical
15449938

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 NCOA1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, 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-103, AND MASSSPECTROMETRY.
"Phosphorylation of steroid receptor coactivator-1. Identification ofthe phosphorylation sites and phosphorylation through the mitogen-activated protein kinase pathway.";
Rowan B.G., Weigel N.L., O'Malley B.W.;
J. Biol. Chem. 275:4475-4483(2000).
Cited for: PHOSPHORYLATION AT SER-372; SER-395; SER-517; SER-569; SER-1033;THR-1179 AND SER-1185.
Sumoylation
ReferencePubMed
"Sumoylation of the progesterone receptor and of the steroid receptorcoactivator SRC-1.";
Chauchereau A., Amazit L., Quesne M., Guiochon-Mantel A., Milgrom E.;
J. Biol. Chem. 278:12335-12343(2003).
Cited for: SUMOYLATION AT LYS-732 AND LYS-774, UBIQUITINATION, AND MUTAGENESIS OFLYS-732; LYS-774; LYS-800; LYS-846 AND LYS-1378.

TOP