位置:首页 > 蛋白库 > ASCL1_MOUSE
ASCL1_MOUSE
ID   ASCL1_MOUSE             Reviewed;         231 AA.
AC   Q02067; Q7TNT5;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   03-AUG-2022, entry version 183.
DE   RecName: Full=Achaete-scute homolog 1 {ECO:0000303|PubMed:8217843, ECO:0000303|PubMed:8424959};
DE            Short=ASH-1 {ECO:0000303|PubMed:8217843, ECO:0000303|PubMed:8424959};
DE            Short=mASH-1 {ECO:0000303|PubMed:8217843, ECO:0000303|PubMed:8424959};
DE            Short=mASH1 {ECO:0000303|PubMed:8217843, ECO:0000303|PubMed:8424959};
GN   Name=Ascl1 {ECO:0000312|MGI:MGI:96919};
GN   Synonyms=Ash1 {ECO:0000303|PubMed:8217843, ECO:0000303|PubMed:8424959},
GN   Mash-1 {ECO:0000303|PubMed:8217843, ECO:0000303|PubMed:8424959},
GN   Mash1 {ECO:0000303|PubMed:8217843, ECO:0000303|PubMed:8424959};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=8424959; DOI=10.1016/0167-4781(93)90076-p;
RA   del Amo F., Gendron-Maguire M., Gridley T.;
RT   "Cloning, sequencing and expression of the mouse mammalian achaete-scute
RT   homolog 1 (MASH1).";
RL   Biochim. Biophys. Acta 1171:323-327(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP   STAGE.
RX   PubMed=8217843; DOI=10.1016/0925-4773(93)90006-j;
RA   Guillemot F., Joyner A.L.;
RT   "Dynamic expression of the murine Achaete-Scute homologue Mash-1 in the
RT   developing nervous system.";
RL   Mech. Dev. 42:171-185(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Eye;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   [7]
RP   SUBCELLULAR LOCATION.
RX   PubMed=1576967; DOI=10.1242/dev.114.1.75;
RA   Johnson J.E., Zimmerman K., Saito T., Anderson D.J.;
RT   "Induction and repression of mammalian achaete-scute homologue (MASH) gene
RT   expression during neuronal differentiation of P19 embryonal carcinoma
RT   cells.";
RL   Development 114:75-87(1992).
RN   [8]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=8221886; DOI=10.1016/0092-8674(93)90381-y;
RA   Guillemot F., Lo L.C., Johnson J.E., Auerbach A., Anderson D.J.,
RA   Joyner A.L.;
RT   "Mammalian achaete-scute homolog 1 is required for the early development of
RT   olfactory and autonomic neurons.";
RL   Cell 75:463-476(1993).
RN   [9]
RP   FUNCTION IN NEUROGENESIS, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX   PubMed=16020526; DOI=10.1073/pnas.0504799102;
RA   Li S., Misra K., Matise M.P., Xiang M.;
RT   "Foxn4 acts synergistically with Mash1 to specify subtype identity of V2
RT   interneurons in the spinal cord.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:10688-10693(2005).
RN   [10]
RP   FUNCTION IN NEUROGENESIS.
RX   PubMed=17728344; DOI=10.1242/dev.005868;
RA   Del Barrio M.G., Taveira-Marques R., Muroyama Y., Yuk D.I., Li S.,
RA   Wines-Samuelson M., Shen J., Smith H.K., Xiang M., Rowitch D.,
RA   Richardson W.D.;
RT   "A regulatory network involving Foxn4, Mash1 and delta-like 4/Notch1
RT   generates V2a and V2b spinal interneurons from a common progenitor pool.";
RL   Development 134:3427-3436(2007).
RN   [11]
RP   FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=18173746; DOI=10.1111/j.1365-2443.2007.01146.x;
RA   Kokubu H., Ohtsuka T., Kageyama R.;
RT   "Mash1 is required for neuroendocrine cell development in the glandular
RT   stomach.";
RL   Genes Cells 13:41-51(2008).
RN   [12]
RP   FUNCTION.
RX   PubMed=20107439; DOI=10.1038/nature08797;
RA   Vierbuchen T., Ostermeier A., Pang Z.P., Kokubu Y., Suedhof T.C.,
RA   Wernig M.;
RT   "Direct conversion of fibroblasts to functional neurons by defined
RT   factors.";
RL   Nature 463:1035-1041(2010).
RN   [13]
RP   FUNCTION, AND DNA-BINDING.
RX   PubMed=24243019; DOI=10.1016/j.cell.2013.09.028;
RA   Wapinski O.L., Vierbuchen T., Qu K., Lee Q.Y., Chanda S., Fuentes D.R.,
RA   Giresi P.G., Ng Y.H., Marro S., Neff N.F., Drechsel D., Martynoga B.,
RA   Castro D.S., Webb A.E., Suedhof T.C., Brunet A., Guillemot F., Chang H.Y.,
RA   Wernig M.;
RT   "Hierarchical mechanisms for direct reprogramming of fibroblasts to
RT   neurons.";
RL   Cell 155:621-635(2013).
RN   [14]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-151, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA   Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA   Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT   identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN   [15]
RP   FUNCTION.
RX   PubMed=27281220; DOI=10.1038/nature18323;
RA   Treutlein B., Lee Q.Y., Camp J.G., Mall M., Koh W., Shariati S.A., Sim S.,
RA   Neff N.F., Skotheim J.M., Wernig M., Quake S.R.;
RT   "Dissecting direct reprogramming from fibroblast to neuron using single-
RT   cell RNA-seq.";
RL   Nature 534:391-395(2016).
CC   -!- FUNCTION: Transcription factor that plays a key role in neuronal
CC       differentiation: acts as a pioneer transcription factor, accessing
CC       closed chromatin to allow other factors to bind and activate neural
CC       pathways (PubMed:24243019). Directly binds the E box motif (5'-CANNTG-
CC       3') on promoters and promotes transcription of neuronal genes
CC       (PubMed:20107439, PubMed:24243019, PubMed:27281220). The combination of
CC       three transcription factors, ASCL1, POU3F2/BRN2 and MYT1L, is
CC       sufficient to reprogram fibroblasts and other somatic cells into
CC       induced neuronal (iN) cells in vitro (PubMed:20107439, PubMed:24243019,
CC       PubMed:27281220). Plays a role at early stages of development of
CC       specific neural lineages in most regions of the CNS, and of several
CC       lineages in the PNS (PubMed:8217843). Essential for the generation of
CC       olfactory and autonomic neurons (PubMed:8221886). Acts synergistically
CC       with FOXN4 to specify the identity of V2b neurons rather than V2a from
CC       bipotential p2 progenitors during spinal cord neurogenesis, probably
CC       through DLL4-NOTCH signaling activation (PubMed:16020526,
CC       PubMed:17728344). Involved in the regulation of neuroendocrine cell
CC       development in the glandular stomach (PubMed:18173746).
CC       {ECO:0000269|PubMed:16020526, ECO:0000269|PubMed:17728344,
CC       ECO:0000269|PubMed:18173746, ECO:0000269|PubMed:20107439,
CC       ECO:0000269|PubMed:24243019, ECO:0000269|PubMed:27281220,
CC       ECO:0000269|PubMed:8217843, ECO:0000269|PubMed:8221886}.
CC   -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC       protein. Forms a heterodimer with TCF3. {ECO:0000250|UniProtKB:P50553}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:1576967}.
CC   -!- TISSUE SPECIFICITY: Developing CNS and PNS at embryonic and postnatal
CC       stages. Expressed in the epithelium of glandular stomach
CC       (PubMed:18173746). {ECO:0000269|PubMed:16020526,
CC       ECO:0000269|PubMed:18173746, ECO:0000269|PubMed:8217843,
CC       ECO:0000269|PubMed:8424959}.
CC   -!- DEVELOPMENTAL STAGE: Between 8.5 dpc and 10.5 dpc it is found in the
CC       neuroepithelium of the midbrain and ventral forebrain, as well as in
CC       the spinal cord. Between 10.5 dpc and 12.5 dpc its expression pattern
CC       changes from a restricted to a widespread zone, it is then found at
CC       variable levels in the ventricular zone in all regions of the brain,
CC       where is expressed in a subset of p2 progenitors that can give rise to
CC       either V2a or V2b interneuron subtypes. From 12.5 dpc to postnatal
CC       stages it is also expressed in cells outside of the ventricular zone
CC       through the brain, and in addition it is also expressed during
CC       development of the olfactory epithelium and neural retina. At 12.5 dpc,
CC       it is highly expressed by differentiating enteric neurons in the
CC       mesenchyme of the stomach. At 14.5 and 16.5 dpc, it is also expressed
CC       in the epithelium of the glandular stomach (PubMed:18173746).
CC       {ECO:0000269|PubMed:16020526, ECO:0000269|PubMed:18173746,
CC       ECO:0000269|PubMed:8217843, ECO:0000269|PubMed:8424959}.
CC   -!- DISRUPTION PHENOTYPE: Lethality at birth caused by severe defects in
CC       neurogenesis. While the brain and spinal cord of the mutants appear
CC       normal, their olfactory epithelium and sympathetic, parasympathetic and
CC       enteric ganglia are severely affected. In the olfactory epithelium,
CC       neuronal progenitors die at an early stage, whereas the non-neuronal
CC       supporting cells are present. In sympathetic ganglia, the development
CC       of neuronal precursors is arrested, preventing the generation of
CC       sympathetic neurons, without affecting glial precursor cells.
CC       Homozygous MASH1-null mice have smaller stomachs than the control, and
CC       neuroendocrine cells are mostly missing, while chief, parietal and pit
CC       cells are formed. However, the wall of the glandular stomach is much
CC       thicker, has a deeper fold structure, and the forestomach epithelium is
CC       villous compared to controls (PubMed:18173746).
CC       {ECO:0000269|PubMed:18173746, ECO:0000269|PubMed:8221886}.
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; M95603; AAA37780.1; -; mRNA.
DR   EMBL; AK143210; BAE25307.1; -; mRNA.
DR   EMBL; AC122360; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466539; EDL21455.1; -; Genomic_DNA.
DR   EMBL; BC055748; AAH55748.1; -; mRNA.
DR   CCDS; CCDS24101.1; -.
DR   PIR; S28186; S28186.
DR   RefSeq; NP_032579.2; NM_008553.4.
DR   AlphaFoldDB; Q02067; -.
DR   SMR; Q02067; -.
DR   BioGRID; 201314; 9.
DR   STRING; 10090.ENSMUSP00000020243; -.
DR   iPTMnet; Q02067; -.
DR   PhosphoSitePlus; Q02067; -.
DR   PaxDb; Q02067; -.
DR   PRIDE; Q02067; -.
DR   ProteomicsDB; 281917; -.
DR   Antibodypedia; 18050; 536 antibodies from 40 providers.
DR   DNASU; 17172; -.
DR   Ensembl; ENSMUST00000020243; ENSMUSP00000020243; ENSMUSG00000020052.
DR   GeneID; 17172; -.
DR   KEGG; mmu:17172; -.
DR   UCSC; uc007gqs.1; mouse.
DR   CTD; 429; -.
DR   MGI; MGI:96919; Ascl1.
DR   VEuPathDB; HostDB:ENSMUSG00000020052; -.
DR   eggNOG; KOG4029; Eukaryota.
DR   GeneTree; ENSGT00940000162483; -.
DR   HOGENOM; CLU_063523_3_0_1; -.
DR   InParanoid; Q02067; -.
DR   OMA; QLIPPAC; -.
DR   OrthoDB; 1131543at2759; -.
DR   PhylomeDB; Q02067; -.
DR   TreeFam; TF322889; -.
DR   BioGRID-ORCS; 17172; 1 hit in 73 CRISPR screens.
DR   ChiTaRS; Ascl1; mouse.
DR   PRO; PR:Q02067; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; Q02067; protein.
DR   Bgee; ENSMUSG00000020052; Expressed in medial ganglionic eminence and 124 other tissues.
DR   Genevisible; Q02067; MM.
DR   GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IBA:GO_Central.
DR   GO; GO:0043425; F:bHLH transcription factor binding; ISO:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR   GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0070888; F:E-box binding; ISO:MGI.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
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; ISO:MGI.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0061104; P:adrenal chromaffin cell differentiation; IMP:MGI.
DR   GO; GO:0061103; P:carotid body glomus cell differentiation; IMP:MGI.
DR   GO; GO:0048469; P:cell maturation; IMP:MGI.
DR   GO; GO:0071259; P:cellular response to magnetism; IEA:Ensembl.
DR   GO; GO:0021954; P:central nervous system neuron development; IMP:MGI.
DR   GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR   GO; GO:0021892; P:cerebral cortex GABAergic interneuron differentiation; IEA:Ensembl.
DR   GO; GO:0021902; P:commitment of neuronal cell to specific neuron type in forebrain; IMP:MGI.
DR   GO; GO:0048484; P:enteric nervous system development; TAS:BHF-UCL.
DR   GO; GO:0021879; P:forebrain neuron differentiation; ISO:MGI.
DR   GO; GO:0097154; P:GABAergic neuron differentiation; IGI:MGI.
DR   GO; GO:0048699; P:generation of neurons; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   GO; GO:0061100; P:lung neuroendocrine cell differentiation; IMP:MGI.
DR   GO; GO:0097475; P:motor neuron migration; IMP:MGI.
DR   GO; GO:0050883; P:musculoskeletal movement, spinal reflex action; IMP:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR   GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR   GO; GO:0007399; P:nervous system development; IDA:UniProtKB.
DR   GO; GO:0061351; P:neural precursor cell proliferation; IMP:MGI.
DR   GO; GO:0007400; P:neuroblast fate determination; IMP:MGI.
DR   GO; GO:0007405; P:neuroblast proliferation; IGI:MGI.
DR   GO; GO:0061101; P:neuroendocrine cell differentiation; IMP:MGI.
DR   GO; GO:0022008; P:neurogenesis; ISO:MGI.
DR   GO; GO:0048666; P:neuron development; IDA:UniProtKB.
DR   GO; GO:0030182; P:neuron differentiation; IDA:UniProtKB.
DR   GO; GO:0048663; P:neuron fate commitment; IDA:UniProtKB.
DR   GO; GO:0048665; P:neuron fate specification; IDA:UniProtKB.
DR   GO; GO:0003358; P:noradrenergic neuron development; IMP:UniProtKB.
DR   GO; GO:0003359; P:noradrenergic neuron fate commitment; ISO:MGI.
DR   GO; GO:0007219; P:Notch signaling pathway; IMP:MGI.
DR   GO; GO:0060166; P:olfactory pit development; IMP:MGI.
DR   GO; GO:0021779; P:oligodendrocyte cell fate commitment; IMP:MGI.
DR   GO; GO:0014003; P:oligodendrocyte development; IMP:MGI.
DR   GO; GO:0048709; P:oligodendrocyte differentiation; IMP:MGI.
DR   GO; GO:0048486; P:parasympathetic nervous system development; TAS:BHF-UCL.
DR   GO; GO:0007389; P:pattern specification process; IMP:MGI.
DR   GO; GO:0048935; P:peripheral nervous system neuron development; IMP:MGI.
DR   GO; GO:0045787; P:positive regulation of cell cycle; IDA:MGI.
DR   GO; GO:2000179; P:positive regulation of neural precursor cell proliferation; IMP:MGI.
DR   GO; GO:0050769; P:positive regulation of neurogenesis; IMP:MGI.
DR   GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:MGI.
DR   GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB.
DR   GO; GO:0045747; P:positive regulation of Notch signaling pathway; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IDA:MGI.
DR   GO; GO:0030856; P:regulation of epithelial cell differentiation; IMP:MGI.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; IMP:MGI.
DR   GO; GO:0050767; P:regulation of neurogenesis; IMP:MGI.
DR   GO; GO:0008593; P:regulation of Notch signaling pathway; IMP:MGI.
DR   GO; GO:0060165; P:regulation of timing of subpallium neuron differentiation; IMP:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:0070849; P:response to epidermal growth factor; IEA:Ensembl.
DR   GO; GO:0051593; P:response to folic acid; IEA:Ensembl.
DR   GO; GO:0010226; P:response to lithium ion; IEA:Ensembl.
DR   GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
DR   GO; GO:0007423; P:sensory organ development; IBA:GO_Central.
DR   GO; GO:0021527; P:spinal cord association neuron differentiation; IMP:MGI.
DR   GO; GO:0021529; P:spinal cord oligodendrocyte cell differentiation; IGI:MGI.
DR   GO; GO:0021530; P:spinal cord oligodendrocyte cell fate specification; IMP:MGI.
DR   GO; GO:0061102; P:stomach neuroendocrine cell differentiation; IMP:MGI.
DR   GO; GO:0060163; P:subpallium neuron fate commitment; IMP:MGI.
DR   GO; GO:0061549; P:sympathetic ganglion development; IMP:UniProtKB.
DR   GO; GO:0048485; P:sympathetic nervous system development; TAS:BHF-UCL.
DR   GO; GO:0060579; P:ventral spinal cord interneuron fate commitment; IMP:UniProtKB.
DR   GO; GO:0021750; P:vestibular nucleus development; IMP:MGI.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   InterPro; IPR015660; MASH1/Ascl1a-like.
DR   PANTHER; PTHR13935; PTHR13935; 1.
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   Acetylation; Activator; Developmental protein; Differentiation;
KW   DNA-binding; Neurogenesis; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..231
FT                   /note="Achaete-scute homolog 1"
FT                   /id="PRO_0000127127"
FT   DOMAIN          113..165
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          39..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..69
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         151
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   CONFLICT        81
FT                   /note="V -> D (in Ref. 1; AAA37780)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        160
FT                   /note="E -> Q (in Ref. 1; AAA37780)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   231 AA;  24741 MW;  454E6937520BD4CA CRC64;
     MESSGKMESG AGQQPQPPQP FLPPAACFFA TAAAAAAAAA AAAQSAQQQQ PQAPPQQAPQ
     LSPVADSQPS GGGHKSAAKQ VKRQRSSSPE LMRCKRRLNF SGFGYSLPQQ QPAAVARRNE
     RERNRVKLVN LGFATLREHV PNGAANKKMS KVETLRSAVE YIRALQQLLD EHDAVSAAFQ
     AGVLSPTISP NYSNDLNSMA GSPVSSYSSD EGSYDPLSPE EQELLDFTNW F
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024