ASCL2_MOUSE
ID ASCL2_MOUSE Reviewed; 263 AA.
AC O35885; Q9WUJ7;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 25-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Achaete-scute homolog 2;
DE Short=ASH-2;
DE Short=mASH-2;
DE Short=mASH2;
GN Name=Ascl2; Synonyms=Mash2;
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 [GENOMIC DNA].
RX PubMed=9175731; DOI=10.1093/hmg/6.6.859;
RA Alders M., Hodges M., Hadjantonakis A.-K., Postmus J., van Wijk I.J.,
RA Bliek J., de Meulemeester M., Westerveld A., Guillemot F., Oudejans C.B.,
RA Little P., Mannens M.;
RT "The human Achaete-Scute homologue 2 (ASCL2,HASH2) maps to chromosome
RT 11p15.5, close to IGF2 and is expressed in extravillus trophoblasts.";
RL Hum. Mol. Genet. 6:859-867(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10495277; DOI=10.1016/s0925-4773(99)00158-6;
RA Tanaka M., Puchyr M., Gertsenstein M., Harpal K., Jaenisch R., Rossant J.,
RA Nagy A.;
RT "Parental origin-specific expression of Mash2 is established at the time of
RT implantation with its imprinting mechanism highly resistant to genome-wide
RT demethylation.";
RL Mech. Dev. 87:129-142(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=10915772; DOI=10.1093/hmg/9.12.1829;
RA Paulsen M., El-Maarri O., Engemann S., Stroedicke M., Franck O., Davies K.,
RA Reinhardt R., Reik W., Walter J.;
RT "Sequence conservation and variability of imprinting in the Beckwith-
RT Wiedemann syndrome gene cluster in human and mouse.";
RL Hum. Mol. Genet. 9:1829-1841(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
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).
CC -!- FUNCTION: AS-C proteins are involved in the determination of the
CC neuronal precursors in the peripheral nervous system and the central
CC nervous system. {ECO:0000250}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Part of a complex composed at least of ASCL2, EMSY, HCFC1,
CC HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this
CC complex may have a histone H3-specific methyltransferase activity.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
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DR EMBL; U77628; AAB86992.1; -; Genomic_DNA.
DR EMBL; AF139595; AAD33794.1; -; Genomic_DNA.
DR EMBL; AJ251835; CAB94773.1; -; Genomic_DNA.
DR EMBL; BC019520; AAH19520.1; -; mRNA.
DR CCDS; CCDS40194.1; -.
DR RefSeq; NP_032580.2; NM_008554.3.
DR RefSeq; XP_006508561.1; XM_006508498.3.
DR RefSeq; XP_011240286.1; XM_011241984.2.
DR AlphaFoldDB; O35885; -.
DR SMR; O35885; -.
DR STRING; 10090.ENSMUSP00000009392; -.
DR PhosphoSitePlus; O35885; -.
DR PaxDb; O35885; -.
DR PRIDE; O35885; -.
DR ProteomicsDB; 277075; -.
DR Antibodypedia; 42100; 222 antibodies from 29 providers.
DR DNASU; 17173; -.
DR Ensembl; ENSMUST00000009392; ENSMUSP00000009392; ENSMUSG00000009248.
DR GeneID; 17173; -.
DR KEGG; mmu:17173; -.
DR UCSC; uc009koj.2; mouse.
DR CTD; 430; -.
DR MGI; MGI:96920; Ascl2.
DR VEuPathDB; HostDB:ENSMUSG00000009248; -.
DR eggNOG; KOG4029; Eukaryota.
DR GeneTree; ENSGT00940000163041; -.
DR HOGENOM; CLU_063523_3_0_1; -.
DR InParanoid; O35885; -.
DR OMA; ACPRESC; -.
DR OrthoDB; 1131543at2759; -.
DR PhylomeDB; O35885; -.
DR TreeFam; TF322889; -.
DR BioGRID-ORCS; 17173; 1 hit in 74 CRISPR screens.
DR PRO; PR:O35885; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; O35885; protein.
DR Bgee; ENSMUSG00000009248; Expressed in trophectoderm and 96 other tissues.
DR ExpressionAtlas; O35885; baseline and differential.
DR Genevisible; O35885; MM.
DR GO; GO:0005737; C:cytoplasm; 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:0003700; F:DNA-binding transcription factor activity; ISO:MGI.
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:0070888; F:E-box 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:0030154; P:cell differentiation; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0010626; P:negative regulation of Schwann cell proliferation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0030182; P:neuron differentiation; IBA:GO_Central.
DR GO; GO:0001890; P:placenta development; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0050767; P:regulation of neurogenesis; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
DR GO; GO:0007423; P:sensory organ development; IBA:GO_Central.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:MGI.
DR GO; GO:0060708; P:spongiotrophoblast differentiation; 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 2: Evidence at transcript level;
KW Developmental protein; Differentiation; DNA-binding; Neurogenesis; Nucleus;
KW Reference proteome.
FT CHAIN 1..263
FT /note="Achaete-scute homolog 2"
FT /id="PRO_0000127131"
FT DOMAIN 118..170
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 104..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 119
FT /note="A -> S (in Ref. 1; AAB86992)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="A -> T (in Ref. 1; AAB86992)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="A -> P (in Ref. 1; AAB86992)"
FT /evidence="ECO:0000305"
FT CONFLICT 200
FT /note="A -> T (in Ref. 1; AAB86992)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="A -> G (in Ref. 1; AAB86992)"
FT /evidence="ECO:0000305"
FT CONFLICT 220..222
FT /note="PDR -> RT (in Ref. 1; AAB86992)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 263 AA; 27784 MW; 9FA907B436E1BA2E CRC64;
MEAHLDWYGV PGLQEASDAC PRESCSSALP EAREGANVHF PPHPVPREHF SCAAPELVAG
AQGLNASLMD GGALPRLMPT SSGVAGACAA RRRQASPELL RCSRRRRSGA TEASSSSAAV
ARRNERERNR VKLVNLGFQA LRQHVPHGGA NKKLSKVETL RSAVEYIRAL QRLLAEHDAV
RAALAGGLLT PATPPSDECA QPSASPASAS LSCASTSPSP DRLGCSEPTS PRSAYSSEES
SCEGELSPME QELLDFSSWL GGY
