MD12L_HUMAN - dbPTM
MD12L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MD12L_HUMAN
UniProt AC Q86YW9
Protein Name Mediator of RNA polymerase II transcription subunit 12-like protein
Gene Name MED12L
Organism Homo sapiens (Human).
Sequence Length 2145
Subcellular Localization Nucleus .
Protein Description May be a 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 (By similarity)..
Protein Sequence MAAFGLLSYEQRPLKRPRLGPPDVYPQDPKQKEDELTAVNVKQGFNNQPAFTGDEHGSARNIVINPSKIGAYFSSILAEKLKLNTFQDTGKKKPQVNAKDNYWLVTARSQSAIHSWFSDLAGNKPLSILAKKVPILSKKEDVFAYLAKYSVPMVRATWLIKMTCAYYSAISEAKIKKRQAPDPNLEWTQISTRYLREQLAKISDFYHMASSTGDGPVPVPPEVEQAMKQWEYNEKLAFHMFQEGMLEKHEYLTWILDVLEKIRPMDDDLLKLLLPLMLQYSDEFVQSAYLSRRLAYFCARRLSLLLSDSPNLLAAHSPHMMIGPNNSSIGAPSPGPPGPGMSPVQLAFSDFLSCAQHGPLVYGLSCMLQTVTLCCPSALVWNYSTNENKSANPGSPLDLLQVAPSSLPMPGGNTAFNQQVRARIYEVEQQIKQRGRAVEVRWSFDKCQESTAGVTISRVLHTLEVLDRHCFDRTDSSNSMETLYHKIFWANQNKDNQEVAPNDEAVVTLLCEWAVSCKRSGKHRAMAVAKLLEKRQAEIEAERCGESEVLDEKESISSSSLAGSSLPVFQNVLLRFLDTQAPSLSDPNSECEKVEFVNLVLLFCEFIRHDVFSHDAYMCTLISRGDLSVTASTRPRSPVGENADEHYSKDHDVKMEIFSPMPGESCENANTSLGRRMSVNCEKLVKREKPRELIFPSNYDLLRHLQYATHFPIPLDESSSHECNQRTILLYGVGKERDEARHQLKKITKDILKILNKKSTTETGVGDEGQKARKNKQETFPTLETVFTKLQLLSYFDQHQVTSQISNNVLEQITSFASGTSYHLPLAHHIQLIFDLMEPALNINGLIDFAIQLLNELSVVEAELLLKSSSLAGSYTTGLCVCIVAVLRRYHSCLILNPDQTAQVFEGLCGVVKHVVNPSECSSPERCILAYLYDLYVSCSHLRSKFGDLFSSACSKVKQTIYNNVMPANSNLRWDPDFMMDFIENPSARSINYSMLGKILSDNAANRYSFVCNTLMNVCMGHQDAGRINDIANFSSELTACCTVLSSEWLGVLKALCCSSNHVWGFNDVLCTVDVSDLSFHDSLATFIAILIARQCFSLEDVVQHVALPSLLAAACGDADAEPGARMTCRLLLHLFRAPQACFLPQATGKPFPGIRSSCDRHLLAAAHNSIEVGAVFAVLKAIMMLGDAKIGNNSVSSLKNDDFTMRGLRCDGNADDIWTASQNPKSCGKSISIETANLREYARYVLRTICQQEWVGEHCLKEPERLCTDKELILDPVLSNMQAQKLLQLICYPHGIKECTEGDNLQRQHIKRILQNLEQWTLRQSWLELQLMIKQCLKDPGSGSVAEMNNLLDNIAKATIEVFQQSADLNNSSNSGMSLFNPNSIGSADTSSTRQNGIKTFLSSSERRGVWLVAPLIARLPTSVQGRVLKAAGEELEKGQHLGSSSKKERDRQKQKSMSLLSQQPFLSLVLTCLKGQDEQREGLLTSLQNQVNQILSNWREERYQDDIKARQMMHEALQLRLNLVGGMFDTVQRSTQWTTDWALLLLQIITSGTVDMHTNNELFTTVLDMLGVLINGTLASDLSNASPGGSEENKRAYMNLVKKLKKELGDKRSESIDKVRQLLPLPKQTCDVITCEPMGSLIDTKGNKIAGFDSIDKKQGLQVSTKQKVSPWDLFEGQKNPAPLSWAWFGTVRVDRRVIKYEEQHHLLLYHTHPMPKPRSYYLQPLPLPPEEEEEEPTSPVSQEPERKSAELSDQGKTTTDEEKKTKGRKRKTKSSSRVDEYPQSNIYRVPPNYSPISSQMMHHPQSTLWGYNLVGQPQQPGFFLQNQSLTPGGSRLDPAGSFVPTNTKQALSNMLQRRSGAMMQPPSLHAITSQQQLIQMKLLQQQQQQRLLRQAQTRPFQQGQPGDQAALFAAQARPSPQLPQYPGLQQAQTMPQGYTMYGTQMPLQQTSQQQAGSVVLSPSYNSRAYPAAHSNPVLMERLRQIQQQPSGYVQQQASPYLQPLTGSQRLNHQALQQSPLVGGGIDAVLTSAHPNLPSVPLPQDPMRPRQPQVRQQQRLLQMQQPQQPQPQQPPQPQQSSQSQSQTLGLQAMQPQQPLFPRQGLQQTQQQQQTAALVRQLQKQLSSNQPQQGVTPYGHPSHF
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
15AcetylationSYEQRPLKRPRLGPP
CCCCCCCCCCCCCCC		64.1425953088
82UbiquitinationSILAEKLKLNTFQDT
HHHHHHHCCCCCCCC		51.24-
91AcetylationNTFQDTGKKKPQVNA
CCCCCCCCCCCCCCC		60.7725953088
137PhosphorylationAKKVPILSKKEDVFA
HHCCCCCCCHHHHHH		42.26-
145PhosphorylationKKEDVFAYLAKYSVP
CHHHHHHHHHHCCCH		8.8418083107
149PhosphorylationVFAYLAKYSVPMVRA
HHHHHHHCCCHHHHH		14.8620068231
150PhosphorylationFAYLAKYSVPMVRAT
HHHHHHCCCHHHHHH		21.0220068231
167PhosphorylationIKMTCAYYSAISEAK
HHHHHHHHHHHHHHH		3.51-
425PhosphorylationQQVRARIYEVEQQIK
HHHHHHHHHHHHHHH		14.3627642862
432UbiquitinationYEVEQQIKQRGRAVE
HHHHHHHHHCCCEEE		29.60-
446UbiquitinationEVRWSFDKCQESTAG
EEEEEECCCCCCCCC		35.49-
462PhosphorylationTISRVLHTLEVLDRH
CHHHHHHHHHHHHHH		22.0618669648
474PhosphorylationDRHCFDRTDSSNSME
HHHHHCCCCCCCCHH		41.9218669648
484PhosphorylationSNSMETLYHKIFWAN
CCCHHHHHHHHHHHC		14.4218669648
530UbiquitinationHRAMAVAKLLEKRQA
HHHHHHHHHHHHHHH		47.18-
628PhosphorylationLISRGDLSVTASTRP
EEECCCEEEEECCCC		23.3528634298
630PhosphorylationSRGDLSVTASTRPRS
ECCCEEEEECCCCCC		16.1230576142
632PhosphorylationGDLSVTASTRPRSPV
CCEEEEECCCCCCCC		18.6430576142
633PhosphorylationDLSVTASTRPRSPVG
CEEEEECCCCCCCCC		42.0830576142
637PhosphorylationTASTRPRSPVGENAD
EECCCCCCCCCCCCH		26.9825849741
647PhosphorylationGENADEHYSKDHDVK
CCCCHHHCCCCCCCC		18.5028634298
648PhosphorylationENADEHYSKDHDVKM
CCCHHHCCCCCCCCE		33.2528634298
659 (in isoform 3)Phosphorylation-26.4223879269
668 (in isoform 3)Phosphorylation-42.7023879269
671PhosphorylationESCENANTSLGRRMS
CCCCCCCCCHHHHHC		23.95-
678PhosphorylationTSLGRRMSVNCEKLV
CCHHHHHCCCHHHHH		14.3623401153
683AcetylationRMSVNCEKLVKREKP
HHCCCHHHHHHCCCC		61.8625953088
735UbiquitinationILLYGVGKERDEARH
EEEEECCCHHHHHHH		47.36-
746UbiquitinationEARHQLKKITKDILK
HHHHHHHHHHHHHHH		65.29-
749UbiquitinationHQLKKITKDILKILN
HHHHHHHHHHHHHHC		46.36-
771UbiquitinationGVGDEGQKARKNKQE
CCCCHHHHHHHCCCC		62.10-
776UbiquitinationGQKARKNKQETFPTL
HHHHHHCCCCCCCHH		53.17-
785PhosphorylationETFPTLETVFTKLQL
CCCCHHHHHHHHHHH		24.8325367160
788PhosphorylationPTLETVFTKLQLLSY
CHHHHHHHHHHHHHH		26.8925367160
922PhosphorylationVVNPSECSSPERCIL
CCCHHHCCCHHHHHH		44.89-
923PhosphorylationVNPSECSSPERCILA
CCHHHCCCHHHHHHH		42.30-
956UbiquitinationLFSSACSKVKQTIYN
HHHHHHHHHHHHHHH		54.02-
958UbiquitinationSSACSKVKQTIYNNV
HHHHHHHHHHHHHCC		45.52-
998UbiquitinationINYSMLGKILSDNAA
CCHHHHHHHHCCCCC		53.78-
1150UbiquitinationFLPQATGKPFPGIRS
CCCCCCCCCCCCCHH		38.85-
1200UbiquitinationNNSVSSLKNDDFTMR
CCCHHHHCCCCCCCC		61.35-
1220PhosphorylationGNADDIWTASQNPKS
CCHHHCEECCCCCCC		19.43-
1222PhosphorylationADDIWTASQNPKSCG
HHHCEECCCCCCCCC		24.10-
1226UbiquitinationWTASQNPKSCGKSIS
EECCCCCCCCCCCEE		66.96-
1230UbiquitinationQNPKSCGKSISIETA
CCCCCCCCCEEEEEC		49.28-
1262AcetylationWVGEHCLKEPERLCT
CCCHHHCCCHHHHCC		76.3025953088
1280PhosphorylationLILDPVLSNMQAQKL
HHHHHHHCHHHHHHH		30.4130576142
1298UbiquitinationICYPHGIKECTEGDN
HHCCCCCCCCCCCCH		51.86-
1339UbiquitinationLMIKQCLKDPGSGSV
HHHHHHHHCCCCCCH		70.29-
1431UbiquitinationSVQGRVLKAAGEELE
CHHHHHHHHHHHHHH		33.08-
1457UbiquitinationERDRQKQKSMSLLSQ
HHHHHHHHHHHHHHC		55.98-
1487PhosphorylationEQREGLLTSLQNQVN
HHHHHHHHHHHHHHH		32.22-
1510UbiquitinationERYQDDIKARQMMHE
HHHHHHHHHHHHHHH		44.50-
1615PhosphorylationKELGDKRSESIDKVR
HHHCCCCCHHHHHHH		41.24-
1650UbiquitinationLIDTKGNKIAGFDSI
EEECCCCEECCCCCC		42.47-
1660UbiquitinationGFDSIDKKQGLQVST
CCCCCCCCCCCCCCC		45.94-
1668UbiquitinationQGLQVSTKQKVSPWD
CCCCCCCCCCCCHHH		40.38-
1670UbiquitinationLQVSTKQKVSPWDLF
CCCCCCCCCCHHHHC		46.35-
1722PhosphorylationHPMPKPRSYYLQPLP
CCCCCCCCCCCCCCC		27.0226074081
1723PhosphorylationPMPKPRSYYLQPLPL
CCCCCCCCCCCCCCC		14.9626074081
1724PhosphorylationMPKPRSYYLQPLPLP
CCCCCCCCCCCCCCC		10.5026074081
1740PhosphorylationEEEEEEPTSPVSQEP
HHCCCCCCCCCCCCC		49.2826074081
1741PhosphorylationEEEEEPTSPVSQEPE
HCCCCCCCCCCCCCC		33.7426074081
1744PhosphorylationEEPTSPVSQEPERKS
CCCCCCCCCCCCHHH		32.0126074081
1751PhosphorylationSQEPERKSAELSDQG
CCCCCHHHHHCCCCC		32.9526074081
1755PhosphorylationERKSAELSDQGKTTT
CHHHHHCCCCCCCCC		21.28-
1779PhosphorylationKRKTKSSSRVDEYPQ
CCCCCCCCCCCCCCH		43.3330576142
1784PhosphorylationSSSRVDEYPQSNIYR
CCCCCCCCCHHHCCC		11.3430576142
1851UbiquitinationSFVPTNTKQALSNML
CCCCCCHHHHHHHHH		35.33-
2116PhosphorylationQTQQQQQTAALVRQL
HHHHHHHHHHHHHHH		15.01-
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 MD12L_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MD12L_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 MD12L_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CND1_HUMANNCAPD2physical
26344197
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 MD12L_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-462; THR-474 ANDTYR-484, AND MASS SPECTROMETRY.

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