NCOA2_HUMAN - dbPTM
NCOA2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NCOA2_HUMAN
UniProt AC Q15596
Protein Name Nuclear receptor coactivator 2
Gene Name NCOA2
Organism Homo sapiens (Human).
Sequence Length 1464
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 (By similarity)..
Protein Sequence MSGMGENTSDPSRAETRKRKECPDQLGPSPKRNTEKRNREQENKYIEELAELIFANFNDIDNFNFKPDKCAILKETVKQIRQIKEQEKAAAANIDEVQKSDVSSTGQGVIDKDALGPMMLEALDGFFFVVNLEGNVVFVSENVTQYLRYNQEELMNKSVYSILHVGDHTEFVKNLLPKSIVNGGSWSGEPPRRNSHTFNCRMLVKPLPDSEEEGHDNQEAHQKYETMQCFAVSQPKSIKEEGEDLQSCLICVARRVPMKERPVLPSSESFTTRQDLQGKITSLDTSTMRAAMKPGWEDLVRRCIQKFHAQHEGESVSYAKRHHHEVLRQGLAFSQIYRFSLSDGTLVAAQTKSKLIRSQTTNEPQLVISLHMLHREQNVCVMNPDLTGQTMGKPLNPISSNSPAHQALCSGNPGQDMTLSSNINFPINGPKEQMGMPMGRFGGSGGMNHVSGMQATTPQGSNYALKMNSPSQSSPGMNPGQPTSMLSPRHRMSPGVAGSPRIPPSQFSPAGSLHSPVGVCSSTGNSHSYTNSSLNALQALSEGHGVSLGSSLASPDLKMGNLQNSPVNMNPPPLSKMGSLDSKDCFGLYGEPSEGTTGQAESSCHPGEQKETNDPNLPPAVSSERADGQSRLHDSKGQTKLLQLLTTKSDQMEPSPLASSLSDTNKDSTGSLPGSGSTHGTSLKEKHKILHRLLQDSSSPVDLAKLTAEATGKDLSQESSSTAPGSEVTIKQEPVSPKKKENALLRYLLDKDDTKDIGLPEITPKLERLDSKTDPASNTKLIAMKTEKEEMSFEPGDQPGSELDNLEEILDDLQNSQLPQLFPDTRPGAPAGSVDKQAIINDLMQLTAENSPVTPVGAQKTALRISQSTFNNPRPGQLGRLLPNQNLPLDITLQSPTGAGPFPPIRNSSPYSVIPQPGMMGNQGMIGNQGNLGNSSTGMIGNSASRPTMPSGEWAPQSSAVRVTCAATTSAMNRPVQGGMIRNPAASIPMRPSSQPGQRQTLQSQVMNIGPSELEMNMGGPQYSQQQAPPNQTAPWPESILPIDQASFASQNRQPFGSSPDDLLCPHPAAESPSDEGALLDQLYLALRNFDGLEEIDRALGIPELVSQSQAVDPEQFSSQDSNIMLEQKAPVFPQQYASQAQMAQGSYSPMQDPNFHTMGQRPSYATLRMQPRPGLRPTGLVQNQPNQLRLQLQHRLQAQQNRQPLMNQISNVSNVNLTLRPGVPTQAPINAQMLAQRQREILNQHLRQRQMHQQQQVQQRTLMMRGQGLNMTPSMVAPSGMPATMSNPRIPQANAQQFPFPPNYGISQQPDPGFTGATTPQSPLMSPRMAHTQSPMMQQSQANPAYQAPSDINGWAQGNMGGNSMFSQQSPPHFGQQANTSMYSNNMNINVSMATNTGGMSSMNQMTGQISMTSVTSVPTSGLSSMGPEQVNDPALRGGNLFPNQLPGMDMIKQEGDTTRKYC
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------MSGMGENTS
------CCCCCCCCC
49.1119413330
2O-linked_Glycosylation------MSGMGENTS
------CCCCCCCCC
49.1130059200
2Phosphorylation------MSGMGENTS
------CCCCCCCCC
49.1119413330
8PhosphorylationMSGMGENTSDPSRAE
CCCCCCCCCCHHHHH
30.15-
29PhosphorylationCPDQLGPSPKRNTEK
CCCCCCCCCCCCHHH
41.0523401153
31AcetylationDQLGPSPKRNTEKRN
CCCCCCCCCCHHHHC
63.7225953088
76PhosphorylationKCAILKETVKQIRQI
HHHHHHHHHHHHHHH
31.2628348404
78AcetylationAILKETVKQIRQIKE
HHHHHHHHHHHHHHH
47.6423749302
99UbiquitinationANIDEVQKSDVSSTG
CCCHHHHHHCCCCCC
54.52-
161PhosphorylationLMNKSVYSILHVGDH
HHCCCHHEEEECCCH
19.27-
195PhosphorylationGEPPRRNSHTFNCRM
CCCCCCCCCCEEEEE
23.3029209046
197PhosphorylationPPRRNSHTFNCRMLV
CCCCCCCCEEEEEEE
19.1629209046
205UbiquitinationFNCRMLVKPLPDSEE
EEEEEEEEECCCCCC
36.55-
210PhosphorylationLVKPLPDSEEEGHDN
EEEECCCCCCCCCCC
44.9929255136
239SumoylationVSQPKSIKEEGEDLQ
CCCCCCHHHCCCCHH
57.72-
239SumoylationVSQPKSIKEEGEDLQ
CCCCCCHHHCCCCHH
57.7228112733
267PhosphorylationERPVLPSSESFTTRQ
CCCCCCCCCCCCCCH
35.0127251275
269PhosphorylationPVLPSSESFTTRQDL
CCCCCCCCCCCCHHH
29.8227251275
279UbiquitinationTRQDLQGKITSLDTS
CCHHHCCCEEECCHH
29.83-
293UbiquitinationSTMRAAMKPGWEDLV
HHHHHHHCCCHHHHH
35.33-
306AcetylationLVRRCIQKFHAQHEG
HHHHHHHHHHHHHCC
21.1426051181
306UbiquitinationLVRRCIQKFHAQHEG
HHHHHHHHHHHHHCC
21.14-
320UbiquitinationGESVSYAKRHHHEVL
CCCCCHHHHHHHHHH
43.99-
338Asymmetric dimethylarginineLAFSQIYRFSLSDGT
CHHHEEEEEECCCCC
19.12-
338MethylationLAFSQIYRFSLSDGT
CHHHEEEEEECCCCC
19.12-
358PhosphorylationTKSKLIRSQTTNEPQ
ECCHHHHCCCCCCCC
25.5320068231
360PhosphorylationSKLIRSQTTNEPQLV
CHHHHCCCCCCCCEE
32.6020068231
361PhosphorylationKLIRSQTTNEPQLVI
HHHHCCCCCCCCEEE
29.9220068231
369PhosphorylationNEPQLVISLHMLHRE
CCCCEEEEEEEEECC
12.5420068231
387PhosphorylationCVMNPDLTGQTMGKP
EEECCCCCCCCCCCC
34.3220068231
399PhosphorylationGKPLNPISSNSPAHQ
CCCCCCCCCCCHHHH
25.4025159151
400PhosphorylationKPLNPISSNSPAHQA
CCCCCCCCCCHHHHH
41.8925159151
402PhosphorylationLNPISSNSPAHQALC
CCCCCCCCHHHHHHH
25.9725159151
410PhosphorylationPAHQALCSGNPGQDM
HHHHHHHCCCCCCCC
42.3228348404
418PhosphorylationGNPGQDMTLSSNINF
CCCCCCCCCCCCCCC
31.6028348404
420PhosphorylationPGQDMTLSSNINFPI
CCCCCCCCCCCCCCC
16.5128348404
421PhosphorylationGQDMTLSSNINFPIN
CCCCCCCCCCCCCCC
44.8628348404
451PhosphorylationSGGMNHVSGMQATTP
CCCCCCCCCCCCCCC
22.4622210691
456PhosphorylationHVSGMQATTPQGSNY
CCCCCCCCCCCCCCE
23.3220068231
457PhosphorylationVSGMQATTPQGSNYA
CCCCCCCCCCCCCEE
19.3420068231
461PhosphorylationQATTPQGSNYALKMN
CCCCCCCCCEEEECC
22.7820068231
463PhosphorylationTTPQGSNYALKMNSP
CCCCCCCEEEECCCC
18.2722210691
469PhosphorylationNYALKMNSPSQSSPG
CEEEECCCCCCCCCC
23.5622158970
471PhosphorylationALKMNSPSQSSPGMN
EEECCCCCCCCCCCC
42.3822199227
473PhosphorylationKMNSPSQSSPGMNPG
ECCCCCCCCCCCCCC
42.7222199227
474PhosphorylationMNSPSQSSPGMNPGQ
CCCCCCCCCCCCCCC
20.1722199227
483PhosphorylationGMNPGQPTSMLSPRH
CCCCCCCCCCCCCCC
20.9122199227
484PhosphorylationMNPGQPTSMLSPRHR
CCCCCCCCCCCCCCC
25.1422199227
487PhosphorylationGQPTSMLSPRHRMSP
CCCCCCCCCCCCCCC
15.9622158970
489DimethylationPTSMLSPRHRMSPGV
CCCCCCCCCCCCCCC
27.03-
489MethylationPTSMLSPRHRMSPGV
CCCCCCCCCCCCCCC
27.0397778549
493PhosphorylationLSPRHRMSPGVAGSP
CCCCCCCCCCCCCCC
20.6119664994
499PhosphorylationMSPGVAGSPRIPPSQ
CCCCCCCCCCCCHHH
10.9822158970
501MethylationPGVAGSPRIPPSQFS
CCCCCCCCCCHHHCC
56.605169887
554PhosphorylationSLGSSLASPDLKMGN
CCCCCCCCCCCCCCC
25.0024275569
565PhosphorylationKMGNLQNSPVNMNPP
CCCCCCCCCCCCCCC
19.7723401153
575PhosphorylationNMNPPPLSKMGSLDS
CCCCCCHHHCCCCCC
26.7729396449
579PhosphorylationPPLSKMGSLDSKDCF
CCHHHCCCCCCCCCC
26.0428985074
636AcetylationQSRLHDSKGQTKLLQ
CCCCCCCCCHHHHHH
62.1819608861
640SumoylationHDSKGQTKLLQLLTT
CCCCCHHHHHHHHHC
39.03-
640AcetylationHDSKGQTKLLQLLTT
CCCCCHHHHHHHHHC
39.0319608861
640SumoylationHDSKGQTKLLQLLTT
CCCCCHHHHHHHHHC
39.0319608861
640UbiquitinationHDSKGQTKLLQLLTT
CCCCCHHHHHHHHHC
39.0319608861
648SumoylationLLQLLTTKSDQMEPS
HHHHHHCCHHHCCCC
46.9628112733
649PhosphorylationLQLLTTKSDQMEPSP
HHHHHCCHHHCCCCC
30.8623312004
655PhosphorylationKSDQMEPSPLASSLS
CHHHCCCCCCHHCCC
21.1725159151
659PhosphorylationMEPSPLASSLSDTNK
CCCCCCHHCCCCCCC
39.2228450419
660PhosphorylationEPSPLASSLSDTNKD
CCCCCHHCCCCCCCC
26.7028450419
662PhosphorylationSPLASSLSDTNKDST
CCCHHCCCCCCCCCC
44.3228450419
664PhosphorylationLASSLSDTNKDSTGS
CHHCCCCCCCCCCCC
40.5723090842
668PhosphorylationLSDTNKDSTGSLPGS
CCCCCCCCCCCCCCC
35.9620068231
669PhosphorylationSDTNKDSTGSLPGSG
CCCCCCCCCCCCCCC
40.7120068231
671PhosphorylationTNKDSTGSLPGSGST
CCCCCCCCCCCCCCC
31.3220068231
675PhosphorylationSTGSLPGSGSTHGTS
CCCCCCCCCCCCCCC
27.8625159151
677PhosphorylationGSLPGSGSTHGTSLK
CCCCCCCCCCCCCHH
20.9420068231
678PhosphorylationSLPGSGSTHGTSLKE
CCCCCCCCCCCCHHH
28.0523401153
681PhosphorylationGSGSTHGTSLKEKHK
CCCCCCCCCHHHHHH
24.2323401153
682PhosphorylationSGSTHGTSLKEKHKI
CCCCCCCCHHHHHHH
41.8720068231
697PhosphorylationLHRLLQDSSSPVDLA
HHHHHCCCCCCCHHH
21.5430266825
698PhosphorylationHRLLQDSSSPVDLAK
HHHHCCCCCCCHHHH
47.1223401153
699PhosphorylationRLLQDSSSPVDLAKL
HHHCCCCCCCHHHHH
32.6619664994
705MethylationSSPVDLAKLTAEATG
CCCCHHHHHHHHHHC
54.38-
705SumoylationSSPVDLAKLTAEATG
CCCCHHHHHHHHHHC
54.3828112733
705UbiquitinationSSPVDLAKLTAEATG
CCCCHHHHHHHHHHC
54.38-
713AcetylationLTAEATGKDLSQESS
HHHHHHCCCCCCCCC
51.6623954790
716PhosphorylationEATGKDLSQESSSTA
HHHCCCCCCCCCCCC
41.8725159151
719PhosphorylationGKDLSQESSSTAPGS
CCCCCCCCCCCCCCC
23.1920068231
720PhosphorylationKDLSQESSSTAPGSE
CCCCCCCCCCCCCCE
30.8428450419
721PhosphorylationDLSQESSSTAPGSEV
CCCCCCCCCCCCCEE
37.5628450419
722PhosphorylationLSQESSSTAPGSEVT
CCCCCCCCCCCCEEE
38.5323927012
726PhosphorylationSSSTAPGSEVTIKQE
CCCCCCCCEEEEEEC
28.0323927012
729PhosphorylationTAPGSEVTIKQEPVS
CCCCCEEEEEECCCC
20.5723927012
731SumoylationPGSEVTIKQEPVSPK
CCCEEEEEECCCCCC
38.96-
731SumoylationPGSEVTIKQEPVSPK
CCCEEEEEECCCCCC
38.9628112733
736PhosphorylationTIKQEPVSPKKKENA
EEEECCCCCCHHHHH
41.5423927012
738AcetylationKQEPVSPKKKENALL
EECCCCCCHHHHHHH
69.8119814913
739AcetylationQEPVSPKKKENALLR
ECCCCCCHHHHHHHH
69.5719814921
747PhosphorylationKENALLRYLLDKDDT
HHHHHHHHHHCCCCC
16.16-
763PhosphorylationDIGLPEITPKLERLD
CCCCCCCCCCHHHHC
16.8321815630
765SumoylationGLPEITPKLERLDSK
CCCCCCCCHHHHCCC
55.09-
765SumoylationGLPEITPKLERLDSK
CCCCCCCCHHHHCCC
55.09-
771PhosphorylationPKLERLDSKTDPASN
CCHHHHCCCCCCCCC
41.8923401153
772AcetylationKLERLDSKTDPASNT
CHHHHCCCCCCCCCC
57.5225953088
773PhosphorylationLERLDSKTDPASNTK
HHHHCCCCCCCCCCE
51.6827794612
777PhosphorylationDSKTDPASNTKLIAM
CCCCCCCCCCEEEEE
50.8828450419
779PhosphorylationKTDPASNTKLIAMKT
CCCCCCCCEEEEEEC
25.4026699800
780AcetylationTDPASNTKLIAMKTE
CCCCCCCEEEEEECC
41.9919608861
785SumoylationNTKLIAMKTEKEEMS
CCEEEEEECCHHCCC
44.50-
785AcetylationNTKLIAMKTEKEEMS
CCEEEEEECCHHCCC
44.5019608861
785SumoylationNTKLIAMKTEKEEMS
CCEEEEEECCHHCCC
44.5028112733
785UbiquitinationNTKLIAMKTEKEEMS
CCEEEEEECCHHCCC
44.5019608861
788SumoylationLIAMKTEKEEMSFEP
EEEEECCHHCCCCCC
65.29-
788SumoylationLIAMKTEKEEMSFEP
EEEEECCHHCCCCCC
65.29-
847PhosphorylationINDLMQLTAENSPVT
HHHHHHHHHCCCCCC
18.2927732954
851PhosphorylationMQLTAENSPVTPVGA
HHHHHCCCCCCCCCH
16.5622199227
854PhosphorylationTAENSPVTPVGAQKT
HHCCCCCCCCCHHHH
18.6822199227
860AcetylationVTPVGAQKTALRISQ
CCCCCHHHHHHEECH
34.9225953088
864Asymmetric dimethylarginineGAQKTALRISQSTFN
CHHHHHHEECHHCCC
24.85-
864MethylationGAQKTALRISQSTFN
CHHHHHHEECHHCCC
24.85-
866PhosphorylationQKTALRISQSTFNNP
HHHHHEECHHCCCCC
16.1928555341
868PhosphorylationTALRISQSTFNNPRP
HHHEECHHCCCCCCC
28.3328555341
874Asymmetric dimethylarginineQSTFNNPRPGQLGRL
HHCCCCCCCCCCCCC
50.53-
874MethylationQSTFNNPRPGQLGRL
HHCCCCCCCCCCCCC
50.5354548471
892PhosphorylationQNLPLDITLQSPTGA
CCCCEEEEEECCCCC
20.5728122231
895PhosphorylationPLDITLQSPTGAGPF
CEEEEEECCCCCCCC
27.7830377224
897PhosphorylationDITLQSPTGAGPFPP
EEEEECCCCCCCCCC
44.9328122231
964O-linked_GlycosylationQSSAVRVTCAATTSA
CCCCEEEEEEHHHCC
5.9530059200
987PhosphorylationMIRNPAASIPMRPSS
CCCCCCCCCCCCCCC
29.3628348404
993PhosphorylationASIPMRPSSQPGQRQ
CCCCCCCCCCCCCHH
31.1028348404
994PhosphorylationSIPMRPSSQPGQRQT
CCCCCCCCCCCCHHH
42.9728348404
1001PhosphorylationSQPGQRQTLQSQVMN
CCCCCHHHHHHHHHH
29.0225332170
1059PhosphorylationNRQPFGSSPDDLLCP
CCCCCCCCHHHCCCC
32.5028464451
1072PhosphorylationCPHPAAESPSDEGAL
CCCCCCCCCCCHHHH
25.6128348404
1074PhosphorylationHPAAESPSDEGALLD
CCCCCCCCCHHHHHH
58.5326657352
1129SumoylationSNIMLEQKAPVFPQQ
CCCCCEECCCCCHHH
45.33-
1162MethylationNFHTMGQRPSYATLR
CCCCCCCCCCCEEEC
19.19115917693
1169MethylationRPSYATLRMQPRPGL
CCCCEEECCCCCCCC
19.82115917697
1173Asymmetric dimethylarginineATLRMQPRPGLRPTG
EEECCCCCCCCCCCC
22.49-
1173MethylationATLRMQPRPGLRPTG
EEECCCCCCCCCCCC
22.4924129315
1177Asymmetric dimethylarginineMQPRPGLRPTGLVQN
CCCCCCCCCCCCCCC
32.42-
1177MethylationMQPRPGLRPTGLVQN
CCCCCCCCCCCCCCC
32.4224129315
1190Asymmetric dimethylarginineQNQPNQLRLQLQHRL
CCCCCHHHHHHHHHH
15.60-
1190MethylationQNQPNQLRLQLQHRL
CCCCCHHHHHHHHHH
15.6024129315
1196Asymmetric dimethylarginineLRLQLQHRLQAQQNR
HHHHHHHHHHHHHHC
18.61-
1196MethylationLRLQLQHRLQAQQNR
HHHHHHHHHHHHHHC
18.6124129315
1203Asymmetric dimethylarginineRLQAQQNRQPLMNQI
HHHHHHHCHHHHHHH
34.85-
1203MethylationRLQAQQNRQPLMNQI
HHHHHHHCHHHHHHH
34.8524129315
1211PhosphorylationQPLMNQISNVSNVNL
HHHHHHHHCCCCCCE
22.7824043423
1214PhosphorylationMNQISNVSNVNLTLR
HHHHHCCCCCCEEEC
39.0324043423
1219PhosphorylationNVSNVNLTLRPGVPT
CCCCCCEEECCCCCC
18.6024719451
1221Asymmetric dimethylarginineSNVNLTLRPGVPTQA
CCCCEEECCCCCCCC
22.23-
1221MethylationSNVNLTLRPGVPTQA
CCCCEEECCCCCCCC
22.2324129315
1240Asymmetric dimethylarginineQMLAQRQREILNQHL
HHHHHHHHHHHHHHH
34.80-
1240MethylationQMLAQRQREILNQHL
HHHHHHHHHHHHHHH
34.8054548487
1248MethylationEILNQHLRQRQMHQQ
HHHHHHHHHHHHHHH
27.7581450733
1250MethylationLNQHLRQRQMHQQQQ
HHHHHHHHHHHHHHH
29.38115386619
1261MethylationQQQQVQQRTLMMRGQ
HHHHHHHHHHHHHCC
16.8524129315
1262PhosphorylationQQQVQQRTLMMRGQG
HHHHHHHHHHHHCCC
18.0524043423
1266Asymmetric dimethylarginineQQRTLMMRGQGLNMT
HHHHHHHHCCCCCCC
21.96-
1266MethylationQQRTLMMRGQGLNMT
HHHHHHHHCCCCCCC
21.9624129315
1273PhosphorylationRGQGLNMTPSMVAPS
HCCCCCCCHHHCCCC
15.9022210691
1275PhosphorylationQGLNMTPSMVAPSGM
CCCCCCHHHCCCCCC
19.4024043423
1280PhosphorylationTPSMVAPSGMPATMS
CHHHCCCCCCCCCCC
37.6822210691
1285PhosphorylationAPSGMPATMSNPRIP
CCCCCCCCCCCCCCC
18.4322210691
1287PhosphorylationSGMPATMSNPRIPQA
CCCCCCCCCCCCCCC
39.0522210691
1454SumoylationLPGMDMIKQEGDTTR
CCCCCCCCCCCCCCC
35.3428112733

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
469SPhosphorylationKinaseCDK9P50750
PSP
469SPhosphorylationKinaseCSNK2A1P68400
GPS
487SPhosphorylationKinaseCDK9P50750
PSP
487SPhosphorylationKinaseCSNK2A1P68400
GPS
493SPhosphorylationKinaseCDK9P50750
PSP
493SPhosphorylationKinaseCSNK2A1P68400
GPS
499SPhosphorylationKinaseCDK9P50750
PSP
499SPhosphorylationKinaseCSNK2A1P68400
GPS
736SPhosphorylationKinaseMAPK1P28482
GPS
736SPhosphorylationKinaseMAPK3P27361
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NCOA2_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 NCOA2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ESR1_HUMANESR1physical
11937504
VDR_HUMANVDRphysical
10748178
ERR2_HUMANESRRBphysical
10598588
GCR_HUMANNR3C1physical
12151000
CCNT1_HUMANCCNT1physical
11704662
ESR1_HUMANESR1physical
18499756
BRCA1_HUMANBRCA1physical
16860316
RARA_HUMANRARAphysical
12503607
MEF2C_HUMANMEF2Cphysical
12130539
CCND3_HUMANCCND3physical
12130539
CDK4_HUMANCDK4physical
12130539
NCOA3_HUMANNCOA3physical
18267973
NCOA1_HUMANNCOA1physical
18267973
ESR1_HUMANESR1physical
14766010
CBP_HUMANCREBBPphysical
9192892
ESR1_HUMANESR1physical
17697320
USO1_HUMANUSO1physical
16051665
UBR5_HUMANUBR5physical
16051665
PYR1_HUMANCADphysical
16051665
WDHD1_HUMANWDHD1physical
16051665
C2D1A_HUMANCC2D1Aphysical
16051665
TBK1_HUMANTBK1physical
16051665
HSP72_HUMANHSPA2physical
16051665
ATR_HUMANATRphysical
16051665
MAGAB_HUMANMAGEA11physical
20448036
EP300_HUMANEP300physical
20448036
MAGAB_HUMANMAGEA11physical
19828458
GCR_HUMANNR3C1physical
9920895
THB_HUMANTHRBphysical
9920895
TAT_HV1H2tatphysical
11704662
PIAS3_MOUSEPias3physical
12208521
PIAS3_HUMANPIAS3physical
12208521
H31T_HUMANHIST3H3physical
14747462
ETV1_HUMANETV1physical
14747462

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 NCOA2_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-636; LYS-640; LYS-780 ANDLYS-785, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-699 AND SER-736, ANDMASS SPECTROMETRY.
"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-29 AND SER-565, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-699, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-493, AND MASSSPECTROMETRY.

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