MED24_HUMAN - dbPTM
MED24_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MED24_HUMAN
UniProt AC O75448
Protein Name Mediator of RNA polymerase II transcription subunit 24
Gene Name MED24
Organism Homo sapiens (Human).
Sequence Length 989
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..
Protein Sequence MKVVNLKQAILQAWKERWSDYQWAINMKKFFPKGATWDILNLADALLEQAMIGPSPNPLILSYLKYAISSQMVSYSSVLTAISKFDDFSRDLCVQALLDIMDMFCDRLSCHGKAEECIGLCRALLSALHWLLRCTAASAERLREGLEAGTPAAGEKQLAMCLQRLEKTLSSTKNRALLHIAKLEEASSWTAIEHSLLKLGEILANLSNPQLRSQAEQCGTLIRSIPTMLSVHAEQMHKTGFPTVHAVILLEGTMNLTGETQSLVEQLTMVKRMQHIPTPLFVLEIWKACFVGLIESPEGTEELKWTAFTFLKIPQVLVKLKKYSHGDKDFTEDVNCAFEFLLKLTPLLDKADQRCNCDCTNFLLQECGKQGLLSEASVNNLMAKRKADREHAPQQKSGENANIQPNIQLILRAEPTVTNILKTMDADHSKSPEGLLGVLGHMLSGKSLDLLLAAAAATGKLKSFARKFINLNEFTTYGSEESTKPASVRALLFDISFLMLCHVAQTYGSEVILSESRTGAEVPFFETWMQTCMPEEGKILNPDHPCFRPDSTKVESLVALLNNSSEMKLVQMKWHEACLSISAAILEILNAWENGVLAFESIQKITDNIKGKVCSLAVCAVAWLVAHVRMLGLDEREKSLQMIRQLAGPLFSENTLQFYNERVVIMNSILERMCADVLQQTATQIKFPSTGVDTMPYWNLLPPKRPIKEVLTDIFAKVLEKGWVDSRSIHIFDTLLHMGGVYWFCNNLIKELLKETRKEHTLRAVELLYSIFCLDMQQVTLVLLGHILPGLLTDSSKWHSLMDPPGTALAKLAVWCALSSYSSHKGQASTRQKKRHREDIEDYISLFPLDDVQPSKLMRLLSSNEDDANILSSPTDRSMSSSLSASQLHTVNMRDPLNRVLANLFLLISSILGSRTAGPHTQFVQWFMEECVDCLEQGGRGSVLQFMPFTTVSELVKVSAMSSPKVVLAITDLSLPLGRQVAAKAIAAL
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
36PhosphorylationKFFPKGATWDILNLA
HHCCCCCHHHHHHHH		32.13-
66PhosphorylationLILSYLKYAISSQMV
HHHHHHHHHHHHCCC		13.4325907765
69PhosphorylationSYLKYAISSQMVSYS
HHHHHHHHHCCCCHH		13.3225907765
70PhosphorylationYLKYAISSQMVSYSS
HHHHHHHHCCCCHHH		19.0425907765
74PhosphorylationAISSQMVSYSSVLTA
HHHHCCCCHHHHHHH		17.6025907765
75PhosphorylationISSQMVSYSSVLTAI
HHHCCCCHHHHHHHH		8.1120068231
76PhosphorylationSSQMVSYSSVLTAIS
HHCCCCHHHHHHHHH		13.3820860994
77PhosphorylationSQMVSYSSVLTAISK
HCCCCHHHHHHHHHC		16.9525907765
80PhosphorylationVSYSSVLTAISKFDD
CCHHHHHHHHHCCCC		21.5725907765
83PhosphorylationSSVLTAISKFDDFSR
HHHHHHHHCCCCCCH		25.4720860994
126PhosphorylationGLCRALLSALHWLLR
HHHHHHHHHHHHHHH		29.6326852163
156UbiquitinationGTPAAGEKQLAMCLQ
CCCCCCHHHHHHHHH		50.09-
167UbiquitinationMCLQRLEKTLSSTKN
HHHHHHHHHHHCHHH		60.40-
171PhosphorylationRLEKTLSSTKNRALL
HHHHHHHCHHHHHHH		46.6520068231
172PhosphorylationLEKTLSSTKNRALLH
HHHHHHCHHHHHHHH		29.0320068231
195PhosphorylationSWTAIEHSLLKLGEI
CCHHHHHHHHHHHHH		23.7024719451
207PhosphorylationGEILANLSNPQLRSQ
HHHHHHCCCHHHHHH		46.3927174698
213PhosphorylationLSNPQLRSQAEQCGT
CCCHHHHHHHHHHCH		42.1927174698
220PhosphorylationSQAEQCGTLIRSIPT
HHHHHHCHHHHHHHH		27.0027174698
239PhosphorylationHAEQMHKTGFPTVHA
CHHHHHHHCCCCEEE		29.4024043423
243PhosphorylationMHKTGFPTVHAVILL
HHHHCCCCEEEEEEE		23.7424043423
253PhosphorylationAVILLEGTMNLTGET
EEEEEECCCCCCCCH		8.1024043423
257PhosphorylationLEGTMNLTGETQSLV
EECCCCCCCCHHHHH		28.1524043423
260PhosphorylationTMNLTGETQSLVEQL
CCCCCCCHHHHHHHH		25.4624043423
262PhosphorylationNLTGETQSLVEQLTM
CCCCCHHHHHHHHHH		41.6324043423
268PhosphorylationQSLVEQLTMVKRMQH
HHHHHHHHHHHHHCC		21.4424043423
350UbiquitinationKLTPLLDKADQRCNC
HHHHHCCHHHHHCCC		54.56-
360PhosphorylationQRCNCDCTNFLLQEC
HHCCCCCHHHHHHHH		18.76-
374PhosphorylationCGKQGLLSEASVNNL
HHHCCCCCHHHHHHH		35.8425219547
377PhosphorylationQGLLSEASVNNLMAK
CCCCCHHHHHHHHHH		22.7125219547
384UbiquitinationSVNNLMAKRKADREH
HHHHHHHHHHHHHCC		40.23-
397PhosphorylationEHAPQQKSGENANIQ
CCCCCCCCCCCCCCC		47.1820068231
422UbiquitinationPTVTNILKTMDADHS
CCHHHHHHHCCCCCC		37.70-
423PhosphorylationTVTNILKTMDADHSK
CHHHHHHHCCCCCCC		19.48-
429PhosphorylationKTMDADHSKSPEGLL
HHCCCCCCCCHHHHH		35.06-
444PhosphorylationGVLGHMLSGKSLDLL
HHHHHHHCCCCHHHH		36.28-
447PhosphorylationGHMLSGKSLDLLLAA
HHHHCCCCHHHHHHH		30.5525219547
460UbiquitinationAAAAATGKLKSFARK
HHHHHHCCHHHHHHH		48.6821890473
462UbiquitinationAAATGKLKSFARKFI
HHHHCCHHHHHHHHC		47.19-
484UbiquitinationYGSEESTKPASVRAL
CCCCCCCCCHHHHHH		48.1121890473
551PhosphorylationHPCFRPDSTKVESLV
CCCCCCCCCHHHHHH		32.5828270605
552PhosphorylationPCFRPDSTKVESLVA
CCCCCCCCHHHHHHH		46.6328270605
556PhosphorylationPDSTKVESLVALLNN
CCCCHHHHHHHHHCC		31.0028270605
564PhosphorylationLVALLNNSSEMKLVQ
HHHHHCCCCCCEEEH		26.9728270605
565PhosphorylationVALLNNSSEMKLVQM
HHHHCCCCCCEEEHH		43.7828270605
6102-HydroxyisobutyrylationQKITDNIKGKVCSLA
HHHHHCCCCHHHHHH		59.96-
638UbiquitinationLGLDEREKSLQMIRQ
CCCCHHHHHHHHHHH		63.79-
652PhosphorylationQLAGPLFSENTLQFY
HHHCCCCCCCHHHHH		37.30-
655PhosphorylationGPLFSENTLQFYNER
CCCCCCCHHHHHHHH		20.20-
704UbiquitinationYWNLLPPKRPIKEVL
CHHCCCCCCCHHHHH		69.7121890473
708UbiquitinationLPPKRPIKEVLTDIF
CCCCCCHHHHHHHHH		44.4421890473
717UbiquitinationVLTDIFAKVLEKGWV
HHHHHHHHHHHCCCC		36.2821890473
717UbiquitinationVLTDIFAKVLEKGWV
HHHHHHHHHHHCCCC		36.2821890473
721UbiquitinationIFAKVLEKGWVDSRS
HHHHHHHCCCCCCCC		54.6421890473
721UbiquitinationIFAKVLEKGWVDSRS
HHHHHHHCCCCCCCC		54.6421890473
800PhosphorylationTDSSKWHSLMDPPGT
CCHHHHHHHCCCCCH		25.0326270265
807PhosphorylationSLMDPPGTALAKLAV
HHCCCCCHHHHHHHH		25.0326270265
856UbiquitinationLDDVQPSKLMRLLSS
CCCCCHHHHHHHHHC		53.652190698
862PhosphorylationSKLMRLLSSNEDDAN
HHHHHHHHCCCCCCC		35.3929255136
863PhosphorylationKLMRLLSSNEDDANI
HHHHHHHCCCCCCCC		44.1829255136
872PhosphorylationEDDANILSSPTDRSM
CCCCCCCCCCCCCHH		30.4029255136
873PhosphorylationDDANILSSPTDRSMS
CCCCCCCCCCCCHHC		28.5119664994
875PhosphorylationANILSSPTDRSMSSS
CCCCCCCCCCHHCCC		46.0929255136
880PhosphorylationSPTDRSMSSSLSASQ
CCCCCHHCCCCCHHH		20.3030108239
881PhosphorylationPTDRSMSSSLSASQL
CCCCHHCCCCCHHHC		27.0230108239
882PhosphorylationTDRSMSSSLSASQLH
CCCHHCCCCCHHHCC		21.0230108239
884PhosphorylationRSMSSSLSASQLHTV
CHHCCCCCHHHCCCC		28.0230108239
886PhosphorylationMSSSLSASQLHTVNM
HCCCCCHHHCCCCCC		29.8730108239
959PhosphorylationVSELVKVSAMSSPKV
HHHHHHHHCCCCCCE		16.7320068231
965UbiquitinationVSAMSSPKVVLAITD
HHCCCCCCEEEEEEC		47.09-
971PhosphorylationPKVVLAITDLSLPLG
CCEEEEEECCCCCCH		25.86-
984UbiquitinationLGRQVAAKAIAAL--
CHHHHHHHHHHHC--		30.50-
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 MED24_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MED24_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 MED24_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PPARA_HUMANPPARAphysical
9653119
PPARG_HUMANPPARGphysical
9653119
RXRA_HUMANRXRAphysical
9653119
THA_HUMANTHRAphysical
11117530
A4_HUMANAPPphysical
21832049
MED29_HUMANMED29physical
22939629
MED8_HUMANMED8physical
22939629
MED4_HUMANMED4physical
22939629
PP6R1_HUMANPPP6R1physical
22939629
TFP11_HUMANTFIP11physical
22939629
MED1_HUMANMED1physical
26344197
MED11_HUMANMED11physical
26344197
MED13_HUMANMED13physical
26344197
MED17_HUMANMED17physical
26344197
MED19_HUMANMED19physical
26344197
MED25_HUMANMED25physical
26344197
MED27_HUMANMED27physical
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 MED24_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-862 AND SER-873, ANDMASS 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-862 AND SER-873, 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-862 AND SER-873, ANDMASS 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-862 AND SER-873, ANDMASS 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-862 AND SER-873, ANDMASS 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-862 AND SER-873, 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-862, AND MASSSPECTROMETRY.

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