MRTFB_HUMAN
ID MRTFB_HUMAN Reviewed; 1088 AA.
AC Q9ULH7; A6ND53; B4DGT8; Q68CT1; Q6UB16; Q86WW2; Q8N226;
DT 27-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2003, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Myocardin-related transcription factor B {ECO:0000305};
DE Short=MRTF-B {ECO:0000305};
DE AltName: Full=MKL/myocardin-like protein 2;
DE AltName: Full=Megakaryoblastic leukemia 2 {ECO:0000303|PubMed:14565952};
GN Name=MRTFB {ECO:0000312|HGNC:HGNC:29819};
GN Synonyms=KIAA1243, MKL2 {ECO:0000303|PubMed:14565952};
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 4), FUNCTION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH MRTFA AND SRF.
RC TISSUE=Cervix carcinoma;
RX PubMed=14565952; DOI=10.1074/jbc.m305679200;
RA Selvaraj A., Prywes R.;
RT "Megakaryoblastic leukemia-1/2, a transcriptional co-activator of serum
RT response factor, is required for skeletal myogenic differentiation.";
RL J. Biol. Chem. 278:41977-41987(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).
RC TISSUE=Brain, and Thymus;
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].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5).
RC TISSUE=Brain, Medulla oblongata, 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 261-1088 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [7]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 415-1088 (ISOFORM 1).
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; THR-367; THR-370 AND
RP SER-921, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP CHROMOSOMAL TRANSLOCATION WITH ZFTA.
RX PubMed=20607705; DOI=10.1002/gcc.20788;
RA Huang D., Sumegi J., Dal Cin P., Reith J.D., Yasuda T., Nelson M.,
RA Muirhead D., Bridge J.A.;
RT "C11orf95-MKL2 is the resulting fusion oncogene of t(11;16)(q13;p13) in
RT chondroid lipoma.";
RL Genes Chromosomes Cancer 49:810-818(2010).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-541, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-543 AND SER-921, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 (ISOFORMS 4 AND 5), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-628, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [17]
RP VARIANT GLY-390.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
CC -!- FUNCTION: Acts as a transcriptional coactivator of serum response
CC factor (SRF). Required for skeletal myogenic differentiation.
CC {ECO:0000269|PubMed:14565952}.
CC -!- SUBUNIT: Interacts with MRTFA and SRF. {ECO:0000269|PubMed:14565952}.
CC -!- INTERACTION:
CC Q9ULH7; O00629: KPNA4; NbExp=3; IntAct=EBI-493007, EBI-396343;
CC Q9ULH7; P11831: SRF; NbExp=3; IntAct=EBI-493007, EBI-493034;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9ULH7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ULH7-2; Sequence=VSP_007653, VSP_007654, VSP_007655;
CC Name=3;
CC IsoId=Q9ULH7-3; Sequence=VSP_007656, VSP_007657;
CC Name=4;
CC IsoId=Q9ULH7-4; Sequence=VSP_013355, VSP_013356;
CC Name=5;
CC IsoId=Q9ULH7-5; Sequence=VSP_013355;
CC -!- DOMAIN: The N-terminal region is required for nuclear localization and
CC the C-terminal region mediates transcriptional activity. {ECO:0000250}.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- DISEASE: Note=A chromosomal aberration involving ZFTA is found in 3
CC chondroid lipomas. Translocation t(11;16)(q13;p13) with ZFTA produces a
CC ZFTA-MRTFB fusion protein (PubMed:20607705).
CC {ECO:0000269|PubMed:20607705}.
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DR EMBL; AY374297; AAQ82435.1; -; mRNA.
DR EMBL; AK093577; BAC04200.1; -; mRNA.
DR EMBL; AK294765; BAG57899.1; -; mRNA.
DR EMBL; AC012626; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC040173; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC130650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85112.1; -; Genomic_DNA.
DR EMBL; BC047761; AAH47761.1; -; mRNA.
DR EMBL; BC136260; AAI36261.1; -; mRNA.
DR EMBL; BC171750; AAI71750.1; -; mRNA.
DR EMBL; AB033069; BAA86557.2; -; mRNA.
DR EMBL; CR749797; CAH18657.1; -; mRNA.
DR CCDS; CCDS32391.1; -. [Q9ULH7-4]
DR CCDS; CCDS76823.1; -. [Q9ULH7-5]
DR RefSeq; NP_001295071.1; NM_001308142.1. [Q9ULH7-5]
DR RefSeq; NP_054767.3; NM_014048.4. [Q9ULH7-4]
DR RefSeq; XP_005255509.1; XM_005255452.3. [Q9ULH7-5]
DR RefSeq; XP_005255510.1; XM_005255453.4. [Q9ULH7-5]
DR RefSeq; XP_005255512.1; XM_005255455.3.
DR RefSeq; XP_006720971.1; XM_006720908.3. [Q9ULH7-5]
DR RefSeq; XP_006720972.1; XM_006720909.3. [Q9ULH7-5]
DR RefSeq; XP_006720977.1; XM_006720914.2. [Q9ULH7-4]
DR RefSeq; XP_011520870.1; XM_011522568.2. [Q9ULH7-5]
DR RefSeq; XP_016878990.1; XM_017023501.1. [Q9ULH7-5]
DR RefSeq; XP_016878991.1; XM_017023502.1. [Q9ULH7-5]
DR AlphaFoldDB; Q9ULH7; -.
DR SMR; Q9ULH7; -.
DR BioGRID; 121563; 38.
DR ELM; Q9ULH7; -.
DR IntAct; Q9ULH7; 19.
DR MINT; Q9ULH7; -.
DR STRING; 9606.ENSP00000339086; -.
DR GlyGen; Q9ULH7; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9ULH7; -.
DR MetOSite; Q9ULH7; -.
DR PhosphoSitePlus; Q9ULH7; -.
DR BioMuta; MKL2; -.
DR DMDM; 32363203; -.
DR EPD; Q9ULH7; -.
DR jPOST; Q9ULH7; -.
DR MassIVE; Q9ULH7; -.
DR MaxQB; Q9ULH7; -.
DR PaxDb; Q9ULH7; -.
DR PeptideAtlas; Q9ULH7; -.
DR PRIDE; Q9ULH7; -.
DR ProteomicsDB; 4158; -.
DR ProteomicsDB; 85028; -. [Q9ULH7-1]
DR ProteomicsDB; 85029; -. [Q9ULH7-2]
DR ProteomicsDB; 85030; -. [Q9ULH7-3]
DR ProteomicsDB; 85031; -. [Q9ULH7-4]
DR Antibodypedia; 1832; 123 antibodies from 25 providers.
DR DNASU; 57496; -.
DR Ensembl; ENST00000318282.9; ENSP00000339086.4; ENSG00000186260.17. [Q9ULH7-4]
DR Ensembl; ENST00000571589.6; ENSP00000459626.2; ENSG00000186260.17. [Q9ULH7-5]
DR Ensembl; ENST00000573051.1; ENSP00000460589.1; ENSG00000186260.17. [Q9ULH7-2]
DR Ensembl; ENST00000574045.5; ENSP00000459205.1; ENSG00000186260.17. [Q9ULH7-4]
DR GeneID; 57496; -.
DR KEGG; hsa:57496; -.
DR MANE-Select; ENST00000571589.6; ENSP00000459626.2; NM_001308142.2; NP_001295071.1. [Q9ULH7-5]
DR UCSC; uc002dcg.4; human. [Q9ULH7-1]
DR CTD; 57496; -.
DR DisGeNET; 57496; -.
DR GeneCards; MRTFB; -.
DR HGNC; HGNC:29819; MRTFB.
DR HPA; ENSG00000186260; Low tissue specificity.
DR MIM; 609463; gene.
DR neXtProt; NX_Q9ULH7; -.
DR OpenTargets; ENSG00000186260; -.
DR PharmGKB; PA134981329; -.
DR VEuPathDB; HostDB:ENSG00000186260; -.
DR eggNOG; ENOG502QU1Z; Eukaryota.
DR GeneTree; ENSGT00950000182979; -.
DR HOGENOM; CLU_007042_0_0_1; -.
DR InParanoid; Q9ULH7; -.
DR OMA; TMCNNTA; -.
DR OrthoDB; 190145at2759; -.
DR PhylomeDB; Q9ULH7; -.
DR TreeFam; TF326024; -.
DR PathwayCommons; Q9ULH7; -.
DR SignaLink; Q9ULH7; -.
DR SIGNOR; Q9ULH7; -.
DR BioGRID-ORCS; 57496; 7 hits in 1083 CRISPR screens.
DR ChiTaRS; MKL2; human.
DR GeneWiki; MKL2; -.
DR GenomeRNAi; 57496; -.
DR Pharos; Q9ULH7; Tbio.
DR PRO; PR:Q9ULH7; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9ULH7; protein.
DR Bgee; ENSG00000186260; Expressed in Brodmann (1909) area 23 and 207 other tissues.
DR ExpressionAtlas; Q9ULH7; baseline and differential.
DR Genevisible; Q9ULH7; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IGI:ARUK-UCL.
DR GO; GO:0045844; P:positive regulation of striated muscle tissue development; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0051145; P:smooth muscle cell differentiation; IBA:GO_Central.
DR Gene3D; 1.10.720.30; -; 1.
DR InterPro; IPR043451; Myocardin-like.
DR InterPro; IPR004018; RPEL_repeat.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR PANTHER; PTHR22793; PTHR22793; 1.
DR Pfam; PF02755; RPEL; 2.
DR Pfam; PF02037; SAP; 1.
DR SMART; SM00707; RPEL; 3.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS51073; RPEL; 3.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Chromosomal rearrangement; Coiled coil;
KW Developmental protein; Differentiation; Glycoprotein; Isopeptide bond;
KW Myogenesis; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1088
FT /note="Myocardin-related transcription factor B"
FT /id="PRO_0000126628"
FT REPEAT 40..65
FT /note="RPEL 1"
FT REPEAT 84..109
FT /note="RPEL 2"
FT REPEAT 128..153
FT /note="RPEL 3"
FT DOMAIN 389..423
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT REGION 165..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..591
FT /note="Required for interaction with itself and with MRTFA"
FT REGION 595..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 545..601
FT /evidence="ECO:0000255"
FT COMPBIAS 177..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..249
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..293
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..645
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 394
FT /note="Breakpoint for translocation to form ZFTA-MRTFB
FT fusion protein"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 367
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 370
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 921
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 628
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0007744|PubMed:25114211"
FT VAR_SEQ 1..41
FT /note="MIDSSKKQQQGFPEILTAGDFEPLKEKECLEGSNQKSLKEV -> M (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007653"
FT VAR_SEQ 1..40
FT /note="MIDSSKKQQQGFPEILTAGDFEPLKEKECLEGSNQKSLKE -> MDHTGAID
FT TEDEVGPLAHLAPSPQSEAVAHEFQELSLQSSQNLPPLNERKN (in isoform 4
FT and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14565952,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334"
FT /id="VSP_013355"
FT VAR_SEQ 350..461
FT /note="PLNDKNSNSGNSALNNATPNTPRQNTSTPVRKPGPLPSSLDDLKVSELKTEL
FT KLRGLPVSGTKPDLIERLKPYQEVNSSGLAAGGIVAVSSSAIVTSNPEVTVALPVTTLH
FT N -> YGGAHAILNAGFSVVFMRNYKLPKVECCHLFVLSNDFHFFVIRAYHTVSEVHMV
FT RVACIPFQFLSSKIGSEFLQVRNAFSQLFIQICLLLEHQNSTRCSEKSVSSIIPGINS
FT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_007656"
FT VAR_SEQ 350..418
FT /note="PLNDKNSNSGNSALNNATPNTPRQNTSTPVRKPGPLPSSLDDLKVSELKTEL
FT KLRGLPVSGTKPDLIER -> AYHTVSEVHMVRVACIPFQFLSSKIGSEFLQVRNAFSQ
FT LFIQICLLLEHQNSTRCSEKSVSSIIPGINS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007654"
FT VAR_SEQ 419..1088
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007655"
FT VAR_SEQ 462..1088
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_007657"
FT VAR_SEQ 689..738
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14565952"
FT /id="VSP_013356"
FT VARIANT 390
FT /note="D -> G (found in a renal cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064732"
FT CONFLICT 266
FT /note="K -> R (in Ref. 2; BAC04200)"
FT /evidence="ECO:0000305"
FT CONFLICT 350
FT /note="P -> A (in Ref. 1; AAQ82435)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="E -> G (in Ref. 8; CAH18657)"
FT /evidence="ECO:0000305"
FT CONFLICT 598
FT /note="Q -> R (in Ref. 1; AAQ82435)"
FT /evidence="ECO:0000305"
FT CONFLICT 629
FT /note="D -> G (in Ref. 1; AAQ82435)"
FT /evidence="ECO:0000305"
FT MOD_RES Q9ULH7-4:22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES Q9ULH7-5:22
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
SQ SEQUENCE 1088 AA; 118127 MW; 0CA4A52A115C0C83 CRC64;
MIDSSKKQQQ GFPEILTAGD FEPLKEKECL EGSNQKSLKE VLQLRLQQRR TREQLVDQGI
MPPLKSPAAF HEQIKSLERA RTENFLKHKI RSRPDRSELV RMHILEETFA EPSLQATQMK
LKRARLADDL NEKIAQRPGP MELVEKNILP VDSSVKEAII GVGKEDYPHT QGDFSFDEDS
SDALSPDQPA SQESQGSAAS PSEPKVSESP SPVTTNTPAQ FASVSPTVPE FLKTPPTADQ
PPPRPAAPVL PTNTVSSAKP GPALVKQSHP KNPNDKHRSK KCKDPKPRVK KLKYHQYIPP
DQKGEKNEPQ MDSNYARLLQ QQQLFLQLQI LSQQKQHYNY QTILPAPFKP LNDKNSNSGN
SALNNATPNT PRQNTSTPVR KPGPLPSSLD DLKVSELKTE LKLRGLPVSG TKPDLIERLK
PYQEVNSSGL AAGGIVAVSS SAIVTSNPEV TVALPVTTLH NTVTSSVSTL KAELPPTGTS
NATRVENVHS PLPISPSPSE QSSLSTDDTN MADTFTEIMT MMSPSQFLSS SPLRMTNNED
SLSPTSSTLS NLELDAAEKD RKLQEKEKQI EELKRKLEQE QKLVEVLKMQ LEVEKRGQQQ
RPLEAQPSAP GHSVKSDQKH GSLGSSIKDE ASLPDCSSSR QPIPVASHAV GQPVSTGGQT
LVAKKAVVIK QEVPVGQAEQ QSVVSQFYVS SQGQPPPAVV AQPQALLTTQ TAQLLLPVSI
QGSSVTSVQL PVGSLKLQTS PQAGMQTQPQ IATAAQIPTA ALASGLAPTV PQTQDTFPQH
VLSQPQQVRK VFTNSASSNT VLPYQRHPAP AVQQPFINKA SNSVLQSRNA PLPSLQNGPN
TPNKPSSPPP PQQFVVQHSL FGSPVAKTKD PPRYEEAIKQ TRSTQAPLPE ISNAHSQQMD
DLFDILIKSG EISLPIKEEP SPISKMRPVT ASITTMPVNT VVSRPPPQVQ MAPPVSLEPM
GSLSASLENQ LEAFLDGTLP SANEIPPLQS SSEDREPFSL IEDLQNDLLS HSGMLDHSHS
PMETSETQFA AGTPCLSLDL SDSNLDNMEW LDITMPNSSS GLTPLSTTAP SMFSADFLDP
QDLPLPWD
