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Class A basic helix-loop-helix protein 15 (bHLHa15) (Class B basic helix-loop-helix protein 8) (bHLHb8) (Muscle, intestine and stomach expression 1) (MIST-1)

 BHA15_HUMAN             Reviewed;         189 AA.
Q7RTS1; A4D271; Q14DE4;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
15-DEC-2003, sequence version 1.
25-OCT-2017, entry version 115.
RecName: Full=Class A basic helix-loop-helix protein 15;
Short=bHLHa15;
AltName: Full=Class B basic helix-loop-helix protein 8;
Short=bHLHb8;
AltName: Full=Muscle, intestine and stomach expression 1;
Short=MIST-1;
Name=BHLHA15; Synonyms=BHLHB8, MIST1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
IDENTIFICATION, AND TISSUE SPECIFICITY.
PubMed=14516699; DOI=10.1016/S0925-4773(03)00130-8;
McLellan A.S., Langlands K., Kealey T.;
"Exhaustive identification of human class II basic helix-loop-helix
proteins by virtual library screening.";
Mech. Dev. 119:S285-S291(2002).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
-!- FUNCTION: Plays a role in controlling the transcriptional activity
of MYOD1, ensuring that expanding myoblast populations remain
undifferentiated. Repression may occur through muscle-specific E-
box occupancy by homodimers. May also negatively regulate bHLH-
mediated transcription through an N-terminal repressor domain.
Serves as a key regulator of acinar cell function, stability, and
identity. Also required for normal organelle localization in
exocrine cells and for mitochondrial calcium ion transport. May
function as a unique regulator of gene expression in several
different embryonic and postnatal cell lineages. Binds to the E-
box consensus sequence 5'-CANNTG-3' (By similarity).
{ECO:0000250|UniProtKB:Q9QYC3}.
-!- SUBUNIT: Forms homodimers or heterodimers with TCF3 gene products
E12 and E47. These dimers bind to the E-box site, however,
heterodimer with MYOD1 does not bind target DNA (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in brain, liver, spleen and skeletal
muscle. {ECO:0000269|PubMed:14516699}.
-!- DOMAIN: Lacks a classic transcription activation domain and
instead possesses an N-terminal region capable of inhibiting
heterologous activators. {ECO:0000250}.
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EMBL; AC025605; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH236956; EAL23893.1; -; Genomic_DNA.
EMBL; BC113394; AAI13395.1; -; mRNA.
EMBL; BC113396; AAI13397.1; -; mRNA.
EMBL; BK000276; DAA01056.1; -; mRNA.
CCDS; CCDS5655.1; -.
RefSeq; NP_803238.1; NM_177455.3.
UniGene; Hs.511979; -.
UniGene; Hs.674510; -.
ProteinModelPortal; Q7RTS1; -.
SMR; Q7RTS1; -.
BioGrid; 127970; 45.
IntAct; Q7RTS1; 2.
STRING; 9606.ENSP00000326391; -.
iPTMnet; Q7RTS1; -.
PhosphoSitePlus; Q7RTS1; -.
BioMuta; BHLHA15; -.
DMDM; 50400944; -.
EPD; Q7RTS1; -.
MaxQB; Q7RTS1; -.
PaxDb; Q7RTS1; -.
PeptideAtlas; Q7RTS1; -.
PRIDE; Q7RTS1; -.
Ensembl; ENST00000314018; ENSP00000326391; ENSG00000180535.
Ensembl; ENST00000609256; ENSP00000476312; ENSG00000180535.
GeneID; 168620; -.
KEGG; hsa:168620; -.
UCSC; uc003upe.2; human.
CTD; 168620; -.
DisGeNET; 168620; -.
EuPathDB; HostDB:ENSG00000180535.3; -.
GeneCards; BHLHA15; -.
HGNC; HGNC:22265; BHLHA15.
HPA; CAB034083; -.
HPA; HPA047834; -.
MIM; 608606; gene.
neXtProt; NX_Q7RTS1; -.
OpenTargets; ENSG00000180535; -.
PharmGKB; PA164716601; -.
eggNOG; ENOG410IQ4H; Eukaryota.
eggNOG; ENOG4111ZMK; LUCA.
GeneTree; ENSGT00680000099860; -.
HOGENOM; HOG000095227; -.
InParanoid; Q7RTS1; -.
KO; K08040; -.
OMA; HRYSTQI; -.
OrthoDB; EOG091G15AI; -.
PhylomeDB; Q7RTS1; -.
TreeFam; TF315153; -.
GeneWiki; BHLHB8; -.
GenomeRNAi; 168620; -.
PRO; PR:Q7RTS1; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000180535; -.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IEA:Ensembl.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IEA:Ensembl.
GO; GO:0019722; P:calcium-mediated signaling; IEA:Ensembl.
GO; GO:0048469; P:cell maturation; IEA:Ensembl.
GO; GO:0007267; P:cell-cell signaling; IEA:Ensembl.
GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB.
GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISS:UniProtKB.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IEA:Ensembl.
GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
GO; GO:0007030; P:Golgi organization; IEA:Ensembl.
GO; GO:0048312; P:intracellular distribution of mitochondria; IEA:Ensembl.
GO; GO:0006851; P:mitochondrial calcium ion transmembrane transport; IEA:Ensembl.
GO; GO:0010832; P:negative regulation of myotube differentiation; ISS:UniProtKB.
CDD; cd00083; HLH; 1.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR036638; HLH_DNA-bd_sf.
Pfam; PF00010; HLH; 1.
SMART; SM00353; HLH; 1.
SUPFAM; SSF47459; SSF47459; 1.
PROSITE; PS50888; BHLH; 1.
1: Evidence at protein level;
Complete proteome; DNA-binding; Nucleus; Phosphoprotein;
Reference proteome; Repressor; Transcription;
Transcription regulation.
CHAIN 1 189 Class A basic helix-loop-helix protein
15.
/FTId=PRO_0000127150.
DOMAIN 75 127 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
MOD_RES 25 25 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9QYC3}.
SEQUENCE 189 AA; 20818 MW; 38D7230D85F16D22 CRC64;
MKTKNRPPRR RAPVQDTEAT PGEGTPDGSL PNPGPEPAKG LRSRPARAAA RAPGEGRRRR
PGPSGPGGRR DSSIQRRLES NERERQRMHK LNNAFQALRE VIPHVRADKK LSKIETLTLA
KNYIKSLTAT ILTMSSSRLP GLEGPGPKLY QHYQQQQQVA GGALGATEAQ PQGHLQRYST
QIHSFREGT


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