MED23_HUMAN - dbPTM
MED23_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MED23_HUMAN
UniProt AC Q9ULK4
Protein Name Mediator of RNA polymerase II transcription subunit 23
Gene Name MED23
Organism Homo sapiens (Human).
Sequence Length 1368
Subcellular Localization Nucleus .
Protein Description Required for transcriptional activation subsequent to the assembly of the pre-initiation complex (By similarity). 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. Required for transcriptional activation by adenovirus E1A protein. Required for ELK1-dependent transcriptional activation in response to activated Ras signaling..
Protein Sequence METQLQSIFEEVVKTEVIEEAFPGMFMDTPEDEKTKLISCLGAFRQFWGGLSQESHEQCIQWIVKFIHGQHSPKRISFLYDCLAMAVETGLLPPRLVCESLINSDTLEWERTQLWALTFKLVRKIIGGVDYKGVRDLLKVILEKILTIPNTVSSAVVQQLLAAREVIAYILERNACLLPAYFAVTEIRKLYPEGKLPHWLLGNLVSDFVDTFRPTARINSICGRCSLLPVVNNSGAICNSWKLDPATLRFPLKGLLPYDKDLFEPQTALLRYVLEQPYSRDMVCNMLGLNKQHKQRCPVLEDQLVDLVVYAMERSETEEKFDDGGTSQLLWQHLSSQLIFFVLFQFASFPHMVLSLHQKLAGRGLIKGRDHLMWVLLQFISGSIQKNALADFLPVMKLFDLLYPEKEYIPVPDINKPQSTHAFAMTCIWIHLNRKAQNDNSKLQIPIPHSLRLHHEFLQQSLRNKSLQMNDYKIALLCNAYSTNSECFTLPMGALVETIYGNGIMRIPLPGTNCMASGSITPLPMNLLDSLTVHAKMSLIHSIATRVIKLAHAKSSVALAPALVETYSRLLVYMEIESLGIKGFISQLLPTVFKSHAWGILHTLLEMFSYRMHHIQPHYRVQLLSHLHTLAAVAQTNQNQLHLCVESTALRLITALGSSEVQPQFTRFLSDPKTVLSAESEELNRALILTLARATHVTDFFTGSDSIQGTWCKDILQTIMSFTPHNWASHTLSCFPGPLQAFFKQNNVPQESRFNLKKNVEEEYRKWKSMSNENDIITHFSMQGSPPLFLCLLWKMLLETDHINQIGYRVLERIGARALVAHVRTFADFLVYEFSTSAGGQQLNKCIEILNDMVWKYNIVTLDRLILCLAMRSHEGNEAQVCYFIIQLLLLKPNDFRNRVSDFVKENSPEHWLQNDWHTKHMNYHKKYPEKLYFEGLAEQVDPPVQIQSPYLPIYFGNVCLRFLPVFDIVIHRFLELLPVSKSLETLLDHLGGLYKFHDRPVTYLYNTLHYYEMHLRDRAFLKRKLVHAIIGSLKDNRPQGWCLSDTYLKCAMNAREENPWVPDDTYYCRLIGRLVDTMAGKSPGPFPNCDWRFNEFPNPAAHALHVTCVELMALAVSGKEVGNALLNVVLKSQPLVPRENITAWMNAIGLIITALPEPYWIVLHDRIVSVISSPSLTSETEWVGYPFRLFDFTACHQSYSEMSCSYTLALAHAVWHHSSIGQLSLIPKFLTEVLLPIVKTEFQLLYVYHLVGPFLQRFQQERTRCMIEIGVAFYDMLLNVDQCSTHLNYMDPICDFLYHMKYMFTGDSVKEQVEKIICNLKPALKLRLRFITHISKMEPAAVPPQAMNSGSPAPQSNQVPVSLPVTQ
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
3Phosphorylation-----METQLQSIFE
-----CHHHHHHHHH
46.5724043423
7Phosphorylation-METQLQSIFEEVVK
-CHHHHHHHHHHHHH
37.5324043423
242UbiquitinationGAICNSWKLDPATLR
CCCCCCCCCCCCCCC
42.72-
242AcetylationGAICNSWKLDPATLR
CCCCCCCCCCCCCCC
42.7225953088
242UbiquitinationGAICNSWKLDPATLR
CCCCCCCCCCCCCCC
42.72-
253 (in isoform 5)Ubiquitination-47.9921890473
253 (in isoform 3)Ubiquitination-47.9921890473
253UbiquitinationATLRFPLKGLLPYDK
CCCCCCCCCCCCCCC
47.9921890473
253 (in isoform 4)Ubiquitination-47.9921890473
253UbiquitinationATLRFPLKGLLPYDK
CCCCCCCCCCCCCCC
47.9921890473
253 (in isoform 2)Ubiquitination-47.9921890473
253 (in isoform 1)Ubiquitination-47.9921890473
260 (in isoform 5)Ubiquitination-50.9521890473
260UbiquitinationKGLLPYDKDLFEPQT
CCCCCCCCCCCCHHH
50.9521890473
260 (in isoform 4)Ubiquitination-50.9521890473
260 (in isoform 2)Ubiquitination-50.9521890473
260 (in isoform 3)Ubiquitination-50.9521890473
260 (in isoform 1)Ubiquitination-50.9521890473
260UbiquitinationKGLLPYDKDLFEPQT
CCCCCCCCCCCCHHH
50.9521890473
291UbiquitinationCNMLGLNKQHKQRCP
HHHHCCCHHHHCCCC
59.84-
291AcetylationCNMLGLNKQHKQRCP
HHHHCCCHHHHCCCC
59.8425953088
291UbiquitinationCNMLGLNKQHKQRCP
HHHHCCCHHHHCCCC
59.84-
294UbiquitinationLGLNKQHKQRCPVLE
HCCCHHHHCCCCCHH
36.62-
294UbiquitinationLGLNKQHKQRCPVLE
HCCCHHHHCCCCCHH
36.62-
450PhosphorylationLQIPIPHSLRLHHEF
CCCCCCHHHHHHHHH
15.1627080861
465 (in isoform 5)Ubiquitination-46.2221890473
465 (in isoform 4)Ubiquitination-46.2221890473
465UbiquitinationLQQSLRNKSLQMNDY
HHHHHHCCCCCCCHH
46.2221906983
465 (in isoform 1)Ubiquitination-46.2221890473
466PhosphorylationQQSLRNKSLQMNDYK
HHHHHCCCCCCCHHH
27.6424114839
471 (in isoform 2)Ubiquitination-40.5421890473
471 (in isoform 3)Ubiquitination-40.5421890473
512PhosphorylationMRIPLPGTNCMASGS
EEECCCCCCCCCCCC
24.25-
530PhosphorylationLPMNLLDSLTVHAKM
CCCCHHHHHHHHHHH
26.3823532336
532PhosphorylationMNLLDSLTVHAKMSL
CCHHHHHHHHHHHHH
17.7523532336
545PhosphorylationSLIHSIATRVIKLAH
HHHHHHHHHHHHHHH
24.65-
554UbiquitinationVIKLAHAKSSVALAP
HHHHHHHHHHHHHHH
33.14-
555PhosphorylationIKLAHAKSSVALAPA
HHHHHHHHHHHHHHH
30.72-
556PhosphorylationKLAHAKSSVALAPAL
HHHHHHHHHHHHHHH
15.6529759185
568PhosphorylationPALVETYSRLLVYME
HHHHHHHHHHHHHHH
24.7129759185
654PhosphorylationSTALRLITALGSSEV
HHHHHHHHHHCCCCC
22.0320068231
658PhosphorylationRLITALGSSEVQPQF
HHHHHHCCCCCCCCH
24.9520068231
659PhosphorylationLITALGSSEVQPQFT
HHHHHCCCCCCCCHH
39.7320068231
666PhosphorylationSEVQPQFTRFLSDPK
CCCCCCHHHHHCCCC
18.4420068231
673 (in isoform 1)Ubiquitination-57.1421890473
673UbiquitinationTRFLSDPKTVLSAES
HHHHCCCCCCCCCCC
57.1421906983
673 (in isoform 5)Ubiquitination-57.1421890473
673 (in isoform 4)Ubiquitination-57.1421890473
679 (in isoform 3)Ubiquitination-56.1321890473
679 (in isoform 2)Ubiquitination-56.1321890473
690PhosphorylationLNRALILTLARATHV
HHHHHHHHHHHHHCC
16.0424719451
758UbiquitinationESRFNLKKNVEEEYR
HHHCCCCHHHHHHHH
70.19-
766UbiquitinationNVEEEYRKWKSMSNE
HHHHHHHHHHHCCCC
59.06-
868S-palmitoylationTLDRLILCLAMRSHE
HHHHHHHHHHHCCCC
1.4829575903
905UbiquitinationNRVSDFVKENSPEHW
HHHHHHHHHCCHHHH
51.69-
920UbiquitinationLQNDWHTKHMNYHKK
HHCCHHHHCCCHHHH
28.15-
1050UbiquitinationCLSDTYLKCAMNARE
CCCHHHHHHHHCCCC
14.99-
1082UbiquitinationLVDTMAGKSPGPFPN
HHHHHCCCCCCCCCC
43.89-
1132 (in isoform 5)Ubiquitination-35.1221890473
1132 (in isoform 1)Ubiquitination-35.1221890473
1132UbiquitinationALLNVVLKSQPLVPR
HHHHHHHHCCCCCCH
35.122190698
1132 (in isoform 4)Ubiquitination-35.1221890473
1138 (in isoform 3)Ubiquitination-45.6221890473
1176PhosphorylationVSVISSPSLTSETEW
EEECCCCCCCCCCCC
46.34-
1311AcetylationMFTGDSVKEQVEKII
HHCCCCHHHHHHHHH
46.5126051181
1316UbiquitinationSVKEQVEKIICNLKP
CHHHHHHHHHHCCHH
38.22-
1322UbiquitinationEKIICNLKPALKLRL
HHHHHCCHHHHHHHH
17.79-
1326AcetylationCNLKPALKLRLRFIT
HCCHHHHHHHHHHHH
33.4025953088
1350PhosphorylationVPPQAMNSGSPAPQS
CCCCCCCCCCCCCCC
27.8018691976
1352PhosphorylationPQAMNSGSPAPQSNQ
CCCCCCCCCCCCCCC
20.0820068231
1357PhosphorylationSGSPAPQSNQVPVSL
CCCCCCCCCCCCCCC
28.3326074081
1363PhosphorylationQSNQVPVSLPVTQ--
CCCCCCCCCCCCC--
22.3820068231
1367PhosphorylationVPVSLPVTQ------
CCCCCCCCC------
26.9920068231

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 MED23_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MED23_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 MED23_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CEBPB_HUMANCEBPBphysical
14759369
PLPP_HUMANPDXPphysical
22939629
ELF3_HUMANELF3physical
15025473
MED10_HUMANMED10physical
26344197
MED14_HUMANMED14physical
26344197
MED22_HUMANMED22physical
26344197
MED24_HUMANMED24physical
26344197
MED25_HUMANMED25physical
26344197
ELF3_HUMANELF3physical
23464919
MRGBP_HUMANMRGBPphysical
25281560
EPC2_HUMANEPC2physical
25281560
LSR_HUMANLSRphysical
25281560
EVI1_HUMANMECOMphysical
25281560
MED30_HUMANMED30physical
25281560
YETS4_HUMANYEATS4physical
25281560
FBRS_HUMANFBRSphysical
25281560
PUM3_HUMANKIAA0020physical
25281560
MBIP1_HUMANMBIPphysical
25281560
PAXI1_HUMANPAXIP1physical
25281560
ZN608_HUMANZNF608physical
25281560
PSA2_HUMANPSMA2physical
25281560
SPC24_HUMANSPC24physical
25281560
MED29_HUMANMED29physical
25281560
MED22_HUMANMED22physical
25281560
MED9_HUMANMED9physical
25281560
MED25_HUMANMED25physical
25281560
SP20H_HUMANSUPT20Hphysical
25281560
KAT5_HUMANKAT5physical
25281560
EPC1_HUMANEPC1physical
25281560
NCOA2_HUMANNCOA2physical
25281560
MED19_HUMANMED19physical
25281560
KAT2B_HUMANKAT2Bphysical
25281560
MED18_HUMANMED18physical
25281560
PSMD6_HUMANPSMD6physical
25281560
MED21_HUMANMED21physical
25281560
MED31_HUMANMED31physical
25281560
MED6_HUMANMED6physical
25281560
CCNC_HUMANCCNCphysical
25281560
PSMD7_HUMANPSMD7physical
25281560
EP300_HUMANEP300physical
25281560
MED10_HUMANMED10physical
25281560
SUH_HUMANRBPJphysical
25281560
ZN516_HUMANZNF516physical
25281560
CDK8_HUMANCDK8physical
25281560
CBP_HUMANCREBBPphysical
25281560
RPB1_HUMANPOLR2Aphysical
25281560
NEB2_HUMANPPP1R9Bphysical
25281560
MYPT1_HUMANPPP1R12Aphysical
25281560
MED16_HUMANMED16physical
25281560
RB_HUMANRB1physical
25281560
MED20_HUMANMED20physical
25281560
MED27_HUMANMED27physical
25281560
PP1B_HUMANPPP1CBphysical
25281560
VCIP1_HUMANVCPIP1physical
25281560
MED13_HUMANMED13physical
25281560
MD13L_HUMANMED13Lphysical
25281560
MED17_HUMANMED17physical
25281560
MED8_HUMANMED8physical
25281560
MED4_HUMANMED4physical
25281560
TAF6L_HUMANTAF6Lphysical
25281560
MED24_HUMANMED24physical
25281560
MED15_HUMANMED15physical
25281560
MED12_HUMANMED12physical
25281560
ZN687_HUMANZNF687physical
25281560
ZN592_HUMANZNF592physical
25281560
EP400_HUMANEP400physical
25281560
MED14_HUMANMED14physical
25281560
MED1_HUMANMED1physical
25281560
MINT_HUMANSPENphysical
25281560
PP1RA_HUMANPPP1R10physical
25281560
GBG12_HUMANGNG12physical
25281560
TCEA1_HUMANTCEA1physical
25281560
PLSL_HUMANLCP1physical
25281560
KPBB_HUMANPHKBphysical
25281560
PHKG2_HUMANPHKG2physical
25281560
RBM15_HUMANRBM15physical
25281560
SC16A_HUMANSEC16Aphysical
25281560
SSRA_HUMANSSR1physical
25281560
VPS18_HUMANVPS18physical
25281560
SRRM1_HUMANSRRM1physical
25281560
AGK_HUMANAGKphysical
25281560
DOCK7_HUMANDOCK7physical
25281560
PDIP2_HUMANPOLDIP2physical
25281560
HACD3_HUMANPTPLAD1physical
25281560
RAD50_HUMANRAD50physical
25281560
RING1_HUMANRING1physical
25281560
BRE1A_HUMANRNF20physical
25281560
SC61B_HUMANSEC61Bphysical
25281560
SRP54_HUMANSRP54physical
25281560
VDAC2_HUMANVDAC2physical
25281560
CN37_HUMANCNPphysical
25281560
COR1C_HUMANCORO1Cphysical
25281560
AP2A1_HUMANAP2A1physical
25281560
DYR1B_HUMANDYRK1Bphysical
25281560
KDM1A_HUMANKDM1Aphysical
25281560
MAP7_HUMANMAP7physical
25281560
PTCD3_HUMANPTCD3physical
25281560
FL2D_HUMANWTAPphysical
25281560
CYC_HUMANCYCSphysical
25281560
CRIPT_HUMANCRIPTphysical
25281560
CAP2_HUMANCAP2physical
25281560
ECHB_HUMANHADHBphysical
25281560
ZN503_HUMANZNF503physical
25281560
NCBP1_HUMANNCBP1physical
25281560
ATIF1_HUMANATPIF1physical
25281560
PSD10_HUMANPSMD10physical
25281560
PHB_HUMANPHBphysical
25281560
TNR6B_HUMANTNRC6Bphysical
25281560
RBM14_HUMANRBM14physical
25281560
RCOR1_HUMANRCOR1physical
25281560
EXOS8_HUMANEXOSC8physical
25281560
SYK_HUMANKARSphysical
25281560
RUXG_HUMANSNRPGphysical
25281560
TRA2B_HUMANTRA2Bphysical
25281560
CO3_HUMANC3physical
25281560
BAG6_HUMANBAG6physical
25281560
CND3_HUMANNCAPGphysical
25281560
ENY2_HUMANENY2physical
25281560
RSRC2_HUMANRSRC2physical
25281560
LTBP1_HUMANLTBP1physical
25281560
PGRC1_HUMANPGRMC1physical
25281560
CPSF7_HUMANCPSF7physical
25281560
HMBX1_HUMANHMBOX1physical
25281560
ZN703_HUMANZNF703physical
25281560
TTC28_HUMANTTC28physical
25281560
QPCT_HUMANQPCTphysical
25281560
ECHA_HUMANHADHAphysical
25281560
TBA1A_HUMANTUBA1Aphysical
25281560
CSK22_HUMANCSNK2A2physical
25281560
RIOK1_HUMANRIOK1physical
25281560
DYR1A_HUMANDYRK1Aphysical
25281560
CTBP1_HUMANCTBP1physical
25281560
CEP76_HUMANCEP76physical
25281560
ROCK1_HUMANROCK1physical
25281560
DIAP1_HUMANDIAPH1physical
25281560
DCAF7_HUMANDCAF7physical
25281560
CTBP2_HUMANCTBP2physical
25281560

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614249Mental retardation, autosomal recessive 18 (MRT18)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MED23_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1352, AND MASSSPECTROMETRY.

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