MED26_HUMAN - dbPTM
MED26_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MED26_HUMAN
UniProt AC O95402
Protein Name Mediator of RNA polymerase II transcription subunit 26
Gene Name MED26
Organism Homo sapiens (Human).
Sequence Length 600
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 pre-initiation complex with RNA polymerase II and the general transcription factors..
Protein Sequence MTAAPASPQQIRDRLLQAIDPQSNIRNMVAVLEVISSLEKYPITKEALEETRLGKLINDVRKKTKNEELAKRAKKLLRSWQKLIEPAHQHEAALRGLAGATGSANGGAHNCRPEVGAAGPPRSIHDLKSRNDLQRLPGQRLDRLGSRKRRGDQRDLGHPGPPPKVSKASHDPLVPNSSPLPTNGISGSPESFASSLDGSGHAGPEGSRLERDENDKHSGKIPVNAVRPHTSSPGLGKPPGPCLQPKASVLQQLDRVDETPGPPHPKGPPRCSFSPRNSRHEGSFARQQSLYAPKGSVPSPSPRPQALDATQVPSPLPLAQPSTPPVRRLELLPSAESPVCWLEQPESHQRLAGPGCKAGLSPAEPLLSRAGFSPDSSKADSDAASSGGSDSKKKKRYRPRDYTVNLDGQVAEAGVKPVRLKERKLTFDPMTRQIKPLTQKEPVRADSPVHMEQQSRTELDKQEAKASLQSPFEQTNWKELSRNEIIQSYLSRQSSLLSSSGAQTPGAHHFMSEYLKQEESTRQGARQLHVLVPQSPPTDLPGLTREVTQDDLDRIQASQWPGVNGCQDTQGNWYDWTQCISLDPHGDDGRLNILPYVCLD
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------MTAAPASPQ
------CCCCCCCHH
31.3723186163
7Phosphorylation-MTAAPASPQQIRDR
-CCCCCCCHHHHHHH
23.3723401153
40UbiquitinationEVISSLEKYPITKEA
HHHHHHHHCCCCHHH
62.71-
55UbiquitinationLEETRLGKLINDVRK
HHHHHHHHHHHHHHH
51.2729967540
71AcetylationTKNEELAKRAKKLLR
HCCHHHHHHHHHHHH
66.5620167786
169PhosphorylationPPKVSKASHDPLVPN
CCCCCCCCCCCCCCC
31.9623186163
177PhosphorylationHDPLVPNSSPLPTNG
CCCCCCCCCCCCCCC
27.5423401153
178PhosphorylationDPLVPNSSPLPTNGI
CCCCCCCCCCCCCCC
36.7825850435
182PhosphorylationPNSSPLPTNGISGSP
CCCCCCCCCCCCCCH
54.4823186163
186PhosphorylationPLPTNGISGSPESFA
CCCCCCCCCCHHHHH
34.3223186163
188PhosphorylationPTNGISGSPESFASS
CCCCCCCCHHHHHHH
20.7825850435
191PhosphorylationGISGSPESFASSLDG
CCCCCHHHHHHHCCC
29.5128464451
194PhosphorylationGSPESFASSLDGSGH
CCHHHHHHHCCCCCC
29.4423186163
195PhosphorylationSPESFASSLDGSGHA
CHHHHHHHCCCCCCC
27.3523186163
230PhosphorylationVNAVRPHTSSPGLGK
CCEECCCCCCCCCCC
33.3228152594
231PhosphorylationNAVRPHTSSPGLGKP
CEECCCCCCCCCCCC
31.3428152594
232PhosphorylationAVRPHTSSPGLGKPP
EECCCCCCCCCCCCC
24.9225159151
259PhosphorylationQLDRVDETPGPPHPK
HHHCCCCCCCCCCCC
29.1428555341
272PhosphorylationPKGPPRCSFSPRNSR
CCCCCCCCCCCCCCC
30.0021712546
274PhosphorylationGPPRCSFSPRNSRHE
CCCCCCCCCCCCCCC
13.4730576142
289PhosphorylationGSFARQQSLYAPKGS
CCCCCCCCCCCCCCC
18.2723312004
291PhosphorylationFARQQSLYAPKGSVP
CCCCCCCCCCCCCCC
26.5527080861
296PhosphorylationSLYAPKGSVPSPSPR
CCCCCCCCCCCCCCC
36.6623927012
299PhosphorylationAPKGSVPSPSPRPQA
CCCCCCCCCCCCCCC
35.5423927012
301PhosphorylationKGSVPSPSPRPQALD
CCCCCCCCCCCCCCC
37.5730266825
310PhosphorylationRPQALDATQVPSPLP
CCCCCCCCCCCCCCC
29.7530266825
314PhosphorylationLDATQVPSPLPLAQP
CCCCCCCCCCCCCCC
39.9730266825
322PhosphorylationPLPLAQPSTPPVRRL
CCCCCCCCCCCEEEE
41.2730266825
323PhosphorylationLPLAQPSTPPVRRLE
CCCCCCCCCCEEEEE
37.9930266825
334PhosphorylationRRLELLPSAESPVCW
EEEEECCCCCCCEEE
44.6428450419
337PhosphorylationELLPSAESPVCWLEQ
EECCCCCCCEEECCC
23.5025159151
361PhosphorylationPGCKAGLSPAEPLLS
CCCCCCCCCCHHHHH
22.5825159151
368PhosphorylationSPAEPLLSRAGFSPD
CCCHHHHHHCCCCCC
27.9723663014
373PhosphorylationLLSRAGFSPDSSKAD
HHHHCCCCCCCHHHC
27.2129255136
376PhosphorylationRAGFSPDSSKADSDA
HCCCCCCCHHHCHHH
36.8030108239
377PhosphorylationAGFSPDSSKADSDAA
CCCCCCCHHHCHHHH
38.9625159151
381PhosphorylationPDSSKADSDAASSGG
CCCHHHCHHHHHCCC
33.7328450419
385PhosphorylationKADSDAASSGGSDSK
HHCHHHHHCCCCCCC
31.1028450419
386PhosphorylationADSDAASSGGSDSKK
HCHHHHHCCCCCCCC
42.3123403867
389PhosphorylationDAASSGGSDSKKKKR
HHHHCCCCCCCCCCC
42.0923403867
391PhosphorylationASSGGSDSKKKKRYR
HHCCCCCCCCCCCCC
48.3423403867
416AcetylationQVAEAGVKPVRLKER
HHHCCCCCCEECCCC
36.5625953088
426PhosphorylationRLKERKLTFDPMTRQ
ECCCCCCCCCCCCCC
29.0930576142
431PhosphorylationKLTFDPMTRQIKPLT
CCCCCCCCCCCCCCC
25.4727732954
438PhosphorylationTRQIKPLTQKEPVRA
CCCCCCCCCCCCCCC
46.2323403867
447PhosphorylationKEPVRADSPVHMEQQ
CCCCCCCCCCCHHHH
28.0429255136
455PhosphorylationPVHMEQQSRTELDKQ
CCCHHHHCCHHHHHH
40.6430266825
467PhosphorylationDKQEAKASLQSPFEQ
HHHHHHHHCCCHHHH
26.6628985074
470PhosphorylationEAKASLQSPFEQTNW
HHHHHCCCHHHHCCH
36.5325159151
475PhosphorylationLQSPFEQTNWKELSR
CCCHHHHCCHHHHHH
35.5326552605
481PhosphorylationQTNWKELSRNEIIQS
HCCHHHHHHHHHHHH
33.8628555341
488PhosphorylationSRNEIIQSYLSRQSS
HHHHHHHHHHHHHHH
20.0328634298
489PhosphorylationRNEIIQSYLSRQSSL
HHHHHHHHHHHHHHH
7.7228634298
491PhosphorylationEIIQSYLSRQSSLLS
HHHHHHHHHHHHHHH
21.7528555341
494PhosphorylationQSYLSRQSSLLSSSG
HHHHHHHHHHHHCCC
23.1127251275
495PhosphorylationSYLSRQSSLLSSSGA
HHHHHHHHHHHCCCC
25.6222210691
498PhosphorylationSRQSSLLSSSGAQTP
HHHHHHHHCCCCCCC
27.9628348404
499PhosphorylationRQSSLLSSSGAQTPG
HHHHHHHCCCCCCCC
32.5322210691
500PhosphorylationQSSLLSSSGAQTPGA
HHHHHHCCCCCCCCH
34.4728348404
504PhosphorylationLSSSGAQTPGAHHFM
HHCCCCCCCCHHHHH
24.1322210691
512PhosphorylationPGAHHFMSEYLKQEE
CCHHHHHHHHHHHHH
23.3428348404
535PhosphorylationLHVLVPQSPPTDLPG
EEEECCCCCCCCCCC
27.1223401153
538PhosphorylationLVPQSPPTDLPGLTR
ECCCCCCCCCCCCCE
54.2630266825
544PhosphorylationPTDLPGLTREVTQDD
CCCCCCCCEEECHHH
30.6030266825

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 MED26_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MED26_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 MED26_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MD13L_HUMANMED13Lphysical
15175163
MED13_HUMANMED13physical
15175163
MED12_HUMANMED12physical
15175163
MED1_HUMANMED1physical
15175163
MED14_HUMANMED14physical
15175163
MED23_HUMANMED23physical
15175163
MED15_HUMANMED15physical
15175163
MED24_HUMANMED24physical
15175163
MED16_HUMANMED16physical
15175163
MED25_HUMANMED25physical
15175163
MED17_HUMANMED17physical
15175163
CDK8_HUMANCDK8physical
15175163
CDK19_HUMANCDK19physical
15175163
MED27_HUMANMED27physical
15175163
MED4_HUMANMED4physical
15175163
MED19_HUMANMED19physical
15175163
MED6_HUMANMED6physical
15175163
MED7_HUMANMED7physical
15175163
MED8_HUMANMED8physical
15175163
MED18_HUMANMED18physical
15175163
MED20_HUMANMED20physical
15175163
MED9_HUMANMED9physical
15175163
MED29_HUMANMED29physical
15175163
MED30_HUMANMED30physical
15175163
MED28_HUMANMED28physical
15175163
MED21_HUMANMED21physical
15175163
MED22_HUMANMED22physical
15175163
MED11_HUMANMED11physical
15175163
MED31_HUMANMED31physical
15175163
MED10_HUMANMED10physical
15175163
RPB11_HUMANPOLR2Jphysical
15175163
RPB4_HUMANPOLR2Dphysical
15175163
RPB1_HUMANPOLR2Aphysical
15175163
RPB2_HUMANPOLR2Bphysical
15175163
RPB3_HUMANPOLR2Cphysical
15175163
RPAB1_HUMANPOLR2Ephysical
15175163
RPAB2_HUMANPOLR2Fphysical
15175163
RPB7_HUMANPOLR2Gphysical
15175163
RPAB3_HUMANPOLR2Hphysical
15175163
RPB9_HUMANPOLR2Iphysical
15175163
RPAB5_HUMANPOLR2Lphysical
15175163
CEBPB_HUMANCEBPBphysical
14759369
RPB1_HUMANPOLR2Aphysical
21729782
MED1_HUMANMED1physical
21729782
MED4_HUMANMED4physical
21729782
MED6_HUMANMED6physical
21729782
MED8_HUMANMED8physical
21729782
MED17_HUMANMED17physical
21729782
MED18_HUMANMED18physical
21729782
EAF1_HUMANEAF1physical
21729782
ELL_HUMANELLphysical
21729782
CDK9_HUMANCDK9physical
21729782
TAF1_HUMANTAF1physical
21729782
TAF4_HUMANTAF4physical
21729782
TAF6_HUMANTAF6physical
21729782
CCNT1_HUMANCCNT1physical
21729782
CCNT2_HUMANCCNT2physical
21729782
AFF4_HUMANAFF4physical
21729782
AF9_HUMANMLLT3physical
21729782
TBP_HUMANTBPphysical
21729782
MED7_HUMANMED7physical
21729782
MED9_HUMANMED9physical
21729782
MED10_HUMANMED10physical
21729782
MED11_HUMANMED11physical
21729782
MED14_HUMANMED14physical
21729782
MED15_HUMANMED15physical
21729782
MED16_HUMANMED16physical
21729782
MED19_HUMANMED19physical
21729782
MED20_HUMANMED20physical
21729782
MED21_HUMANMED21physical
21729782
MED23_HUMANMED23physical
21729782
MED25_HUMANMED25physical
21729782
MED27_HUMANMED27physical
21729782
MED28_HUMANMED28physical
21729782
MED29_HUMANMED29physical
21729782
MED30_HUMANMED30physical
21729782
MED31_HUMANMED31physical
21729782
MED12_HUMANMED12physical
21729782
MED13_HUMANMED13physical
21729782
MD13L_HUMANMED13Lphysical
21729782
CDK8_HUMANCDK8physical
21729782
CDK19_HUMANCDK19physical
21729782
CCNC_HUMANCCNCphysical
21729782
RPB2_HUMANPOLR2Bphysical
21729782
RPB3_HUMANPOLR2Cphysical
21729782
RPB4_HUMANPOLR2Dphysical
21729782
RPAB1_HUMANPOLR2Ephysical
21729782
RPAB2_HUMANPOLR2Fphysical
21729782
RPB7_HUMANPOLR2Gphysical
21729782
RPAB3_HUMANPOLR2Hphysical
21729782
RPB9_HUMANPOLR2Iphysical
21729782
RPAB5_HUMANPOLR2Lphysical
21729782
RPB11_HUMANPOLR2Jphysical
21729782
RPAB4_HUMANPOLR2Kphysical
21729782
TAF2_HUMANTAF2physical
21729782
TAF3_HUMANTAF3physical
21729782
TAF4B_HUMANTAF4Bphysical
21729782
TAF5_HUMANTAF5physical
21729782
TAF7_HUMANTAF7physical
21729782
TAF8_HUMANTAF8physical
21729782
TAF9_HUMANTAF9physical
21729782
TAF10_HUMANTAF10physical
21729782
TAF11_HUMANTAF11physical
21729782
TAF13_HUMANTAF13physical
21729782
RBP56_HUMANTAF15physical
21729782
ELL2_HUMANELL2physical
21729782
EAF2_HUMANEAF2physical
21729782
AFF1_HUMANAFF1physical
21729782
ENL_HUMANMLLT1physical
21729782
ICE1_HUMANICE1physical
21729782
ICE2_HUMANICE2physical
21729782

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 MED26_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-314 AND SER-361, 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-361, 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-337 AND SER-447, ANDMASS SPECTROMETRY.

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