ID   ASCL5_HUMAN             Reviewed;         278 AA.
AC   Q7RTU5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   27-MAR-2024, entry version 129.
DE   RecName: Full=Achaete-scute homolog 5;
DE            Short=ASH-5;
DE            Short=hASH5;
DE   AltName: Full=Class A basic helix-loop-helix protein 47;
DE            Short=bHLHa47;
GN   Name=ASCL5; Synonyms=BHLHA47;
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=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [2]
RP   IDENTIFICATION.
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).
CC   -!- FUNCTION: Transcription factor. Probably binds E-box motifs 5'-CANNTG-
CC       3' in complex with transcription factor TCF3/E12. Negatively modulates
CC       transcription of target genes such as CDH1/E-cadherin, perhaps by
CC       recruiting the PRC2 repressive complex to regulatory elements.
CC       Regulates ameloblast development and tooth germ growth, perhaps acting
CC       by positively modulating migration of inner enamel epithelium (IEE)
CC       cells. Plays a role in enamel formation.
CC       {ECO:0000250|UniProtKB:M0QWB7}.
CC   -!- SUBUNIT: Interacts with transcription factor TCF3/E12.
CC       {ECO:0000250|UniProtKB:M0QWB7}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=DAA00301.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AL139159; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BK000139; DAA00301.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q7RTU5; -.
DR   SMR; Q7RTU5; -.
DR   IntAct; Q7RTU5; 2.
DR   STRING; 9606.ENSP00000472681; -.
DR   PhosphoSitePlus; Q7RTU5; -.
DR   BioMuta; ASCL5; -.
DR   DMDM; 166988402; -.
DR   MassIVE; Q7RTU5; -.
DR   PaxDb; 9606-ENSP00000472681; -.
DR   PeptideAtlas; Q7RTU5; -.
DR   UCSC; uc031prl.1; human.
DR   AGR; HGNC:33169; -.
DR   GeneCards; ASCL5; -.
DR   HGNC; HGNC:33169; ASCL5.
DR   neXtProt; NX_Q7RTU5; -.
DR   VEuPathDB; HostDB:ENSG00000232237; -.
DR   eggNOG; KOG4029; Eukaryota.
DR   InParanoid; Q7RTU5; -.
DR   PhylomeDB; Q7RTU5; -.
DR   PathwayCommons; Q7RTU5; -.
DR   SignaLink; Q7RTU5; -.
DR   Pharos; Q7RTU5; Tdark.
DR   PRO; PR:Q7RTU5; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q7RTU5; Protein.
DR   Bgee; ENSG00000232237; Expressed in body of pancreas and 60 other cell types or tissues.
DR   ExpressionAtlas; Q7RTU5; baseline and differential.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd19747; bHLH_TS_ASCL5; 1.
DR   Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   PANTHER; PTHR23349; BASIC HELIX-LOOP-HELIX TRANSCRIPTION FACTOR, TWIST; 1.
DR   PANTHER; PTHR23349:SF57; FACTOR IN THE GERMLINE ALPHA; 1.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR   PROSITE; PS50888; BHLH; 1.
DR   Genevisible; Q7RTU5; HS.
PE   3: Inferred from homology;
KW   DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..278
FT                   /note="Achaete-scute homolog 5"
FT                   /id="PRO_0000317298"
FT   DOMAIN          155..207
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          1..66
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          214..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..242
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..270
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   278 AA;  29462 MW;  96DC775BDA61C176 CRC64;
     MPMGAAERGA GPQSSAAPWA GSEKAAKRGP SKSWYPRAAA SDVTCPTGGD GADPKPGPFG
     GGLALGPAPR GTMNNNFCRA LVDRRPLGPP SCMQLGVMPP PRQAPLPPAE PLGNVPFLLY
     PGPAEPPYYD AYAGVFPYVP FPGAFGVYEY PFEPAFIQKR NERERQRVKC VNEGYARLRG
     HLPGALAEKR LSKVETLRAA IRYIKYLQEL LSSAPDGSTP PASRGLPGTG PCPAPPATPR
     PDRPGDGEAR APSSLVPESS ESSCFSPSPF LESEESWH
//