NCOA3_HUMAN - dbPTM
NCOA3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NCOA3_HUMAN
UniProt AC Q9Y6Q9
Protein Name Nuclear receptor coactivator 3
Gene Name NCOA3
Organism Homo sapiens (Human).
Sequence Length 1424
Subcellular Localization Cytoplasm. Nucleus. Mainly cytoplasmic and weakly nuclear. Upon TNF activation and subsequent phosphorylation, it translocates from the cytoplasm to the nucleus.
Protein Description Nuclear receptor coactivator that directly binds nuclear receptors and stimulates the transcriptional activities in a hormone-dependent fashion. Plays a central role in creating a multisubunit coactivator complex, which probably acts via remodeling of chromatin. Involved in the coactivation of different nuclear receptors, such as for steroids (GR and ER), retinoids (RARs and RXRs), thyroid hormone (TRs), vitamin D3 (VDR) and prostanoids (PPARs). Displays histone acetyltransferase activity. Also involved in the coactivation of the NF-kappa-B pathway via its interaction with the NFKB1 subunit..
Protein Sequence MSGLGENLDPLASDSRKRKLPCDTPGQGLTCSGEKRRREQESKYIEELAELISANLSDIDNFNVKPDKCAILKETVRQIRQIKEQGKTISNDDDVQKADVSSTGQGVIDKDSLGPLLLQALDGFLFVVNRDGNIVFVSENVTQYLQYKQEDLVNTSVYNILHEEDRKDFLKNLPKSTVNGVSWTNETQRQKSHTFNCRMLMKTPHDILEDINASPEMRQRYETMQCFALSQPRAMMEEGEDLQSCMICVARRITTGERTFPSNPESFITRHDLSGKVVNIDTNSLRSSMRPGFEDIIRRCIQRFFSLNDGQSWSQKRHYQEAYLNGHAETPVYRFSLADGTIVTAQTKSKLFRNPVTNDRHGFVSTHFLQREQNGYRPNPNPVGQGIRPPMAGCNSSVGGMSMSPNQGLQMPSSRAYGLADPSTTGQMSGARYGGSSNIASLTPGPGMQSPSSYQNNNYGLNMSSPPHGSPGLAPNQQNIMISPRNRGSPKIASHQFSPVAGVHSPMASSGNTGNHSFSSSSLSALQAISEGVGTSLLSTLSSPGPKLDNSPNMNITQPSKVSNQDSKSPLGFYCDQNPVESSMCQSNSRDHLSDKESKESSVEGAENQRGPLESKGHKKLLQLLTCSSDDRGHSSLTNSPLDSSCKESSVSVTSPSGVSSSTSGGVSSTSNMHGSLLQEKHRILHKLLQNGNSPAEVAKITAEATGKDTSSITSCGDGNVVKQEQLSPKKKENNALLRYLLDRDDPSDALSKELQPQVEGVDNKMSQCTSSTIPSSSQEKDPKIKTETSEEGSGDLDNLDAILGDLTSSDFYNNSISSNGSHLGTKQQVFQGTNSLGLKSSQSVQSIRPPYNRAVSLDSPVSVGSSPPVKNISAFPMLPKQPMLGGNPRMMDSQENYGSSMGGPNRNVTVTQTPSSGDWGLPNSKAGRMEPMNSNSMGRPGGDYNTSLPRPALGGSIPTLPLRSNSIPGARPVLQQQQQMLQMRPGEIPMGMGANPYGQAAASNQLGSWPDGMLSMEQVSHGTQNRPLLRNSLDDLVGPPSNLEGQSDERALLDQLHTLLSNTDATGLEEIDRALGIPELVNQGQALEPKQDAFQGQEAAVMMDQKAGLYGQTYPAQGPPMQGGFHLQGQSPSFNSMMNQMNQQGNFPLQGMHPRANIMRPRTNTPKQLRMQLQQRLQGQQFLNQSRQALELKMENPTAGGAAVMRPMMQPQVSSQQGFLNAQMVAQRSRELLSHHFRQQRVAMMMQQQQQQQQQQQQQQQQQQQQQQQQQQQQQTQAFSPPPNVTASPSMDGLLAGPTMPQAPPQQFPYQPNYGMGQQPDPAFGRVSSPPNAMMSSRMGPSQNPMMQHPQAASIYQSSEMKGWPSGNLARNSSFSQQQFAHQGNPAVYSMVHMNGSSGHMGQMNMNPMPMSGMPMGPDQKYC
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------MSGLGENLD
------CCCCCCCCC
54.7722814378
13PhosphorylationENLDPLASDSRKRKL
CCCCCCCCCHHCCCC
43.7525627689
24PhosphorylationKRKLPCDTPGQGLTC
CCCCCCCCCCCCCCC
35.7222817900
30PhosphorylationDTPGQGLTCSGEKRR
CCCCCCCCCCCHHHH
16.0830576142
32PhosphorylationPGQGLTCSGEKRRRE
CCCCCCCCCHHHHHH
44.7621815630
35AcetylationGLTCSGEKRRREQES
CCCCCCHHHHHHHHH
55.5225953088
65UbiquitinationDIDNFNVKPDKCAIL
CCCCCCCCCHHHHHH
48.91-
73AcetylationPDKCAILKETVRQIR
CHHHHHHHHHHHHHH
45.2726051181
87AcetylationRQIKEQGKTISNDDD
HHHHHHCCCCCCCHH
42.2425953088
90O-linked_GlycosylationKEQGKTISNDDDVQK
HHHCCCCCCCHHHHH
39.1623301498
97UbiquitinationSNDDDVQKADVSSTG
CCCHHHHHCCCCCCC
46.53-
101PhosphorylationDVQKADVSSTGQGVI
HHHHCCCCCCCCCCC
23.8021577200
102PhosphorylationVQKADVSSTGQGVID
HHHCCCCCCCCCCCC
36.0821577200
167UbiquitinationILHEEDRKDFLKNLP
HCCHHHHHHHHHHCC
66.22-
184PhosphorylationTVNGVSWTNETQRQK
HCCCCCCCCHHHHHH
18.70-
191UbiquitinationTNETQRQKSHTFNCR
CCHHHHHHHCCEEEE
46.52-
203PhosphorylationNCRMLMKTPHDILED
EEEEECCCHHHHHHH
16.3423403867
214PhosphorylationILEDINASPEMRQRY
HHHHCCCCHHHHHHH
19.5329255136
230PhosphorylationTMQCFALSQPRAMME
HHHHHHHHCCHHHHH
34.4124719451
244PhosphorylationEEGEDLQSCMICVAR
HCCCCHHHHHHHHHC
16.98-
251MethylationSCMICVARRITTGER
HHHHHHHCCCCCCCC
15.335172407
274PhosphorylationFITRHDLSGKVVNID
CCCHHHCCCCEEEEC
42.5020068231
276AcetylationTRHDLSGKVVNIDTN
CHHHCCCCEEEECCH
39.3722424773
282PhosphorylationGKVVNIDTNSLRSSM
CCEEEECCHHHHHHC
23.9420068231
284PhosphorylationVVNIDTNSLRSSMRP
EEEECCHHHHHHCCC
27.5320068231
287PhosphorylationIDTNSLRSSMRPGFE
ECCHHHHHHCCCCHH
33.5020068231
288PhosphorylationDTNSLRSSMRPGFED
CCHHHHHHCCCCHHH
16.6320068231
306PhosphorylationRCIQRFFSLNDGQSW
HHHHHHHCCCCCCCH
24.4527251275
316UbiquitinationDGQSWSQKRHYQEAY
CCCCHHHHHHHHHHH
35.31-
413PhosphorylationNQGLQMPSSRAYGLA
CCCCCCCCCCCCCCC
27.4122210691
414PhosphorylationQGLQMPSSRAYGLAD
CCCCCCCCCCCCCCC
18.3022210691
417PhosphorylationQMPSSRAYGLADPST
CCCCCCCCCCCCCCC
16.1520068231
423PhosphorylationAYGLADPSTTGQMSG
CCCCCCCCCCCCCCC
38.8720068231
424PhosphorylationYGLADPSTTGQMSGA
CCCCCCCCCCCCCCC
40.0920068231
425PhosphorylationGLADPSTTGQMSGAR
CCCCCCCCCCCCCCC
29.7420068231
429PhosphorylationPSTTGQMSGARYGGS
CCCCCCCCCCCCCCC
22.7820068231
450PhosphorylationTPGPGMQSPSSYQNN
CCCCCCCCCHHHCCC
20.1828348404
452PhosphorylationGPGMQSPSSYQNNNY
CCCCCCCHHHCCCCC
47.1028348404
453PhosphorylationPGMQSPSSYQNNNYG
CCCCCCHHHCCCCCC
33.8428348404
454PhosphorylationGMQSPSSYQNNNYGL
CCCCCHHHCCCCCCC
21.4328348404
459PhosphorylationSSYQNNNYGLNMSSP
HHHCCCCCCCCCCCC
25.7228348404
464PhosphorylationNNYGLNMSSPPHGSP
CCCCCCCCCCCCCCC
38.3226074081
465PhosphorylationNYGLNMSSPPHGSPG
CCCCCCCCCCCCCCC
31.5126074081
470PhosphorylationMSSPPHGSPGLAPNQ
CCCCCCCCCCCCCCC
16.8626074081
505PhosphorylationSPVAGVHSPMASSGN
CCCCCCCCCCCCCCC
17.6016760465
509PhosphorylationGVHSPMASSGNTGNH
CCCCCCCCCCCCCCC
32.3117574025
543PhosphorylationSLLSTLSSPGPKLDN
HHHHHHCCCCCCCCC
36.6716760465
551PhosphorylationPGPKLDNSPNMNITQ
CCCCCCCCCCCCCCC
19.8129255136
557PhosphorylationNSPNMNITQPSKVSN
CCCCCCCCCCHHCCC
29.4423403867
560PhosphorylationNMNITQPSKVSNQDS
CCCCCCCHHCCCCCC
35.5523403867
561AcetylationMNITQPSKVSNQDSK
CCCCCCHHCCCCCCC
57.2625953088
563PhosphorylationITQPSKVSNQDSKSP
CCCCHHCCCCCCCCC
32.2923927012
567PhosphorylationSKVSNQDSKSPLGFY
HHCCCCCCCCCCCEE
25.8523927012
569PhosphorylationVSNQDSKSPLGFYCD
CCCCCCCCCCCEECC
29.3423401153
574PhosphorylationSKSPLGFYCDQNPVE
CCCCCCEECCCCCCC
8.0423927012
582PhosphorylationCDQNPVESSMCQSNS
CCCCCCCCCCCCCCC
24.4923403867
583PhosphorylationDQNPVESSMCQSNSR
CCCCCCCCCCCCCCC
15.2923403867
587PhosphorylationVESSMCQSNSRDHLS
CCCCCCCCCCCCCCC
31.6725627689
589PhosphorylationSSMCQSNSRDHLSDK
CCCCCCCCCCCCCHH
44.3125627689
598PhosphorylationDHLSDKESKESSVEG
CCCCHHHHHHHHHCC
47.6829083192
601PhosphorylationSDKESKESSVEGAEN
CHHHHHHHHHCCHHH
43.3422817900
602PhosphorylationDKESKESSVEGAENQ
HHHHHHHHHCCHHHC
25.8621815630
615PhosphorylationNQRGPLESKGHKKLL
HCCCCCCCHHHHHHH
52.1720068231
616AcetylationQRGPLESKGHKKLLQ
CCCCCCCHHHHHHHH
56.5110490106
619AcetylationPLESKGHKKLLQLLT
CCCCHHHHHHHHHHH
54.5110490106
620AcetylationLESKGHKKLLQLLTC
CCCHHHHHHHHHHHC
49.0710490106
620UbiquitinationLESKGHKKLLQLLTC
CCCHHHHHHHHHHHC
49.0710490106
626PhosphorylationKKLLQLLTCSSDDRG
HHHHHHHHCCCCCCC
20.9523401153
628PhosphorylationLLQLLTCSSDDRGHS
HHHHHHCCCCCCCCC
31.4123898821
629PhosphorylationLQLLTCSSDDRGHSS
HHHHHCCCCCCCCCC
45.7521815630
635PhosphorylationSSDDRGHSSLTNSPL
CCCCCCCCCCCCCCC
29.8425849741
636PhosphorylationSDDRGHSSLTNSPLD
CCCCCCCCCCCCCCC
33.2723927012
638PhosphorylationDRGHSSLTNSPLDSS
CCCCCCCCCCCCCCC
35.2825849741
640PhosphorylationGHSSLTNSPLDSSCK
CCCCCCCCCCCCCCC
22.9222167270
644PhosphorylationLTNSPLDSSCKESSV
CCCCCCCCCCCCCCC
45.3723927012
645PhosphorylationTNSPLDSSCKESSVS
CCCCCCCCCCCCCCE
28.9523927012
649PhosphorylationLDSSCKESSVSVTSP
CCCCCCCCCCEEECC
22.8727080861
650PhosphorylationDSSCKESSVSVTSPS
CCCCCCCCCEEECCC
21.3627080861
652PhosphorylationSCKESSVSVTSPSGV
CCCCCCCEEECCCCC
22.9427080861
654PhosphorylationKESSVSVTSPSGVSS
CCCCCEEECCCCCCC
27.6725850435
655PhosphorylationESSVSVTSPSGVSSS
CCCCEEECCCCCCCC
18.2130576142
657PhosphorylationSVSVTSPSGVSSSTS
CCEEECCCCCCCCCC
52.1525850435
660PhosphorylationVTSPSGVSSSTSGGV
EECCCCCCCCCCCCC
23.3027080861
661PhosphorylationTSPSGVSSSTSGGVS
ECCCCCCCCCCCCCC
34.9227080861
662PhosphorylationSPSGVSSSTSGGVSS
CCCCCCCCCCCCCCC
21.0627080861
663PhosphorylationPSGVSSSTSGGVSST
CCCCCCCCCCCCCCC
33.0827080861
664PhosphorylationSGVSSSTSGGVSSTS
CCCCCCCCCCCCCCC
35.1827080861
681AcetylationHGSLLQEKHRILHKL
CCHHHHHHHHHHHHH
25.8126051181
687AcetylationEKHRILHKLLQNGNS
HHHHHHHHHHHCCCC
47.6619608861
694PhosphorylationKLLQNGNSPAEVAKI
HHHHCCCCHHHHHHE
27.2130266825
697AcetylationQNGNSPAEVAKITAE
HCCCCHHHHHHEEEE
46.5219608861
702PhosphorylationPAEVAKITAEATGKD
HHHHHHEEEEHHCCC
20.1023312004
706PhosphorylationAKITAEATGKDTSSI
HHEEEEHHCCCCCCC
35.9523312004
708AcetylationITAEATGKDTSSITS
EEEEHHCCCCCCCEE
54.1825953088
710PhosphorylationAEATGKDTSSITSCG
EEHHCCCCCCCEECC
28.0523403867
711PhosphorylationEATGKDTSSITSCGD
EHHCCCCCCCEECCC
29.8523403867
712PhosphorylationATGKDTSSITSCGDG
HHCCCCCCCEECCCC
31.7923403867
714PhosphorylationGKDTSSITSCGDGNV
CCCCCCCEECCCCCC
21.6623403867
715PhosphorylationKDTSSITSCGDGNVV
CCCCCCEECCCCCCC
17.9023927012
723SumoylationCGDGNVVKQEQLSPK
CCCCCCCCHHHCCCC
43.78-
723SumoylationCGDGNVVKQEQLSPK
CCCCCCCCHHHCCCC
43.78-
723UbiquitinationCGDGNVVKQEQLSPK
CCCCCCCCHHHCCCC
43.78-
728PhosphorylationVVKQEQLSPKKKENN
CCCHHHCCCCHHHCH
34.0729255136
753UbiquitinationDPSDALSKELQPQVE
CHHHHHHHHHHHHHC
64.39-
767PhosphorylationEGVDNKMSQCTSSTI
CCCCCCHHHHCCCCC
24.5828674151
770PhosphorylationDNKMSQCTSSTIPSS
CCCHHHHCCCCCCCC
20.3428674151
771PhosphorylationNKMSQCTSSTIPSSS
CCHHHHCCCCCCCCC
32.8628674151
772PhosphorylationKMSQCTSSTIPSSSQ
CHHHHCCCCCCCCCC
16.5328674151
773PhosphorylationMSQCTSSTIPSSSQE
HHHHCCCCCCCCCCC
36.3528674151
776PhosphorylationCTSSTIPSSSQEKDP
HCCCCCCCCCCCCCC
38.4825627689
777PhosphorylationTSSTIPSSSQEKDPK
CCCCCCCCCCCCCCC
30.5925627689
778PhosphorylationSSTIPSSSQEKDPKI
CCCCCCCCCCCCCCC
46.8525159151
781AcetylationIPSSSQEKDPKIKTE
CCCCCCCCCCCCCCC
72.2325953088
786SumoylationQEKDPKIKTETSEEG
CCCCCCCCCCCCCCC
46.57-
786SumoylationQEKDPKIKTETSEEG
CCCCCCCCCCCCCCC
46.57-
786UbiquitinationQEKDPKIKTETSEEG
CCCCCCCCCCCCCCC
46.57-
834PhosphorylationKQQVFQGTNSLGLKS
CCCEEECCCCCCCCC
15.7327251275
836PhosphorylationQVFQGTNSLGLKSSQ
CEEECCCCCCCCCCC
24.5325159151
840MethylationGTNSLGLKSSQSVQS
CCCCCCCCCCCCHHC
46.38-
841PhosphorylationTNSLGLKSSQSVQSI
CCCCCCCCCCCHHCC
38.3623186163
842PhosphorylationNSLGLKSSQSVQSIR
CCCCCCCCCCHHCCC
25.5323186163
844PhosphorylationLGLKSSQSVQSIRPP
CCCCCCCCHHCCCCC
24.8723186163
849MethylationSQSVQSIRPPYNRAV
CCCHHCCCCCCCCCC
31.244726625
857O-linked_GlycosylationPPYNRAVSLDSPVSV
CCCCCCCCCCCCCCC
26.0223301498
857PhosphorylationPPYNRAVSLDSPVSV
CCCCCCCCCCCCCCC
26.0229255136
860PhosphorylationNRAVSLDSPVSVGSS
CCCCCCCCCCCCCCC
32.2830266825
863O-linked_GlycosylationVSLDSPVSVGSSPPV
CCCCCCCCCCCCCCC
24.9323301498
863PhosphorylationVSLDSPVSVGSSPPV
CCCCCCCCCCCCCCC
24.9330266825
866PhosphorylationDSPVSVGSSPPVKNI
CCCCCCCCCCCCCCC
37.2030266825
867PhosphorylationSPVSVGSSPPVKNIS
CCCCCCCCCCCCCCC
27.5629255136
871AcetylationVGSSPPVKNISAFPM
CCCCCCCCCCCCCCC
55.1025953088
894 (in isoform 2)Phosphorylation-22.8422210691
904 (in isoform 3)Phosphorylation-13.9922210691
910O-linked_GlycosylationGGPNRNVTVTQTPSS
CCCCCCEEEEECCCC
22.7623301498
912O-linked_GlycosylationPNRNVTVTQTPSSGD
CCCCEEEEECCCCCC
19.8423301498
912PhosphorylationPNRNVTVTQTPSSGD
CCCCEEEEECCCCCC
19.8428555341
914PhosphorylationRNVTVTQTPSSGDWG
CCEEEEECCCCCCCC
18.7728555341
916PhosphorylationVTVTQTPSSGDWGLP
EEEEECCCCCCCCCC
50.7925627689
917O-linked_GlycosylationTVTQTPSSGDWGLPN
EEEECCCCCCCCCCC
41.8123301498
917PhosphorylationTVTQTPSSGDWGLPN
EEEECCCCCCCCCCC
41.8125627689
926AcetylationDWGLPNSKAGRMEPM
CCCCCCCCCCCCCCC
62.5925953088
926UbiquitinationDWGLPNSKAGRMEPM
CCCCCCCCCCCCCCC
62.59-
945PhosphorylationMGRPGGDYNTSLPRP
CCCCCCCCCCCCCCC
24.5020873877
947PhosphorylationRPGGDYNTSLPRPAL
CCCCCCCCCCCCCCC
25.9720873877
948PhosphorylationPGGDYNTSLPRPALG
CCCCCCCCCCCCCCC
32.5120873877
951DimethylationDYNTSLPRPALGGSI
CCCCCCCCCCCCCCC
34.12-
951MethylationDYNTSLPRPALGGSI
CCCCCCCCCCCCCCC
34.1254561831
1033PhosphorylationNRPLLRNSLDDLVGP
CCHHHHCCHHHHCCC
27.0925849741
1042PhosphorylationDDLVGPPSNLEGQSD
HHHCCCCHHCCCCCH
58.1222817900
1048PhosphorylationPSNLEGQSDERALLD
CHHCCCCCHHHHHHH
52.9022817900
1059PhosphorylationALLDQLHTLLSNTDA
HHHHHHHHHHHCCCC
37.6822817900
1062PhosphorylationDQLHTLLSNTDATGL
HHHHHHHHCCCCCCH
40.5722817900
1064PhosphorylationLHTLLSNTDATGLEE
HHHHHHCCCCCCHHH
24.5222817900
1067PhosphorylationLLSNTDATGLEEIDR
HHHCCCCCCHHHHHH
45.1422817900
1091MethylationQGQALEPKQDAFQGQ
CCCCCCCCCCCCCCC
51.97-
1114PhosphorylationKAGLYGQTYPAQGPP
CCCCCCCCCCCCCCC
27.4022817900
1171Asymmetric dimethylarginineTNTPKQLRMQLQQRL
CCCHHHHHHHHHHHH
14.33-
1171MethylationTNTPKQLRMQLQQRL
CCCHHHHHHHHHHHH
14.3324129315
1177Asymmetric dimethylarginineLRMQLQQRLQGQQFL
HHHHHHHHHHHHHHH
18.93-
1177MethylationLRMQLQQRLQGQQFL
HHHHHHHHHHHHHHH
18.9324129315
1188Asymmetric dimethylarginineQQFLNQSRQALELKM
HHHHHHHHHHHHHHC
18.94-
1188MethylationQQFLNQSRQALELKM
HHHHHHHHHHHHHHC
18.9424129315
1194SumoylationSRQALELKMENPTAG
HHHHHHHHCCCCCCC
34.49-
1194SumoylationSRQALELKMENPTAG
HHHHHHHHCCCCCCC
34.49-
1329PhosphorylationDPAFGRVSSPPNAMM
CCCCCCCCCCCCHHH
35.4530266825
1330PhosphorylationPAFGRVSSPPNAMMS
CCCCCCCCCCCHHHC
41.3330266825
1337PhosphorylationSPPNAMMSSRMGPSQ
CCCCHHHCCCCCCCC
11.1630266825
1338PhosphorylationPPNAMMSSRMGPSQN
CCCHHHCCCCCCCCC
14.3730266825
1357PhosphorylationHPQAASIYQSSEMKG
CCCHHHHHHCCCCCC
10.3922817900

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
24TPhosphorylationKinaseMAPK8P45983
GPS
24TPhosphorylationKinaseJNK-SUBFAMILY-GPS
102SPhosphorylationKinaseCSNK1EP49674
GPS
505SPhosphorylationKinaseERK-SUBFAMILY-GPS
505SPhosphorylationKinaseGSK-FAMILY-GPS
505SPhosphorylationKinaseGSK3AP49840
PSP
505SPhosphorylationKinaseMAPK14Q16539
GPS
505SPhosphorylationKinaseJNK-SUBFAMILY-GPS
505SPhosphorylationKinaseP38-SUBFAMILY-GPS
505SPhosphorylationKinaseMAPK8P45983
GPS
509SPhosphorylationKinaseGSK3AP49840
PSP
543SPhosphorylationKinaseJNK-SUBFAMILY-GPS
543SPhosphorylationKinaseMAPK14Q16539
GPS
543SPhosphorylationKinaseMAPK8P45983
GPS
543SPhosphorylationKinaseP38-SUBFAMILY-GPS
601SPhosphorylationKinaseCSNK1DP48730
GPS
601SPhosphorylationKinaseCK1-Uniprot
728SPhosphorylationKinaseCDK1P06493
PSP
857SPhosphorylationKinaseMAPK6Q16659
GPS
857SPhosphorylationKinasePRKACAP17612
GPS
857SPhosphorylationKinaseCHUKO15111
GPS
857SPhosphorylationKinasePKA-FAMILY-GPS
857SPhosphorylationKinaseIKK-FAMILY-GPS
860SPhosphorylationKinaseP38-SUBFAMILY-GPS
860SPhosphorylationKinaseJNK-SUBFAMILY-GPS
860SPhosphorylationKinaseMAPK8P45983
GPS
860SPhosphorylationKinaseMAPK14Q16539
GPS
867SPhosphorylationKinaseJNK-SUBFAMILY-GPS
867SPhosphorylationKinaseMAPK8P45983
GPS
867SPhosphorylationKinaseP38-SUBFAMILY-GPS
867SPhosphorylationKinaseMAPK14Q16539
GPS
867SPhosphorylationKinaseCDK1P06493
PSP
1033SPhosphorylationKinasePRKCZQ05513
GPS
1042SPhosphorylationKinasePRKCZQ05513
GPS
1048SPhosphorylationKinasePRKCZQ05513
GPS
1059TPhosphorylationKinasePRKCZQ05513
GPS
1062SPhosphorylationKinaseKISQ8TAS1
PSP
1062SPhosphorylationKinasePRKCZQ05513
GPS
1064TPhosphorylationKinasePRKCZQ05513
GPS
1067TPhosphorylationKinaseKISQ8TAS1
PSP
1067TPhosphorylationKinasePRKCZQ05513
GPS
1114TPhosphorylationKinasePRKCZQ05513
GPS
1330SPhosphorylationKinaseDYRK3O43781
PSP
1357YPhosphorylationKinaseABL1P00519
GPS
-KUbiquitinationE3 ubiquitin ligaseSPOPO43791
PMID:21577200
-KUbiquitinationE3 ubiquitin ligaseFBXW7Q969H0
PMID:24658274
-KUbiquitinationE3 ubiquitin ligaseSTUB1Q9UNE7
PMID:19198599
-KUbiquitinationE3 ubiquitin ligaseUBE3AQ05086
PMID:16951183

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
601SPhosphorylation

19339517

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 NCOA3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EP300_HUMANEP300physical
10655477
ANR11_HUMANANKRD11physical
15184363
RXRA_HUMANRXRAphysical
9267036
CCND1_HUMANCCND1physical
9832502
ERR1_HUMANESRRAphysical
10598588
ERR2_HUMANESRRBphysical
10598588
CBP_HUMANCREBBPphysical
11076796
ESR1_HUMANESR1physical
11389589
ESR2_HUMANESR2physical
11389589
NR0B2_HUMANNR0B2physical
11668176
NR5A2_HUMANNR5A2physical
11668176
NCOA2_HUMANNCOA2physical
11971985
CBP_HUMANCREBBPphysical
11971985
RO52_HUMANTRIM21physical
11971985
NEMO_HUMANIKBKGphysical
11971985
IKKB_HUMANIKBKBphysical
11971985
IKKA_HUMANCHUKphysical
11971985
ESR2_HUMANESR2physical
10681591
VDR_HUMANVDRphysical
10681591
PRGR_HUMANPGRphysical
10757795
H31T_HUMANHIST3H3physical
11163245
CARM1_HUMANCARM1physical
17043108
CBP_HUMANCREBBPphysical
17043108
CARM1_HUMANCARM1physical
16923966
EP300_HUMANEP300physical
16923966
ESR1_HUMANESR1physical
16923966
BRCA1_HUMANBRCA1physical
16860316
ABL1_HUMANABL1physical
18765637
NCOR1_HUMANNCOR1physical
12089344
EP300_HUMANEP300physical
11823864
ETS1_HUMANETS1physical
15788656
ETS2_HUMANETS2physical
15788656
NCOA2_HUMANNCOA2physical
18267973
NCOA1_HUMANNCOA1physical
18267973
VDR_HUMANVDRphysical
10224118
ESR1_HUMANESR1physical
14766010
CBP_HUMANCREBBPphysical
9192892
RARA_HUMANRARAphysical
17475621
NCOR2_HUMANNCOR2physical
20392877
SPOP_HUMANSPOPphysical
21577200
CDKN3_HUMANCDKN3physical
21577200
IQCK_HUMANIQCKphysical
21577200
BABA2_HUMANBREphysical
21577200
DCTN6_HUMANDCTN6physical
21577200
KC1E_HUMANCSNK1Ephysical
21577200
RARA_HUMANRARAphysical
15604093
RARG_HUMANRARGphysical
15604093
ERR1_HUMANESRRAphysical
15604093
NR1H3_HUMANNR1H3physical
15604093
NR1H2_HUMANNR1H2physical
15604093
PPARG_HUMANPPARGphysical
15604093
SPTA1_HUMANSPTA1physical
16051665
MYH9_HUMANMYH9physical
16051665
ACTS_HUMANACTA1physical
16051665
ANXA2_HUMANANXA2physical
16051665
TPR_HUMANTPRphysical
16051665
MORC2_HUMANMORC2physical
16051665
NFAC3_HUMANNFATC3physical
16051665
PSME3_HUMANPSME3physical
16051665
IKKA_HUMANCHUKphysical
16051665
IKKB_HUMANIKBKBphysical
16051665
NEMO_HUMANIKBKGphysical
16051665
RO52_HUMANTRIM21physical
16051665
KAT2B_HUMANKAT2Bphysical
9346901
CBP_HUMANCREBBPphysical
9346901
EP300_HUMANEP300physical
10866661
NFKB1_HUMANNFKB1physical
15383283
EP300_HUMANEP300physical
20368990
ESR1_HUMANESR1physical
20181721
RFX1_HUMANRFX1physical
20181721
ESR1_HUMANESR1physical
19491275
CBP_HUMANCREBBPphysical
21914189
TP53B_HUMANTP53BP1physical
21914189
ANDR_HUMANARphysical
21047772
PRS8_HUMANPSMC5physical
19144644
KPCZ_HUMANPRKCZphysical
18313384
TFF1_HUMANTFF1genetic
18313384
MYCD_HUMANMYOCDphysical
17360478
MYCD_HUMANMYOCDgenetic
17360478
ESR1_HUMANESR1physical
17158759
ESR2_HUMANESR2physical
17158759
CEBPA_HUMANCEBPAgenetic
17098861
CEBPD_HUMANCEBPDgenetic
17098861
UBE3A_HUMANUBE3Aphysical
16951183
E2F1_HUMANE2F1physical
16648476
PSME3_HUMANPSME3physical
16439211
PIN1_HUMANPIN1physical
16227615
CBP_HUMANCREBBPphysical
16227615
EP300_HUMANEP300physical
16227615
MMS19_HUMANMMS19physical
11279242
E2F1_HUMANE2F1physical
15169882
PTEN_HUMANPTENphysical
23514585
FBXW7_HUMANFBXW7physical
23514585
SPOP_HUMANSPOPphysical
23559371
H31T_HUMANHIST3H3physical
14747462
ETV1_HUMANETV1physical
14747462
ESR1_HUMANESR1physical
10490106
MKL1_HUMANMKL1physical
17360478
MKL2_HUMANMKL2physical
17360478
CBP_HUMANCREBBPphysical
21632823
HNF1A_HUMANHNF1Aphysical
10777539
TF65_HUMANRELAphysical
16331275
PIAS1_HUMANPIAS1physical
22283414
EP300_HUMANEP300physical
25728767
NKX21_HUMANNKX2-1physical
15449938

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NCOA3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-687, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-551 AND SER-857, ANDMASS SPECTROMETRY.
"CK1delta modulates the transcriptional activity of ERalpha via AIB1in an estrogen-dependent manner and regulates ERalpha-AIB1interactions.";
Giamas G., Castellano L., Feng Q., Knippschild U., Jacob J.,Thomas R.S., Coombes R.C., Smith C.L., Jiao L.R., Stebbing J.;
Nucleic Acids Res. 37:3110-3123(2009).
Cited for: PHOSPHORYLATION AT SER-601 BY CSNK1D/CK1, AND INTERACTION WITH CSNK1D.
"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-551; SER-857 ANDSER-867, AND MASS SPECTROMETRY.
"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-214; SER-551; SER-728;SER-857 AND SER-867, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-857 AND SER-867, ANDMASS SPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-857, AND MASSSPECTROMETRY.

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