MASTR_HUMAN
ID MASTR_HUMAN Reviewed; 415 AA.
AC Q6ZN01; B7ZKX4; Q3KQU9; Q8N9Y3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=MEF2-activating motif and SAP domain-containing transcriptional regulator;
DE AltName: Full=MEF2-activating SAP transcriptional regulatory protein;
GN Name=MAMSTR; Synonyms=MASTR;
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] (ISOFORMS 1 AND 2).
RC TISSUE=Skeletal muscle, 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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Brain, and Uterus;
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 [4]
RP TISSUE SPECIFICITY.
RX PubMed=16818234; DOI=10.1016/j.molcel.2006.05.026;
RA Creemers E.E., Sutherland L.B., Oh J., Barbosa A.C., Olson E.N.;
RT "Coactivation of MEF2 by the SAP domain proteins myocardin and MASTR.";
RL Mol. Cell 23:83-96(2006).
CC -!- FUNCTION: Transcriptional coactivator. Stimulates the transcriptional
CC activity of MEF2C. Stimulates MYOD1 activity in part via MEF2,
CC resulting in an enhancement of skeletal muscle differentiation (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with MEF2C. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6ZN01-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZN01-2; Sequence=VSP_031554;
CC Name=3;
CC IsoId=Q6ZN01-3; Sequence=VSP_031554, VSP_031555;
CC -!- TISSUE SPECIFICITY: Expressed in skeletal muscle, brain, placenta and
CC spleen. {ECO:0000269|PubMed:16818234}.
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DR EMBL; AK093389; BAC04152.1; -; mRNA.
DR EMBL; AK131427; BAD18574.1; -; mRNA.
DR EMBL; CH471177; EAW52390.1; -; Genomic_DNA.
DR EMBL; CH471177; EAW52392.1; -; Genomic_DNA.
DR EMBL; BC105056; AAI05057.1; -; mRNA.
DR EMBL; BC105058; AAI05059.1; -; mRNA.
DR EMBL; BC106047; AAI06048.1; -; mRNA.
DR EMBL; BC143443; AAI43444.1; -; mRNA.
DR CCDS; CCDS12730.1; -. [Q6ZN01-2]
DR CCDS; CCDS46137.1; -. [Q6ZN01-1]
DR CCDS; CCDS74415.1; -. [Q6ZN01-3]
DR RefSeq; NP_001124387.1; NM_001130915.1. [Q6ZN01-1]
DR RefSeq; NP_001284682.1; NM_001297753.1. [Q6ZN01-3]
DR RefSeq; NP_872380.1; NM_182574.2. [Q6ZN01-2]
DR RefSeq; XP_011525109.1; XM_011526807.2. [Q6ZN01-2]
DR RefSeq; XP_011525111.1; XM_011526809.2. [Q6ZN01-3]
DR RefSeq; XP_016882134.1; XM_017026645.1.
DR AlphaFoldDB; Q6ZN01; -.
DR SMR; Q6ZN01; -.
DR IntAct; Q6ZN01; 1.
DR STRING; 9606.ENSP00000324175; -.
DR iPTMnet; Q6ZN01; -.
DR PhosphoSitePlus; Q6ZN01; -.
DR BioMuta; MAMSTR; -.
DR DMDM; 74722919; -.
DR MassIVE; Q6ZN01; -.
DR PaxDb; Q6ZN01; -.
DR PeptideAtlas; Q6ZN01; -.
DR PRIDE; Q6ZN01; -.
DR ProteomicsDB; 67946; -. [Q6ZN01-1]
DR ProteomicsDB; 67947; -. [Q6ZN01-2]
DR Antibodypedia; 45786; 88 antibodies from 14 providers.
DR DNASU; 284358; -.
DR Ensembl; ENST00000318083.11; ENSP00000324175.5; ENSG00000176909.12. [Q6ZN01-1]
DR Ensembl; ENST00000356751.8; ENSP00000349192.3; ENSG00000176909.12. [Q6ZN01-2]
DR Ensembl; ENST00000594582.1; ENSP00000471590.1; ENSG00000176909.12. [Q6ZN01-3]
DR GeneID; 284358; -.
DR KEGG; hsa:284358; -.
DR MANE-Select; ENST00000318083.11; ENSP00000324175.5; NM_001130915.2; NP_001124387.1.
DR UCSC; uc002pkf.3; human. [Q6ZN01-1]
DR CTD; 284358; -.
DR DisGeNET; 284358; -.
DR GeneCards; MAMSTR; -.
DR HGNC; HGNC:26689; MAMSTR.
DR HPA; ENSG00000176909; Group enriched (adrenal gland, skeletal muscle, tongue).
DR MIM; 610349; gene.
DR neXtProt; NX_Q6ZN01; -.
DR OpenTargets; ENSG00000176909; -.
DR PharmGKB; PA165393645; -.
DR VEuPathDB; HostDB:ENSG00000176909; -.
DR eggNOG; ENOG502RJE6; Eukaryota.
DR GeneTree; ENSGT00940000154181; -.
DR HOGENOM; CLU_055830_0_0_1; -.
DR InParanoid; Q6ZN01; -.
DR OMA; PKISQHW; -.
DR OrthoDB; 1127316at2759; -.
DR PhylomeDB; Q6ZN01; -.
DR PathwayCommons; Q6ZN01; -.
DR SignaLink; Q6ZN01; -.
DR BioGRID-ORCS; 284358; 15 hits in 1075 CRISPR screens.
DR ChiTaRS; MAMSTR; human.
DR GenomeRNAi; 284358; -.
DR Pharos; Q6ZN01; Tbio.
DR PRO; PR:Q6ZN01; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q6ZN01; protein.
DR Bgee; ENSG00000176909; Expressed in hindlimb stylopod muscle and 120 other tissues.
DR ExpressionAtlas; Q6ZN01; baseline and differential.
DR Genevisible; Q6ZN01; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0010831; P:positive regulation of myotube differentiation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 1.10.720.30; -; 1.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR Pfam; PF02037; SAP; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR PROSITE; PS50800; SAP; 1.
PE 2: Evidence at transcript level;
KW Activator; Alternative splicing; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..415
FT /note="MEF2-activating motif and SAP domain-containing
FT transcriptional regulator"
FT /id="PRO_0000319981"
FT DOMAIN 172..206
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT REGION 28..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..415
FT /note="Transcription activation"
FT /evidence="ECO:0000250"
FT MOTIF 12..28
FT /note="MEF2-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 74..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..163
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..277
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..103
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_031554"
FT VAR_SEQ 178..242
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031555"
FT CONFLICT 271
FT /note="A -> T (in Ref. 3; AAI06048)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 415 AA; 44632 MW; 61D6E8C60DCC2DE7 CRC64;
MTLAASSQRS QIIRSKFRSV LQLRIHRRNQ EQISDPDPWI SASDPPLAPA LPSGTAPFLF
SPGVLLPEPE YCPPWRSPKK ESPKISQRWR ESKPRGNLTY HQYMPPEPRQ GSRADPQAEG
SALGPPGPSL WEGTDSQQPH PRMKPSPLTP CPPGVPSPSP PPHKLELQTL KLEELTVSEL
RQQLRLRGLP VSGTKSMLLE RMRGGAPPRE RPKPRREDSP AGAPWPRLKP KALAAARRQG
SVKPSAASHR PPLPRAADTP GTAPAPTPTP APAAAPALTP SSGPGSAALT LEEELQEAIR
RAQLLPNRGI DDILEDQVEP DDPLPPIPLD FPGSFDVLSP SPDSEGLSSV FSSSLPSPTN
SSSPSPRDPT DSLDWLEALS GGPPLGSGPP PPSIFSADLS DSSSSRLWDL LEDPW
