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	Protein Summary
	AS Summary
	Protein Functional Features
	Gene Isoform Structures and Expression Levels
	Protein Structures
	pLDDT Score Distribution
	Ramachandran Plot of Protein Structures
	Potential Active Site Information
	Protein Structure and Feature Comparision
	Protein-Protein Interaction
	Related Drugs
	Related Diseases
	Clinically Important Variants

Protein:RUNX1

Protein Summary

Gene summary

Gene name: RUNX1
ASpdb.0 ID: 861
	Gene
Gene symbol	RUNX1
Gene ID	861
Gene name	RUNX family transcription factor 1
Synonyms	AML1\|AML1-EVI-1\|AMLCR1\|CBF2alpha\|CBFA2\|EVI-1\|PEBP2aB\|PEBP2alpha
Cytomap	21q22.12
Type of gene	protein-coding
Description	runt-related transcription factor 1AML1-ETO fusionAML1-ETO fusion proteinAML1-EVI-1 fusion proteinPEA2-alpha BPEBP2-alpha BSL3-3 enhancer factor 1 alpha B subunitSL3/AKV core-binding factor alpha B subunitacute myeloid leukemia 1 proteincore-bind
Modification date	20240407
UniProtAcc	Q01196

Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez

Partner	Gene	GO ID	GO term	PubMed ID
Gene	RUNX1	GO:0000976	transcription cis-regulatory region binding	21873977
Gene	RUNX1	GO:0000977	RNA polymerase II transcription regulatory region sequence-specific DNA binding	9199349
Gene	RUNX1	GO:0000978	RNA polymerase II cis-regulatory region sequence-specific DNA binding	17377532
Gene	RUNX1	GO:0001228	DNA-binding transcription activator activity, RNA polymerase II-specific	9199349
Gene	RUNX1	GO:0005634	nucleus	7862156
Gene	RUNX1	GO:0005654	nucleoplasm	-
Gene	RUNX1	GO:0030097	hemopoiesis	21873977
Gene	RUNX1	GO:0043231	intracellular membrane-bounded organelle	-
Gene	RUNX1	GO:0045893	positive regulation of DNA-templated transcription	10207087\|14970218
Gene	RUNX1	GO:0045944	positive regulation of transcription by RNA polymerase II	9199349\|10207087\|14970218\|21873977

AS Summary

Information of the canonical protein with experimentally identified structure from PDB (2023).

UniProt Acc	File name	PDB ID	Method	Resolution	Chain	Start	End
Q01196-1	Q01196-1_1h9d_A.pdb	1H9D	X-ray	2.6	A	54	178

ASpdb's canonical and alternatively spliced isoform information.

accession_id	gene_name	canonical_id	alternative_id	canonical_length	alternative_length	canonical_start	canonical_end	type	originalSEQ	variationSEQ	alternative_start	alternative_end
Q01196	RUNX1	Q01196-1	Q01196-10	453	468	1	5	Substitution	MRIPV	MPAAPRGPAQGEAAARTRSR	1	20
Q01196	RUNX1	Q01196-1	Q01196-11	453	348	1	105	Deletion	none	none	0	0
Q01196	RUNX1	Q01196-1	Q01196-2	453	472	440	453	Substitution	APSARLEEAVWRPY	GGASCSRQARRDPGPWARTPSWGRGRPTDRISL	440	472
Q01196	RUNX1	Q01196-1	Q01196-3	453	250	242	250	Substitution	DTRQIQPSP	EEDTAPWRC	242	250
Q01196	RUNX1	Q01196-1	Q01196-3	453	250	251	453	Deletion	none	none	250	250
Q01196	RUNX1	Q01196-1	Q01196-4	453	257	258	453	Deletion	none	none	257	257
Q01196	RUNX1	Q01196-1	Q01196-5	453	224	178	224	Substitution	RHRQKLDDQTKPGSLSFSERLSELEQLRRTAMRVSPHHPAPTPNPRA	SKCIHLGLVHPPGWYTLQAGILRDHVSDSLGSTFPPGGWQAPVKPKS	178	224
Q01196	RUNX1	Q01196-1	Q01196-5	453	224	225	453	Deletion	none	none	224	224
Q01196	RUNX1	Q01196-1	Q01196-6	453	188	178	188	Substitution	RHRQKLDDQTK	NSLTWPRYPHI	178	188
Q01196	RUNX1	Q01196-1	Q01196-6	453	188	189	453	Deletion	none	none	188	188
Q01196	RUNX1	Q01196-1	Q01196-7	453	242	137	242	Substitution	VGRSGRGKSFTLTITVFTNPPQVATYHRAIKITVDGPREPRRHRQKLDDQTKPGSLSFSERLSELEQLRRTAMRVSPHHPAPTPNPRASLNHSTAFNPQPQSQMQD	VDGPREPRRHRQKLDDQTKPGSLSFSERLSELEQLRRTAMRVSPHHPAPTPNPRASLNHSTAFNPQPQSQMQDTRQIQPSPPWSYDQSYQYLGSIASPSVHPATPI	137	242
Q01196	RUNX1	Q01196-1	Q01196-7	453	242	243	453	Deletion	none	none	242	242
Q01196	RUNX1	Q01196-1	Q01196-8	453	480	1	5	Substitution	MRIPV	MASDSIFESFPSYPQCFMRECILGMNPSRDVH	1	32
Q01196	RUNX1	Q01196-1	Q01196-9	453	456	1	5	Substitution	MRIPV	MNPSRDVH	1	8

Multiple sequence alignment of our canonical and alternatively spliced RUNX1

Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of RUNX1

UniProt-id	ENSG	ENST	ENSP
Q01196-1	ENSG00000159216.19	ENST00000344691.8	ENSP00000340690.4
Q01196-3	ENSG00000159216.19	ENST00000358356.9	ENSP00000351123.5
Q01196-8	ENSG00000159216.19	ENST00000300305.7	ENSP00000300305.3
Q01196-8	ENSG00000159216.19	ENST00000437180.5	ENSP00000409227.1
Q01196-8	ENSG00000159216.19	ENST00000675419.1	ENSP00000501943.1

UniProt-id	NM ID	NP ID
Q01196-1	NM_001001890.2	NP_001001890.1
Q01196-10	XM_005261068.3	XP_005261125.1
Q01196-3	NM_001122607.1	NP_001116079.1
Q01196-8	NM_001754.4	NP_001745.2
Q01196-8	XM_011529766.2	XP_011528068.1

Amino acid sequences of our canonical and alternatively spliced RUNX1

accession_id	Protein sequence
Q01196-1	MRIPVDASTSRRFTPPSTALSPGKMSEALPLGAPDAGAALAGKLRSGDRSMVEVLADHPGELVRTDSPNFLCSVLPTHWRCNKTLPIAFK VVALGDVPDGTLVTVMAGNDENYSAELRNATAAMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKITVDGPREPRRHR QKLDDQTKPGSLSFSERLSELEQLRRTAMRVSPHHPAPTPNPRASLNHSTAFNPQPQSQMQDTRQIQPSPPWSYDQSYQYLGSIASPSVH PATPISPGRASGMTTLSAELSSRLSTAPDLTAFSDPRQFPALPSISDPRMHYPGAFTYSPTPVTSGIGIGMSAMGSATRYHTYLPPPYPG SSQAQGGPFQASSPSYHLYYGASAGSYQFSMVGGERSPPRILPPCTNASTGSALLNPSLPNQSDVVEAEGSHSNSPTNMAPSARLEEAVW
Q01196-10	MPAAPRGPAQGEAAARTRSRDASTSRRFTPPSTALSPGKMSEALPLGAPDAGAALAGKLRSGDRSMVEVLADHPGELVRTDSPNFLCSVL PTHWRCNKTLPIAFKVVALGDVPDGTLVTVMAGNDENYSAELRNATAAMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRA IKITVDGPREPRRHRQKLDDQTKPGSLSFSERLSELEQLRRTAMRVSPHHPAPTPNPRASLNHSTAFNPQPQSQMQDTRQIQPSPPWSYD QSYQYLGSIASPSVHPATPISPGRASGMTTLSAELSSRLSTAPDLTAFSDPRQFPALPSISDPRMHYPGAFTYSPTPVTSGIGIGMSAMG SATRYHTYLPPPYPGSSQAQGGPFQASSPSYHLYYGASAGSYQFSMVGGERSPPRILPPCTNASTGSALLNPSLPNQSDVVEAEGSHSNS
Q01196-11	MAGNDENYSAELRNATAAMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKITVDGPREPRRHRQKLDDQTKPGSLSFS ERLSELEQLRRTAMRVSPHHPAPTPNPRASLNHSTAFNPQPQSQMQDTRQIQPSPPWSYDQSYQYLGSIASPSVHPATPISPGRASGMTT LSAELSSRLSTAPDLTAFSDPRQFPALPSISDPRMHYPGAFTYSPTPVTSGIGIGMSAMGSATRYHTYLPPPYPGSSQAQGGPFQASSPS
Q01196-2	MRIPVDASTSRRFTPPSTALSPGKMSEALPLGAPDAGAALAGKLRSGDRSMVEVLADHPGELVRTDSPNFLCSVLPTHWRCNKTLPIAFK VVALGDVPDGTLVTVMAGNDENYSAELRNATAAMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKITVDGPREPRRHR QKLDDQTKPGSLSFSERLSELEQLRRTAMRVSPHHPAPTPNPRASLNHSTAFNPQPQSQMQDTRQIQPSPPWSYDQSYQYLGSIASPSVH PATPISPGRASGMTTLSAELSSRLSTAPDLTAFSDPRQFPALPSISDPRMHYPGAFTYSPTPVTSGIGIGMSAMGSATRYHTYLPPPYPG SSQAQGGPFQASSPSYHLYYGASAGSYQFSMVGGERSPPRILPPCTNASTGSALLNPSLPNQSDVVEAEGSHSNSPTNMGGASCSRQARR
Q01196-3	MRIPVDASTSRRFTPPSTALSPGKMSEALPLGAPDAGAALAGKLRSGDRSMVEVLADHPGELVRTDSPNFLCSVLPTHWRCNKTLPIAFK VVALGDVPDGTLVTVMAGNDENYSAELRNATAAMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKITVDGPREPRRHR
Q01196-4	MRIPVDASTSRRFTPPSTALSPGKMSEALPLGAPDAGAALAGKLRSGDRSMVEVLADHPGELVRTDSPNFLCSVLPTHWRCNKTLPIAFK VVALGDVPDGTLVTVMAGNDENYSAELRNATAAMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKITVDGPREPRRHR
Q01196-5	MRIPVDASTSRRFTPPSTALSPGKMSEALPLGAPDAGAALAGKLRSGDRSMVEVLADHPGELVRTDSPNFLCSVLPTHWRCNKTLPIAFK VVALGDVPDGTLVTVMAGNDENYSAELRNATAAMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKITVDGPREPRSKC
Q01196-6	MRIPVDASTSRRFTPPSTALSPGKMSEALPLGAPDAGAALAGKLRSGDRSMVEVLADHPGELVRTDSPNFLCSVLPTHWRCNKTLPIAFK VVALGDVPDGTLVTVMAGNDENYSAELRNATAAMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKITVDGPREPRNSL
Q01196-7	MRIPVDASTSRRFTPPSTALSPGKMSEALPLGAPDAGAALAGKLRSGDRSMVEVLADHPGELVRTDSPNFLCSVLPTHWRCNKTLPIAFK VVALGDVPDGTLVTVMAGNDENYSAELRNATAAMKNQVARFNDLRFVDGPREPRRHRQKLDDQTKPGSLSFSERLSELEQLRRTAMRVSP
Q01196-8	MASDSIFESFPSYPQCFMRECILGMNPSRDVHDASTSRRFTPPSTALSPGKMSEALPLGAPDAGAALAGKLRSGDRSMVEVLADHPGELV RTDSPNFLCSVLPTHWRCNKTLPIAFKVVALGDVPDGTLVTVMAGNDENYSAELRNATAAMKNQVARFNDLRFVGRSGRGKSFTLTITVF TNPPQVATYHRAIKITVDGPREPRRHRQKLDDQTKPGSLSFSERLSELEQLRRTAMRVSPHHPAPTPNPRASLNHSTAFNPQPQSQMQDT RQIQPSPPWSYDQSYQYLGSIASPSVHPATPISPGRASGMTTLSAELSSRLSTAPDLTAFSDPRQFPALPSISDPRMHYPGAFTYSPTPV TSGIGIGMSAMGSATRYHTYLPPPYPGSSQAQGGPFQASSPSYHLYYGASAGSYQFSMVGGERSPPRILPPCTNASTGSALLNPSLPNQS
Q01196-9	MNPSRDVHDASTSRRFTPPSTALSPGKMSEALPLGAPDAGAALAGKLRSGDRSMVEVLADHPGELVRTDSPNFLCSVLPTHWRCNKTLPI AFKVVALGDVPDGTLVTVMAGNDENYSAELRNATAAMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKITVDGPREPR RHRQKLDDQTKPGSLSFSERLSELEQLRRTAMRVSPHHPAPTPNPRASLNHSTAFNPQPQSQMQDTRQIQPSPPWSYDQSYQYLGSIASP SVHPATPISPGRASGMTTLSAELSSRLSTAPDLTAFSDPRQFPALPSISDPRMHYPGAFTYSPTPVTSGIGIGMSAMGSATRYHTYLPPP YPGSSQAQGGPFQASSPSYHLYYGASAGSYQFSMVGGERSPPRILPPCTNASTGSALLNPSLPNQSDVVEAEGSHSNSPTNMAPSARLEE

Protein Functional Features

Main function of this protein. (from UniProt)

RUNX1 (go to UniProt):Q01196

Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at
download page
* Minus value of BPloci means that the break pointn is located before the CDS.

- Retained protein feature among the 13 regional features.

Accession_id	Subsection	Start	End	Funcitonal feature	Splicing information
Q01196	Domain	50	178	Note=Runt;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00399	Type=Deletion;Start=1;End=105
Q01196	Domain	50	178	Note=Runt;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00399	Type=Substitution;Start=178;End=224
Q01196	Domain	50	178	Note=Runt;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00399	Type=Substitution;Start=178;End=188
Q01196	Domain	50	178	Note=Runt;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00399	Type=Substitution;Start=137;End=242
Q01196	Region	1	26	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=1;End=5
Q01196	Region	1	26	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=1;End=105
Q01196	Region	1	26	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=1;End=5
Q01196	Region	1	26	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=1;End=5
Q01196	Region	80	84	Note=Interaction with DNA	Type=Deletion;Start=1;End=105
Q01196	Region	135	143	Note=Interaction with DNA	Type=Substitution;Start=137;End=242
Q01196	Region	168	177	Note=Interaction with DNA	Type=Substitution;Start=137;End=242
Q01196	Region	171	195	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=178;End=224
Q01196	Region	171	195	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=178;End=188
Q01196	Region	171	195	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=189;End=453
Q01196	Region	171	195	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=137;End=242
Q01196	Region	209	252	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=242;End=250
Q01196	Region	209	252	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=251;End=453
Q01196	Region	209	252	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=178;End=224
Q01196	Region	209	252	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=225;End=453
Q01196	Region	209	252	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=189;End=453
Q01196	Region	209	252	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=137;End=242
Q01196	Region	209	252	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=243;End=453
Q01196	Region	291	371	Note=Interaction with KAT6A;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:11742995;Dbxref=PMID:11742995	Type=Deletion;Start=251;End=453
Q01196	Region	291	371	Note=Interaction with KAT6A;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:11742995;Dbxref=PMID:11742995	Type=Deletion;Start=258;End=453
Q01196	Region	291	371	Note=Interaction with KAT6A;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:11742995;Dbxref=PMID:11742995	Type=Deletion;Start=225;End=453
Q01196	Region	291	371	Note=Interaction with KAT6A;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:11742995;Dbxref=PMID:11742995	Type=Deletion;Start=189;End=453
Q01196	Region	291	371	Note=Interaction with KAT6A;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:11742995;Dbxref=PMID:11742995	Type=Deletion;Start=243;End=453
Q01196	Region	307	400	Note=Interaction with KAT6B;Ontology_term=ECO:0000250;evidence=ECO:0000250	Type=Deletion;Start=251;End=453
Q01196	Region	307	400	Note=Interaction with KAT6B;Ontology_term=ECO:0000250;evidence=ECO:0000250	Type=Deletion;Start=258;End=453
Q01196	Region	307	400	Note=Interaction with KAT6B;Ontology_term=ECO:0000250;evidence=ECO:0000250	Type=Deletion;Start=225;End=453
Q01196	Region	307	400	Note=Interaction with KAT6B;Ontology_term=ECO:0000250;evidence=ECO:0000250	Type=Deletion;Start=189;End=453
Q01196	Region	307	400	Note=Interaction with KAT6B;Ontology_term=ECO:0000250;evidence=ECO:0000250	Type=Deletion;Start=243;End=453
Q01196	Region	362	402	Note=Interaction with FOXP3;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:17377532;Dbxref=PMID:17377532	Type=Deletion;Start=251;End=453
Q01196	Region	362	402	Note=Interaction with FOXP3;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:17377532;Dbxref=PMID:17377532	Type=Deletion;Start=258;End=453
Q01196	Region	362	402	Note=Interaction with FOXP3;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:17377532;Dbxref=PMID:17377532	Type=Deletion;Start=225;End=453
Q01196	Region	362	402	Note=Interaction with FOXP3;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:17377532;Dbxref=PMID:17377532	Type=Deletion;Start=189;End=453
Q01196	Region	362	402	Note=Interaction with FOXP3;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:17377532;Dbxref=PMID:17377532	Type=Deletion;Start=243;End=453
Q01196	Region	404	445	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=440;End=453
Q01196	Region	404	445	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=251;End=453
Q01196	Region	404	445	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=258;End=453
Q01196	Region	404	445	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=225;End=453
Q01196	Region	404	445	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=189;End=453
Q01196	Region	404	445	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=243;End=453
Q01196	Compositional bias	171	186	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=178;End=224
Q01196	Compositional bias	171	186	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=178;End=188
Q01196	Compositional bias	171	186	Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=137;End=242
Q01196	Compositional bias	222	252	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=242;End=250
Q01196	Compositional bias	222	252	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=251;End=453
Q01196	Compositional bias	222	252	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=178;End=224
Q01196	Compositional bias	222	252	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=225;End=453
Q01196	Compositional bias	222	252	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=189;End=453
Q01196	Compositional bias	222	252	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=137;End=242
Q01196	Compositional bias	222	252	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=243;End=453
Q01196	Compositional bias	404	441	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Substitution;Start=440;End=453
Q01196	Compositional bias	404	441	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=251;End=453
Q01196	Compositional bias	404	441	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=258;End=453
Q01196	Compositional bias	404	441	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=225;End=453
Q01196	Compositional bias	404	441	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=189;End=453
Q01196	Compositional bias	404	441	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=243;End=453

Gene Isoform Structures and Expression Levels for RUNX1

Gene structures of our canonical and alternative spliced genes of RUNX1
* Click on the image to open the UCSC genome browser with custom track showing this image in a new window.

Expression levels of gene isoforms across GTEx.

Expression levels of gene isoforms across TCGA.

Protein Structures

PDB and CIF files of the predicted protein structures
* Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format.

3D view using mol* of Q01196-1

3D view using mol* of Q01196-10

3D view using mol* of Q01196-11

3D view using mol* of Q01196-2

3D view using mol* of Q01196-3

3D view using mol* of Q01196-4

3D view using mol* of Q01196-5

3D view using mol* of Q01196-6

3D view using mol* of Q01196-7

3D view using mol* of Q01196-8

3D view using mol* of Q01196-9

pLDDT Score Distribution

pLDDT score distribution of the predicted protein structures from AlphaFold2
* AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100.

pLDDT distribution across the protein length of Q01196-1

pLDDT distribution across the protein length of Q01196-10

pLDDT distribution across the protein length of Q01196-11

pLDDT distribution across the protein length of Q01196-2

pLDDT distribution across the protein length of Q01196-3

pLDDT distribution across the protein length of Q01196-4

pLDDT distribution across the protein length of Q01196-5

pLDDT distribution across the protein length of Q01196-6

pLDDT distribution across the protein length of Q01196-7

pLDDT distribution across the protein length of Q01196-8

pLDDT distribution across the protein length of Q01196-9

Ramachandran Plot of Protein Structures

Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide.

Ramachandran plot of Q01196-1

Ramachandran plot of Q01196-11

Ramachandran plot of Q01196-3

Ramachandran plot of Q01196-4

Ramachandran plot of Q01196-7

Ramachandran plot of Q01196-9

Potential Active Site Information

The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite.

UniProt-id	Site score	Size	D score	Volume	Exposure	Enclosure	Contact	Phobic	Philic	Balance	Don/Acc	Residues
Q01196-1	0.592	20	0.573	52.479	0.775	0.551	0.706	0.525	0.547	0.96	1.128	106,107,108,109,113,114,115,117,147,149
Q01196-10	0.61	22	0.586	64.484	0.766	0.574	0.756	0.622	0.611	1.017	0.832	121,122,123,128,129,130,162,164
Q01196-11	1.01	114	1.046	188.993	0.37	0.68	0.958	1.021	0.925	1.104	0.494	1,2,12,15,16,17,18,19,24,26,29,31,43,44,45,46,47,4 8
Q01196-2	0.589	18	0.549	60.025	0.735	0.599	0.882	0.678	0.642	1.056	1.213	106,107,108,113,114,115,147,149
Q01196-3	0.57	18	0.526	56.252	0.788	0.582	0.798	0.502	0.682	0.737	1.593	106,107,108,113,114,115,117,147,149
Q01196-4	0.6	22	0.565	60.025	0.788	0.579	0.736	0.429	0.683	0.628	1.117	106,107,108,113,114,115,117,147,149
Q01196-5	0.628	27	0.624	85.407	0.83	0.529	0.675	0.576	0.559	1.03	0.853	106,107,108,113,114,115,116,117,147,148,149
Q01196-6	0.609	18	0.594	58.653	0.775	0.58	0.808	0.978	0.469	2.083	1.049	106,107,108,109,113,114,115,117,147,149
Q01196-7	0.877	65	0.886	162.925	0.629	0.666	0.904	0.874	0.834	1.048	1.837	75,76,77,78,79,80,81,85,107,108,109,111,112,115,13 6,138,139,140,141
Q01196-8	0.665	27	0.637	71.001	0.693	0.623	0.806	0.535	0.691	0.773	1.134	133,134,135,136,140,141,142,144,174,175,176
Q01196-9	0.599	22	0.572	58.653	0.773	0.563	0.729	0.635	0.635	1	1.283	109,110,111,116,117,118,120,150,152

Protein Structure and Feature Comparision

Protein Structure Comparision Using Template Modeling Scores (TM-score).

Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green)

3D view using mol* of Q01196-1_Q01196-1_1h9d_A.pdb

Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green)

3D view using mol* of Q01196-1_1h9d_A_Q01196-10.pdb

3D view using mol* of Q01196-1_1h9d_A_Q01196-11.pdb

3D view using mol* of Q01196-1_1h9d_A_Q01196-2.pdb

3D view using mol* of Q01196-1_1h9d_A_Q01196-3.pdb

3D view using mol* of Q01196-1_1h9d_A_Q01196-4.pdb

3D view using mol* of Q01196-1_1h9d_A_Q01196-5.pdb

3D view using mol* of Q01196-1_1h9d_A_Q01196-6.pdb

3D view using mol* of Q01196-1_1h9d_A_Q01196-7.pdb

3D view using mol* of Q01196-1_1h9d_A_Q01196-8.pdb

3D view using mol* of Q01196-1_1h9d_A_Q01196-9.pdb

Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green)

3D view using mol* of Q01196-1_Q01196-10.pdb

3D view using mol* of Q01196-1_Q01196-11.pdb

3D view using mol* of Q01196-1_Q01196-2.pdb

3D view using mol* of Q01196-1_Q01196-3.pdb

3D view using mol* of Q01196-1_Q01196-4.pdb

3D view using mol* of Q01196-1_Q01196-5.pdb

3D view using mol* of Q01196-1_Q01196-6.pdb

3D view using mol* of Q01196-1_Q01196-7.pdb

3D view using mol* of Q01196-1_Q01196-8.pdb

3D view using mol* of Q01196-1_Q01196-9.pdb

Protein Feature Comparison of the protein sequendary structures among the protiens.

./stats/secondary_structure/figure/Q01196-1_vs_Q01196-10.png

./stats/secondary_structure/figure/Q01196-1_vs_Q01196-11.png

./stats/secondary_structure/figure/Q01196-1_vs_Q01196-2.png

./stats/secondary_structure/figure/Q01196-1_vs_Q01196-3.png

./stats/secondary_structure/figure/Q01196-1_vs_Q01196-4.png

./stats/secondary_structure/figure/Q01196-1_vs_Q01196-5.png

./stats/secondary_structure/figure/Q01196-1_vs_Q01196-6.png

./stats/secondary_structure/figure/Q01196-1_vs_Q01196-7.png

./stats/secondary_structure/figure/Q01196-1_vs_Q01196-8.png

./stats/secondary_structure/figure/Q01196-1_vs_Q01196-9.png

Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens.

./stats/relative_asa/Q01196-1_vs_Q01196-10.png

./stats/relative_asa/Q01196-1_vs_Q01196-11.png

./stats/relative_asa/Q01196-1_vs_Q01196-2.png

./stats/relative_asa/Q01196-1_vs_Q01196-3.png

./stats/relative_asa/Q01196-1_vs_Q01196-4.png

./stats/relative_asa/Q01196-1_vs_Q01196-5.png

./stats/relative_asa/Q01196-1_vs_Q01196-6.png

./stats/relative_asa/Q01196-1_vs_Q01196-7.png

./stats/relative_asa/Q01196-1_vs_Q01196-8.png

./stats/relative_asa/Q01196-1_vs_Q01196-9.png

Protein-Protein Interaction

Interactors from UniProt.

Accession_id	Subsection	Start	End	Funcitonal feature	Splicing information
Q01196	Region	80	84	Note=Interaction with DNA	Type=Deletion;Start=1;End=105
Q01196	Region	135	143	Note=Interaction with DNA	Type=Substitution;Start=137;End=242
Q01196	Region	168	177	Note=Interaction with DNA	Type=Substitution;Start=137;End=242
Q01196	Region	291	371	Note=Interaction with KAT6A;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:11742995;Dbxref=PMID:11742995	Type=Deletion;Start=251;End=453
Q01196	Region	291	371	Note=Interaction with KAT6A;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:11742995;Dbxref=PMID:11742995	Type=Deletion;Start=258;End=453
Q01196	Region	291	371	Note=Interaction with KAT6A;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:11742995;Dbxref=PMID:11742995	Type=Deletion;Start=225;End=453
Q01196	Region	291	371	Note=Interaction with KAT6A;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:11742995;Dbxref=PMID:11742995	Type=Deletion;Start=189;End=453
Q01196	Region	291	371	Note=Interaction with KAT6A;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:11742995;Dbxref=PMID:11742995	Type=Deletion;Start=243;End=453
Q01196	Region	307	400	Note=Interaction with KAT6B;Ontology_term=ECO:0000250;evidence=ECO:0000250	Type=Deletion;Start=251;End=453
Q01196	Region	307	400	Note=Interaction with KAT6B;Ontology_term=ECO:0000250;evidence=ECO:0000250	Type=Deletion;Start=258;End=453
Q01196	Region	307	400	Note=Interaction with KAT6B;Ontology_term=ECO:0000250;evidence=ECO:0000250	Type=Deletion;Start=225;End=453
Q01196	Region	307	400	Note=Interaction with KAT6B;Ontology_term=ECO:0000250;evidence=ECO:0000250	Type=Deletion;Start=189;End=453
Q01196	Region	307	400	Note=Interaction with KAT6B;Ontology_term=ECO:0000250;evidence=ECO:0000250	Type=Deletion;Start=243;End=453
Q01196	Region	362	402	Note=Interaction with FOXP3;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:17377532;Dbxref=PMID:17377532	Type=Deletion;Start=251;End=453
Q01196	Region	362	402	Note=Interaction with FOXP3;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:17377532;Dbxref=PMID:17377532	Type=Deletion;Start=258;End=453
Q01196	Region	362	402	Note=Interaction with FOXP3;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:17377532;Dbxref=PMID:17377532	Type=Deletion;Start=225;End=453
Q01196	Region	362	402	Note=Interaction with FOXP3;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:17377532;Dbxref=PMID:17377532	Type=Deletion;Start=189;End=453
Q01196	Region	362	402	Note=Interaction with FOXP3;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:17377532;Dbxref=PMID:17377532	Type=Deletion;Start=243;End=453

Interactors from STRING.

Gene name

Interactors

Related Drugs to RUNX1

Drugs targeting this gene/protein.
(DrugBank)

UniProt accession

Gene name

DrugBank ID

Drug name

Drug group

Actions

Related Diseases to RUNX1

Previous studies relating to the alternative splicing of RUNX1 and disease information from the MeSH term (PubMed)

Gene	PMID	Title	Abstract	MeSH ID	MeSH term
RUNX1	7651838	Alternative splicing and genomic structure of the AML1 gene involved in acute myeloid leukemia.	We previously isolated the AML1 gene, which is rearranged by the t(8;21) translocation in acute myeloid leukemia. The AML1 gene is highly homologous to the Drosophila segmentation gene runt and the mouse transcription factor PEBP2 alpha subunit gene. This region of homology, called the Runt domain, is responsible for DNA-binding and protein--protein interaction. In this study, we isolated and characterized various forms of AML1 cDNAs which reflect a complex pattern of mRNA species. Analysis of these cDNAs has led to the identification of two distinct AML1 proteins, designated AML1b (453 amino acids) and AML1c (480 amino acids), which differ markedly from the previously reported AML1a (250 amino acids) with regard to their C-terminal regions, although all three contain the Runt domain. The large C-terminal region common to AML1b and AML1c is suggested to be a transcriptional activation domain. AML1c differs from AML1b by only 32 amino acids in the N-terminal. Characterization of the genomic structure revealed that the AML1 gene consists of nine exons and spans > 150 kb of genomic DNA. Northern blot analysis demonstrated the presence of six major transcripts, encoding AML1b or AML1c, which can all be explained by the existence of two promoters, alternative splicing and differential usage of three polyadenylation sites. A minor transcript encoding AML1a which results from alternative splicing of a separate exon can be detected only by reverse transcription-polymerase chain reaction amplification. The distinct proteins encoded by the AML1 gene may have different functions, which could contribute to regulating cell growth and/or differentiation through transcriptional regulation of a specific subset of target genes.	D015470	Leukemia, Myeloid, Acute
RUNX1	7651838	Alternative splicing and genomic structure of the AML1 gene involved in acute myeloid leukemia.	We previously isolated the AML1 gene, which is rearranged by the t(8;21) translocation in acute myeloid leukemia. The AML1 gene is highly homologous to the Drosophila segmentation gene runt and the mouse transcription factor PEBP2 alpha subunit gene. This region of homology, called the Runt domain, is responsible for DNA-binding and protein--protein interaction. In this study, we isolated and characterized various forms of AML1 cDNAs which reflect a complex pattern of mRNA species. Analysis of these cDNAs has led to the identification of two distinct AML1 proteins, designated AML1b (453 amino acids) and AML1c (480 amino acids), which differ markedly from the previously reported AML1a (250 amino acids) with regard to their C-terminal regions, although all three contain the Runt domain. The large C-terminal region common to AML1b and AML1c is suggested to be a transcriptional activation domain. AML1c differs from AML1b by only 32 amino acids in the N-terminal. Characterization of the genomic structure revealed that the AML1 gene consists of nine exons and spans > 150 kb of genomic DNA. Northern blot analysis demonstrated the presence of six major transcripts, encoding AML1b or AML1c, which can all be explained by the existence of two promoters, alternative splicing and differential usage of three polyadenylation sites. A minor transcript encoding AML1a which results from alternative splicing of a separate exon can be detected only by reverse transcription-polymerase chain reaction amplification. The distinct proteins encoded by the AML1 gene may have different functions, which could contribute to regulating cell growth and/or differentiation through transcriptional regulation of a specific subset of target genes.	D014178	Translocation, Genetic
RUNX1	15723339	MYND-less splice variants of AML1-MTG8 (RUNX1-CBFA2T1) are expressed in leukemia with t(8;21).	The AML1-MTG8 fusion gene is generated by chromosome translocation t(8;21), which is frequently observed in acute myeloid leukemia. The fusion gene produces a chimeric transcription factor that suppresses the expression of AML1-target genes via the MTG8 part of the chimeric protein, which is thought to be the primary cause of leukemia. The C-terminal region of MTG8 contains the MYND domain, represented by highly conserved zinc-finger-like protein motifs, and is known to interact with corepressor proteins. We found that, instead of the MYND domain, an alternative last exon of MTG8 encoding 27 amino acids in-frame is expressed naturally in human adult testis and in several leukemia cell lines. This type of alternative splicing also occurred in the AML1-MTG8 fusion gene at high levels in leukemia cell lines with t(8;21), as well as in blast cells of leukemia patients with t(8;21). The variant proteins of both MTG8 and AML1-MTG8 reduced transcriptional repressor activity in a mammalian two-hybrid assay. However, mixed expression of these variants with wild-type MTG8 recovered their repressor activity, suggesting that these variants also act as repressors in vivo where wild-type MTG8 and other family members exist in abundance. On the other hand, the MYND-less variants acquired a higher affinity for binding to MTG8 and formed a multimer, whereas the wild-type protein forms a dimer. Thus, expression of the MYND-less variants by the dysregulation of splicing machinery, which stimulates the oligomerization of fusion proteins in leukemia cells, may enhance malignant conversion of hematopoietic cells.	D007938	Leukemia
RUNX1	15723339	MYND-less splice variants of AML1-MTG8 (RUNX1-CBFA2T1) are expressed in leukemia with t(8;21).	The AML1-MTG8 fusion gene is generated by chromosome translocation t(8;21), which is frequently observed in acute myeloid leukemia. The fusion gene produces a chimeric transcription factor that suppresses the expression of AML1-target genes via the MTG8 part of the chimeric protein, which is thought to be the primary cause of leukemia. The C-terminal region of MTG8 contains the MYND domain, represented by highly conserved zinc-finger-like protein motifs, and is known to interact with corepressor proteins. We found that, instead of the MYND domain, an alternative last exon of MTG8 encoding 27 amino acids in-frame is expressed naturally in human adult testis and in several leukemia cell lines. This type of alternative splicing also occurred in the AML1-MTG8 fusion gene at high levels in leukemia cell lines with t(8;21), as well as in blast cells of leukemia patients with t(8;21). The variant proteins of both MTG8 and AML1-MTG8 reduced transcriptional repressor activity in a mammalian two-hybrid assay. However, mixed expression of these variants with wild-type MTG8 recovered their repressor activity, suggesting that these variants also act as repressors in vivo where wild-type MTG8 and other family members exist in abundance. On the other hand, the MYND-less variants acquired a higher affinity for binding to MTG8 and formed a multimer, whereas the wild-type protein forms a dimer. Thus, expression of the MYND-less variants by the dysregulation of splicing machinery, which stimulates the oligomerization of fusion proteins in leukemia cells, may enhance malignant conversion of hematopoietic cells.	D014178	Translocation, Genetic
RUNX1	17072347	Identification of a novel splice variant of AML1b in ovarian cancer patients conferring loss of wild-type tumor suppressive functions.	Acute myeloid leukemia (AML) 1 is often disrupted by chromosomal translocations generating oncogenic fusions in human leukemias. However, its role in epithelial cancers has not been extensively investigated. Herein, we show a marked accumulation of AML1 transcripts including a high frequency of a novel alternatively spliced AML1b transcript lacking exon 6 (AML1b(Del179-242)) in ovarian cancer patients. The increases in RNA transcripts for total wild-type AML1 and AML1b(Del179-242) are associated with poor patient outcomes. We have shown that although both wild-type AML1b and AML1b(Del179-242) are localized to nuclear speckles, AML1b(Del179-242) was observed to have dramatically reduced transactivation potential with the plasminogen activator inhibitor-1 promoters and behaved as a weak dominant negative of wild-type AML1b. Wild-type AML1b was found to inhibit the growth of immortalized ovarian epithelial cells (T29) decreasing colony-forming ability. Moreover, we have identified a novel function of AML1b where it inhibits ovarian cell migration. In contrast, AML1b(Del179-242) has lost the ability to inhibit both ovarian cell proliferation and migration indicating that the functional effects observed with wild-type AML1b are dependent on amino acids 179-242. Collectively, these studies suggest that deregulated alternative splicing of AML1b transcripts may potentially contribute to the pathophysiology of ovarian cancers.	D002291	Carcinoma, Papillary
RUNX1	17072347	Identification of a novel splice variant of AML1b in ovarian cancer patients conferring loss of wild-type tumor suppressive functions.	Acute myeloid leukemia (AML) 1 is often disrupted by chromosomal translocations generating oncogenic fusions in human leukemias. However, its role in epithelial cancers has not been extensively investigated. Herein, we show a marked accumulation of AML1 transcripts including a high frequency of a novel alternatively spliced AML1b transcript lacking exon 6 (AML1b(Del179-242)) in ovarian cancer patients. The increases in RNA transcripts for total wild-type AML1 and AML1b(Del179-242) are associated with poor patient outcomes. We have shown that although both wild-type AML1b and AML1b(Del179-242) are localized to nuclear speckles, AML1b(Del179-242) was observed to have dramatically reduced transactivation potential with the plasminogen activator inhibitor-1 promoters and behaved as a weak dominant negative of wild-type AML1b. Wild-type AML1b was found to inhibit the growth of immortalized ovarian epithelial cells (T29) decreasing colony-forming ability. Moreover, we have identified a novel function of AML1b where it inhibits ovarian cell migration. In contrast, AML1b(Del179-242) has lost the ability to inhibit both ovarian cell proliferation and migration indicating that the functional effects observed with wild-type AML1b are dependent on amino acids 179-242. Collectively, these studies suggest that deregulated alternative splicing of AML1b transcripts may potentially contribute to the pathophysiology of ovarian cancers.	D002471	Cell Transformation, Neoplastic
RUNX1	17072347	Identification of a novel splice variant of AML1b in ovarian cancer patients conferring loss of wild-type tumor suppressive functions.	Acute myeloid leukemia (AML) 1 is often disrupted by chromosomal translocations generating oncogenic fusions in human leukemias. However, its role in epithelial cancers has not been extensively investigated. Herein, we show a marked accumulation of AML1 transcripts including a high frequency of a novel alternatively spliced AML1b transcript lacking exon 6 (AML1b(Del179-242)) in ovarian cancer patients. The increases in RNA transcripts for total wild-type AML1 and AML1b(Del179-242) are associated with poor patient outcomes. We have shown that although both wild-type AML1b and AML1b(Del179-242) are localized to nuclear speckles, AML1b(Del179-242) was observed to have dramatically reduced transactivation potential with the plasminogen activator inhibitor-1 promoters and behaved as a weak dominant negative of wild-type AML1b. Wild-type AML1b was found to inhibit the growth of immortalized ovarian epithelial cells (T29) decreasing colony-forming ability. Moreover, we have identified a novel function of AML1b where it inhibits ovarian cell migration. In contrast, AML1b(Del179-242) has lost the ability to inhibit both ovarian cell proliferation and migration indicating that the functional effects observed with wild-type AML1b are dependent on amino acids 179-242. Collectively, these studies suggest that deregulated alternative splicing of AML1b transcripts may potentially contribute to the pathophysiology of ovarian cancers.	D018284	Cystadenocarcinoma, Serous
RUNX1	17072347	Identification of a novel splice variant of AML1b in ovarian cancer patients conferring loss of wild-type tumor suppressive functions.	Acute myeloid leukemia (AML) 1 is often disrupted by chromosomal translocations generating oncogenic fusions in human leukemias. However, its role in epithelial cancers has not been extensively investigated. Herein, we show a marked accumulation of AML1 transcripts including a high frequency of a novel alternatively spliced AML1b transcript lacking exon 6 (AML1b(Del179-242)) in ovarian cancer patients. The increases in RNA transcripts for total wild-type AML1 and AML1b(Del179-242) are associated with poor patient outcomes. We have shown that although both wild-type AML1b and AML1b(Del179-242) are localized to nuclear speckles, AML1b(Del179-242) was observed to have dramatically reduced transactivation potential with the plasminogen activator inhibitor-1 promoters and behaved as a weak dominant negative of wild-type AML1b. Wild-type AML1b was found to inhibit the growth of immortalized ovarian epithelial cells (T29) decreasing colony-forming ability. Moreover, we have identified a novel function of AML1b where it inhibits ovarian cell migration. In contrast, AML1b(Del179-242) has lost the ability to inhibit both ovarian cell proliferation and migration indicating that the functional effects observed with wild-type AML1b are dependent on amino acids 179-242. Collectively, these studies suggest that deregulated alternative splicing of AML1b transcripts may potentially contribute to the pathophysiology of ovarian cancers.	D009375	Neoplasms, Glandular and Epithelial
RUNX1	17072347	Identification of a novel splice variant of AML1b in ovarian cancer patients conferring loss of wild-type tumor suppressive functions.	Acute myeloid leukemia (AML) 1 is often disrupted by chromosomal translocations generating oncogenic fusions in human leukemias. However, its role in epithelial cancers has not been extensively investigated. Herein, we show a marked accumulation of AML1 transcripts including a high frequency of a novel alternatively spliced AML1b transcript lacking exon 6 (AML1b(Del179-242)) in ovarian cancer patients. The increases in RNA transcripts for total wild-type AML1 and AML1b(Del179-242) are associated with poor patient outcomes. We have shown that although both wild-type AML1b and AML1b(Del179-242) are localized to nuclear speckles, AML1b(Del179-242) was observed to have dramatically reduced transactivation potential with the plasminogen activator inhibitor-1 promoters and behaved as a weak dominant negative of wild-type AML1b. Wild-type AML1b was found to inhibit the growth of immortalized ovarian epithelial cells (T29) decreasing colony-forming ability. Moreover, we have identified a novel function of AML1b where it inhibits ovarian cell migration. In contrast, AML1b(Del179-242) has lost the ability to inhibit both ovarian cell proliferation and migration indicating that the functional effects observed with wild-type AML1b are dependent on amino acids 179-242. Collectively, these studies suggest that deregulated alternative splicing of AML1b transcripts may potentially contribute to the pathophysiology of ovarian cancers.	D010051	Ovarian Neoplasms
RUNX1	19151769	Overexpression of an isoform of AML1 in acute leukemia and its potential role in leukemogenesis.	AML1/RUNX1 is a critical transcription factor in hematopoietic cell differentiation and proliferation. From the AML1 gene, at least three isoforms, AML1a, AML1b and AML1c, are produced through alternative splicing. AML1a interferes with the function of AML1b/1c, which are often called AML1. In this study, we found a higher expression level of AML1a in acute lymphoblastic leukemia and acute myeloid leukemia (AML)-M2 patients in comparison to the controls. Additionally, AML1a represses transcription of promoter of macrophage colony-stimulating factor receptor mediated by AML1b, indicating that AML1a antagonized the effect of AML1b. To investigate the role of AML1a in hematopoiesis and leukemogenesis in vivo, murine bone marrow mononuclear cells were transduced with AML1a and then transplanted into lethally irradiated mice, which developed lymphoblastic leukemia after transplantation. Taken together, these results indicate that overexpression of AML1a may be an important contributing factor to leukemogenesis.	D000208	Acute Disease
RUNX1	19151769	Overexpression of an isoform of AML1 in acute leukemia and its potential role in leukemogenesis.	AML1/RUNX1 is a critical transcription factor in hematopoietic cell differentiation and proliferation. From the AML1 gene, at least three isoforms, AML1a, AML1b and AML1c, are produced through alternative splicing. AML1a interferes with the function of AML1b/1c, which are often called AML1. In this study, we found a higher expression level of AML1a in acute lymphoblastic leukemia and acute myeloid leukemia (AML)-M2 patients in comparison to the controls. Additionally, AML1a represses transcription of promoter of macrophage colony-stimulating factor receptor mediated by AML1b, indicating that AML1a antagonized the effect of AML1b. To investigate the role of AML1a in hematopoiesis and leukemogenesis in vivo, murine bone marrow mononuclear cells were transduced with AML1a and then transplanted into lethally irradiated mice, which developed lymphoblastic leukemia after transplantation. Taken together, these results indicate that overexpression of AML1a may be an important contributing factor to leukemogenesis.	D007938	Leukemia
RUNX1	19151769	Overexpression of an isoform of AML1 in acute leukemia and its potential role in leukemogenesis.	AML1/RUNX1 is a critical transcription factor in hematopoietic cell differentiation and proliferation. From the AML1 gene, at least three isoforms, AML1a, AML1b and AML1c, are produced through alternative splicing. AML1a interferes with the function of AML1b/1c, which are often called AML1. In this study, we found a higher expression level of AML1a in acute lymphoblastic leukemia and acute myeloid leukemia (AML)-M2 patients in comparison to the controls. Additionally, AML1a represses transcription of promoter of macrophage colony-stimulating factor receptor mediated by AML1b, indicating that AML1a antagonized the effect of AML1b. To investigate the role of AML1a in hematopoiesis and leukemogenesis in vivo, murine bone marrow mononuclear cells were transduced with AML1a and then transplanted into lethally irradiated mice, which developed lymphoblastic leukemia after transplantation. Taken together, these results indicate that overexpression of AML1a may be an important contributing factor to leukemogenesis.	D015470	Leukemia, Myeloid, Acute
RUNX1	19151769	Overexpression of an isoform of AML1 in acute leukemia and its potential role in leukemogenesis.	AML1/RUNX1 is a critical transcription factor in hematopoietic cell differentiation and proliferation. From the AML1 gene, at least three isoforms, AML1a, AML1b and AML1c, are produced through alternative splicing. AML1a interferes with the function of AML1b/1c, which are often called AML1. In this study, we found a higher expression level of AML1a in acute lymphoblastic leukemia and acute myeloid leukemia (AML)-M2 patients in comparison to the controls. Additionally, AML1a represses transcription of promoter of macrophage colony-stimulating factor receptor mediated by AML1b, indicating that AML1a antagonized the effect of AML1b. To investigate the role of AML1a in hematopoiesis and leukemogenesis in vivo, murine bone marrow mononuclear cells were transduced with AML1a and then transplanted into lethally irradiated mice, which developed lymphoblastic leukemia after transplantation. Taken together, these results indicate that overexpression of AML1a may be an important contributing factor to leukemogenesis.	D054198	Precursor Cell Lymphoblastic Leukemia-Lymphoma

Clinically important variants in RUNX1

(ClinVar, 04/20/2024)

accession_id

uniprot_id

gene_name

Type

Variant

Clinical_significance