ID   TAL1_HUMAN              Reviewed;         331 AA.
AC   P17542; D3DQ24;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 2.
DT   24-JAN-2024, entry version 218.
DE   RecName: Full=T-cell acute lymphocytic leukemia protein 1;
DE            Short=TAL-1;
DE   AltName: Full=Class A basic helix-loop-helix protein 17;
DE            Short=bHLHa17;
DE   AltName: Full=Stem cell protein;
DE   AltName: Full=T-cell leukemia/lymphoma protein 5;
GN   Name=TAL1; Synonyms=BHLHA17, SCL, TCL5;
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 [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING.
RX   PubMed=2247063; DOI=10.1128/mcb.10.12.6426-6435.1990;
RA   Aplan P.D., Begley C.G., Bertness V., Nussmeier M., Ezquerra A.,
RA   Coligan J., Kirsch I.R.;
RT   "The SCL gene is formed from a transcriptionally complex locus.";
RL   Mol. Cell. Biol. 10:6426-6435(1990).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 106-148.
RX   PubMed=2230650; DOI=10.1084/jem.172.5.1403;
RA   Chen Q., Yang C.Y.C., Tsan J.T., Xia Y., Ragab A.H., Peiper S.C.,
RA   Carroll A., Baer R.;
RT   "Coding sequences of the tal-1 gene are disrupted by chromosome
RT   translocation in human T cell leukemia.";
RL   J. Exp. Med. 172:1403-1408(1990).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 118-331.
RC   TISSUE=Bone marrow;
RX   PubMed=2602361; DOI=10.1073/pnas.86.24.10128;
RA   Begley C.G., Aplan P.D., Denning S.M., Haynes B.F., Waldmann T.A.,
RA   Kirsch I.R.;
RT   "The gene SCL is expressed during early hematopoiesis and encodes a
RT   differentiation-related DNA-binding motif.";
RL   Proc. Natl. Acad. Sci. U.S.A. 86:10128-10132(1989).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 181-331, AND CHROMOSOMAL TRANSLOCATION.
RX   PubMed=2303035; DOI=10.1002/j.1460-2075.1990.tb08126.x;
RA   Chen Q., Cheng J.-T., Tsai L.H., Schneider N., Buchanan G., Carroll A.,
RA   Crist W., Ozanne B., Siciliano M.J., Baer R.;
RT   "The tal gene undergoes chromosome translocation in T cell leukemia and
RT   potentially encodes a helix-loop-helix protein.";
RL   EMBO J. 9:415-424(1990).
RN   [7]
RP   FUNCTION.
RX   PubMed=1396592; DOI=10.1002/j.1460-2075.1992.tb05500.x;
RA   Aplan P.D., Nakahara K., Orkin S.H., Kirsch I.R.;
RT   "The SCL gene product: a positive regulator of erythroid differentiation.";
RL   EMBO J. 11:4073-4081(1992).
RN   [8]
RP   PHOSPHORYLATION.
RX   PubMed=8437851;
RA   Cheng J.-T., Hsu H.-L., Hwang L.-Y., Baer R.;
RT   "Products of the TAL1 oncogene: basic helix-loop-helix proteins
RT   phosphorylated at serine residues.";
RL   Oncogene 8:677-683(1993).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-122, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(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 (By similarity).
CC       {ECO:0000250, ECO:0000269|PubMed:1396592}.
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. Interacts with SBNO2; this interaction
CC       inhibits TAL1 occupancy of the DCSTAMP promoter, leading to the
CC       activation of the DCSTAMP promoter by the transcription factor MITF.
CC       {ECO:0000250|UniProtKB:P22091}.
CC   -!- INTERACTION:
CC       P17542; P14921: ETS1; NbExp=2; IntAct=EBI-1753878, EBI-913209;
CC       P17542; O60341-1: KDM1A; NbExp=5; IntAct=EBI-1753878, EBI-15599570;
CC       P17542; P10242: MYB; NbExp=2; IntAct=EBI-1753878, EBI-298355;
CC       P17542; Q01196: RUNX1; NbExp=3; IntAct=EBI-1753878, EBI-925904;
CC       P17542; Q99081: TCF12; NbExp=6; IntAct=EBI-1753878, EBI-722877;
CC       P17542; P15923: TCF3; NbExp=9; IntAct=EBI-1753878, EBI-769630;
CC       P17542; P15884: TCF4; NbExp=4; IntAct=EBI-1753878, EBI-533224;
CC       P17542; P25801: Lmo2; Xeno; NbExp=5; IntAct=EBI-1753878, EBI-3903256;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC         Comment=The splicing pattern is cell-lineage dependent.;
CC       Name=PP42-TAL1;
CC         IsoId=P17542-1; Sequence=Displayed;
CC       Name=PP39-TAL1;
CC         IsoId=P17542-2; Sequence=VSP_002153;
CC       Name=PP22-TAL1;
CC         IsoId=P17542-3; Sequence=VSP_002154;
CC   -!- TISSUE SPECIFICITY: Leukemic stem cell.
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 is
CC       strongly stimulated by hypoxia (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- DISEASE: Note=A chromosomal aberration involving TAL1 may be a cause of
CC       some T-cell acute lymphoblastic leukemias (T-ALL). Translocation
CC       t(1;14)(p32;q11) with T-cell receptor alpha chain (TCRA) genes.
CC       {ECO:0000269|PubMed:2303035}.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/15/TAL1";
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DR   EMBL; M61108; AAA36600.1; -; mRNA.
DR   EMBL; M61103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; M61104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; M61105; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; M63572; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; M63589; AAA36599.1; -; Genomic_DNA.
DR   EMBL; M63576; AAA36599.1; JOINED; Genomic_DNA.
DR   EMBL; M63584; AAA36599.1; JOINED; Genomic_DNA.
DR   EMBL; AL135960; CAB72103.1; -; Genomic_DNA.
DR   EMBL; CH471059; EAX06875.1; -; Genomic_DNA.
DR   EMBL; CH471059; EAX06876.1; -; Genomic_DNA.
DR   EMBL; CH471059; EAX06877.1; -; Genomic_DNA.
DR   EMBL; X58621; CAA41476.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; X58622; CAA41477.1; -; Genomic_DNA.
DR   EMBL; M29038; AAA36598.1; -; mRNA.
DR   EMBL; X51990; CAA36246.1; -; mRNA.
DR   CCDS; CCDS547.1; -. [P17542-1]
DR   PIR; A36358; A36358.
DR   PIR; I38253; I38253.
DR   RefSeq; NP_001274276.1; NM_001287347.2. [P17542-1]
DR   RefSeq; NP_001277332.1; NM_001290403.1. [P17542-1]
DR   RefSeq; NP_001277333.1; NM_001290404.1. [P17542-1]
DR   RefSeq; NP_001277334.1; NM_001290405.1. [P17542-1]
DR   RefSeq; NP_001277335.1; NM_001290406.1.
DR   RefSeq; NP_003180.1; NM_003189.5. [P17542-1]
DR   RefSeq; XP_005271217.1; XM_005271160.4.
DR   RefSeq; XP_016857676.1; XM_017002187.1.
DR   RefSeq; XP_016857677.1; XM_017002188.1.
DR   RefSeq; XP_016857678.1; XM_017002189.1.
DR   RefSeq; XP_016857679.1; XM_017002190.1.
DR   RefSeq; XP_016857680.1; XM_017002191.1. [P17542-1]
DR   PDB; 2YPA; X-ray; 2.80 A; A=180-253.
DR   PDB; 2YPB; X-ray; 2.87 A; A=180-253.
DR   PDBsum; 2YPA; -.
DR   PDBsum; 2YPB; -.
DR   AlphaFoldDB; P17542; -.
DR   SMR; P17542; -.
DR   BioGRID; 112749; 89.
DR   CORUM; P17542; -.
DR   DIP; DIP-40640N; -.
DR   ELM; P17542; -.
DR   IntAct; P17542; 68.
DR   MINT; P17542; -.
DR   STRING; 9606.ENSP00000294339; -.
DR   iPTMnet; P17542; -.
DR   PhosphoSitePlus; P17542; -.
DR   BioMuta; TAL1; -.
DR   DMDM; 134305; -.
DR   MassIVE; P17542; -.
DR   MaxQB; P17542; -.
DR   PaxDb; 9606-ENSP00000294339; -.
DR   PeptideAtlas; P17542; -.
DR   ProteomicsDB; 53484; -. [P17542-1]
DR   ProteomicsDB; 53485; -. [P17542-2]
DR   ProteomicsDB; 53486; -. [P17542-3]
DR   Pumba; P17542; -.
DR   Antibodypedia; 4499; 885 antibodies from 39 providers.
DR   DNASU; 6886; -.
DR   Ensembl; ENST00000294339.3; ENSP00000294339.3; ENSG00000162367.12. [P17542-1]
DR   Ensembl; ENST00000371884.6; ENSP00000360951.1; ENSG00000162367.12. [P17542-1]
DR   Ensembl; ENST00000691006.1; ENSP00000510655.1; ENSG00000162367.12. [P17542-1]
DR   GeneID; 6886; -.
DR   KEGG; hsa:6886; -.
DR   MANE-Select; ENST00000691006.1; ENSP00000510655.1; NM_001290403.2; NP_001277332.1.
DR   UCSC; uc001cqx.4; human. [P17542-1]
DR   AGR; HGNC:11556; -.
DR   CTD; 6886; -.
DR   DisGeNET; 6886; -.
DR   GeneCards; TAL1; -.
DR   HGNC; HGNC:11556; TAL1.
DR   HPA; ENSG00000162367; Tissue enhanced (bone).
DR   MalaCards; TAL1; -.
DR   MIM; 187040; gene.
DR   neXtProt; NX_P17542; -.
DR   OpenTargets; ENSG00000162367; -.
DR   Orphanet; 99861; Precursor T-cell acute lymphoblastic leukemia.
DR   PharmGKB; PA36326; -.
DR   VEuPathDB; HostDB:ENSG00000162367; -.
DR   eggNOG; KOG4029; Eukaryota.
DR   GeneTree; ENSGT00940000159889; -.
DR   HOGENOM; CLU_059203_0_0_1; -.
DR   InParanoid; P17542; -.
DR   OMA; HMDERNH; -.
DR   OrthoDB; 3476499at2759; -.
DR   PhylomeDB; P17542; -.
DR   TreeFam; TF315153; -.
DR   PathwayCommons; P17542; -.
DR   Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR   Reactome; R-HSA-9616222; Transcriptional regulation of granulopoiesis.
DR   SignaLink; P17542; -.
DR   SIGNOR; P17542; -.
DR   BioGRID-ORCS; 6886; 24 hits in 1179 CRISPR screens.
DR   ChiTaRS; TAL1; human.
DR   GeneWiki; TAL1; -.
DR   GenomeRNAi; 6886; -.
DR   Pharos; P17542; Tbio.
DR   PRO; PR:P17542; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; P17542; Protein.
DR   Bgee; ENSG00000162367; Expressed in trabecular bone tissue and 128 other cell types or tissues.
DR   GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR   GO; GO:0005667; C:transcription regulator complex; IDA:BHF-UCL.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:BHF-UCL.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0070888; F:E-box binding; IDA:BHF-UCL.
DR   GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
DR   GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
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; IBA:GO_Central.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:BHF-UCL.
DR   GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR   GO; GO:0060018; P:astrocyte fate commitment; IEA:Ensembl.
DR   GO; GO:0030221; P:basophil differentiation; IEP:BHF-UCL.
DR   GO; GO:0045165; P:cell fate commitment; ISS:BHF-UCL.
DR   GO; GO:0060216; P:definitive hemopoiesis; IEA:Ensembl.
DR   GO; GO:0035162; P:embryonic hemopoiesis; ISS:UniProtKB.
DR   GO; GO:0030218; P:erythrocyte differentiation; IMP:BHF-UCL.
DR   GO; GO:0043249; P:erythrocyte maturation; IEA:Ensembl.
DR   GO; GO:0060217; P:hemangioblast cell differentiation; IEA:Ensembl.
DR   GO; GO:0060218; P:hematopoietic stem cell differentiation; IEA:Ensembl.
DR   GO; GO:0030097; P:hemopoiesis; ISS:BHF-UCL.
DR   GO; GO:0007626; P:locomotory behavior; IEA:Ensembl.
DR   GO; GO:0035855; P:megakaryocyte development; IEA:Ensembl.
DR   GO; GO:0030219; P:megakaryocyte differentiation; IEP:BHF-UCL.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0030220; P:platelet formation; IEA:Ensembl.
DR   GO; GO:0051781; P:positive regulation of cell division; IMP:BHF-UCL.
DR   GO; GO:1905269; P:positive regulation of chromatin organization; IMP:BHF-UCL.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB.
DR   GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IDA:UniProtKB.
DR   GO; GO:0045931; P:positive regulation of mitotic cell cycle; IMP:BHF-UCL.
DR   GO; GO:0031334; P:positive regulation of protein-containing complex assembly; IDA:BHF-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR   GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0060375; P:regulation of mast cell differentiation; IEA:Ensembl.
DR   GO; GO:1904672; P:regulation of somatic stem cell population maintenance; IEA:Ensembl.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR   GO; GO:0021527; P:spinal cord association neuron differentiation; IEA:Ensembl.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR   CDD; cd19706; bHLH_TS_TAL1; 1.
DR   Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR   IDEAL; IID00543; -.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   InterPro; IPR040238; TAL-like.
DR   PANTHER; PTHR13864:SF16; T-CELL ACUTE LYMPHOCYTIC LEUKEMIA PROTEIN 1; 1.
DR   PANTHER; PTHR13864; T-CELL ACUTE LYMPHOCYTIC LEUKEMIA/STEM CELL LEUKEMIA-RELATED; 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; P17542; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Chromosomal rearrangement;
KW   Developmental protein; Differentiation; DNA-binding; Nucleus;
KW   Phosphoprotein; Proto-oncogene; Reference proteome; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   CHAIN           1..331
FT                   /note="T-cell acute lymphocytic leukemia protein 1"
FT                   /id="PRO_0000127454"
FT   DOMAIN          187..239
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          40..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          249..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..300
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         12
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         122
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         172
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P22091"
FT   VAR_SEQ         1..175
FT                   /note="Missing (in isoform PP22-TAL1)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_002154"
FT   VAR_SEQ         1..25
FT                   /note="Missing (in isoform PP39-TAL1)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_002153"
FT   HELIX           184..211
FT                   /evidence="ECO:0007829|PDB:2YPA"
FT   HELIX           225..245
FT                   /evidence="ECO:0007829|PDB:2YPA"
SQ   SEQUENCE   331 AA;  34271 MW;  33BBE31589DBB7C7 CRC64;
     MTERPPSEAA RSDPQLEGRD AAEASMAPPH LVLLNGVAKE TSRAAAAEPP VIELGARGGP
     GGGPAGGGGA ARDLKGRDAA TAEARHRVPT TELCRPPGPA PAPAPASVTA ELPGDGRMVQ
     LSPPALAAPA APGRALLYSL SQPLASLGSG FFGEPDAFPM FTTNNRVKRR PSPYEMEITD
     GPHTKVVRRI FTNSRERWRQ QNVNGAFAEL RKLIPTHPPD KKLSKNEILR LAMKYINFLA
     KLLNDQEEEG TQRAKTGKDP VVGAGGGGGG GGGGAPPDDL LQDVLSPNSS CGSSLDGAAS
     PDSYTEEPAP KHTARSLHPA MLPAADGAGP R
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