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T-cell acute lymphocytic leukemia protein 1 homolog (TAL-1) (Stem cell protein)

 TAL1_MOUSE              Reviewed;         329 AA.
P22091;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
01-AUG-1991, sequence version 1.
25-OCT-2017, entry version 157.
RecName: Full=T-cell acute lymphocytic leukemia protein 1 homolog;
Short=TAL-1;
AltName: Full=Stem cell protein;
Name=Tal1; Synonyms=Scl, Tal-1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Bone marrow macrophage;
PubMed=1704135; DOI=10.1073/pnas.88.3.869;
Begley C.G., Visvader J., Green A.R., Aplan P.D., Metcalf D.,
Kirsch I.R., Gough N.M.;
"Molecular cloning and chromosomal localization of the murine homolog
of the human helix-loop-helix gene SCL.";
Proc. Natl. Acad. Sci. U.S.A. 88:869-873(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
FUNCTION, INTERACTION WITH LMO2, IDENTIFICATION IN A COMPLEX WITH LDB1
AND LMO2, AND SUBCELLULAR LOCATION.
PubMed=9391090; DOI=10.1073/pnas.94.25.13707;
Visvader J.E., Mao X., Fujiwara Y., Hahm K., Orkin S.H.;
"The LIM-domain binding protein Ldb1 and its partner LMO2 act as
negative regulators of erythroid differentiation.";
Proc. Natl. Acad. Sci. U.S.A. 94:13707-13712(1997).
[4]
PHOSPHORYLATION AT SER-122, MUTAGENESIS OF SER-122, AND
UBIQUITINATION.
PubMed=11904294; DOI=10.1074/jbc.M109812200;
Tang T., Arbiser J.L., Brandt S.J.;
"Phosphorylation by mitogen-activated protein kinase mediates the
hypoxia-induced turnover of the TAL1/SCL transcription factor in
endothelial cells.";
J. Biol. Chem. 277:18365-18372(2002).
[5]
INTERACTION WITH CBFA2T3.
PubMed=16407974; DOI=10.1038/sj.emboj.7600934;
Goardon N., Lambert J.A., Rodriguez P., Nissaire P., Herblot S.,
Thibault P., Dumenil D., Strouboulis J., Romeo P.-H., Hoang T.;
"ETO2 coordinates cellular proliferation and differentiation during
erythropoiesis.";
EMBO J. 25:357-366(2006).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-172, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
INTERACTION WITH SBNO2.
PubMed=23980096; DOI=10.1084/jem.20130512;
Maruyama K., Uematsu S., Kondo T., Takeuchi O., Martino M.M.,
Kawasaki T., Akira S.;
"Strawberry notch homologue 2 regulates osteoclast fusion by enhancing
the expression of DC-STAMP.";
J. Exp. Med. 210:1947-1960(2013).
-!- FUNCTION: Implicated in the genesis of hemopoietic malignancies.
It may play an important role in hemopoietic differentiation.
Serves as a positive regulator of erythroid differentiation.
{ECO:0000269|PubMed:9391090}.
-!- SUBUNIT: Efficient DNA binding requires dimerization with another
bHLH protein. Forms heterodimers with TCF3. Binds to the LIM
domain containing protein LMO2 and to DRG1. Can assemble in a
complex with LDB1 and LMO2. Component of a TAL-1 complex composed
at least of CBFA2T3, LDB1, TAL1 and TCF3 (PubMed:9391090).
Interacts with SBNO2; this interaction inhibits TAL1 occupancy of
the DCSTAMP promoter, leading to the activation of the DCSTAMP
promoter by the transcription factor MITF (PubMed:23980096).
{ECO:0000269|PubMed:23980096, ECO:0000269|PubMed:9391090}.
-!- INTERACTION:
O70374:Cbfa2t2; NbExp=8; IntAct=EBI-8006437, EBI-8006755;
O54972:Cbfa2t3; NbExp=11; IntAct=EBI-8006437, EBI-8006703;
P17679:Gata1; NbExp=2; IntAct=EBI-8006437, EBI-3903251;
O09106:Hdac1; NbExp=3; IntAct=EBI-8006437, EBI-301912;
O60341-1:KDM1A (xeno); NbExp=2; IntAct=EBI-8006437, EBI-15599570;
P70662:Ldb1; NbExp=4; IntAct=EBI-8006437, EBI-6272082;
P25801:Lmo2; NbExp=2; IntAct=EBI-8006437, EBI-3903256;
Q61286:Tcf12; NbExp=2; IntAct=EBI-8006437, EBI-8006499;
P15806:Tcf3; NbExp=4; IntAct=EBI-8006437, EBI-81370;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00981, ECO:0000269|PubMed:9391090}.
-!- TISSUE SPECIFICITY: Erythroid and myeloid cells.
-!- DOMAIN: The helix-loop-helix domain is necessary and sufficient
for the interaction with DRG1.
-!- PTM: Phosphorylated on serine residues. Phosphorylation of Ser-122
by MAPK is strongly stimulated by hypoxia.
{ECO:0000269|PubMed:11904294}.
-!- PTM: Ubiquitinated; subsequent to hypoxia-dependent
phosphorylation of Ser-122, ubiquitination targets the protein for
rapid degradation via the ubiquitin system. This process may be
characteristic for microvascular endothelial cells, since it could
not be observed in large vessel endothelial cells.
{ECO:0000269|PubMed:11904294}.
-----------------------------------------------------------------------
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EMBL; M59764; AAA40097.1; -; mRNA.
EMBL; U01530; AAA86937.1; -; Genomic_DNA.
EMBL; BC063060; AAH63060.1; -; mRNA.
CCDS; CCDS18486.1; -.
PIR; A37864; A37864.
RefSeq; NP_001274317.1; NM_001287388.1.
RefSeq; NP_035657.1; NM_011527.3.
RefSeq; XP_006502973.1; XM_006502910.3.
RefSeq; XP_006502975.1; XM_006502912.3.
RefSeq; XP_006502976.1; XM_006502913.3.
RefSeq; XP_006502977.1; XM_006502914.3.
RefSeq; XP_006502978.1; XM_006502915.3.
RefSeq; XP_006502979.1; XM_006502916.2.
UniGene; Mm.239869; -.
UniGene; Mm.439685; -.
ProteinModelPortal; P22091; -.
SMR; P22091; -.
BioGrid; 203962; 11.
CORUM; P22091; -.
DIP; DIP-42839N; -.
IntAct; P22091; 21.
MINT; MINT-2567683; -.
STRING; 10090.ENSMUSP00000030489; -.
iPTMnet; P22091; -.
PhosphoSitePlus; P22091; -.
PaxDb; P22091; -.
PRIDE; P22091; -.
Ensembl; ENSMUST00000030489; ENSMUSP00000030489; ENSMUSG00000028717.
Ensembl; ENSMUST00000161601; ENSMUSP00000125202; ENSMUSG00000028717.
Ensembl; ENSMUST00000162489; ENSMUSP00000124983; ENSMUSG00000028717.
GeneID; 21349; -.
KEGG; mmu:21349; -.
UCSC; uc008uek.1; mouse.
CTD; 6886; -.
MGI; MGI:98480; Tal1.
eggNOG; KOG4029; Eukaryota.
eggNOG; ENOG411227D; LUCA.
GeneTree; ENSGT00760000119097; -.
HOGENOM; HOG000113414; -.
HOVERGEN; HBG005018; -.
InParanoid; P22091; -.
KO; K09068; -.
OMA; QELCPGS; -.
OrthoDB; EOG091G0ESI; -.
PhylomeDB; P22091; -.
TreeFam; TF315153; -.
Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
PRO; PR:P22091; -.
Proteomes; UP000000589; Chromosome 4.
Bgee; ENSMUSG00000028717; -.
CleanEx; MM_TAL1; -.
ExpressionAtlas; P22091; baseline and differential.
Genevisible; P22091; MM.
GO; GO:0000118; C:histone deacetylase complex; IEA:Ensembl.
GO; GO:0033193; C:Lsd1/2 complex; IEA:Ensembl.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; IPI:UniProtKB.
GO; GO:0005667; C:transcription factor complex; IDA:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0070888; F:E-box binding; IDA:MGI.
GO; GO:0019899; F:enzyme binding; ISO:MGI.
GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:MGI.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; IDA:MGI.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IDA:MGI.
GO; GO:0001085; F:RNA polymerase II transcription factor binding; ISO:MGI.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISO:MGI.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0001525; P:angiogenesis; IMP:MGI.
GO; GO:0060018; P:astrocyte fate commitment; IMP:MGI.
GO; GO:0030221; P:basophil differentiation; IEA:Ensembl.
GO; GO:0045165; P:cell fate commitment; IMP:MGI.
GO; GO:0060216; P:definitive hemopoiesis; IMP:MGI.
GO; GO:0035162; P:embryonic hemopoiesis; IMP:UniProtKB.
GO; GO:0030218; P:erythrocyte differentiation; IDA:MGI.
GO; GO:0043249; P:erythrocyte maturation; IMP:MGI.
GO; GO:0048699; P:generation of neurons; IMP:MGI.
GO; GO:0060217; P:hemangioblast cell differentiation; IMP:MGI.
GO; GO:0060218; P:hematopoietic stem cell differentiation; IMP:MGI.
GO; GO:0030097; P:hemopoiesis; IDA:MGI.
GO; GO:0007626; P:locomotory behavior; IMP:MGI.
GO; GO:0035855; P:megakaryocyte development; IMP:MGI.
GO; GO:0030219; P:megakaryocyte differentiation; IMP:MGI.
GO; GO:0030099; P:myeloid cell differentiation; IDA:MGI.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IGI:MGI.
GO; GO:0030182; P:neuron differentiation; IMP:MGI.
GO; GO:0030220; P:platelet formation; IMP:MGI.
GO; GO:0051781; P:positive regulation of cell division; ISO:MGI.
GO; GO:0045799; P:positive regulation of chromatin assembly or disassembly; ISO:MGI.
GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IDA:BHF-UCL.
GO; GO:0045931; P:positive regulation of mitotic cell cycle; ISO:MGI.
GO; GO:0031334; P:positive regulation of protein complex assembly; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0042127; P:regulation of cell proliferation; IMP:MGI.
GO; GO:0060375; P:regulation of mast cell differentiation; IMP:MGI.
GO; GO:0045637; P:regulation of myeloid cell differentiation; IMP:MGI.
GO; GO:2000036; P:regulation of stem cell population maintenance; IMP:MGI.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0021527; P:spinal cord association neuron differentiation; IGI:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00083; HLH; 1.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR036638; HLH_DNA-bd_sf.
Pfam; PF00010; HLH; 1.
SMART; SM00353; HLH; 1.
SUPFAM; SSF47459; SSF47459; 1.
PROSITE; PS50888; BHLH; 1.
1: Evidence at protein level;
Chromosomal rearrangement; Complete proteome; Developmental protein;
Differentiation; DNA-binding; Nucleus; Phosphoprotein; Proto-oncogene;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 329 T-cell acute lymphocytic leukemia protein
1 homolog.
/FTId=PRO_0000127455.
DOMAIN 187 239 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
COMPBIAS 263 272 Poly-Gly.
MOD_RES 12 12 Phosphoserine.
{ECO:0000250|UniProtKB:P17542}.
MOD_RES 122 122 Phosphoserine; by MAPK.
{ECO:0000269|PubMed:11904294}.
MOD_RES 172 172 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MUTAGEN 122 122 S->A: Remains stable, even in the face of
severe hypoxia.
{ECO:0000269|PubMed:11904294}.
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


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