MD13L_HUMAN - dbPTM
MD13L_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MD13L_HUMAN
UniProt AC Q71F56
Protein Name Mediator of RNA polymerase II transcription subunit 13-like
Gene Name MED13L
Organism Homo sapiens (Human).
Sequence Length 2210
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 MTAAANWVANGASLEDCHSNLFSLAELTGIKWRRYNFGGHGDCGPIISAPAQDDPILLSFIRCLQANLLCVWRRDVKPDCKELWIFWWGDEPNLVGVIHHELQVVEEGLWENGLSYECRTLLFKAIHNLLERCLMDKNFVRIGKWFVRPYEKDEKPVNKSEHLSCAFTFFLHGESNVCTSVEIAQHQPIYLINEEHIHMAQSSPAPFQVLVSPYGLNGTLTGQAYKMSDPATRKLIEEWQYFYPMVLKKKEESKEEDELGYDDDFPVAVEVIVGGVRMVYPSAFVLISQNDIPVPQSVASAGGHIAVGQQGLGSVKDPSNCGMPLTPPTSPEQAILGESGGMQSAASHLVSQDGGMITMHSPKRSGKIPPKLHNHMVHRVWKECILNRTQSKRSQMSTPTLEEEPASNPATWDFVDPTQRVSCSCSRHKLLKRCAVGPNRPPTVSQPGFSAGPSSSSSLPPPASSKHKTAERQEKGDKLQKRPLIPFHHRPSVAEELCMEQDTPGQKLGLAGIDSSLEVSSSRKYDKQMAVPSRNTSKQMNLNPMDSPHSPISPLPPTLSPQPRGQETESLDPPSVPVNPALYGNGLELQQLSTLDDRTVLVGQRLPLMAEVSETALYCGIRPSNPESSEKWWHSYRLPPSDDAEFRPPELQGERCDAKMEVNSESTALQRLLAQPNKRFKIWQDKQPQLQPLHFLDPLPLSQQPGDSLGEVNDPYTFEDGDIKYIFTANKKCKQGTEKDSLKKNKSEDGFGTKDVTTPGHSTPVPDGKNAMSIFSSATKTDVRQDNAAGRAGSSSLTQVTDLAPSLHDLDNIFDNSDDDELGAVSPALRSSKMPAVGTEDRPLGKDGRAAVPYPPTVADLQRMFPTPPSLEQHPAFSPVMNYKDGISSETVTALGMMESPMVSMVSTQLTEFKMEVEDGLGSPKPEEIKDFSYVHKVPSFQPFVGSSMFAPLKMLPSHCLLPLKIPDACLFRPSWAIPPKIEQLPMPPAATFIRDGYNNVPSVGSLADPDYLNTPQMNTPVTLNSAAPASNSGAGVLPSPATPRFSVPTPRTPRTPRTPRGGGTASGQGSVKYDSTDQGSPASTPSTTRPLNSVEPATMQPIPEAHSLYVTLILSDSVMNIFKDRNFDSCCICACNMNIKGADVGLYIPDSSNEDQYRCTCGFSAIMNRKLGYNSGLFLEDELDIFGKNSDIGQAAERRLMMCQSTFLPQVEGTKKPQEPPISLLLLLQNQHTQPFASLNFLDYISSNNRQTLPCVSWSYDRVQADNNDYWTECFNALEQGRQYVDNPTGGKVDEALVRSATVHSWPHSNVLDISMLSSQDVVRMLLSLQPFLQDAIQKKRTGRTWENIQHVQGPLTWQQFHKMAGRGTYGSEESPEPLPIPTLLVGYDKDFLTISPFSLPFWERLLLDPYGGHRDVAYIVVCPENEALLEGAKTFFRDLSAVYEMCRLGQHKPICKVLRDGIMRVGKTVAQKLTDELVSEWFNQPWSGEENDNHSRLKLYAQVCRHHLAPYLATLQLDSSLLIPPKYQTPPAAAQGQATPGNAGPLAPNGSAAPPAGSAFNPTSNSSSTNPAASSSASGSSVPPVSSSASAPGISQISTTSSSGFSGSVGGQNPSTGGISADRTQGNIGCGGDTDPGQSSSQPSQDGQESVTERERIGIPTEPDSADSHAHPPAVVIYMVDPFTYAAEEDSTSGNFWLLSLMRCYTEMLDNLPEHMRNSFILQIVPCQYMLQTMKDEQVFYIQYLKSMAFSVYCQCRRPLPTQIHIKSLTGFGPAASIEMTLKNPERPSPIQLYSPPFILAPIKDKQTELGETFGEASQKYNVLFVGYCLSHDQRWLLASCTDLHGELLETCVVNIALPNRSRRSKVSARKIGLQKLWEWCIGIVQMTSLPWRVVIGRLGRLGHGELKDWSILLGECSLQTISKKLKDVCRMCGISAADSPSILSACLVAMEPQGSFVVMPDAVTMGSVFGRSTALNMQSSQLNTPQDASCTHILVFPTSSTIQVAPANYPNEDGFSPNNDDMFVDLPFPDDMDNDIGILMTGNLHSSPNSSPVPSPGSPSGIGVGSHFQHSRSQGERLLSREAPEELKQQPLALGYFVSTAKAENLPQWFWSSCPQAQNQCPLFLKASLHHHISVAQTDELLPARNSQRVPHPLDSKTTSDVLRFVLEQYNALSWLTCNPATQDRTSCLPVHFVVLTQLYNAIMNIL
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
2Phosphorylation------MTAAANWVA
------CCCHHHHHH		35.9925002506
13PhosphorylationNWVANGASLEDCHSN
HHHHCCCCHHHHHHH		33.4225002506
19PhosphorylationASLEDCHSNLFSLAE
CCHHHHHHHHHHHHH		41.3725002506
23PhosphorylationDCHSNLFSLAELTGI
HHHHHHHHHHHHHCC		29.8125002506
28PhosphorylationLFSLAELTGIKWRRY
HHHHHHHHCCCEEEE		28.5025002506
232PhosphorylationYKMSDPATRKLIEEW
EECCCHHHHHHHHHH		33.4530576142
326PhosphorylationSNCGMPLTPPTSPEQ
HHCCCCCCCCCCHHH		22.7328348404
329PhosphorylationGMPLTPPTSPEQAIL
CCCCCCCCCHHHHHH		59.1128348404
330PhosphorylationMPLTPPTSPEQAILG
CCCCCCCCHHHHHHC		32.0128348404
365PhosphorylationTMHSPKRSGKIPPKL
EECCCCCCCCCCHHH		51.03-
389PhosphorylationKECILNRTQSKRSQM
HHHHHHHHHHHCCCC		35.8018452278
391PhosphorylationCILNRTQSKRSQMST
HHHHHHHHHCCCCCC		29.4418452278
394PhosphorylationNRTQSKRSQMSTPTL
HHHHHHCCCCCCCCC		33.6923401153
397PhosphorylationQSKRSQMSTPTLEEE
HHHCCCCCCCCCCCC		24.4928450419
398PhosphorylationSKRSQMSTPTLEEEP
HHCCCCCCCCCCCCC		18.2319369195
400PhosphorylationRSQMSTPTLEEEPAS
CCCCCCCCCCCCCCC		47.0628450419
407PhosphorylationTLEEEPASNPATWDF
CCCCCCCCCCCCCCC		54.8028450419
411PhosphorylationEPASNPATWDFVDPT
CCCCCCCCCCCCCCC		27.1628111955
492PhosphorylationIPFHHRPSVAEELCM
CCCCCCCCHHHHHHH		33.6427251275
520PhosphorylationIDSSLEVSSSRKYDK
CCCCCEECCCCCCCC		17.1428348404
521PhosphorylationDSSLEVSSSRKYDKQ
CCCCEECCCCCCCCC		39.0617192257
522PhosphorylationSSLEVSSSRKYDKQM
CCCEECCCCCCCCCC		25.8628122231
524AcetylationLEVSSSRKYDKQMAV
CEECCCCCCCCCCCC		60.8025953088
533PhosphorylationDKQMAVPSRNTSKQM
CCCCCCCCCCCCCCC		31.4023532336
537PhosphorylationAVPSRNTSKQMNLNP
CCCCCCCCCCCCCCC		25.1728674151
547PhosphorylationMNLNPMDSPHSPISP
CCCCCCCCCCCCCCC		20.4722617229
550PhosphorylationNPMDSPHSPISPLPP
CCCCCCCCCCCCCCC		27.5822617229
553PhosphorylationDSPHSPISPLPPTLS
CCCCCCCCCCCCCCC		24.6222617229
558PhosphorylationPISPLPPTLSPQPRG
CCCCCCCCCCCCCCC		37.6220068231
560PhosphorylationSPLPPTLSPQPRGQE
CCCCCCCCCCCCCCC		24.7822617229
575PhosphorylationTESLDPPSVPVNPAL
CCCCCCCCCCCCHHH		44.4322817900
678AcetylationRLLAQPNKRFKIWQD
HHHCCCCCCCCCCCC		66.9325953088
678UbiquitinationRLLAQPNKRFKIWQD
HHHCCCCCCCCCCCC		66.93-
702PhosphorylationFLDPLPLSQQPGDSL
ECCCCCCCCCCCCCC		25.4829523821
708PhosphorylationLSQQPGDSLGEVNDP
CCCCCCCCCCCCCCC		44.1629523821
731AcetylationKYIFTANKKCKQGTE
EEEEECCCCCCCCCC		58.0225953088
732AcetylationYIFTANKKCKQGTEK
EEEECCCCCCCCCCC		46.6130585983
746AcetylationKDSLKKNKSEDGFGT
CHHCCCCCCCCCCCC		65.1926051181
747PhosphorylationDSLKKNKSEDGFGTK
HHCCCCCCCCCCCCC		50.7623312004
754AcetylationSEDGFGTKDVTTPGH
CCCCCCCCCCCCCCC		51.0523236377
757PhosphorylationGFGTKDVTTPGHSTP
CCCCCCCCCCCCCCC		37.0930266825
758PhosphorylationFGTKDVTTPGHSTPV
CCCCCCCCCCCCCCC		27.4130266825
762PhosphorylationDVTTPGHSTPVPDGK
CCCCCCCCCCCCCCC		40.0830266825
763PhosphorylationVTTPGHSTPVPDGKN
CCCCCCCCCCCCCCC		23.7230266825
769AcetylationSTPVPDGKNAMSIFS
CCCCCCCCCHHHHHH		49.2526051181
773PhosphorylationPDGKNAMSIFSSATK
CCCCCHHHHHHHCCC		20.3321712546
776PhosphorylationKNAMSIFSSATKTDV
CCHHHHHHHCCCCCH		19.8618691976
777PhosphorylationNAMSIFSSATKTDVR
CHHHHHHHCCCCCHH		29.2525159151
779PhosphorylationMSIFSSATKTDVRQD
HHHHHHCCCCCHHHC		36.1022199227
780AcetylationSIFSSATKTDVRQDN
HHHHHCCCCCHHHCC		42.3025953088
781PhosphorylationIFSSATKTDVRQDNA
HHHHCCCCCHHHCCC		35.0628555341
794PhosphorylationNAAGRAGSSSLTQVT
CCCCCCCCCCCHHHH		18.7720068231
795PhosphorylationAAGRAGSSSLTQVTD
CCCCCCCCCCHHHHH		28.5720068231
796PhosphorylationAGRAGSSSLTQVTDL
CCCCCCCCCHHHHHC		36.8120068231
798PhosphorylationRAGSSSLTQVTDLAP
CCCCCCCHHHHHCCC		23.9620068231
801PhosphorylationSSSLTQVTDLAPSLH
CCCCHHHHHCCCCHH		18.5820068231
806PhosphorylationQVTDLAPSLHDLDNI
HHHHCCCCHHHHHHC		32.5028464451
817PhosphorylationLDNIFDNSDDDELGA
HHHCCCCCCCCHHHC		44.2425159151
826PhosphorylationDDELGAVSPALRSSK
CCHHHCCCHHHHHCC		12.1525159151
831PhosphorylationAVSPALRSSKMPAVG
CCCHHHHHCCCCCCC		34.8526074081
833AcetylationSPALRSSKMPAVGTE
CHHHHHCCCCCCCCC		50.5825953088
839PhosphorylationSKMPAVGTEDRPLGK
CCCCCCCCCCCCCCC		28.2828387310
846AcetylationTEDRPLGKDGRAAVP
CCCCCCCCCCCCCCC		65.7725953088
867PhosphorylationDLQRMFPTPPSLEQH
HHHHHCCCCCCHHHC		36.2421712546
870PhosphorylationRMFPTPPSLEQHPAF
HHCCCCCCHHHCCCC		45.8222115753
878PhosphorylationLEQHPAFSPVMNYKD
HHHCCCCCCCCCCCC		20.7725159151
883PhosphorylationAFSPVMNYKDGISSE
CCCCCCCCCCCCCHH		7.7428450419
888PhosphorylationMNYKDGISSETVTAL
CCCCCCCCHHHHHHH		27.8726074081
889PhosphorylationNYKDGISSETVTALG
CCCCCCCHHHHHHHH		35.0526074081
900PhosphorylationTALGMMESPMVSMVS
HHHHCCCCHHHHHHH		10.6228348404
923PhosphorylationEVEDGLGSPKPEEIK
HHCCCCCCCCHHHHC		34.4929255136
933PhosphorylationPEEIKDFSYVHKVPS
HHHHCCCCEEECCCC		36.0623663014
934PhosphorylationEEIKDFSYVHKVPSF
HHHCCCCEEECCCCC		13.4323663014
940PhosphorylationSYVHKVPSFQPFVGS
CEEECCCCCCCCCCC		39.2320068231
947PhosphorylationSFQPFVGSSMFAPLK
CCCCCCCCCCCCCCC		17.2120068231
948PhosphorylationFQPFVGSSMFAPLKM
CCCCCCCCCCCCCCC		16.4020068231
958PhosphorylationAPLKMLPSHCLLPLK
CCCCCCCHHCEEECC		23.9130576142
1003PhosphorylationDGYNNVPSVGSLADP
CCCCCCCCCHHCCCH		34.5228348404
1006PhosphorylationNNVPSVGSLADPDYL
CCCCCCHHCCCHHHC		20.4428348404
1012PhosphorylationGSLADPDYLNTPQMN
HHCCCHHHCCCCCCC		13.7728348404
1015PhosphorylationADPDYLNTPQMNTPV
CCHHHCCCCCCCCCC		16.5928348404
1020PhosphorylationLNTPQMNTPVTLNSA
CCCCCCCCCCCCCCC		17.5028348404
1023PhosphorylationPQMNTPVTLNSAAPA
CCCCCCCCCCCCCCC		22.7928348404
1026PhosphorylationNTPVTLNSAAPASNS
CCCCCCCCCCCCCCC		28.9928348404
1047PhosphorylationSPATPRFSVPTPRTP
CCCCCCCCCCCCCCC		28.5923312004
1050PhosphorylationTPRFSVPTPRTPRTP
CCCCCCCCCCCCCCC		24.2130266825
1053PhosphorylationFSVPTPRTPRTPRTP
CCCCCCCCCCCCCCC		20.5128985074
1056PhosphorylationPTPRTPRTPRTPRGG
CCCCCCCCCCCCCCC		20.5128985074
1059PhosphorylationRTPRTPRTPRGGGTA
CCCCCCCCCCCCCCC		20.6722817900
1061MethylationPRTPRTPRGGGTASG
CCCCCCCCCCCCCCC		56.63115368241
1065PhosphorylationRTPRGGGTASGQGSV
CCCCCCCCCCCCCCE		22.4124275569
1071PhosphorylationGTASGQGSVKYDSTD
CCCCCCCCEEECCCC		13.9328985074
1074PhosphorylationSGQGSVKYDSTDQGS
CCCCCEEECCCCCCC		16.9918691976
1076PhosphorylationQGSVKYDSTDQGSPA
CCCEEECCCCCCCCC		30.6927732954
1077PhosphorylationGSVKYDSTDQGSPAS
CCEEECCCCCCCCCC		29.4627732954
1081PhosphorylationYDSTDQGSPASTPST
ECCCCCCCCCCCCCC		16.2019664994
1084PhosphorylationTDQGSPASTPSTTRP
CCCCCCCCCCCCCCC		44.2127732954
1085PhosphorylationDQGSPASTPSTTRPL
CCCCCCCCCCCCCCC		24.3027732954
1087PhosphorylationGSPASTPSTTRPLNS
CCCCCCCCCCCCCCC		42.3627732954
1088PhosphorylationSPASTPSTTRPLNSV
CCCCCCCCCCCCCCC		28.2027732954
1089PhosphorylationPASTPSTTRPLNSVE
CCCCCCCCCCCCCCC		34.3327732954
1130PhosphorylationFKDRNFDSCCICACN
HCCCCCCCCEEEEEC		13.5229978859
1148PhosphorylationKGADVGLYIPDSSNE
CCCCEEEECCCCCCC		12.41-
1152PhosphorylationVGLYIPDSSNEDQYR
EEEECCCCCCCCCEE		29.7028985074
1158PhosphorylationDSSNEDQYRCTCGFS
CCCCCCCEEECCCHH		21.70-
1161PhosphorylationNEDQYRCTCGFSAIM
CCCCEEECCCHHHHH		13.48-
1165PhosphorylationYRCTCGFSAIMNRKL
EEECCCHHHHHCCCC		11.36-
1215PhosphorylationFLPQVEGTKKPQEPP
CCHHCCCCCCCCCCC		23.5324719451
1293UbiquitinationVDNPTGGKVDEALVR
CCCCCCCCCCHHHHH		48.1021906983
1306PhosphorylationVRSATVHSWPHSNVL
HHHCCCCCCCCCCCC		37.66-
1320PhosphorylationLDISMLSSQDVVRML
CCHHHCCHHHHHHHH		26.83-
1329PhosphorylationDVVRMLLSLQPFLQD
HHHHHHHHHHHHHHH		22.4625599653
1340UbiquitinationFLQDAIQKKRTGRTW
HHHHHHHHHCCCCCH		37.8021906983
1373PhosphorylationAGRGTYGSEESPEPL
CCCCCCCCCCCCCCC		27.9825332170
1376PhosphorylationGTYGSEESPEPLPIP
CCCCCCCCCCCCCCC		30.4325332170
1389PhosphorylationIPTLLVGYDKDFLTI
CCEEEEECCCCCCEE		16.6125332170
1474UbiquitinationVGKTVAQKLTDELVS
HCHHHHHHHHHHHHH		43.55-
1502PhosphorylationNHSRLKLYAQVCRHH
CHHHHHHHHHHHHHC		8.0620068231
1521PhosphorylationLATLQLDSSLLIPPK
HHHEEECCCCCCCCC		31.32-
1522PhosphorylationATLQLDSSLLIPPKY
HHEEECCCCCCCCCC		27.19-
1643PhosphorylationTDPGQSSSQPSQDGQ
CCCCCCCCCCCCCCC		51.8917525332
1764PhosphorylationQCRRPLPTQIHIKSL
CCCCCCCCEEEEEEC		48.0823403867
1770PhosphorylationPTQIHIKSLTGFGPA
CCEEEEEECCCCCCC		30.4724275569
1808UbiquitinationILAPIKDKQTELGET
EEEECCCCCCHHHCH		54.8621906983
1810PhosphorylationAPIKDKQTELGETFG
EECCCCCCHHHCHHH		38.6326437602
1815PhosphorylationKQTELGETFGEASQK
CCCHHHCHHHHHHHH		34.8326437602
2076PhosphorylationSHFQHSRSQGERLLS
HHHCCCCHHHHHHHH		45.6224247654
2083PhosphorylationSQGERLLSREAPEEL
HHHHHHHHCCCCHHH		32.4428355574
2091UbiquitinationREAPEELKQQPLALG
CCCCHHHHCCCCCHH		50.6021906983
2099PhosphorylationQQPLALGYFVSTAKA
CCCCCHHHHHCHHCH		11.1423186163
2102PhosphorylationLALGYFVSTAKAENL
CCHHHHHCHHCHHCC		16.8529214152
2103PhosphorylationALGYFVSTAKAENLP
CHHHHHCHHCHHCCC		27.2029214152
2160UbiquitinationVPHPLDSKTTSDVLR
CCCCCCCCCHHHHHH		56.3321906983
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
-KUbiquitinationE3 ubiquitin ligaseFBXW7Q969H0
PMID:23322298
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MD13L_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 MD13L_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MED10_HUMANMED10physical
26344197
MED16_HUMANMED16physical
26344197
MED27_HUMANMED27physical
26344197
MED6_HUMANMED6physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
608808Transposition of the great arteries dextro-looped 1 (DTGA1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MD13L_HUMAN

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Related Literatures of Post-Translational Modification
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-553; SER-560; SER-817AND THR-867, AND MASS SPECTROMETRY.
"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-394; SER-397; THR-398;SER-547; SER-550; SER-553; THR-558; SER-560; SER-575; SER-762;SER-817; SER-826; SER-870; SER-923; TYR-1074; SER-1076; SER-1152 ANDSER-2083, 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-521; SER-817; SER-826;SER-923 AND SER-2083, AND MASS SPECTROMETRY.
"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-1643, AND MASSSPECTROMETRY.

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