Details for: MED1
Associated with
Significant Cells
Cell Significance Index (CSI) scores for the chosen context(s)
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CSI 5.89rCSI 5.88%PRS 63.29
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CSI 5.75rCSI 12.89%PRS 51.68
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CSI 4.24rCSI 3.69%PRS 80.25
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CSI 4.11rCSI 4.91%PRS 50.79
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CSI 3.97rCSI 7.01%PRS 50.1
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CSI 3.82rCSI 5.76%PRS 74.86
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CSI 3.69rCSI 7.33%PRS 66.37
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CSI 3.53rCSI 2.45%PRS 81.21
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CSI 3.5rCSI 21.87%PRS 61.15
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CSI 3.49rCSI 2.06%PRS 86.07
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CSI 3.45rCSI 2.9%PRS 84.93
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CSI 3.39rCSI 2.58%PRS 82.48
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CSI 3.15rCSI 3.78%PRS 68.13
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CSI 3.11rCSI 3.65%PRS 84.82
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CSI 3.1rCSI 3.05%PRS 72.42
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CSI 3.01rCSI 4.63%PRS 79.02
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CSI 2.98rCSI 2.08%PRS 72.7
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CSI 2.9rCSI 2.16%PRS 84.72
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CSI 2.85rCSI 2.99%PRS 73.35
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CSI 2.74rCSI 2.94%PRS 70.13
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CSI 2.72rCSI 4.57%PRS 51.01
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CSI 2.65rCSI 5.33%PRS 59.02
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CSI 2.65rCSI 1.85%PRS 84.46
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CSI 2.6rCSI 1.92%PRS 62.55
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CSI 2.58rCSI 2.04%PRS 57.01
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CSI 2.55rCSI 2.11%PRS 72.23
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CSI 2.48rCSI 1.67%PRS 82.97
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CSI 2.38rCSI 2.06%PRS 74.5
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CSI 2.38rCSI 1.58%PRS 72.66
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CSI 2.36rCSI 2.88%PRS 77.07
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CSI 2.33rCSI 4.18%PRS 69.15
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CSI 2.3rCSI 1.65%PRS 83.21
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CSI 2.29rCSI 2.12%PRS 71.51
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CSI 2.23rCSI 3.04%PRS 75.52
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CSI 2.22rCSI 1.65%PRS 82.36
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CSI 2.19rCSI 3.1%PRS 65.96
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CSI 2.17rCSI 1.9%PRS 78.43
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CSI 2.16rCSI 1.75%PRS 71.6
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CSI 2.11rCSI 2.52%PRS 87.14
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CSI 2.1rCSI 3.45%PRS 58.81
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CSI 2.08rCSI 3.96%PRS 82.57
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CSI 2.02rCSI 3.79%PRS 57.59
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CSI 2.01rCSI 1.51%PRS 75.57
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CSI 1.96rCSI 3.98%PRS 48.06
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CSI 1.95rCSI 1.62%PRS 69.71
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CSI 1.92rCSI 2.22%PRS 60.73
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CSI 1.88rCSI 1.75%PRS 70.6
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CSI 1.88rCSI 1.65%PRS 75.14
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CSI 1.87rCSI 1.65%PRS 57.78
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CSI 1.87rCSI 2.39%PRS 74.08
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CSI 1.69rCSI 1.3%PRS 71.48
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CSI 1.66rCSI 1.6%PRS 61.43
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CSI 1.65rCSI 2.06%PRS 49.05
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CSI 1.61rCSI 2.19%PRS 70.78
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CSI 1.6rCSI 4.14%PRS 64.65
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CSI 1.5rCSI 1.94%PRS 52.33
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CSI 1.48rCSI 1.9%PRS 66.44
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CSI 1.48rCSI 2.35%PRS 62.43
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CSI 1.47rCSI 1.82%PRS 66.73
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CSI 1.47rCSI 2.27%PRS 68.52
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CSI 1.45rCSI 1.76%PRS 78.79
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CSI 1.42rCSI 3.46%PRS 62.82
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CSI 1.4rCSI 1.91%PRS 61.26
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CSI 1.38rCSI 1.73%PRS 79.79
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CSI 1.3rCSI 1.74%PRS 69.61
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CSI 1.28rCSI 3.25%PRS 59.36
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CSI 1.24rCSI 1.12%PRS 67.09
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CSI 1.22rCSI 1.75%PRS 59.23
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CSI 1.19rCSI 1.92%PRS 52.94
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CSI 1.12rCSI 1.8%PRS 59.2
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CSI 1.1rCSI 3.58%PRS 69.1
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CSI 1.08rCSI 4.2%PRS 87.89
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CSI 1rCSI 1.03%PRS 75.46
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CSI 0.85rCSI 2.46%PRS 59.07
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CSI 0.7rCSI 6.03%PRS 56.96
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CSI 0.7rCSI 1.69%PRS 49.41
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CSI 0.65rCSI 2.88%PRS 70.02
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CSI 0.63rCSI 2.26%PRS 49.16
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CSI 0.6rCSI 2.27%PRS 51.57
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CSI 0.59rCSI 1.99%PRS 54.37
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CSI 0.53rCSI 1.66%PRS 55.22
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CSI 0.51rCSI 2.54%PRS 82.13
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CSI 0.46rCSI 1.44%PRS 52.76
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CSI 0.41rCSI 3.32%PRS 63.22
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CSI 0.31rCSI 1.8%PRS 77.49
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.
Network Configuration
Explore relationships of the current gene. Select an Interaction Source: 'ONTOLOGY' for shared pathways (GO/Reactome) or 'STRING' for protein-protein interactions. Further refine by selecting context genes and comparing Cell Significance Index (CSI) scores between baseline and target cell types and their specific contexts.
Legend:
- Query Gene
-
Node Color (Target Cell CSI, relative to current network):
- Very High
- High
- Medium
- Low
- Very Low
- CSI N/A
- Node Size: Proportional to Target Cell CSI magnitude
- STRING PPI Edge
- Shared Pathway Edge (ONTOLOGY)
Other Information
This section provides additional information about the gene, including a description generated by an AI language model and details about associated proteins.
Genular Protein ID: 305185906
Symbol: MED1_HUMAN
Name: Mediator of RNA polymerase II transcription subunit 1
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 9444950
Title: Identification of RB18A, a 205 kDa new p53 regulatory protein which shares antigenic and functional properties with p53.
PubMed ID: 9444950
PubMed ID: 9653119
Title: The TRAP220 component of a thyroid hormone receptor-associated protein (TRAP) coactivator complex interacts directly with nuclear receptors in a ligand-dependent fashion.
PubMed ID: 9653119
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 10235267
Title: Composite co-activator ARC mediates chromatin-directed transcriptional activation.
PubMed ID: 10235267
DOI: 10.1038/19789
PubMed ID: 10733574
Title: The DRIP complex and SRC-1/p160 coactivators share similar nuclear receptor binding determinants but constitute functionally distinct complexes.
PubMed ID: 10733574
PubMed ID: 10235266
Title: Ligand-dependent transcription activation by nuclear receptors requires the DRIP complex.
PubMed ID: 10235266
DOI: 10.1038/19783
PubMed ID: 7776974
Title: Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor.
PubMed ID: 7776974
PubMed ID: 10024883
Title: A novel human SRB/MED-containing cofactor complex, SMCC, involved in transcription regulation.
PubMed ID: 10024883
PubMed ID: 10406464
Title: Identification of mouse TRAP100: a transcriptional coregulatory factor for thyroid hormone and vitamin D receptors.
PubMed ID: 10406464
PubMed ID: 10478845
Title: Coactivators for the orphan nuclear receptor RORalpha.
PubMed ID: 10478845
PubMed ID: 10770935
Title: Functional interactions between the estrogen receptor and DRIP205, a subunit of the heteromeric DRIP coactivator complex.
PubMed ID: 10770935
PubMed ID: 11303023
Title: Differential recruitment of the mammalian mediator subunit TRAP220 by estrogen receptors ERalpha and ERbeta.
PubMed ID: 11303023
PubMed ID: 12218053
Title: A coregulatory role for the TRAP-mediator complex in androgen receptor-mediated gene expression.
PubMed ID: 12218053
PubMed ID: 12037571
Title: Transcription coactivator TRAP220 is required for PPAR gamma 2-stimulated adipogenesis.
PubMed ID: 12037571
DOI: 10.1038/417563a
PubMed ID: 11867769
Title: The TRAP/Mediator coactivator complex interacts directly with estrogen receptors alpha and beta through the TRAP220 subunit and directly enhances estrogen receptor function in vitro.
PubMed ID: 11867769
PubMed ID: 12034878
Title: Ordered recruitment of histone acetyltransferases and the TRAP/Mediator complex to thyroid hormone-responsive promoters in vivo.
PubMed ID: 12034878
PubMed ID: 12556447
Title: An extended LXXLL motif sequence determines the nuclear receptor binding specificity of TRAP220.
PubMed ID: 12556447
PubMed ID: 14636573
Title: Coordination of p300-mediated chromatin remodeling and TRAP/mediator function through coactivator PGC-1alpha.
PubMed ID: 14636573
PubMed ID: 15471764
Title: Vitamin D-interacting protein 205 (DRIP205) coactivation of estrogen receptor alpha (ERalpha) involves multiple domains of both proteins.
PubMed ID: 15471764
PubMed ID: 15175163
Title: A set of consensus mammalian mediator subunits identified by multidimensional protein identification technology.
PubMed ID: 15175163
PubMed ID: 15340084
Title: Structural and functional organization of TRAP220, the TRAP/mediator subunit that is targeted by nuclear receptors.
PubMed ID: 15340084
PubMed ID: 15989967
Title: MED1/TRAP220 exists predominantly in a TRAP/Mediator subpopulation enriched in RNA polymerase II and is required for ER-mediated transcription.
PubMed ID: 15989967
PubMed ID: 16314496
Title: Activation of TRAP/mediator subunit TRAP220/Med1 is regulated by mitogen-activated protein kinase-dependent phosphorylation.
PubMed ID: 16314496
PubMed ID: 17081983
Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
PubMed ID: 17081983
PubMed ID: 16574658
Title: Regulation of Aurora-A kinase gene expression via GABP recruitment of TRAP220/MED1.
PubMed ID: 16574658
PubMed ID: 17000779
Title: Mediator modulates Gli3-dependent Sonic hedgehog signaling.
PubMed ID: 17000779
DOI: 10.1128/mcb.00443-06
PubMed ID: 16964243
Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.
PubMed ID: 16964243
DOI: 10.1038/nbt1240
PubMed ID: 17525332
Title: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.
PubMed ID: 17525332
PubMed ID: 18691976
Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.
PubMed ID: 18691976
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19413330
Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
PubMed ID: 19413330
DOI: 10.1021/ac9004309
PubMed ID: 19369195
Title: Large-scale proteomics analysis of the human kinome.
PubMed ID: 19369195
PubMed ID: 19786558
Title: The basic helix-loop-helix proteins differentiated embryo chondrocyte (DEC) 1 and DEC2 function as corepressors of retinoid X receptors.
PubMed ID: 19786558
PubMed ID: 19690332
Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
PubMed ID: 19690332
PubMed ID: 19608861
Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.
PubMed ID: 19608861
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21406692
Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
PubMed ID: 21406692
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 24245781
Title: CCAR1/CoCoA pair-mediated recruitment of the Mediator defines a novel pathway for GATA1 function.
PubMed ID: 24245781
DOI: 10.1111/gtc.12104
PubMed ID: 24275569
Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
PubMed ID: 24275569
PubMed ID: 29997176
Title: Affinity switching of the LEDGF/p75 IBD interactome is governed by kinase-dependent phosphorylation.
PubMed ID: 29997176
Sequence Information:
- Length: 1581
- Mass: 168478
- Checksum: FCE0FE87EF08B887
- Sequence:
MKAQGETEES EKLSKMSSLL ERLHAKFNQN RPWSETIKLV RQVMEKRVVM SSGGHQHLVS CLETLQKALK VTSLPAMTDR LESIARQNGL GSHLSASGTE CYITSDMFYV EVQLDPAGQL CDVKVAHHGE NPVSCPELVQ QLREKNFDEF SKHLKGLVNL YNLPGDNKLK TKMYLALQSL EQDLSKMAIM YWKATNAGPL DKILHGSVGY LTPRSGGHLM NLKYYVSPSD LLDDKTASPI ILHENNVSRS LGMNASVTIE GTSAVYKLPI APLIMGSHPV DNKWTPSFSS ITSANSVDLP ACFFLKFPQP IPVSRAFVQK LQNCTGIPLF ETQPTYAPLY ELITQFELSK DPDPIPLNHN MRFYAALPGQ QHCYFLNKDA PLPDGRSLQG TLVSKITFQH PGRVPLILNL IRHQVAYNTL IGSCVKRTIL KEDSPGLLQF EVCPLSESRF SVSFQHPVND SLVCVVMDVQ DSTHVSCKLY KGLSDALICT DDFIAKVVQR CMSIPVTMRA IRRKAETIQA DTPALSLIAE TVEDMVKKNL PPASSPGYGM TTGNNPMSGT TTPTNTFPGG PITTLFNMSM SIKDRHESVG HGEDFSKVSQ NPILTSLLQI TGNGGSTIGS SPTPPHHTPP PVSSMAGNTK NHPMLMNLLK DNPAQDFSTL YGSSPLERQN SSSGSPRMEI CSGSNKTKKK KSSRLPPEKP KHQTEDDFQR ELFSMDVDSQ NPIFDVNMTA DTLDTPHITP APSQCSTPPT TYPQPVPHPQ PSIQRMVRLS SSDSIGPDVT DILSDIAEEA SKLPSTSDDC PAIGTPLRDS SSSGHSQSTL FDSDVFQTNN NENPYTDPAD LIADAAGSPS SDSPTNHFFH DGVDFNPDLL NSQSQSGFGE EYFDESSQSG DNDDFKGFAS QALNTLGVPM LGGDNGETKF KGNNQADTVD FSIISVAGKA LAPADLMEHH SGSQGPLLTT GDLGKEKTQK RVKEGNGTSN STLSGPGLDS KPGKRSRTPS NDGKSKDKPP KRKKADTEGK SPSHSSSNRP FTPPTSTGGS KSPGSAGRSQ TPPGVATPPI PKITIQIPKG TVMVGKPSSH SQYTSSGSVS SSGSKSHHSH SSSSSSSAST SGKMKSSKSE GSSSSKLSSS MYSSQGSSGS SQSKNSSQSG GKPGSSPITK HGLSSGSSST KMKPQGKPSS LMNPSLSKPN ISPSHSRPPG GSDKLASPMK PVPGTPPSSK AKSPISSGSG GSHMSGTSSS SGMKSSSGLG SSGSLSQKTP PSSNSCTASS SSFSSSGSSM SSSQNQHGSS KGKSPSRNKK PSLTAVIDKL KHGVVTSGPG GEDPLDGQMG VSTNSSSHPM SSKHNMSGGE FQGKREKSDK DKSKVSTSGS SVDSSKKTSE SKNVGSTGVA KIIISKHDGG SPSIKAKVTL QKPGESSGEG LRPQMASSKN YGSPLISGST PKHERGSPSH SKSPAYTPQN LDSESESGSS IAEKSYQNSP SSDDGIRPLP EYSTEKHKKH KKEKKKVKDK DRDRDRDKDR DKKKSHSIKP ESWSKSPISS DQSLSMTSNT ILSADRPSRL SPDFMIGEED DDLMDVALIG N