BHA15_HUMAN
ID BHA15_HUMAN Reviewed; 189 AA.
AC Q7RTS1; A4D271; Q14DE4;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Class A basic helix-loop-helix protein 15;
DE Short=bHLHa15;
DE AltName: Full=Class B basic helix-loop-helix protein 8;
DE Short=bHLHb8;
DE AltName: Full=Muscle, intestine and stomach expression 1;
DE Short=MIST-1;
GN Name=BHLHA15; Synonyms=BHLHB8, MIST1;
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 GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=14516699; DOI=10.1016/s0925-4773(03)00130-8;
RA McLellan A.S., Langlands K., Kealey T.;
RT "Exhaustive identification of human class II basic helix-loop-helix
RT proteins by virtual library screening.";
RL Mech. Dev. 119:S285-S291(2002).
RN [5]
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).
CC -!- FUNCTION: Plays a role in controlling the transcriptional activity of
CC MYOD1, ensuring that expanding myoblast populations remain
CC undifferentiated. Repression may occur through muscle-specific E-box
CC occupancy by homodimers. May also negatively regulate bHLH-mediated
CC transcription through an N-terminal repressor domain. Serves as a key
CC regulator of acinar cell function, stability, and identity. Also
CC required for normal organelle localization in exocrine cells and for
CC mitochondrial calcium ion transport. May function as a unique regulator
CC of gene expression in several different embryonic and postnatal cell
CC lineages. Binds to the E-box consensus sequence 5'-CANNTG-3' (By
CC similarity). {ECO:0000250|UniProtKB:Q9QYC3}.
CC -!- SUBUNIT: Forms homodimers or heterodimers with TCF3 gene products E12
CC and E47. These dimers bind to the E-box site, however, heterodimer with
CC MYOD1 does not bind target DNA (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q7RTS1; P15173: MYOG; NbExp=3; IntAct=EBI-8844218, EBI-3906629;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in brain, liver, spleen and skeletal
CC muscle. {ECO:0000269|PubMed:14516699}.
CC -!- DOMAIN: Lacks a classic transcription activation domain and instead
CC possesses an N-terminal region capable of inhibiting heterologous
CC activators. {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC025605; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236956; EAL23893.1; -; Genomic_DNA.
DR EMBL; BC113394; AAI13395.1; -; mRNA.
DR EMBL; BC113396; AAI13397.1; -; mRNA.
DR EMBL; BK000276; DAA01056.1; -; mRNA.
DR CCDS; CCDS5655.1; -.
DR RefSeq; NP_803238.1; NM_177455.3.
DR AlphaFoldDB; Q7RTS1; -.
DR SMR; Q7RTS1; -.
DR BioGRID; 127970; 73.
DR IntAct; Q7RTS1; 43.
DR MINT; Q7RTS1; -.
DR STRING; 9606.ENSP00000476312; -.
DR iPTMnet; Q7RTS1; -.
DR PhosphoSitePlus; Q7RTS1; -.
DR BioMuta; BHLHA15; -.
DR DMDM; 50400944; -.
DR jPOST; Q7RTS1; -.
DR MassIVE; Q7RTS1; -.
DR MaxQB; Q7RTS1; -.
DR PaxDb; Q7RTS1; -.
DR PeptideAtlas; Q7RTS1; -.
DR PRIDE; Q7RTS1; -.
DR ProteomicsDB; 68891; -.
DR Antibodypedia; 30223; 125 antibodies from 25 providers.
DR DNASU; 168620; -.
DR Ensembl; ENST00000314018.2; ENSP00000326391.2; ENSG00000180535.4.
DR Ensembl; ENST00000609256.2; ENSP00000476312.1; ENSG00000180535.4.
DR GeneID; 168620; -.
DR KEGG; hsa:168620; -.
DR MANE-Select; ENST00000609256.2; ENSP00000476312.1; NM_177455.4; NP_803238.1.
DR UCSC; uc003upe.2; human.
DR CTD; 168620; -.
DR DisGeNET; 168620; -.
DR GeneCards; BHLHA15; -.
DR HGNC; HGNC:22265; BHLHA15.
DR HPA; ENSG00000180535; Group enriched (pancreas, salivary gland).
DR MIM; 608606; gene.
DR neXtProt; NX_Q7RTS1; -.
DR OpenTargets; ENSG00000180535; -.
DR PharmGKB; PA164716601; -.
DR VEuPathDB; HostDB:ENSG00000180535; -.
DR eggNOG; KOG3898; Eukaryota.
DR GeneTree; ENSGT00940000161824; -.
DR HOGENOM; CLU_097977_2_0_1; -.
DR InParanoid; Q7RTS1; -.
DR OMA; HRYSTQI; -.
DR OrthoDB; 1528350at2759; -.
DR PhylomeDB; Q7RTS1; -.
DR TreeFam; TF315153; -.
DR PathwayCommons; Q7RTS1; -.
DR SignaLink; Q7RTS1; -.
DR BioGRID-ORCS; 168620; 52 hits in 1091 CRISPR screens.
DR GeneWiki; BHLHB8; -.
DR GenomeRNAi; 168620; -.
DR Pharos; Q7RTS1; Tbio.
DR PRO; PR:Q7RTS1; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q7RTS1; protein.
DR Bgee; ENSG00000180535; Expressed in parotid gland and 101 other tissues.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:Ensembl.
DR GO; GO:0007267; P:cell-cell signaling; IEA:Ensembl.
DR GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; ISS:UniProtKB.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
DR GO; GO:0007030; P:Golgi organization; IEA:Ensembl.
DR GO; GO:0048312; P:intracellular distribution of mitochondria; IEA:Ensembl.
DR GO; GO:0006851; P:mitochondrial calcium ion transmembrane transport; IEA:Ensembl.
DR GO; GO:0010832; P:negative regulation of myotube differentiation; ISS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0072560; P:type B pancreatic cell maturation; IEA:Ensembl.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..189
FT /note="Class A basic helix-loop-helix protein 15"
FT /id="PRO_0000127150"
FT DOMAIN 75..127
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9QYC3"
SQ 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
