MED29_HUMAN - dbPTM
MED29_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MED29_HUMAN
UniProt AC Q9NX70
Protein Name Mediator of RNA polymerase II transcription subunit 29
Gene Name MED29
Organism Homo sapiens (Human).
Sequence Length 200
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 MAASQQQASAASSAAGVSGPSSAGGPGPQQQPQPPAQLVGPAQSGLLQQQQQDFDPVQRYKMLIPQLKESLQTLMKVAAQNLIQNTNIDNGQKSSDGPIQRFDKCLEEFYALCDQLELCLRLAHECLSQSCDSAKHSPTLVPTATKPDAVQPDSLPYPQYLAVIKAQISCAKDIHTALLDCANKVTGKTPAPPAGPGGTL
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
2Acetylation------MAASQQQAS
------CCHHHHHHH
18.8019413330
60PhosphorylationDFDPVQRYKMLIPQL
CCCHHHHHHHHHHHH
5.44-
61UbiquitinationFDPVQRYKMLIPQLK
CCHHHHHHHHHHHHH
29.4421890473
61UbiquitinationFDPVQRYKMLIPQLK
CCHHHHHHHHHHHHH
29.4421890473
70PhosphorylationLIPQLKESLQTLMKV
HHHHHHHHHHHHHHH
24.96-
76UbiquitinationESLQTLMKVAAQNLI
HHHHHHHHHHHHHHH
31.6621890473
76UbiquitinationESLQTLMKVAAQNLI
HHHHHHHHHHHHHHH
31.6621890473
82UbiquitinationMKVAAQNLIQNTNID
HHHHHHHHHHCCCCC
2.5721890473
93UbiquitinationTNIDNGQKSSDGPIQ
CCCCCCCCCCCCCHH
54.012190698
97UbiquitinationNGQKSSDGPIQRFDK
CCCCCCCCCHHHHHH
24.1321890473
110PhosphorylationDKCLEEFYALCDQLE
HHHHHHHHHHHHHHH
11.27-
114UbiquitinationEEFYALCDQLELCLR
HHHHHHHHHHHHHHH
57.8821890473
128PhosphorylationRLAHECLSQSCDSAK
HHHHHHHHHHCHHCC
31.5426074081
130PhosphorylationAHECLSQSCDSAKHS
HHHHHHHHCHHCCCC
19.2626074081
133PhosphorylationCLSQSCDSAKHSPTL
HHHHHCHHCCCCCCC
43.4726074081
137PhosphorylationSCDSAKHSPTLVPTA
HCHHCCCCCCCCCCC
20.9030576142
139PhosphorylationDSAKHSPTLVPTATK
HHCCCCCCCCCCCCC
43.3230576142
143PhosphorylationHSPTLVPTATKPDAV
CCCCCCCCCCCCCCC
39.2126074081
145PhosphorylationPTLVPTATKPDAVQP
CCCCCCCCCCCCCCC
45.6630576142
154PhosphorylationPDAVQPDSLPYPQYL
CCCCCCCCCCCHHHH
37.6227080861
157PhosphorylationVQPDSLPYPQYLAVI
CCCCCCCCHHHHHHH
14.3026074081
158PhosphorylationQPDSLPYPQYLAVIK
CCCCCCCHHHHHHHH
17.88-
160PhosphorylationDSLPYPQYLAVIKAQ
CCCCCHHHHHHHHHH
7.6626074081
167UbiquitinationYLAVIKAQISCAKDI
HHHHHHHHHHHHHHH
24.11-
176PhosphorylationSCAKDIHTALLDCAN
HHHHHHHHHHHHHHH
21.23-
184UbiquitinationALLDCANKVTGKTPA
HHHHHHHHHCCCCCC
23.73-
184MalonylationALLDCANKVTGKTPA
HHHHHHHHHCCCCCC
23.7332601280
184AcetylationALLDCANKVTGKTPA
HHHHHHHHHCCCCCC
23.7326051181
186PhosphorylationLDCANKVTGKTPAPP
HHHHHHHCCCCCCCC
34.27-
188UbiquitinationCANKVTGKTPAPPAG
HHHHHCCCCCCCCCC
41.80-
193UbiquitinationTGKTPAPPAGPGGTL
CCCCCCCCCCCCCCC
52.54-
199PhosphorylationPPAGPGGTL------
CCCCCCCCC------
34.9025159151
205UbiquitinationGTL------------
CCC------------
-
209Ubiquitination----------------
----------------
-
220Phosphorylation---------------------------
---------------------------
-

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 MED29_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MED29_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 MED29_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
MED26_HUMANMED26physical
15175163
CCNC_HUMANCCNCphysical
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
MED29_HUMANMED29physical
14638676
MED1_HUMANMED1physical
14638676
MED17_HUMANMED17physical
14638676
MED19_HUMANMED19physical
14638676
MED4_HUMANMED4physical
14638676
MED8_HUMANMED8physical
14638676
MED18_HUMANMED18physical
14638676
MED11_HUMANMED11physical
14638676
MED17_HUMANMED17physical
14576168
MED6_HUMANMED6physical
14576168
MED8_HUMANMED8physical
14576168
MED20_HUMANMED20physical
14576168
MED29_HUMANMED29physical
14576168
MED31_HUMANMED31physical
14576168
MED18_HUMANMED18physical
14576168
MED11_HUMANMED11physical
14576168
MED13_HUMANMED13physical
15989967
MED12_HUMANMED12physical
15989967
MED1_HUMANMED1physical
15989967
MED17_HUMANMED17physical
15989967
MED20_HUMANMED20physical
15989967
MED21_HUMANMED21physical
15989967
MED4_HUMANMED4physical
22939629
MED8_HUMANMED8physical
22939629
MED6_HUMANMED6physical
22939629
RABL6_HUMANRABL6physical
22939629
MED1_HUMANMED1physical
26344197
MED10_HUMANMED10physical
26344197
MED11_HUMANMED11physical
26344197
MED14_HUMANMED14physical
26344197
MED15_HUMANMED15physical
26344197
MED16_HUMANMED16physical
26344197
MED17_HUMANMED17physical
26344197
MED18_HUMANMED18physical
26344197
MED19_HUMANMED19physical
26344197
MED20_HUMANMED20physical
26344197
MED24_HUMANMED24physical
26344197
MED27_HUMANMED27physical
26344197
MED4_HUMANMED4physical
26344197
MED6_HUMANMED6physical
26344197
MED8_HUMANMED8physical
26344197
MED9_HUMANMED9physical
14638676

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 MED29_HUMAN

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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 ALA-2, AND MASS SPECTROMETRY.

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