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Database: UniProt
Entry: Q02080
LinkDB: Q02080
Original site: Q02080 
ID   MEF2B_HUMAN             Reviewed;         365 AA.
AC   Q02080; A0AV80; B4DVH7; B7ZVY1; G5E9M1;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   29-SEP-2021, entry version 182.
DE   RecName: Full=Myocyte-specific enhancer factor 2B;
DE   AltName: Full=RSRFR2;
DE   AltName: Full=Serum response factor-like protein 2;
GN   Name=MEF2B; Synonyms=XMEF2;
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 1).
RC   TISSUE=Heart, and Skeletal muscle;
RX   PubMed=1516833; DOI=10.1101/gad.6.9.1783;
RA   Yu Y.-T., Breitbart R.E., Smoot L.B., Lee Y., Mahdavi V., Nadal-Ginard B.;
RT   "Human myocyte-specific enhancer factor 2 comprises a group of tissue-
RT   restricted MADS box transcription factors.";
RL   Genes Dev. 6:1783-1798(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Placenta;
RX   PubMed=1748287; DOI=10.1101/gad.5.12a.2327;
RA   Pollock R., Treisman R.;
RT   "Human SRF-related proteins: DNA-binding properties and potential
RT   regulatory targets.";
RL   Genes Dev. 5:2327-2341(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Spleen;
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=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton 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 1).
RC   TISSUE=Brain, and Testis;
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   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2-94.
RX   PubMed=12700764; DOI=10.1038/nature01555;
RA   Han A., Pan F., Stroud J.C., Youn H.-D., Liu J.O., Chen L.;
RT   "Sequence-specific recruitment of transcriptional co-repressor Cabin1 by
RT   myocyte enhancer factor-2.";
RL   Nature 422:730-734(2003).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-93 IN COMPLEX WITH HDAC9 AND
RP   DNA.
RX   PubMed=15567413; DOI=10.1016/j.jmb.2004.10.033;
RA   Han A., He J., Wu Y., Liu J.O., Chen L.;
RT   "Mechanism of recruitment of class II histone deacetylases by myocyte
RT   enhancer factor-2.";
RL   J. Mol. Biol. 345:91-102(2005).
CC   -!- FUNCTION: Transcriptional activator which binds specifically to the
CC       MEF2 element, 5'-YTA[AT](4)TAR-3', found in numerous muscle-specific
CC       genes. Activates transcription via this element. May be involved in
CC       muscle-specific and/or growth factor-related transcription.
CC   -!- SUBUNIT: Interacts with HDAC7 (By similarity). Heterodimer. Interacts
CC       with HDAC9. {ECO:0000250, ECO:0000269|PubMed:15567413}.
CC   -!- INTERACTION:
CC       Q02080; Q9Y6J0: CABIN1; NbExp=3; IntAct=EBI-6427785, EBI-2795712;
CC       Q02080; P56524-2: HDAC4; NbExp=3; IntAct=EBI-6427785, EBI-11953488;
CC       Q02080; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-6427785, EBI-750487;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q02080-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q02080-2; Sequence=VSP_042322;
CC   -!- TISSUE SPECIFICITY: Expressed in skeletal and cardiac muscle and brain.
CC   -!- SIMILARITY: Belongs to the MEF2 family. {ECO:0000305}.
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DR   EMBL; X68502; CAA48515.1; -; mRNA.
DR   EMBL; X63380; CAA44978.1; -; mRNA.
DR   EMBL; AK301086; BAG62689.1; -; mRNA.
DR   EMBL; AK316328; BAH14699.1; -; mRNA.
DR   EMBL; AC002126; AAB86982.1; -; Genomic_DNA.
DR   EMBL; CH471106; EAW84788.1; -; Genomic_DNA.
DR   EMBL; BC126245; AAI26246.1; -; mRNA.
DR   EMBL; BC136457; AAI36458.1; -; mRNA.
DR   EMBL; BC171767; AAI71767.1; -; mRNA.
DR   CCDS; CCDS12394.1; -. [Q02080-1]
DR   CCDS; CCDS46024.1; -. [Q02080-2]
DR   PIR; A39481; A39481.
DR   RefSeq; NP_001139257.1; NM_001145785.1. [Q02080-2]
DR   RefSeq; NP_005910.1; NM_005919.3. [Q02080-1]
DR   PDB; 1N6J; X-ray; 2.20 A; A/B=2-94.
DR   PDB; 1TQE; X-ray; 2.70 A; P/Q/R/S=1-93.
DR   PDB; 6BYY; X-ray; 2.30 A; A/B/C/D=63-91.
DR   PDB; 6BZ1; X-ray; 2.97 A; A/B/C/D=65-91.
DR   PDB; 6C9L; X-ray; 2.30 A; A/B/C/D/E/F=1-93.
DR   PDB; 6WC2; X-ray; 2.10 A; A/B/C/D/I/J=1-8, A/B/C/D/I/J=73-91.
DR   PDB; 6WC5; X-ray; 2.90 A; A/B/C/D=2-91.
DR   PDBsum; 1N6J; -.
DR   PDBsum; 1TQE; -.
DR   PDBsum; 6BYY; -.
DR   PDBsum; 6BZ1; -.
DR   PDBsum; 6C9L; -.
DR   PDBsum; 6WC2; -.
DR   PDBsum; 6WC5; -.
DR   SMR; Q02080; -.
DR   BioGRID; 110371; 9.
DR   BioGRID; 938509; 10.
DR   IntAct; Q02080; 8.
DR   STRING; 9606.ENSP00000390762; -.
DR   iPTMnet; Q02080; -.
DR   PhosphoSitePlus; Q02080; -.
DR   BioMuta; MEF2B; -.
DR   DMDM; 1346514; -.
DR   MassIVE; Q02080; -.
DR   MaxQB; Q02080; -.
DR   PaxDb; Q02080; -.
DR   PeptideAtlas; Q02080; -.
DR   PRIDE; Q02080; -.
DR   ProteomicsDB; 58042; -. [Q02080-1]
DR   ProteomicsDB; 58043; -. [Q02080-2]
DR   Antibodypedia; 47983; 161 antibodies.
DR   DNASU; 4207; -.
DR   Ensembl; ENST00000424583; ENSP00000402154; ENSG00000213999. [Q02080-2]
DR   Ensembl; ENST00000444486; ENSP00000390762; ENSG00000213999. [Q02080-1]
DR   GeneID; 100271849; -.
DR   GeneID; 4207; -.
DR   KEGG; hsa:100271849; -.
DR   KEGG; hsa:4207; -.
DR   UCSC; uc002nll.3; human. [Q02080-1]
DR   CTD; 100271849; -.
DR   CTD; 4207; -.
DR   DisGeNET; 100271849; -.
DR   DisGeNET; 4207; -.
DR   GeneCards; MEF2B; -.
DR   HGNC; HGNC:6995; MEF2B.
DR   HPA; ENSG00000213999; Tissue enriched (lymphoid).
DR   MIM; 600661; gene.
DR   neXtProt; NX_Q02080; -.
DR   OpenTargets; ENSG00000213999; -.
DR   VEuPathDB; HostDB:ENSG00000213999; -.
DR   eggNOG; KOG0014; Eukaryota.
DR   GeneTree; ENSGT00940000160699; -.
DR   InParanoid; Q02080; -.
DR   PhylomeDB; Q02080; -.
DR   TreeFam; TF314067; -.
DR   PathwayCommons; Q02080; -.
DR   Reactome; R-HSA-525793; Myogenesis.
DR   BioGRID-ORCS; 100271849; 15 hits in 637 CRISPR screens.
DR   BioGRID-ORCS; 4207; 10 hits in 548 CRISPR screens.
DR   EvolutionaryTrace; Q02080; -.
DR   GeneWiki; MEF2B; -.
DR   Pharos; Q02080; Tbio.
DR   PRO; PR:Q02080; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; Q02080; protein.
DR   Bgee; ENSG00000213999; Expressed in muscle tissue and 113 other tissues.
DR   ExpressionAtlas; Q02080; baseline and differential.
DR   Genevisible; Q02080; HS.
DR   GO; GO:0030054; C:cell junction; IDA:HPA.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR   GO; GO:0005667; C:transcription regulator complex; IDA:BHF-UCL.
DR   GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:ProtInc.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR   GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR   GO; GO:0007517; P:muscle organ development; TAS:ProtInc.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd00265; MADS_MEF2_like; 1.
DR   Gene3D; 3.40.1810.10; -; 1.
DR   InterPro; IPR033896; MADS_MEF2-like.
DR   InterPro; IPR002100; TF_MADSbox.
DR   InterPro; IPR036879; TF_MADSbox_sf.
DR   Pfam; PF00319; SRF-TF; 1.
DR   PRINTS; PR00404; MADSDOMAIN.
DR   SMART; SM00432; MADS; 1.
DR   SUPFAM; SSF55455; SSF55455; 1.
DR   PROSITE; PS00350; MADS_BOX_1; 1.
DR   PROSITE; PS50066; MADS_BOX_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Alternative splicing; DNA-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..365
FT                   /note="Myocyte-specific enhancer factor 2B"
FT                   /id="PRO_0000199431"
FT   DOMAIN          3..57
FT                   /note="MADS-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00251"
FT   DNA_BIND        58..86
FT                   /note="Mef2-type"
FT                   /evidence="ECO:0000255"
FT   REGION          94..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          142..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          321..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..241
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..365
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         257..365
FT                   /note="VGAEAWARRVPQPAAPPRRPPQSASSLSASLRPPGAPATFLRPSPIPCSSPG
FT                   PWQSLCGLGPPCAGCPWPTAGPGRRSPGGTSPERSPGTARARGDPTSLQASSEKTQQ
FT                   -> EYGLGDPPPPPGLLQPPTLAPWQPSRGDGPPAVSSQPSGGRSLGEEGPPTRGASPP
FT                   TPPVSIKSERLSPAPGGPGDFPKTFPYPLLLARSLAEPLRPGPALRRLPLADGWPR
FT                   (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_042322"
FT   CONFLICT        195
FT                   /note="K -> R (in Ref. 3; BAG62689/BAH14699)"
FT                   /evidence="ECO:0000305"
FT   HELIX           14..39
FT                   /evidence="ECO:0007829|PDB:1N6J"
FT   STRAND          42..48
FT                   /evidence="ECO:0007829|PDB:1N6J"
FT   STRAND          54..60
FT                   /evidence="ECO:0007829|PDB:1N6J"
FT   HELIX           62..70
FT                   /evidence="ECO:0007829|PDB:1N6J"
FT   STRAND          77..79
FT                   /evidence="ECO:0007829|PDB:6WC2"
FT   HELIX           81..90
FT                   /evidence="ECO:0007829|PDB:6WC2"
SQ   SEQUENCE   365 AA;  38639 MW;  B12A19B1F659C7C7 CRC64;
     MGRKKIQISR ILDQRNRQVT FTKRKFGLMK KAYELSVLCD CEIALIIFNS ANRLFQYAST
     DMDRVLLKYT EYSEPHESRT NTDILETLKR RGIGLDGPEL EPDEGPEEPG EKFRRLAGEG
     GDPALPRPRL YPAAPAMPSP DVVYGALPPP GCDPSGLGEA LPAQSRPSPF RPAAPKAGPP
     GLVHPLFSPS HLTSKTPPPL YLPTEGRRSD LPGGLAGPRG GLNTSRSLYS GLQNPCSTAT
     PGPPLGSFPF LPGGPPVGAE AWARRVPQPA APPRRPPQSA SSLSASLRPP GAPATFLRPS
     PIPCSSPGPW QSLCGLGPPC AGCPWPTAGP GRRSPGGTSP ERSPGTARAR GDPTSLQASS
     EKTQQ
//
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