MED30_HUMAN - dbPTM
MED30_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MED30_HUMAN
UniProt AC Q96HR3
Protein Name Mediator of RNA polymerase II transcription subunit 30
Gene Name MED30
Organism Homo sapiens (Human).
Sequence Length 178
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 MSTPPLAASGMAPGPFAGPQAQQAAREVNTASLCRIGQETVQDIVYRTMEIFQLLRNMQLPNGVTYHTGTYQDRLTKLQDNLRQLSVLFRKLRLVYDKCNENCGGMDPIPVEQLIPYVEEDGSKNDDRAGPPRFASEERREIAEVNKKLKQKNQQLKQIMDQLRNLIWDINAMLAMRN
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------MSTPPLAAS
------CCCCCCCCC		50.0123401153
2Acetylation------MSTPPLAAS
------CCCCCCCCC		50.0118691976
3Phosphorylation-----MSTPPLAASG
-----CCCCCCCCCC		27.8519413330
9PhosphorylationSTPPLAASGMAPGPF
CCCCCCCCCCCCCCC		24.4028464451
46PhosphorylationETVQDIVYRTMEIFQ
HHHHHHHHHHHHHHH		10.7423917254
65PhosphorylationMQLPNGVTYHTGTYQ
CCCCCCCEECCCCHH		15.8128796482
66PhosphorylationQLPNGVTYHTGTYQD
CCCCCCEECCCCHHH		8.5828796482
68PhosphorylationPNGVTYHTGTYQDRL
CCCCEECCCCHHHHH		22.3228796482
70PhosphorylationGVTYHTGTYQDRLTK
CCEECCCCHHHHHHH		21.1128796482
71PhosphorylationVTYHTGTYQDRLTKL
CEECCCCHHHHHHHH		15.1228796482
77UbiquitinationTYQDRLTKLQDNLRQ
CHHHHHHHHHHHHHH		49.0633845483
77UbiquitinationTYQDRLTKLQDNLRQ
CHHHHHHHHHHHHHH		49.06-
77AcetylationTYQDRLTKLQDNLRQ
CHHHHHHHHHHHHHH		49.0625953088
98AcetylationKLRLVYDKCNENCGG
HHHHHHHHHCCCCCC		22.6726051181
117UbiquitinationPVEQLIPYVEEDGSK
CHHHHHHHHCCCCCC		17.3122817900
122UbiquitinationIPYVEEDGSKNDDRA
HHHHCCCCCCCCCCC		43.7421890473
122UbiquitinationIPYVEEDGSKNDDRA
HHHHCCCCCCCCCCC		43.7421890473
147AcetylationREIAEVNKKLKQKNQ
HHHHHHHHHHHHHHH		65.7425953088
147UbiquitinationREIAEVNKKLKQKNQ
HHHHHHHHHHHHHHH		65.74-
148UbiquitinationEIAEVNKKLKQKNQQ
HHHHHHHHHHHHHHH		56.57-
152UbiquitinationVNKKLKQKNQQLKQI
HHHHHHHHHHHHHHH		55.9522817900
152AcetylationVNKKLKQKNQQLKQI
HHHHHHHHHHHHHHH		55.9566726575
157SumoylationKQKNQQLKQIMDQLR
HHHHHHHHHHHHHHH		33.18-
157UbiquitinationKQKNQQLKQIMDQLR
HHHHHHHHHHHHHHH		33.1821890473
157AcetylationKQKNQQLKQIMDQLR
HHHHHHHHHHHHHHH		33.1866726581
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 MED30_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MED30_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 MED30_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MED27_HUMANMED27physical
12584197
MED6_HUMANMED6physical
12584197
MED8_HUMANMED8physical
12584197
MED21_HUMANMED21physical
12584197
MED4_HUMANMED4physical
12584197
MED22_HUMANMED22physical
12584197
MED13_HUMANMED13physical
15989967
MED12_HUMANMED12physical
15989967
RPB1_HUMANPOLR2Aphysical
15989967
MED1_HUMANMED1physical
15989967
MED24_HUMANMED24physical
15989967
MED16_HUMANMED16physical
15989967
MED17_HUMANMED17physical
15989967
MED6_HUMANMED6physical
15989967
MED20_HUMANMED20physical
15989967
MED21_HUMANMED21physical
15989967
RPAB2_HUMANPOLR2Fphysical
15989967
MED12_HUMANMED12physical
18691967
EHMT2_HUMANEHMT2physical
18691967
MED1_HUMANMED1physical
18691967
MED23_HUMANMED23physical
18691967
CDK8_HUMANCDK8physical
18691967
MED6_HUMANMED6physical
18691967
MED30_HUMANMED30physical
18691967
A4_HUMANAPPphysical
21832049
KR109_HUMANKRTAP10-9physical
25416956
MED11_HUMANMED11physical
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 MED30_HUMAN

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Related Literatures of Post-Translational Modification
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 SER-2 AND THR-3, 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3, AND MASSSPECTROMETRY.
"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 THR-3, AND MASSSPECTROMETRY.

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