MED12_HUMAN - dbPTM
MED12_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MED12_HUMAN
UniProt AC Q93074
Protein Name Mediator of RNA polymerase II transcription subunit 12
Gene Name MED12
Organism Homo sapiens (Human).
Sequence Length 2177
Subcellular Localization Nucleus .
Protein Description Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. This subunit may specifically regulate transcription of targets of the Wnt signaling pathway and SHH signaling pathway..
Protein Sequence MAAFGILSYEHRPLKRPRLGPPDVYPQDPKQKEDELTALNVKQGFNNQPAVSGDEHGSAKNVSFNPAKISSNFSSIIAEKLRCNTLPDTGRRKPQVNQKDNFWLVTARSQSAINTWFTDLAGTKPLTQLAKKVPIFSKKEEVFGYLAKYTVPVMRAAWLIKMTCAYYAAISETKVKKRHVDPFMEWTQIITKYLWEQLQKMAEYYRPGPAGSGGCGSTIGPLPHDVEVAIRQWDYTEKLAMFMFQDGMLDRHEFLTWVLECFEKIRPGEDELLKLLLPLLLRYSGEFVQSAYLSRRLAYFCTRRLALQLDGVSSHSSHVISAQSTSTLPTTPAPQPPTSSTPSTPFSDLLMCPQHRPLVFGLSCILQTILLCCPSALVWHYSLTDSRIKTGSPLDHLPIAPSNLPMPEGNSAFTQQVRAKLREIEQQIKERGQAVEVRWSFDKCQEATAGFTIGRVLHTLEVLDSHSFERSDFSNSLDSLCNRIFGLGPSKDGHEISSDDDAVVSLLCEWAVSCKRSGRHRAMVVAKLLEKRQAEIEAERCGESEAADEKGSIASGSLSAPSAPIFQDVLLQFLDTQAPMLTDPRSESERVEFFNLVLLFCELIRHDVFSHNMYTCTLISRGDLAFGAPGPRPPSPFDDPADDPEHKEAEGSSSSKLEDPGLSESMDIDPSSSVLFEDMEKPDFSLFSPTMPCEGKGSPSPEKPDVEKEVKPPPKEKIEGTLGVLYDQPRHVQYATHFPIPQEESCSHECNQRLVVLFGVGKQRDDARHAIKKITKDILKVLNRKGTAETDQLAPIVPLNPGDLTFLGGEDGQKRRRNRPEAFPTAEDIFAKFQHLSHYDQHQVTAQVSRNVLEQITSFALGMSYHLPLVQHVQFIFDLMEYSLSISGLIDFAIQLLNELSVVEAELLLKSSDLVGSYTTSLCLCIVAVLRHYHACLILNQDQMAQVFEGLCGVVKHGMNRSDGSSAERCILAYLYDLYTSCSHLKNKFGELFSDFCSKVKNTIYCNVEPSESNMRWAPEFMIDTLENPAAHTFTYTGLGKSLSENPANRYSFVCNALMHVCVGHHDPDRVNDIAILCAELTGYCKSLSAEWLGVLKALCCSSNNGTCGFNDLLCNVDVSDLSFHDSLATFVAILIARQCLLLEDLIRCAAIPSLLNAACSEQDSEPGARLTCRILLHLFKTPQLNPCQSDGNKPTVGIRSSCDRHLLAASQNRIVDGAVFAVLKAVFVLGDAELKGSGFTVTGGTEELPEEEGGGGSGGRRQGGRNISVETASLDVYAKYVLRSICQQEWVGERCLKSLCEDSNDLQDPVLSSAQAQRLMQLICYPHRLLDNEDGENPQRQRIKRILQNLDQWTMRQSSLELQLMIKQTPNNEMNSLLENIAKATIEVFQQSAETGSSSGSTASNMPSSSKTKPVLSSLERSGVWLVAPLIAKLPTSVQGHVLKAAGEELEKGQHLGSSSRKERDRQKQKSMSLLSQQPFLSLVLTCLKGQDEQREGLLTSLYSQVHQIVNNWRDDQYLDDCKPKQLMHEALKLRLNLVGGMFDTVQRSTQQTTEWAMLLLEIIISGTVDMQSNNELFTTVLDMLSVLINGTLAADMSSISQGSMEENKRAYMNLAKKLQKELGERQSDSLEKVRQLLPLPKQTRDVITCEPQGSLIDTKGNKIAGFDSIFKKEGLQVSTKQKISPWDLFEGLKPSAPLSWGWFGTVRVDRRVARGEEQQRLLLYHTHLRPRPRAYYLEPLPLPPEDEEPPAPTLLEPEKKAPEPPKTDKPGAAPPSTEERKKKSTKGKKRSQPATKTEDYGMGPGRSGPYGVTVPPDLLHHPNPGSITHLNYRQGSIGLYTQNQPLPAGGPRVDPYRPVRLPMQKLPTRPTYPGVLPTTMTGVMGLEPSSYKTSVYRQQQPAVPQGQRLRQQLQQSQGMLGQSSVHQMTPSSSYGLQTSQGYTPYVSHVGLQQHTGPAGTMVPPSYSSQPYQSTHPSTNPTLVDPTRHLQQRPSGYVHQQAPTYGHGLTSTQRFSHQTLQQTPMISTMTPMSAQGVQAGVRSTAILPEQQQQQQQQQQQQQQQQQQQQQQQQQQYHIRQQQQQQILRQQQQQQQQQQQQQQQQQQQQQQQQQQHQQQQQQQAAPPQPQPQSQPQFQRQGLQQTQQQQQTAALVRQLQQQLSNTQPQPSTNIFGRY
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
15AcetylationSYEHRPLKRPRLGPP
CCCCCCCCCCCCCCC		64.1425953088
32UbiquitinationYPQDPKQKEDELTAL
CCCCHHCCHHHHHHC		73.5729967540
32 (in isoform 2)Ubiquitination-73.57-
42UbiquitinationELTALNVKQGFNNQP
HHHHCHHHCCCCCCC		43.5629967540
60AcetylationGDEHGSAKNVSFNPA
CCCCCCCCCCCCCHH		60.6326051181
60UbiquitinationGDEHGSAKNVSFNPA
CCCCCCCCCCCCCHH		60.6329967540
60 (in isoform 2)Ubiquitination-60.63-
68AcetylationNVSFNPAKISSNFSS
CCCCCHHHHHCCHHH		44.3626051181
68UbiquitinationNVSFNPAKISSNFSS
CCCCCHHHHHCCHHH		44.3629967540
68 (in isoform 2)Ubiquitination-44.36-
80AcetylationFSSIIAEKLRCNTLP
HHHHHHHHHCCCCCC		32.0123236377
80UbiquitinationFSSIIAEKLRCNTLP
HHHHHHHHHCCCCCC		32.0121987572
80 (in isoform 1)Ubiquitination-32.0121890473
80 (in isoform 2)Ubiquitination-32.0121890473
80 (in isoform 3)Ubiquitination-32.0121890473
115 (in isoform 3)Ubiquitination-18.8221890473
124UbiquitinationFTDLAGTKPLTQLAK
HHHHCCCCCHHHHHH		36.79-
124 (in isoform 2)Ubiquitination-36.79-
132UbiquitinationPLTQLAKKVPIFSKK
CHHHHHHHCCCCCCH		47.8629967540
132 (in isoform 2)Ubiquitination-47.86-
137PhosphorylationAKKVPIFSKKEEVFG
HHHCCCCCCHHHHHH		43.4624719451
138 (in isoform 2)Ubiquitination-54.15-
139UbiquitinationKVPIFSKKEEVFGYL
HCCCCCCHHHHHHHH		58.8929967540
139 (in isoform 2)Ubiquitination-58.89-
163PhosphorylationAAWLIKMTCAYYAAI
HHHHHHHHHHHHHHH		6.7523401153
166PhosphorylationLIKMTCAYYAAISET
HHHHHHHHHHHHCCC		8.8623401153
167PhosphorylationIKMTCAYYAAISETK
HHHHHHHHHHHCCCC		3.2223401153
171PhosphorylationCAYYAAISETKVKKR
HHHHHHHCCCCCCHH		34.1923401153
173PhosphorylationYYAAISETKVKKRHV
HHHHHCCCCCCHHCC		34.0523401153
204PhosphorylationQLQKMAEYYRPGPAG
HHHHHHHHHCCCCCC		8.6722210691
205PhosphorylationLQKMAEYYRPGPAGS
HHHHHHHHCCCCCCC		11.2222210691
212PhosphorylationYRPGPAGSGGCGSTI
HCCCCCCCCCCCCCC		33.8322210691
236PhosphorylationAIRQWDYTEKLAMFM
HHHHCCCHHHHHHHH		24.9522210691
302PhosphorylationRRLAYFCTRRLALQL
HHHHHHHHHHHHHHC		14.66-
429UbiquitinationREIEQQIKERGQAVE
HHHHHHHHHHCCCEE		36.70-
429 (in isoform 2)Ubiquitination-36.70-
443UbiquitinationEVRWSFDKCQEATAG
EEEECCCCCCHHCCC		35.4922505724
443 (in isoform 2)Ubiquitination-35.49-
443 (in isoform 3)Ubiquitination-35.49-
471PhosphorylationDSHSFERSDFSNSLD
HCCCCCCCCCHHHHH		35.49-
474PhosphorylationSFERSDFSNSLDSLC
CCCCCCCHHHHHHHH		30.42-
476PhosphorylationERSDFSNSLDSLCNR
CCCCCHHHHHHHHHH		32.15-
479PhosphorylationDFSNSLDSLCNRIFG
CCHHHHHHHHHHHHC		39.8625159151
515UbiquitinationCEWAVSCKRSGRHRA
HHHHHHCCCCCCHHH		41.9329967540
527UbiquitinationHRAMVVAKLLEKRQA
HHHHHHHHHHHHHHH		41.83-
527 (in isoform 2)Ubiquitination-41.83-
531UbiquitinationVVAKLLEKRQAEIEA
HHHHHHHHHHHHHHH		50.1829967540
531 (in isoform 2)Ubiquitination-50.18-
552PhosphorylationEAADEKGSIASGSLS
CCCCCCCCCCCCCCC		26.5027080861
555PhosphorylationDEKGSIASGSLSAPS
CCCCCCCCCCCCCCC		27.5220873877
557PhosphorylationKGSIASGSLSAPSAP
CCCCCCCCCCCCCCC		19.3620873877
559PhosphorylationSIASGSLSAPSAPIF
CCCCCCCCCCCCCCH		39.5720873877
562PhosphorylationSGSLSAPSAPIFQDV
CCCCCCCCCCCHHHH		46.5220873877
576PhosphorylationVLLQFLDTQAPMLTD
HHHHHHHCCCCCCCC		28.8627251275
582PhosphorylationDTQAPMLTDPRSESE
HCCCCCCCCCCCHHH		37.3926074081
635PhosphorylationAPGPRPPSPFDDPAD
CCCCCCCCCCCCCCC		40.6629255136
652PhosphorylationEHKEAEGSSSSKLED
HHHCCCCCCCCCCCC		20.6723186163
653PhosphorylationHKEAEGSSSSKLEDP
HHCCCCCCCCCCCCC		49.8723186163
663PhosphorylationKLEDPGLSESMDIDP
CCCCCCCCCCCCCCC		33.2720068231
665PhosphorylationEDPGLSESMDIDPSS
CCCCCCCCCCCCCCC		20.5520068231
670PhosphorylationSESMDIDPSSSVLFE
CCCCCCCCCCCCEEC		36.1217081983
671PhosphorylationESMDIDPSSSVLFED
CCCCCCCCCCCEECC		31.3420068231
672PhosphorylationSMDIDPSSSVLFEDM
CCCCCCCCCCEECCC		29.8320068231
673PhosphorylationMDIDPSSSVLFEDME
CCCCCCCCCEECCCC		27.4620068231
685PhosphorylationDMEKPDFSLFSPTMP
CCCCCCCCCCCCCCC		35.5726074081
688PhosphorylationKPDFSLFSPTMPCEG
CCCCCCCCCCCCCCC		25.4225849741
690PhosphorylationDFSLFSPTMPCEGKG
CCCCCCCCCCCCCCC		32.3325850435
698PhosphorylationMPCEGKGSPSPEKPD
CCCCCCCCCCCCCCC		26.2029255136
700PhosphorylationCEGKGSPSPEKPDVE
CCCCCCCCCCCCCCC		47.6030266825
726 (in isoform 2)Phosphorylation-15.3227642862
762UbiquitinationVVLFGVGKQRDDARH
EEEECCCCCHHHHHH		39.4929967540
762 (in isoform 2)Ubiquitination-39.49-
773UbiquitinationDARHAIKKITKDILK
HHHHHHHHHHHHHHH		49.87-
776UbiquitinationHAIKKITKDILKVLN
HHHHHHHHHHHHHHH		46.36-
780UbiquitinationKITKDILKVLNRKGT
HHHHHHHHHHHCCCC		45.0429967540
780 (in isoform 1)Ubiquitination-45.0421890473
780 (in isoform 2)Ubiquitination-45.0421890473
780 (in isoform 3)Ubiquitination-45.0421890473
785UbiquitinationILKVLNRKGTAETDQ
HHHHHHCCCCCCCCC		60.5929967540
785 (in isoform 2)Ubiquitination-60.59-
814AcetylationLGGEDGQKRRRNRPE
CCCCCCCCCCCCCCC		54.0926051181
814UbiquitinationLGGEDGQKRRRNRPE
CCCCCCCCCCCCCCC		54.0922505724
814 (in isoform 2)Ubiquitination-54.09-
814 (in isoform 3)Ubiquitination-54.09-
815 (in isoform 3)Ubiquitination-34.6021890473
832UbiquitinationTAEDIFAKFQHLSHY
CHHHHHHHHHCHHCC		34.50-
832 (in isoform 2)Ubiquitination-34.50-
988AcetylationSCSHLKNKFGELFSD
HHHHHHHHHHHHHHH		53.8326051181
988UbiquitinationSCSHLKNKFGELFSD
HHHHHHHHHHHHHHH		53.8329967540
988 (in isoform 2)Ubiquitination-53.83-
999AcetylationLFSDFCSKVKNTIYC
HHHHHHHHCCCEEEE		59.417681875
999UbiquitinationLFSDFCSKVKNTIYC
HHHHHHHHCCCEEEE		59.4121963094
999 (in isoform 2)Ubiquitination-59.41-
1001UbiquitinationSDFCSKVKNTIYCNV
HHHHHHCCCEEEECC		52.7022817900
1001 (in isoform 2)Ubiquitination-52.70-
1003PhosphorylationFCSKVKNTIYCNVEP
HHHHCCCEEEECCCC		13.9625262027
1005PhosphorylationSKVKNTIYCNVEPSE
HHCCCEEEECCCCCC		3.9525262027
1011PhosphorylationIYCNVEPSESNMRWA
EEECCCCCCCCCCCC		39.9025262027
1013PhosphorylationCNVEPSESNMRWAPE
ECCCCCCCCCCCCCE		40.0225262027
1181UbiquitinationRILLHLFKTPQLNPC
HHHHHHHCCCCCCCC		66.70-
1181 (in isoform 2)Ubiquitination-66.70-
1194UbiquitinationPCQSDGNKPTVGIRS
CCCCCCCCCCCCCHH		47.8229967540
1194 (in isoform 2)Ubiquitination-47.82-
1238PhosphorylationGDAELKGSGFTVTGG
CCCCCCCCCEEECCC		29.1923186163
1241PhosphorylationELKGSGFTVTGGTEE
CCCCCCEEECCCCCC		22.2321955146
1243PhosphorylationKGSGFTVTGGTEELP
CCCCEEECCCCCCCC		27.1721955146
1246PhosphorylationGFTVTGGTEELPEEE
CEEECCCCCCCCCCC		27.8621955146
1258PhosphorylationEEEGGGGSGGRRQGG
CCCCCCCCCCCCCCC		41.1530266825
1269PhosphorylationRQGGRNISVETASLD
CCCCCCCEEEEECHH		19.9017192257
1298UbiquitinationWVGERCLKSLCEDSN
CHHHHHHHHHHCCCC		45.0321963094
1298 (in isoform 2)Ubiquitination-45.03-
1298 (in isoform 3)Ubiquitination-45.03-
1304PhosphorylationLKSLCEDSNDLQDPV
HHHHHCCCCCCCCCC		15.2218691976
1414UbiquitinationMPSSSKTKPVLSSLE
CCCCCCCCCCHHHHH		36.5429967540
1414 (in isoform 2)Ubiquitination-36.54-
1418PhosphorylationSKTKPVLSSLERSGV
CCCCCCHHHHHHCCC		32.8624719451
1434UbiquitinationLVAPLIAKLPTSVQG
EEEHHHHCCCCCHHH		48.26-
1434 (in isoform 2)Ubiquitination-48.26-
1445UbiquitinationSVQGHVLKAAGEELE
CHHHHHHHHHHHHHH		34.7929967540
1445 (in isoform 2)Ubiquitination-34.79-
1453UbiquitinationAAGEELEKGQHLGSS
HHHHHHHHCCCCCCC		76.2129967540
1453 (in isoform 2)Ubiquitination-76.21-
1471UbiquitinationERDRQKQKSMSLLSQ
HHHHHHHHHHHHHHC		55.98-
1524UbiquitinationDQYLDDCKPKQLMHE
CCCHHCCCHHHHHHH		63.3429967540
1534UbiquitinationQLMHEALKLRLNLVG
HHHHHHHHHHHHHHH		38.31-
1567PhosphorylationLLLEIIISGTVDMQS
HHHHHHHHCCCCCCC		20.2926074081
1569PhosphorylationLEIIISGTVDMQSNN
HHHHHHCCCCCCCCC		13.4226074081
1574PhosphorylationSGTVDMQSNNELFTT
HCCCCCCCCCHHHHH		34.6826074081
1580PhosphorylationQSNNELFTTVLDMLS
CCCCHHHHHHHHHHH		28.7226074081
1581PhosphorylationSNNELFTTVLDMLSV
CCCHHHHHHHHHHHH		16.2526074081
1618AcetylationRAYMNLAKKLQKELG
HHHHHHHHHHHHHHH		58.1225953088
1618 (in isoform 2)Ubiquitination-58.12-
1619UbiquitinationAYMNLAKKLQKELGE
HHHHHHHHHHHHHHH		51.0129967540
1619 (in isoform 2)Ubiquitination-51.01-
1622UbiquitinationNLAKKLQKELGERQS
HHHHHHHHHHHHCCC		66.4029967540
1622 (in isoform 2)Ubiquitination-66.40-
1629PhosphorylationKELGERQSDSLEKVR
HHHHHCCCHHHHHHH		35.0722210691
1631PhosphorylationLGERQSDSLEKVRQL
HHHCCCHHHHHHHHH		43.6129083192
1634UbiquitinationRQSDSLEKVRQLLPL
CCCHHHHHHHHHCCC		48.2729967540
1634 (in isoform 2)Ubiquitination-48.27-
1643UbiquitinationRQLLPLPKQTRDVIT
HHHCCCCCCCCCEEE		72.4929967540
1643 (in isoform 2)Ubiquitination-72.49-
1661UbiquitinationQGSLIDTKGNKIAGF
CCCEEECCCCEECCC		57.6522505724
1661 (in isoform 2)Ubiquitination-57.65-
1661 (in isoform 3)Ubiquitination-57.65-
1664UbiquitinationLIDTKGNKIAGFDSI
EEECCCCEECCCCHH		42.4729967540
1664 (in isoform 2)Ubiquitination-42.47-
1670PhosphorylationNKIAGFDSIFKKEGL
CEECCCCHHHHCCCC		27.8824719451
1673UbiquitinationAGFDSIFKKEGLQVS
CCCCHHHHCCCCCCC		48.5221890473
1673 (in isoform 1)Ubiquitination-48.5221890473
1673 (in isoform 2)Ubiquitination-48.5221890473
1673 (in isoform 3)Ubiquitination-48.5221890473
1674UbiquitinationGFDSIFKKEGLQVST
CCCHHHHCCCCCCCC		46.3929967540
1674 (in isoform 2)Ubiquitination-46.39-
1682UbiquitinationEGLQVSTKQKISPWD
CCCCCCCCCCCCHHH		41.9329967540
1682 (in isoform 2)Ubiquitination-41.93-
1684 (in isoform 2)Ubiquitination-46.86-
1708 (in isoform 3)Ubiquitination-6.0121890473
1761AcetylationPTLLEPEKKAPEPPK
CCCCCCCCCCCCCCC		66.0226051181
1761UbiquitinationPTLLEPEKKAPEPPK
CCCCCCCCCCCCCCC		66.02-
1768AcetylationKKAPEPPKTDKPGAA
CCCCCCCCCCCCCCC		78.9025953088
1769PhosphorylationKAPEPPKTDKPGAAP
CCCCCCCCCCCCCCC		55.8426330541
1771AcetylationPEPPKTDKPGAAPPS
CCCCCCCCCCCCCCC		51.0525953088
1778PhosphorylationKPGAAPPSTEERKKK
CCCCCCCCHHHHHHH		47.6018691976
1779PhosphorylationPGAAPPSTEERKKKS
CCCCCCCHHHHHHHC		47.8725159151
1785UbiquitinationSTEERKKKSTKGKKR
CHHHHHHHCCCCCCC		67.4124816145
1786PhosphorylationTEERKKKSTKGKKRS
HHHHHHHCCCCCCCC		44.2026670566
1787PhosphorylationEERKKKSTKGKKRSQ
HHHHHHCCCCCCCCC		53.3326670566
1798AcetylationKRSQPATKTEDYGMG
CCCCCCCCCCCCCCC		52.6126051181
1798UbiquitinationKRSQPATKTEDYGMG
CCCCCCCCCCCCCCC		52.61-
1798 (in isoform 2)Ubiquitination-52.61-
1838PhosphorylationHLNYRQGSIGLYTQN
EEEECCCCEEEEECC		12.7328348404
1854MethylationPLPAGGPRVDPYRPV
CCCCCCCCCCCCCCC		49.0654548401
1859DimethylationGPRVDPYRPVRLPMQ
CCCCCCCCCCCCCCC		28.73-
1859MethylationGPRVDPYRPVRLPMQ
CCCCCCCCCCCCCCC		28.7354548405
1862DimethylationVDPYRPVRLPMQKLP
CCCCCCCCCCCCCCC		35.44-
1862MethylationVDPYRPVRLPMQKLP
CCCCCCCCCCCCCCC		35.4454548409
1871DimethylationPMQKLPTRPTYPGVL
CCCCCCCCCCCCCCC		21.44-
1871MethylationPMQKLPTRPTYPGVL
CCCCCCCCCCCCCCC		21.44116265311
1899Asymmetric dimethylarginineSYKTSVYRQQQPAVP
CCCCCCHHCCCCCCC		26.19-
1899MethylationSYKTSVYRQQQPAVP
CCCCCCHHCCCCCCC		26.1958858511
1910MethylationPAVPQGQRLRQQLQQ
CCCCHHHHHHHHHHH		38.3758858519
1912DimethylationVPQGQRLRQQLQQSQ
CCHHHHHHHHHHHHC		25.12-
1912MethylationVPQGQRLRQQLQQSQ
CCHHHHHHHHHHHHC		25.1230762587
1912 (in isoform 2)Methylation-25.12-
1994Asymmetric dimethylargininePTRHLQQRPSGYVHQ
CCCHHHCCCCCCCCC		17.87-
1994MethylationPTRHLQQRPSGYVHQ
CCCHHHCCCCCCCCC		17.8724129315
1996PhosphorylationRHLQQRPSGYVHQQA
CHHHCCCCCCCCCCC		44.9729978859
1998PhosphorylationLQQRPSGYVHQQAPT
HHCCCCCCCCCCCCC		10.0929978859
2005PhosphorylationYVHQQAPTYGHGLTS
CCCCCCCCCCCCCCC		45.1929978859
2006PhosphorylationVHQQAPTYGHGLTST
CCCCCCCCCCCCCCC		13.1829978859
2011PhosphorylationPTYGHGLTSTQRFSH
CCCCCCCCCCCCCCC		34.0329978859
2012PhosphorylationTYGHGLTSTQRFSHQ
CCCCCCCCCCCCCCH		27.8229978859
2013PhosphorylationYGHGLTSTQRFSHQT
CCCCCCCCCCCCCHH		20.6629978859
2015Asymmetric dimethylarginineHGLTSTQRFSHQTLQ
CCCCCCCCCCCHHHC		34.81-
2015MethylationHGLTSTQRFSHQTLQ
CCCCCCCCCCCHHHC		34.8124129315
2151PhosphorylationQTQQQQQTAALVRQL
HHHHHHHHHHHHHHH		15.01-
2163PhosphorylationRQLQQQLSNTQPQPS
HHHHHHHHCCCCCCC		33.2328450419
2165PhosphorylationLQQQLSNTQPQPSTN
HHHHHHCCCCCCCCC		37.9528450419
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

Oops, there are no upstream regulatory protein records of MED12_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MED12_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 MED12_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SOX9_HUMANSOX9physical
12136106
NANOG_HUMANNANOGphysical
19036726
GLI3_HUMANGLI3physical
17000779
EHMT2_HUMANEHMT2physical
18691967
MED13_HUMANMED13physical
20133760
CCNC_HUMANCCNCphysical
20133760
MED25_HUMANMED25physical
20133760
MED16_HUMANMED16physical
20133760
MED17_HUMANMED17physical
20133760
MED1_HUMANMED1physical
20133760
MED28_HUMANMED28physical
20133760
MED24_HUMANMED24physical
20133760
MED22_HUMANMED22physical
20133760
MED23_HUMANMED23physical
20133760
MED4_HUMANMED4physical
20133760
MED29_HUMANMED29physical
20133760
MED8_HUMANMED8physical
20133760
MED31_HUMANMED31physical
20133760
MED15_HUMANMED15physical
20133760
MED6_HUMANMED6physical
20133760
MED14_HUMANMED14physical
20133760
CDK19_HUMANCDK19physical
20133760
MED30_HUMANMED30physical
20133760
MED10_HUMANMED10physical
20133760
MED18_HUMANMED18physical
20133760
RCOR1_HUMANRCOR1physical
20133760
RPAB1_HUMANPOLR2Ephysical
20133760
MED27_HUMANMED27physical
20133760
MED20_HUMANMED20physical
20133760
MED11_HUMANMED11physical
20133760
MED21_HUMANMED21physical
20133760
CDK9_HUMANCDK9physical
20133760
MED29_HUMANMED29physical
22939629
MED8_HUMANMED8physical
22939629
MED16_HUMANMED16physical
22939629
MED6_HUMANMED6physical
22939629
MED24_HUMANMED24physical
22939629
MED21_HUMANMED21physical
22939629
MED4_HUMANMED4physical
22939629
MED27_HUMANMED27physical
22939629
MED1_HUMANMED1physical
23563140
MED26_HUMANMED26physical
23563140
MED14_HUMANMED14physical
23563140
U5S1_HUMANEFTUD2physical
26344197
MED13_HUMANMED13physical
26344197
MD13L_HUMANMED13Lphysical
26344197
PRP8_HUMANPRPF8physical
26344197
U520_HUMANSNRNP200physical
26344197
CDK8_HUMANCDK8physical
26496610
KAT2A_HUMANKAT2Aphysical
26496610
MEN1_HUMANMEN1physical
26496610
MED1_HUMANMED1physical
26496610
MED22_HUMANMED22physical
26496610
RBP56_HUMANTAF15physical
26496610
MED14_HUMANMED14physical
26496610
MED21_HUMANMED21physical
26496610
MED23_HUMANMED23physical
26496610
MED17_HUMANMED17physical
26496610
MED27_HUMANMED27physical
26496610
MED7_HUMANMED7physical
26496610
MED20_HUMANMED20physical
26496610
MED24_HUMANMED24physical
26496610
MED13_HUMANMED13physical
26496610
MED6_HUMANMED6physical
26496610
MED16_HUMANMED16physical
26496610
TADA3_HUMANTADA3physical
26496610
SPTC1_HUMANSPTLC1physical
26496610
SC61B_HUMANSEC61Bphysical
26496610
ECD_HUMANECDphysical
26496610
CASC3_HUMANCASC3physical
26496610
CDK19_HUMANCDK19physical
26496610
MD13L_HUMANMED13Lphysical
26496610
WBP2_HUMANWBP2physical
26496610
MED4_HUMANMED4physical
26496610
MED31_HUMANMED31physical
26496610
SIR6_HUMANSIRT6physical
26496610
MED15_HUMANMED15physical
26496610
MED18_HUMANMED18physical
26496610
MED9_HUMANMED9physical
26496610
MED29_HUMANMED29physical
26496610
KLH12_HUMANKLHL12physical
26496610
CCD82_HUMANCCDC82physical
26496610
MED25_HUMANMED25physical
26496610
MED10_HUMANMED10physical
26496610
LZTS2_HUMANLZTS2physical
26496610
MED30_HUMANMED30physical
26496610
MED8_HUMANMED8physical
26496610
COX20_HUMANCOX20physical
26496610
MED11_HUMANMED11physical
26496610
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
305450Opitz-Kaveggia syndrome (OKS)
309520Lujan-Fryns syndrome (LUJFRYS)
300895Ohdo syndrome, X-linked (OHDOX)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MED12_HUMAN

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Related Literatures of Post-Translational Modification
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-635; SER-698; SER-700;SER-1258 AND SER-1269, AND MASS SPECTROMETRY.
"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-635; SER-698; SER-700;SER-1258 AND SER-1269, AND MASS SPECTROMETRY.
"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-635, AND MASSSPECTROMETRY.
"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 TYR-166, AND MASSSPECTROMETRY.

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