MED15_HUMAN - dbPTM
MED15_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MED15_HUMAN
UniProt AC Q96RN5
Protein Name Mediator of RNA polymerase II transcription subunit 15
Gene Name MED15
Organism Homo sapiens (Human).
Sequence Length 788
Subcellular Localization Cytoplasm. 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. Required for cholesterol-dependent gene regulation. Positively regulates the Nodal signaling pathway..
Protein Sequence MDVSGQETDWRSTAFRQKLVSQIEDAMRKAGVAHSKSSKDMESHVFLKAKTRDEYLSLVARLIIHFRDIHNKKSQASVSDPMNALQSLTGGPAAGAAGIGMPPRGPGQSLGGMGSLGAMGQPMSLSGQPPPGTSGMAPHSMAVVSTATPQTQLQLQQVALQQQQQQQQFQQQQQAALQQQQQQQQQQQFQAQQSAMQQQFQAVVQQQQQLQQQQQQQQHLIKLHHQNQQQIQQQQQQLQRIAQLQLQQQQQQQQQQQQQQQQALQAQPPIQQPPMQQPQPPPSQALPQQLQQMHHTQHHQPPPQPQQPPVAQNQPSQLPPQSQTQPLVSQAQALPGQMLYTQPPLKFVRAPMVVQQPPVQPQVQQQQTAVQTAQAAQMVAPGVQMITEALAQGGMHIRARFPPTTAVSAIPSSSIPLGRQPMAQVSQSSLPMLSSPSPGQQVQTPQSMPPPPQPSPQPGQPSSQPNSNVSSGPAPSPSSFLPSPSPQPSQSPVTARTPQNFSVPSPGPLNTPVNPSSVMSPAGSSQAEEQQYLDKLKQLSKYIEPLRRMINKIDKNEDRKKDLSKMKSLLDILTDPSKRCPLKTLQKCEIALEKLKNDMAVPTPPPPPVPPTKQQYLCQPLLDAVLANIRSPVFNHSLYRTFVPAMTAIHGPPITAPVVCTRKRRLEDDERQSIPSVLQGEVARLDPKFLVNLDPSHCSNNGTVHLICKLDDKDLPSVPPLELSVPADYPAQSPLWIDRQWQYDANPFLQSVHRCMTSRLLQLPDKHSVTALLNTWAQSVHQACLSAA
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
1Acetylation-------MDVSGQET
-------CCCCCCCC		11.79-
4O-linked_Glycosylation----MDVSGQETDWR
----CCCCCCCCCHH		30.4130379171
18UbiquitinationRSTAFRQKLVSQIED
HHHHHHHHHHHHHHH		46.75-
21PhosphorylationAFRQKLVSQIEDAMR
HHHHHHHHHHHHHHH		35.5630622161
35PhosphorylationRKAGVAHSKSSKDME
HHHCCCCCCCCCCHH		25.21-
324O-linked_GlycosylationQLPPQSQTQPLVSQA
CCCCCCCCCCCHHHH		37.08OGP
349Asymmetric dimethylarginineQPPLKFVRAPMVVQQ
CCCCCEEECCEEECC		35.79-
349MethylationQPPLKFVRAPMVVQQ
CCCCCEEECCEEECC		35.79-
405O-linked_GlycosylationRARFPPTTAVSAIPS
EEECCCCCCEEECCC		30.7330379171
489PhosphorylationPSPSPQPSQSPVTAR
CCCCCCCCCCCCCCC		37.7326074081
491PhosphorylationPSPQPSQSPVTARTP
CCCCCCCCCCCCCCC		26.1926074081
497PhosphorylationQSPVTARTPQNFSVP
CCCCCCCCCCCCCCC		27.1123403867
502PhosphorylationARTPQNFSVPSPGPL
CCCCCCCCCCCCCCC		40.4428450419
505PhosphorylationPQNFSVPSPGPLNTP
CCCCCCCCCCCCCCC		40.0928348404
511PhosphorylationPSPGPLNTPVNPSSV
CCCCCCCCCCCHHHC		35.9828450419
516PhosphorylationLNTPVNPSSVMSPAG
CCCCCCHHHCCCCCC		30.2928450419
517PhosphorylationNTPVNPSSVMSPAGS
CCCCCHHHCCCCCCC		24.0928450419
520PhosphorylationVNPSSVMSPAGSSQA
CCHHHCCCCCCCCHH		14.9422199227
524PhosphorylationSVMSPAGSSQAEEQQ
HCCCCCCCCHHHHHH		22.7622199227
525PhosphorylationVMSPAGSSQAEEQQY
CCCCCCCCHHHHHHH		32.2722199227
532PhosphorylationSQAEEQQYLDKLKQL
CHHHHHHHHHHHHHH		19.3022199227
535AcetylationEEQQYLDKLKQLSKY
HHHHHHHHHHHHHHH		55.8026051181
535UbiquitinationEEQQYLDKLKQLSKY
HHHHHHHHHHHHHHH		55.80-
542PhosphorylationKLKQLSKYIEPLRRM
HHHHHHHHHHHHHHH		13.7223403867
567UbiquitinationKKDLSKMKSLLDILT
HHHHHHHHHHHHHHH		41.51-
568PhosphorylationKDLSKMKSLLDILTD
HHHHHHHHHHHHHHC		30.5729083192
574PhosphorylationKSLLDILTDPSKRCP
HHHHHHHHCHHHCCC		46.3129083192
577PhosphorylationLDILTDPSKRCPLKT
HHHHHCHHHCCCCHH		35.2329083192
578AcetylationDILTDPSKRCPLKTL
HHHHCHHHCCCCHHH		64.5126051181
578UbiquitinationDILTDPSKRCPLKTL
HHHHCHHHCCCCHHH		64.5121139048
583UbiquitinationPSKRCPLKTLQKCEI
HHHCCCCHHHHHHHH		32.12-
583AcetylationPSKRCPLKTLQKCEI
HHHCCCCHHHHHHHH		32.1225953088
584O-linked_GlycosylationSKRCPLKTLQKCEIA
HHCCCCHHHHHHHHH		41.9530379171
587AcetylationCPLKTLQKCEIALEK
CCCHHHHHHHHHHHH		36.6326051181
603PhosphorylationKNDMAVPTPPPPPVP
CCCCCCCCCCCCCCC		41.6629255136
612PhosphorylationPPPPVPPTKQQYLCQ
CCCCCCCCCCHHHHH		35.1025867546
616PhosphorylationVPPTKQQYLCQPLLD
CCCCCCHHHHHHHHH		13.6226074081
631PhosphorylationAVLANIRSPVFNHSL
HHHHHCCCCCCCHHH		22.9422199227
637PhosphorylationRSPVFNHSLYRTFVP
CCCCCCHHHHHHHHC		28.3528857561
639PhosphorylationPVFNHSLYRTFVPAM
CCCCHHHHHHHHCHH		15.6024719451
655PhosphorylationAIHGPPITAPVVCTR
HCCCCCCCCCEEECC		30.5924719451
661PhosphorylationITAPVVCTRKRRLED
CCCCEEECCCCCCCC		27.8424719451
673PhosphorylationLEDDERQSIPSVLQG
CCCHHHCCHHHHHHH		42.5628555341
676PhosphorylationDERQSIPSVLQGEVA
HHHCCHHHHHHHHHH		33.51-
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 ligaseTRIM11Q96F44
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MED15_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 MED15_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRI11_HUMANTRIM11physical
16904669
MED12_HUMANMED12physical
14657022
MED13_HUMANMED13physical
14657022
MED1_HUMANMED1physical
14657022
MED14_HUMANMED14physical
14657022
MED23_HUMANMED23physical
14657022
MED25_HUMANMED25physical
14657022
MED16_HUMANMED16physical
14657022
MED17_HUMANMED17physical
14657022
MED26_HUMANMED26physical
14657022
CDK8_HUMANCDK8physical
14657022
MED6_HUMANMED6physical
14657022
MED7_HUMANMED7physical
14657022
SRBP1_HUMANSREBF1physical
16799563
UBP2L_HUMANUBAP2Lphysical
22939629
SC24C_HUMANSEC24Cphysical
22939629
NCOA6_HUMANNCOA6physical
22939629
MED1_HUMANMED1physical
26344197
MED10_HUMANMED10physical
26344197
MED11_HUMANMED11physical
26344197
MED14_HUMANMED14physical
26344197
MED16_HUMANMED16physical
26344197
MED17_HUMANMED17physical
26344197
MED24_HUMANMED24physical
26344197
MED27_HUMANMED27physical
26344197
MED4_HUMANMED4physical
26344197
MED8_HUMANMED8physical
26344197
P73_HUMANTP73physical
25893286
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 MED15_HUMAN

loading...

Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-603, AND MASS SPECTROMETRY.
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 THR-603, AND MASSSPECTROMETRY.
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT THR-603, AND MASS 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 THR-603, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory