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   27-MAR-2024, entry version 186.
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; 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.
DR   RefSeq; XP_005255512.1; XM_005255455.3.
DR   RefSeq; XP_006720971.1; XM_006720908.3.
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; 54.
DR   ELM; Q9ULH7; -.
DR   IntAct; Q9ULH7; 20.
DR   MINT; Q9ULH7; -.
DR   STRING; 9606.ENSP00000459626; -.
DR   GlyCosmos; Q9ULH7; 1 site, 1 glycan.
DR   GlyGen; Q9ULH7; 5 sites, 1 O-linked glycan (5 sites).
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; 9606-ENSP00000339086; -.
DR   PeptideAtlas; 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   Pumba; Q9ULH7; -.
DR   Antibodypedia; 1832; 138 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   AGR; HGNC:29819; -.
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; 2997330at2759; -.
DR   PhylomeDB; Q9ULH7; -.
DR   TreeFam; TF326024; -.
DR   PathwayCommons; Q9ULH7; -.
DR   SignaLink; Q9ULH7; -.
DR   SIGNOR; Q9ULH7; -.
DR   BioGRID-ORCS; 57496; 7 hits in 1161 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 209 other cell types or tissues.
DR   ExpressionAtlas; Q9ULH7; baseline and differential.
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; 6.10.140.2040; -; 1.
DR   Gene3D; 6.10.150.10; -; 1.
DR   Gene3D; 1.10.720.30; SAP domain; 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:SF5; MYOCARDIN-RELATED TRANSCRIPTION FACTOR B; 1.
DR   PANTHER; PTHR22793; MYOCARDIN-RELATED TRANSCRIPTION FACTOR-RELATED; 1.
DR   Pfam; PF02755; RPEL; 2.
DR   Pfam; PF02037; SAP; 1.
DR   SMART; SM00707; RPEL; 3.
DR   SMART; SM00513; SAP; 1.
DR   SUPFAM; SSF68906; SAP domain; 1.
DR   PROSITE; PS51073; RPEL; 3.
DR   PROSITE; PS50800; SAP; 1.
DR   Genevisible; Q9ULH7; HS.
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
//