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Overview

Uniprot IDQ15648
Protein NameMediator of RNA polymerase II transcription subunit 1
Gene NameMED1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1126 SEGSSSSKLSSSMYS
1171 SSGSSSTKMKPQGKP
1210 DKLASPMKPVPGTPP
1309 SLTAVIDKLKHGVVT
1377 SSVDSSKKTSESKNV
1382 SKKTSESKNVGSTGV
1391 VGSTGVAKIIISKHD
1396 VAKIIISKHDGGSPS
1405 DGGSPSIKAKVTLQK
1442 LISGSTPKHERGSPS
686 EICSGSNKTKKKKSS
688 CSGSNKTKKKKSSRL
689 SGSNKTKKKKSSRLP

Function

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 (PubMed:10406464, PubMed:11867769, PubMed:12037571, PubMed:12218053, PubMed:12556447, PubMed:14636573, PubMed:15340084, PubMed:15471764, PubMed:15989967, PubMed:16574658, PubMed:9653119). Acts as a coactivator for GATA1-mediated transcriptional activation during erythroid differentiation of K562 erythroleukemia cells (PubMed:24245781)

Protein Sequence

10 MKAQGETEES 20 EKLSKMSSLL 30 ERLHAKFNQN 40 RPWSETIKLV 50 RQVMEKRVVM 60 SSGGHQHLVS 70 CLETLQKALK 80 VTSLPAMTDR 90 LESIARQNGL 100 GSHLSASGTE 110 CYITSDMFYV 120 EVQLDPAGQL 130 CDVKVAHHGE 140 NPVSCPELVQ 150 QLREKNFDEF 160 SKHLKGLVNL 170 YNLPGDNKLK 180 TKMYLALQSL 190 EQDLSKMAIM 200 YWKATNAGPL 210 DKILHGSVGY 220 LTPRSGGHLM 230 NLKYYVSPSD 240 LLDDKTASPI 250 ILHENNVSRS 260 LGMNASVTIE 270 GTSAVYKLPI 280 APLIMGSHPV 290 DNKWTPSFSS 300 ITSANSVDLP 310 ACFFLKFPQP 320 IPVSRAFVQK 330 LQNCTGIPLF 340 ETQPTYAPLY 350 ELITQFELSK 360 DPDPIPLNHN 370 MRFYAALPGQ 380 QHCYFLNKDA 390 PLPDGRSLQG 400 TLVSKITFQH 410 PGRVPLILNL 420 IRHQVAYNTL 430 IGSCVKRTIL 440 KEDSPGLLQF 450 EVCPLSESRF 460 SVSFQHPVND 470 SLVCVVMDVQ 480 DSTHVSCKLY 490 KGLSDALICT 500 DDFIAKVVQR 510 CMSIPVTMRA 520 IRRKAETIQA 530 DTPALSLIAE 540 TVEDMVKKNL 550 PPASSPGYGM 560 TTGNNPMSGT 570 TTPTNTFPGG 580 PITTLFNMSM 590 SIKDRHESVG 600 HGEDFSKVSQ 610 NPILTSLLQI 620 TGNGGSTIGS 630 SPTPPHHTPP 640 PVSSMAGNTK 650 NHPMLMNLLK 660 DNPAQDFSTL 670 YGSSPLERQN 680 SSSGSPRMEI 690 CSGSNKTKKK 700 KSSRLPPEKP 710 KHQTEDDFQR 720 ELFSMDVDSQ 730 NPIFDVNMTA 740 DTLDTPHITP 750 APSQCSTPPT 760 TYPQPVPHPQ 770 PSIQRMVRLS 780 SSDSIGPDVT 790 DILSDIAEEA 800 SKLPSTSDDC 810 PAIGTPLRDS 820 SSSGHSQSTL 830 FDSDVFQTNN 840 NENPYTDPAD 850 LIADAAGSPS 860 SDSPTNHFFH 870 DGVDFNPDLL 880 NSQSQSGFGE 890 EYFDESSQSG 900 DNDDFKGFAS 910 QALNTLGVPM 920 LGGDNGETKF 930 KGNNQADTVD 940 FSIISVAGKA 950 LAPADLMEHH 960 SGSQGPLLTT 970 GDLGKEKTQK 980 RVKEGNGTSN 990 STLSGPGLDS 1000 KPGKRSRTPS 1010 NDGKSKDKPP 1020 KRKKADTEGK 1030 SPSHSSSNRP 1040 FTPPTSTGGS 1050 KSPGSAGRSQ 1060 TPPGVATPPI 1070 PKITIQIPKG 1080 TVMVGKPSSH 1090 SQYTSSGSVS 1100 SSGSKSHHSH 1110 SSSSSSSAST 1120 SGKMKSSKSE 1130 GSSSSKLSSS 1140 MYSSQGSSGS 1150 SQSKNSSQSG 1160 GKPGSSPITK 1170 HGLSSGSSST 1180 KMKPQGKPSS 1190 LMNPSLSKPN 1200 ISPSHSRPPG 1210 GSDKLASPMK 1220 PVPGTPPSSK 1230 AKSPISSGSG 1240 GSHMSGTSSS 1250 SGMKSSSGLG 1260 SSGSLSQKTP 1270 PSSNSCTASS 1280 SSFSSSGSSM 1290 SSSQNQHGSS 1300 KGKSPSRNKK 1310 PSLTAVIDKL 1320 KHGVVTSGPG 1330 GEDPLDGQMG 1340 VSTNSSSHPM 1350 SSKHNMSGGE 1360 FQGKREKSDK 1370 DKSKVSTSGS 1380 SVDSSKKTSE 1390 SKNVGSTGVA 1400 KIIISKHDGG 1410 SPSIKAKVTL 1420 QKPGESSGEG 1430 LRPQMASSKN 1440 YGSPLISGST 1450 PKHERGSPSH 1460 SKSPAYTPQN 1470 LDSESESGSS 1480 IAEKSYQNSP 1490 SSDDGIRPLP 1500 EYSTEKHKKH 1510 KKEKKKVKDK 1520 DRDRDRDKDR 1530 DKKKSHSIKP 1540 ESWSKSPISS 1550 DQSLSMTSNT 1560 ILSADRPSRL 1570 SPDFMIGEED 1580 DDLMDVALIG N

Gene Ontology

Classification GO ID Description
Cellular Component GO:0000785 chromatin
Cellular Component GO:0016592 mediator complex
Cellular Component GO:0016020 membrane
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0032993 protein-DNA complex
Cellular Component GO:0000151 ubiquitin ligase complex
Molecular Function GO:0003682 chromatin binding
Molecular Function GO:0031490 chromatin DNA binding
Molecular Function GO:0140297 DNA-binding transcription factor binding
Molecular Function GO:0140296 general transcription initiation factor binding
Molecular Function GO:0035035 histone acetyltransferase binding
Molecular Function GO:0050693 LBD domain binding
Molecular Function GO:0030331 nuclear estrogen receptor binding
Molecular Function GO:0016922 nuclear receptor binding
Molecular Function GO:0042974 nuclear retinoic acid receptor binding
Molecular Function GO:0046966 nuclear thyroid hormone receptor binding
Molecular Function GO:0042809 nuclear vitamin D receptor binding
Molecular Function GO:0042975 peroxisome proliferator activated receptor binding
Molecular Function GO:1990841 promoter-specific chromatin binding
Molecular Function GO:0044877 protein-containing complex binding
Molecular Function GO:0000978 RNA polymerase II cis-regulatory region sequence-specific DNA binding
Molecular Function GO:0003713 transcription coactivator activity
Molecular Function GO:0001223 transcription coactivator binding
Molecular Function GO:0003712 transcription coregulator activity
Molecular Function GO:0003714 transcription corepressor activity
Molecular Function GO:0061630 ubiquitin protein ligase activity
Biological Process GO:0006702 androgen biosynthetic process
Biological Process GO:0001525 angiogenesis
Biological Process GO:0000902 cell morphogenesis
Biological Process GO:0071364 cellular response to epidermal growth factor stimulus
Biological Process GO:0071383 cellular response to steroid hormone stimulus
Biological Process GO:0097067 cellular response to thyroid hormone stimulus
Biological Process GO:0048821 erythrocyte development
Biological Process GO:0045444 fat cell differentiation
Biological Process GO:0030216 keratinocyte differentiation
Biological Process GO:0002088 lens development in camera-type eye
Biological Process GO:0035855 megakaryocyte development
Biological Process GO:0042789 mRNA transcription by RNA polymerase II
Biological Process GO:0043066 negative regulation of apoptotic process
Biological Process GO:0010839 negative regulation of keratinocyte proliferation
Biological Process GO:0045665 negative regulation of neuron differentiation
Biological Process GO:0000122 negative regulation of transcription by RNA polymerase II
Biological Process GO:0030518 nuclear receptor-mediated steroid hormone signaling pathway
Biological Process GO:0045893 positive regulation of DNA-templated transcription
Biological Process GO:0045648 positive regulation of erythrocyte differentiation
Biological Process GO:0010628 positive regulation of gene expression
Biological Process GO:0045618 positive regulation of keratinocyte differentiation
Biological Process GO:0045944 positive regulation of transcription by RNA polymerase II
Biological Process GO:0032968 positive regulation of transcription elongation by RNA polymerase II
Biological Process GO:0060261 positive regulation of transcription initiation by RNA polymerase II
Biological Process GO:0016567 protein ubiquitination
Biological Process GO:2001141 regulation of RNA biosynthetic process
Biological Process GO:0006357 regulation of transcription by RNA polymerase II
Biological Process GO:0003406 retinal pigment epithelium development
Biological Process GO:0051123 RNA polymerase II preinitiation complex assembly
Biological Process GO:0002154 thyroid hormone receptor signaling pathway
Biological Process GO:0003222 ventricular trabecula myocardium morphogenesis

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[4] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.

[5] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[6] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.