MED31_HUMAN
ID MED31_HUMAN Reviewed; 131 AA.
AC Q9Y3C7; B2R4L9;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 31;
DE AltName: Full=Mediator complex subunit 31;
DE AltName: Full=Mediator complex subunit SOH1;
DE Short=hSOH1;
GN Name=MED31; Synonyms=SOH1; ORFNames=CGI-125;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SMCC
RP COMPLEX.
RX PubMed=10024883; DOI=10.1016/s1097-2765(00)80178-1;
RA Gu W., Malik S., Ito M., Yuan C.-X., Fondell J.D., Zhang X., Martinez E.,
RA Qin J., Roeder R.G.;
RT "A novel human SRB/MED-containing cofactor complex, SMCC, involved in
RT transcription regulation.";
RL Mol. Cell 3:97-108(1999).
RN [6]
RP ERRATUM OF PUBMED:10024883.
RA Gu W., Malik S., Ito M., Yuan C.-X., Fondell J.D., Zhang X., Martinez E.,
RA Qin J., Roeder R.G.;
RL Mol. Cell 3:541-541(1999).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR
RP COMPLEX, AND INTERACTION OF THE MEDIATOR COMPLEX WITH ESR1 AND ESR2.
RX PubMed=11867769; DOI=10.1073/pnas.261715899;
RA Kang Y.K., Guermah M., Yuan C.-X., Roeder R.G.;
RT "The TRAP/Mediator coactivator complex interacts directly with estrogen
RT receptors alpha and beta through the TRAP220 subunit and directly enhances
RT estrogen receptor function in vitro.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:2642-2647(2002).
RN [8]
RP INTERACTION WITH MED19.
RX PubMed=12584197; DOI=10.1074/jbc.c300054200;
RA Sato S., Tomomori-Sato C., Banks C.A.S., Sorokina I., Parmely T.J.,
RA Kong S.E., Jin J., Cai Y., Lane W.S., Brower C.S., Conaway R.C.,
RA Conaway J.W.;
RT "Identification of mammalian Mediator subunits with similarities to yeast
RT Mediator subunits Srb5, Srb6, Med11, and Rox3.";
RL J. Biol. Chem. 278:15123-15127(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE MEDIATOR
RP COMPLEX.
RX PubMed=15175163; DOI=10.1016/j.molcel.2004.05.006;
RA Sato S., Tomomori-Sato C., Parmely T.J., Florens L., Zybailov B.,
RA Swanson S.K., Banks C.A.S., Jin J., Cai Y., Washburn M.P., Conaway J.W.,
RA Conaway R.C.;
RT "A set of consensus mammalian mediator subunits identified by
RT multidimensional protein identification technology.";
RL Mol. Cell 14:685-691(2004).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR
RP COMPLEX, AND ASSOCIATION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
RX PubMed=15989967; DOI=10.1016/j.molcel.2005.05.015;
RA Zhang X., Krutchinsky A., Fukuda A., Chen W., Yamamura S., Chait B.T.,
RA Roeder R.G.;
RT "MED1/TRAP220 exists predominantly in a TRAP/Mediator subpopulation
RT enriched in RNA polymerase II and is required for ER-mediated
RT transcription.";
RL Mol. Cell 19:89-100(2005).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Component of the Mediator complex, a coactivator involved in
CC the regulated transcription of nearly all RNA polymerase II-dependent
CC genes. Mediator functions as a bridge to convey information from gene-
CC specific regulatory proteins to the basal RNA polymerase II
CC transcription machinery. Mediator is recruited to promoters by direct
CC interactions with regulatory proteins and serves as a scaffold for the
CC assembly of a functional preinitiation complex with RNA polymerase II
CC and the general transcription factors.
CC -!- SUBUNIT: Component of the Mediator complex, which is composed of MED1,
CC MED4, MED6, MED7, MED8, MED9, MED10, MED11, MED12, MED13, MED13L,
CC MED14, MED15, MED16, MED17, MED18, MED19, MED20, MED21, MED22, MED23,
CC MED24, MED25, MED26, MED27, MED29, MED30, MED31, CCNC, CDK8 and
CC CDC2L6/CDK11. The MED12, MED13, CCNC and CDK8 subunits form a distinct
CC module termed the CDK8 module. Mediator containing the CDK8 module is
CC less active than Mediator lacking this module in supporting
CC transcriptional activation. Individual preparations of the Mediator
CC complex lacking one or more distinct subunits have been variously
CC termed ARC, CRSP, DRIP, PC2, SMCC and TRAP.
CC {ECO:0000269|PubMed:10024883, ECO:0000269|PubMed:11867769,
CC ECO:0000269|PubMed:15175163, ECO:0000269|PubMed:15989967}.
CC -!- INTERACTION:
CC Q9Y3C7; O95257: GADD45G; NbExp=2; IntAct=EBI-394707, EBI-448202;
CC Q9Y3C7; P42858: HTT; NbExp=9; IntAct=EBI-394707, EBI-466029;
CC Q9Y3C7; O43513: MED7; NbExp=3; IntAct=EBI-394707, EBI-394632;
CC Q9Y3C7; Q96HR8: NAF1; NbExp=3; IntAct=EBI-394707, EBI-2515597;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 31 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF151883; AAD34120.1; -; mRNA.
DR EMBL; AK311875; BAG34816.1; -; mRNA.
DR EMBL; CH471108; EAW90301.1; -; Genomic_DNA.
DR EMBL; BC012539; AAH12539.1; -; mRNA.
DR CCDS; CCDS11078.1; -.
DR RefSeq; NP_057144.1; NM_016060.2.
DR PDB; 7EMF; EM; 3.50 A; 4=1-131.
DR PDB; 7ENA; EM; 4.07 A; m=1-131.
DR PDB; 7ENC; EM; 4.13 A; m=1-131.
DR PDB; 7ENJ; EM; 4.40 A; 4=1-131.
DR PDB; 7LBM; EM; 4.80 A; y=1-131.
DR PDB; 7NVR; EM; 4.50 A; o=1-131.
DR PDBsum; 7EMF; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR PDBsum; 7ENJ; -.
DR PDBsum; 7LBM; -.
DR PDBsum; 7NVR; -.
DR AlphaFoldDB; Q9Y3C7; -.
DR SMR; Q9Y3C7; -.
DR BioGRID; 119211; 109.
DR ComplexPortal; CPX-3227; Core mediator complex.
DR CORUM; Q9Y3C7; -.
DR IntAct; Q9Y3C7; 105.
DR MINT; Q9Y3C7; -.
DR STRING; 9606.ENSP00000225728; -.
DR iPTMnet; Q9Y3C7; -.
DR PhosphoSitePlus; Q9Y3C7; -.
DR SwissPalm; Q9Y3C7; -.
DR BioMuta; MED31; -.
DR DMDM; 38258656; -.
DR EPD; Q9Y3C7; -.
DR jPOST; Q9Y3C7; -.
DR MassIVE; Q9Y3C7; -.
DR MaxQB; Q9Y3C7; -.
DR PaxDb; Q9Y3C7; -.
DR PeptideAtlas; Q9Y3C7; -.
DR PRIDE; Q9Y3C7; -.
DR ProteomicsDB; 86016; -.
DR Antibodypedia; 23820; 117 antibodies from 25 providers.
DR DNASU; 51003; -.
DR Ensembl; ENST00000225728.8; ENSP00000225728.3; ENSG00000108590.11.
DR GeneID; 51003; -.
DR KEGG; hsa:51003; -.
DR MANE-Select; ENST00000225728.8; ENSP00000225728.3; NM_016060.3; NP_057144.1.
DR UCSC; uc002gdg.5; human.
DR CTD; 51003; -.
DR DisGeNET; 51003; -.
DR GeneCards; MED31; -.
DR HGNC; HGNC:24260; MED31.
DR HPA; ENSG00000108590; Low tissue specificity.
DR neXtProt; NX_Q9Y3C7; -.
DR OpenTargets; ENSG00000108590; -.
DR PharmGKB; PA134884310; -.
DR VEuPathDB; HostDB:ENSG00000108590; -.
DR eggNOG; KOG4086; Eukaryota.
DR GeneTree; ENSGT00390000015531; -.
DR HOGENOM; CLU_071681_5_1_1; -.
DR InParanoid; Q9Y3C7; -.
DR OMA; QILLWQH; -.
DR OrthoDB; 1480492at2759; -.
DR PhylomeDB; Q9Y3C7; -.
DR TreeFam; TF105799; -.
DR PathwayCommons; Q9Y3C7; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR SignaLink; Q9Y3C7; -.
DR SIGNOR; Q9Y3C7; -.
DR BioGRID-ORCS; 51003; 515 hits in 1087 CRISPR screens.
DR ChiTaRS; MED31; human.
DR GeneWiki; MED31; -.
DR GenomeRNAi; 51003; -.
DR Pharos; Q9Y3C7; Tbio.
DR PRO; PR:Q9Y3C7; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9Y3C7; protein.
DR Bgee; ENSG00000108590; Expressed in lower esophagus mucosa and 164 other tissues.
DR ExpressionAtlas; Q9Y3C7; baseline and differential.
DR Genevisible; Q9Y3C7; HS.
DR GO; GO:0070847; C:core mediator complex; IPI:ComplexPortal.
DR GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0000151; C:ubiquitin ligase complex; IEA:Ensembl.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0060173; P:limb development; IEA:Ensembl.
DR GO; GO:0048147; P:negative regulation of fibroblast proliferation; IEA:Ensembl.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IC:ComplexPortal.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IC:ComplexPortal.
DR Gene3D; 1.10.10.1340; -; 1.
DR InterPro; IPR038089; Med31_sf.
DR InterPro; IPR008831; Mediator_Med31.
DR PANTHER; PTHR13186; PTHR13186; 1.
DR Pfam; PF05669; Med31; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..131
FT /note="Mediator of RNA polymerase II transcription subunit
FT 31"
FT /id="PRO_0000212527"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT HELIX 11..28
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 31..39
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 55..59
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 72..79
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 91..105
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 107..121
FT /evidence="ECO:0007829|PDB:7EMF"
SQ SEQUENCE 131 AA; 15805 MW; 5DC672ADB994D015 CRC64;
MAAAVAMETD DAGNRLRFQL ELEFVQCLAN PNYLNFLAQR GYFKDKAFVN YLKYLLYWKD
PEYAKYLKYP QCLHMLELLQ YEHFRKELVN AQCAKFIDEQ QILHWQHYSR KRMRLQQALA
EQQQQNNTSG K
