TAL1_MOUSE
ID TAL1_MOUSE Reviewed; 329 AA.
AC P22091;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=T-cell acute lymphocytic leukemia protein 1 homolog;
DE Short=TAL-1;
DE AltName: Full=Stem cell protein;
GN Name=Tal1; Synonyms=Scl, Tal-1;
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].
RC TISSUE=Bone marrow macrophage;
RX PubMed=1704135; DOI=10.1073/pnas.88.3.869;
RA Begley C.G., Visvader J., Green A.R., Aplan P.D., Metcalf D., Kirsch I.R.,
RA Gough N.M.;
RT "Molecular cloning and chromosomal localization of the murine homolog of
RT the human helix-loop-helix gene SCL.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:869-873(1991).
RN [2]
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 [3]
RP FUNCTION, INTERACTION WITH LMO2, IDENTIFICATION IN A COMPLEX WITH LDB1 AND
RP LMO2, AND SUBCELLULAR LOCATION.
RX PubMed=9391090; DOI=10.1073/pnas.94.25.13707;
RA Visvader J.E., Mao X., Fujiwara Y., Hahm K., Orkin S.H.;
RT "The LIM-domain binding protein Ldb1 and its partner LMO2 act as negative
RT regulators of erythroid differentiation.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:13707-13712(1997).
RN [4]
RP PHOSPHORYLATION AT SER-122, MUTAGENESIS OF SER-122, AND UBIQUITINATION.
RX PubMed=11904294; DOI=10.1074/jbc.m109812200;
RA Tang T., Arbiser J.L., Brandt S.J.;
RT "Phosphorylation by mitogen-activated protein kinase mediates the hypoxia-
RT induced turnover of the TAL1/SCL transcription factor in endothelial
RT cells.";
RL J. Biol. Chem. 277:18365-18372(2002).
RN [5]
RP INTERACTION WITH CBFA2T3.
RX PubMed=16407974; DOI=10.1038/sj.emboj.7600934;
RA Goardon N., Lambert J.A., Rodriguez P., Nissaire P., Herblot S.,
RA Thibault P., Dumenil D., Strouboulis J., Romeo P.-H., Hoang T.;
RT "ETO2 coordinates cellular proliferation and differentiation during
RT erythropoiesis.";
RL EMBO J. 25:357-366(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP INTERACTION WITH SBNO2.
RX PubMed=23980096; DOI=10.1084/jem.20130512;
RA Maruyama K., Uematsu S., Kondo T., Takeuchi O., Martino M.M., Kawasaki T.,
RA Akira S.;
RT "Strawberry notch homologue 2 regulates osteoclast fusion by enhancing the
RT expression of DC-STAMP.";
RL J. Exp. Med. 210:1947-1960(2013).
CC -!- FUNCTION: Implicated in the genesis of hemopoietic malignancies. It may
CC play an important role in hemopoietic differentiation. Serves as a
CC positive regulator of erythroid differentiation.
CC {ECO:0000269|PubMed:9391090}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Forms heterodimers with TCF3. Binds to the LIM domain
CC containing protein LMO2 and to DRG1. Can assemble in a complex with
CC LDB1 and LMO2. Component of a TAL-1 complex composed at least of
CC CBFA2T3, LDB1, TAL1 and TCF3 (PubMed:9391090). Interacts with SBNO2;
CC this interaction inhibits TAL1 occupancy of the DCSTAMP promoter,
CC leading to the activation of the DCSTAMP promoter by the transcription
CC factor MITF (PubMed:23980096). {ECO:0000269|PubMed:23980096,
CC ECO:0000269|PubMed:9391090}.
CC -!- INTERACTION:
CC P22091; O70374: Cbfa2t2; NbExp=8; IntAct=EBI-8006437, EBI-8006755;
CC P22091; O54972: Cbfa2t3; NbExp=11; IntAct=EBI-8006437, EBI-8006703;
CC P22091; P17679: Gata1; NbExp=2; IntAct=EBI-8006437, EBI-3903251;
CC P22091; O09106: Hdac1; NbExp=3; IntAct=EBI-8006437, EBI-301912;
CC P22091; P70662: Ldb1; NbExp=4; IntAct=EBI-8006437, EBI-6272082;
CC P22091; P25801: Lmo2; NbExp=2; IntAct=EBI-8006437, EBI-3903256;
CC P22091; Q61286: Tcf12; NbExp=2; IntAct=EBI-8006437, EBI-8006499;
CC P22091; P15806: Tcf3; NbExp=4; IntAct=EBI-8006437, EBI-81370;
CC P22091; O60341-1: KDM1A; Xeno; NbExp=2; IntAct=EBI-8006437, EBI-15599570;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:9391090}.
CC -!- TISSUE SPECIFICITY: Erythroid and myeloid cells.
CC -!- DOMAIN: The helix-loop-helix domain is necessary and sufficient for the
CC interaction with DRG1.
CC -!- PTM: Phosphorylated on serine residues. Phosphorylation of Ser-122 by
CC MAPK is strongly stimulated by hypoxia. {ECO:0000269|PubMed:11904294}.
CC -!- PTM: Ubiquitinated; subsequent to hypoxia-dependent phosphorylation of
CC Ser-122, ubiquitination targets the protein for rapid degradation via
CC the ubiquitin system. This process may be characteristic for
CC microvascular endothelial cells, since it could not be observed in
CC large vessel endothelial cells. {ECO:0000269|PubMed:11904294}.
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DR EMBL; M59764; AAA40097.1; -; mRNA.
DR EMBL; U01530; AAA86937.1; -; Genomic_DNA.
DR EMBL; BC063060; AAH63060.1; -; mRNA.
DR CCDS; CCDS18486.1; -.
DR PIR; A37864; A37864.
DR RefSeq; NP_001274317.1; NM_001287388.1.
DR RefSeq; NP_035657.1; NM_011527.3.
DR RefSeq; XP_006502973.1; XM_006502910.3.
DR RefSeq; XP_006502975.1; XM_006502912.3.
DR RefSeq; XP_006502976.1; XM_006502913.3.
DR RefSeq; XP_006502977.1; XM_006502914.3.
DR RefSeq; XP_006502978.1; XM_006502915.3.
DR RefSeq; XP_006502979.1; XM_006502916.2.
DR AlphaFoldDB; P22091; -.
DR SMR; P22091; -.
DR BioGRID; 203962; 11.
DR CORUM; P22091; -.
DR DIP; DIP-42839N; -.
DR IntAct; P22091; 22.
DR MINT; P22091; -.
DR STRING; 10090.ENSMUSP00000125202; -.
DR iPTMnet; P22091; -.
DR PhosphoSitePlus; P22091; -.
DR PaxDb; P22091; -.
DR PRIDE; P22091; -.
DR ProteomicsDB; 263000; -.
DR Antibodypedia; 4499; 784 antibodies from 39 providers.
DR DNASU; 21349; -.
DR Ensembl; ENSMUST00000030489; ENSMUSP00000030489; ENSMUSG00000028717.
DR Ensembl; ENSMUST00000161601; ENSMUSP00000125202; ENSMUSG00000028717.
DR Ensembl; ENSMUST00000162489; ENSMUSP00000124983; ENSMUSG00000028717.
DR GeneID; 21349; -.
DR KEGG; mmu:21349; -.
DR UCSC; uc008uek.1; mouse.
DR CTD; 6886; -.
DR MGI; MGI:98480; Tal1.
DR VEuPathDB; HostDB:ENSMUSG00000028717; -.
DR eggNOG; KOG4029; Eukaryota.
DR GeneTree; ENSGT00940000159889; -.
DR HOGENOM; CLU_059203_0_0_1; -.
DR InParanoid; P22091; -.
DR OMA; HMDERNH; -.
DR PhylomeDB; P22091; -.
DR TreeFam; TF315153; -.
DR Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR BioGRID-ORCS; 21349; 5 hits in 74 CRISPR screens.
DR PRO; PR:P22091; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; P22091; protein.
DR Bgee; ENSMUSG00000028717; Expressed in fetal liver hematopoietic progenitor cell and 158 other tissues.
DR ExpressionAtlas; P22091; baseline and differential.
DR Genevisible; P22091; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IPI:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
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; IDA:MGI.
DR GO; GO:0070888; F:E-box binding; IDA:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0042826; F:histone deacetylase 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; IDA:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:BHF-UCL.
DR GO; GO:0030297; F:transmembrane receptor protein tyrosine kinase activator activity; IDA:MGI.
DR GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR GO; GO:0060018; P:astrocyte fate commitment; IMP:MGI.
DR GO; GO:0045165; P:cell fate commitment; IMP:MGI.
DR GO; GO:0021953; P:central nervous system neuron differentiation; IMP:MGI.
DR GO; GO:0060216; P:definitive hemopoiesis; IMP:MGI.
DR GO; GO:0035162; P:embryonic hemopoiesis; IMP:UniProtKB.
DR GO; GO:0030218; P:erythrocyte differentiation; IDA:MGI.
DR GO; GO:0043249; P:erythrocyte maturation; IMP:MGI.
DR GO; GO:0048699; P:generation of neurons; IMP:MGI.
DR GO; GO:0060217; P:hemangioblast cell differentiation; IMP:MGI.
DR GO; GO:0060218; P:hematopoietic stem cell differentiation; IMP:MGI.
DR GO; GO:0030097; P:hemopoiesis; IDA:MGI.
DR GO; GO:0007626; P:locomotory behavior; IMP:MGI.
DR GO; GO:0035855; P:megakaryocyte development; IMP:MGI.
DR GO; GO:0030219; P:megakaryocyte differentiation; IMP:MGI.
DR GO; GO:0030099; P:myeloid cell differentiation; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0030220; P:platelet formation; IMP:MGI.
DR GO; GO:0051781; P:positive regulation of cell division; ISO:MGI.
DR GO; GO:1905269; P:positive regulation of chromatin organization; ISO:MGI.
DR GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IDA:BHF-UCL.
DR GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISO:MGI.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:MGI.
DR GO; GO:0060375; P:regulation of mast cell differentiation; IMP:MGI.
DR GO; GO:0045637; P:regulation of myeloid cell differentiation; IMP:MGI.
DR GO; GO:1904672; P:regulation of somatic stem cell population maintenance; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0021527; P:spinal cord association neuron differentiation; IGI:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:MGI.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR040238; TAL-like.
DR PANTHER; PTHR13864; PTHR13864; 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 Chromosomal rearrangement; Developmental protein; Differentiation;
KW DNA-binding; Nucleus; Phosphoprotein; Proto-oncogene; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..329
FT /note="T-cell acute lymphocytic leukemia protein 1 homolog"
FT /id="PRO_0000127455"
FT DOMAIN 187..239
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 40..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..108
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17542"
FT MOD_RES 122
FT /note="Phosphoserine; by MAPK"
FT /evidence="ECO:0000269|PubMed:11904294"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 122
FT /note="S->A: Remains stable, even in the face of severe
FT hypoxia."
FT /evidence="ECO:0000269|PubMed:11904294"
SQ SEQUENCE 329 AA; 34279 MW; 189480B6B93CB371 CRC64;
MTERPPSEAA RSDPQLEGQD AAEARMAPPH LVLLNGVAKE TSRAAPAEPP VIELGARSGA
GGGPASGGGA ARDLKGRDAV AAEARLRVPT TELCRPPGPA PAPAPASAPA ELPGDGRMVQ
LSPPALAAPA GPGRALLYSL SQPLASLGSG FFGEPDAFPM FTNNNRVKRR PSPYEMEISD
GPHTKVVRRI FTNSRERWRQ QNVNGAFAEL RKLIPTHPPD KKLSKNEILR LAMKYINFLA
KLLNDQEEEG TQRAKPGKDP VVGAGGGGAG GGIPPEDLLQ DVLSPNSSCG SSLDGAASPD
SYTEEPTPKH TSRSLHPALL PAADGAGPR
