MED22_HUMAN
ID MED22_HUMAN Reviewed; 200 AA.
AC Q15528; B3KW83; B3KWX4; O76072; Q5T8U0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 22;
DE AltName: Full=Mediator complex subunit 22;
DE AltName: Full=Surfeit locus protein 5;
DE Short=Surf-5;
GN Name=MED22; Synonyms=SURF5;
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 [MRNA] (ISOFORM SURF5A).
RX PubMed=8586415; DOI=10.1006/geno.1995.9889;
RA Garson K., Duhig T., Armes N., Colombo P., Fried M.;
RT "Surf5: a gene in the tightly clustered mouse surfeit locus is highly
RT conserved and transcribed divergently from the rpL7A (Surf3) gene.";
RL Genomics 30:163-170(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING.
RX PubMed=11891058; DOI=10.1016/s0378-1119(02)00379-7;
RA Angiolillo A., Russo G., Porcellini A., Smaldone S., D'Alessandro F.,
RA Pietropaolo C.;
RT "The human homologue of the mouse Surf5 gene encodes multiple alternatively
RT spliced transcripts.";
RL Gene 284:169-178(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS SURF5B AND SURF5A).
RC TISSUE=Cerebellum, and Testis;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SURF5A).
RC TISSUE=Muscle, and Skin;
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 [7]
RP INTERACTION WITH MED10; MED11 AND MED30.
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 [8]
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 [9]
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).
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:15989967}.
CC -!- INTERACTION:
CC Q15528; Q9P086: MED11; NbExp=3; IntAct=EBI-394687, EBI-394704;
CC Q15528; Q9NVC6: MED17; NbExp=4; IntAct=EBI-394687, EBI-394562;
CC Q15528; Q9BUE0: MED18; NbExp=3; IntAct=EBI-394687, EBI-394640;
CC Q15528; Q6P2C8: MED27; NbExp=3; IntAct=EBI-394687, EBI-394603;
CC Q15528; Q9H204: MED28; NbExp=2; IntAct=EBI-394687, EBI-514199;
CC Q15528; Q9NX70: MED29; NbExp=4; IntAct=EBI-394687, EBI-394656;
CC Q15528; Q9D8C6: Med11; Xeno; NbExp=2; IntAct=EBI-394687, EBI-6260909;
CC Q15528; Q9CQI9: Med30; Xeno; NbExp=6; IntAct=EBI-394687, EBI-309220;
CC Q15528; Q9D7W5: Med8; Xeno; NbExp=2; IntAct=EBI-394687, EBI-7990252;
CC Q15528-2; O14964: HGS; NbExp=3; IntAct=EBI-12954271, EBI-740220;
CC Q15528-2; P42858: HTT; NbExp=12; IntAct=EBI-12954271, EBI-466029;
CC Q15528-2; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-12954271, EBI-741158;
CC Q15528-2; P60891: PRPS1; NbExp=3; IntAct=EBI-12954271, EBI-749195;
CC Q15528-2; O14530: TXNDC9; NbExp=3; IntAct=EBI-12954271, EBI-707554;
CC Q15528-2; O76024: WFS1; NbExp=3; IntAct=EBI-12954271, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Surf5B;
CC IsoId=Q15528-1; Sequence=Displayed;
CC Name=Surf5A;
CC IsoId=Q15528-2; Sequence=VSP_006309;
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 22 family.
CC {ECO:0000305}.
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DR EMBL; X85178; CAA59462.1; -; mRNA.
DR EMBL; AJ224639; CAA12052.1; -; Genomic_DNA.
DR EMBL; AJ224639; CAA12053.1; -; Genomic_DNA.
DR EMBL; AJ224358; CAA11915.1; -; mRNA.
DR EMBL; AJ224359; CAA11916.1; -; mRNA.
DR EMBL; AK124518; BAG54045.1; -; mRNA.
DR EMBL; AK126069; BAG54286.1; -; mRNA.
DR EMBL; AL158826; CAI12827.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW88056.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW88060.1; -; Genomic_DNA.
DR EMBL; BC024225; AAH24225.1; -; mRNA.
DR EMBL; BC040111; AAH40111.1; -; mRNA.
DR CCDS; CCDS6963.1; -. [Q15528-1]
DR CCDS; CCDS6964.1; -. [Q15528-2]
DR RefSeq; NP_598395.1; NM_133640.4. [Q15528-1]
DR RefSeq; NP_852468.1; NM_181491.2. [Q15528-2]
DR PDB; 7EMF; EM; 3.50 A; V=1-200.
DR PDB; 7ENA; EM; 4.07 A; v=1-200.
DR PDB; 7ENC; EM; 4.13 A; v=1-200.
DR PDB; 7ENJ; EM; 4.40 A; V=1-200.
DR PDB; 7LBM; EM; 4.80 A; m=1-200.
DR PDB; 7NVR; EM; 4.50 A; g=1-200.
DR PDBsum; 7EMF; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR PDBsum; 7ENJ; -.
DR PDBsum; 7LBM; -.
DR PDBsum; 7NVR; -.
DR AlphaFoldDB; Q15528; -.
DR SMR; Q15528; -.
DR BioGRID; 112704; 84.
DR ComplexPortal; CPX-3227; Core mediator complex.
DR CORUM; Q15528; -.
DR IntAct; Q15528; 42.
DR MINT; Q15528; -.
DR STRING; 9606.ENSP00000482438; -.
DR iPTMnet; Q15528; -.
DR PhosphoSitePlus; Q15528; -.
DR BioMuta; MED22; -.
DR DMDM; 6175074; -.
DR EPD; Q15528; -.
DR jPOST; Q15528; -.
DR MassIVE; Q15528; -.
DR MaxQB; Q15528; -.
DR PaxDb; Q15528; -.
DR PeptideAtlas; Q15528; -.
DR PRIDE; Q15528; -.
DR ProteomicsDB; 60619; -. [Q15528-1]
DR ProteomicsDB; 60620; -. [Q15528-2]
DR TopDownProteomics; Q15528-2; -. [Q15528-2]
DR Antibodypedia; 18330; 178 antibodies from 26 providers.
DR DNASU; 6837; -.
DR Ensembl; ENST00000343730.10; ENSP00000342343.5; ENSG00000148297.16. [Q15528-1]
DR Ensembl; ENST00000610672.4; ENSP00000482438.1; ENSG00000148297.16. [Q15528-1]
DR Ensembl; ENST00000610888.4; ENSP00000478773.1; ENSG00000148297.16. [Q15528-2]
DR Ensembl; ENST00000614493.4; ENSP00000481493.1; ENSG00000148297.16. [Q15528-2]
DR Ensembl; ENST00000626118.2; ENSP00000485715.1; ENSG00000281022.3. [Q15528-2]
DR Ensembl; ENST00000629522.2; ENSP00000485880.1; ENSG00000281022.3. [Q15528-1]
DR Ensembl; ENST00000629975.2; ENSP00000486722.1; ENSG00000281022.3. [Q15528-2]
DR Ensembl; ENST00000631196.3; ENSP00000487580.1; ENSG00000281022.3. [Q15528-1]
DR GeneID; 6837; -.
DR KEGG; hsa:6837; -.
DR MANE-Select; ENST00000343730.10; ENSP00000342343.5; NM_133640.5; NP_598395.1.
DR UCSC; uc004cdc.5; human. [Q15528-1]
DR CTD; 6837; -.
DR DisGeNET; 6837; -.
DR GeneCards; MED22; -.
DR HGNC; HGNC:11477; MED22.
DR HPA; ENSG00000148297; Low tissue specificity.
DR MIM; 185641; gene.
DR neXtProt; NX_Q15528; -.
DR OpenTargets; ENSG00000148297; -.
DR PharmGKB; PA162395486; -.
DR VEuPathDB; HostDB:ENSG00000148297; -.
DR eggNOG; KOG3304; Eukaryota.
DR GeneTree; ENSGT00390000004339; -.
DR HOGENOM; CLU_117242_0_0_1; -.
DR InParanoid; Q15528; -.
DR OMA; TQCEQDT; -.
DR PhylomeDB; Q15528; -.
DR TreeFam; TF323390; -.
DR PathwayCommons; Q15528; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR SignaLink; Q15528; -.
DR SIGNOR; Q15528; -.
DR BioGRID-ORCS; 6837; 703 hits in 1092 CRISPR screens.
DR ChiTaRS; MED22; human.
DR GeneWiki; MED22; -.
DR GenomeRNAi; 6837; -.
DR Pharos; Q15528; Tbio.
DR PRO; PR:Q15528; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q15528; protein.
DR Bgee; ENSG00000148297; Expressed in cortical plate and 97 other tissues.
DR ExpressionAtlas; Q15528; baseline and differential.
DR Genevisible; Q15528; HS.
DR GO; GO:0070847; C:core mediator complex; IPI:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0016592; C:mediator complex; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
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:0051123; P:RNA polymerase II preinitiation complex assembly; IC:ComplexPortal.
DR InterPro; IPR009332; Med22.
DR PANTHER; PTHR12434; PTHR12434; 1.
DR Pfam; PF06179; Med22; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Coiled coil; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..200
FT /note="Mediator of RNA polymerase II transcription subunit
FT 22"
FT /id="PRO_0000178838"
FT REGION 166..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 93..122
FT /evidence="ECO:0000255"
FT VAR_SEQ 138..200
FT /note="SSSLCEANDLPLCEAYGRLDLDTDSADGLSAPLLASPEPSAGPLQVAAPAHS
FT HAGGPGPTEHA -> RYK (in isoform Surf5A)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8586415"
FT /id="VSP_006309"
FT HELIX 11..39
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 50..89
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 91..135
FT /evidence="ECO:0007829|PDB:7EMF"
SQ SEQUENCE 200 AA; 22221 MW; 113BBF7C35B03F7B CRC64;
MAQQRALPQS KETLLQSYNK RLKDDIKSIM DNFTEIIKTA KIEDETQVSR ATQGEQDNYE
MHVRAANIVR AGESLMKLVS DLKQFLILND FPSVNEAIDQ RNQQLRTLQE ECDRKLITLR
DEISIDLYEL EEEYYSSSSS LCEANDLPLC EAYGRLDLDT DSADGLSAPL LASPEPSAGP
LQVAAPAHSH AGGPGPTEHA
