ASpdb: an integrative knowledgebase of human protein isoforms from experimental and AI-predicted structures

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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:RUNX1T1

Protein Summary

Gene summary

Gene name: RUNX1T1
ASpdb.0 ID: 862
	Gene
Gene symbol	RUNX1T1
Gene ID	862
Gene name	RUNX1 partner transcriptional co-repressor 1
Synonyms	AML1-MTG8\|AML1T1\|CBFA2T1\|CDR\|ETO\|MTG8\|ZMYND2
Cytomap	8q21.3
Type of gene	protein-coding
Description	protein CBFA2T1RUNX1 translocation partner 1acute myelogenous leukemia 1 translocation 1, cyclin-D relatedcore-binding factor, runt domain, alpha subunit 2; translocated to, 1; cyclin D-relatedeight twenty one proteinmyeloid translocation gene on 8q2
Modification date	20240403
UniProtAcc	Q06455

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

Partner	Gene	GO ID	GO term	PubMed ID
Gene	RUNX1T1	GO:0003714	transcription corepressor activity	10688654
Gene	RUNX1T1	GO:0005654	nucleoplasm	-
Gene	RUNX1T1	GO:0016363	nuclear matrix	10973986
Gene	RUNX1T1	GO:0045892	negative regulation of DNA-templated transcription	23251453

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
Q06455-1	Q06455-1_4jol_A.pdb	4JOL	X-ray	2.91	A	341	400

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
Q06455	RUNX1T1	Q06455-1	Q06455-2	604	577	1	29	Substitution	MISVKRNTWRALSLVIGDCRKKGNFEYCQ	MP	1	2
Q06455	RUNX1T1	Q06455-1	Q06455-3	604	615	1	29	Substitution	MISVKRNTWRALSLVIGDCRKKGNFEYCQ	MCHPDKAFTSDKLQCVFNEYKAAVWVPPRPRPLSRAPLPE	1	40
Q06455	RUNX1T1	Q06455-1	Q06455-4	604	567	1	37	Deletion	none	none	0	0
Q06455	RUNX1T1	Q06455-1	Q06455-5	604	427	427	427	Substitution	D	G	427	427
Q06455	RUNX1T1	Q06455-1	Q06455-5	604	427	428	604	Deletion	none	none	427	427
Q06455	RUNX1T1	Q06455-1	Q06455-6	604	400	1	29	Substitution	MISVKRNTWRALSLVIGDCRKKGNFEYCQ	MP	1	2
Q06455	RUNX1T1	Q06455-1	Q06455-6	604	400	427	427	Substitution	D	G	400	400
Q06455	RUNX1T1	Q06455-1	Q06455-6	604	400	428	604	Deletion	none	none	400	400

Multiple sequence alignment of our canonical and alternatively spliced RUNX1T1

Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of RUNX1T1

UniProt-id	ENSG	ENST	ENSP
Q06455-1	ENSG00000079102.17	ENST00000517919.6	ENSP00000429506.2
Q06455-1	ENSG00000079102.17	ENST00000518954.6	ENSP00000430080.2
Q06455-1	ENSG00000079102.17	ENST00000519847.6	ENSP00000430204.2
Q06455-1	ENSG00000079102.17	ENST00000523629.6	ENSP00000428543.1
Q06455-2	ENSG00000079102.17	ENST00000396218.5	ENSP00000379520.1
Q06455-2	ENSG00000079102.17	ENST00000518317.6	ENSP00000429062.2
Q06455-2	ENSG00000079102.17	ENST00000518844.5	ENSP00000430728.1
Q06455-3	ENSG00000079102.17	ENST00000520724.5	ENSP00000428742.2
Q06455-4	ENSG00000079102.17	ENST00000360348.6	ENSP00000353504.2
Q06455-4	ENSG00000079102.17	ENST00000422361.6	ENSP00000390137.2

UniProt-id	NM ID	NP ID
Q06455-1	NM_001198626.1	NP_001185555.1
Q06455-1	NM_001198627.1	NP_001185556.1
Q06455-1	NM_001198628.1	NP_001185557.1
Q06455-1	NM_001198629.1	NP_001185558.1
Q06455-1	NM_001198630.1	NP_001185559.1
Q06455-1	NM_001198631.1	NP_001185560.1
Q06455-1	NM_175634.2	NP_783552.1
Q06455-1	XM_011517351.2	XP_011515653.1
Q06455-2	NM_001198625.1	NP_001185554.1
Q06455-2	NM_001198632.1	NP_001185561.1
Q06455-2	NM_004349.3	NP_004340.1
Q06455-3	NM_001198634.1	NP_001185563.1
Q06455-4	NM_175635.2	NP_783553.1
Q06455-4	NM_175636.2	NP_783554.1
Q06455-4	XM_017013936.1	XP_016869425.1

Amino acid sequences of our canonical and alternatively spliced RUNX1T1

accession_id	Protein sequence
Q06455-1	MISVKRNTWRALSLVIGDCRKKGNFEYCQDRTEKHSTMPDSPVDVKTQSRLTPPTMPPPPTTQGAPRTSSFTPTTLTNGTSHSPTALNGA PSPPNGFSNGPSSSSSSSLANQQLPPACGARQLSKLKRFLTTLQQFGNDISPEIGERVRTLVLGLVNSTLTIEEFHSKLQEATNFPLRPF VIPFLKANLPLLQRELLHCARLAKQNPAQYLAQHEQLLLDASTTSPVDSSELLLDVNENGKRRTPDRTKENGFDREPLHSEHPSKRPCTI SPGQRYSPNNGLSYQPNGLPHPTPPPPQHYRLDDMAIAHHYRDSYRHPSHRDLRDRNRPMGLHGTRQEEMIDHRLTDREWAEEWKHLDHL LNCIMDMVEKTRRSLTVLRRCQEADREELNYWIRRYSDAEDLKKGGGSSSSHSRQQSPVNPDPVALDAHREFLHRPASGYVPEEIWKKAE EAVNEVKRQAMTELQKAVSEAERKAHDMITTERAKMERTVAEAKRQAAEDALAVINQQEDSSESCWNCGRKASETCSGCNTARYCGSFCQ
Q06455-2	MPDRTEKHSTMPDSPVDVKTQSRLTPPTMPPPPTTQGAPRTSSFTPTTLTNGTSHSPTALNGAPSPPNGFSNGPSSSSSSSLANQQLPPA CGARQLSKLKRFLTTLQQFGNDISPEIGERVRTLVLGLVNSTLTIEEFHSKLQEATNFPLRPFVIPFLKANLPLLQRELLHCARLAKQNP AQYLAQHEQLLLDASTTSPVDSSELLLDVNENGKRRTPDRTKENGFDREPLHSEHPSKRPCTISPGQRYSPNNGLSYQPNGLPHPTPPPP QHYRLDDMAIAHHYRDSYRHPSHRDLRDRNRPMGLHGTRQEEMIDHRLTDREWAEEWKHLDHLLNCIMDMVEKTRRSLTVLRRCQEADRE ELNYWIRRYSDAEDLKKGGGSSSSHSRQQSPVNPDPVALDAHREFLHRPASGYVPEEIWKKAEEAVNEVKRQAMTELQKAVSEAERKAHD MITTERAKMERTVAEAKRQAAEDALAVINQQEDSSESCWNCGRKASETCSGCNTARYCGSFCQHKDWEKHHHICGQTLQAQQQGDTPAVS
Q06455-3	MCHPDKAFTSDKLQCVFNEYKAAVWVPPRPRPLSRAPLPEDRTEKHSTMPDSPVDVKTQSRLTPPTMPPPPTTQGAPRTSSFTPTTLTNG TSHSPTALNGAPSPPNGFSNGPSSSSSSSLANQQLPPACGARQLSKLKRFLTTLQQFGNDISPEIGERVRTLVLGLVNSTLTIEEFHSKL QEATNFPLRPFVIPFLKANLPLLQRELLHCARLAKQNPAQYLAQHEQLLLDASTTSPVDSSELLLDVNENGKRRTPDRTKENGFDREPLH SEHPSKRPCTISPGQRYSPNNGLSYQPNGLPHPTPPPPQHYRLDDMAIAHHYRDSYRHPSHRDLRDRNRPMGLHGTRQEEMIDHRLTDRE WAEEWKHLDHLLNCIMDMVEKTRRSLTVLRRCQEADREELNYWIRRYSDAEDLKKGGGSSSSHSRQQSPVNPDPVALDAHREFLHRPASG YVPEEIWKKAEEAVNEVKRQAMTELQKAVSEAERKAHDMITTERAKMERTVAEAKRQAAEDALAVINQQEDSSESCWNCGRKASETCSGC
Q06455-4	MPDSPVDVKTQSRLTPPTMPPPPTTQGAPRTSSFTPTTLTNGTSHSPTALNGAPSPPNGFSNGPSSSSSSSLANQQLPPACGARQLSKLK RFLTTLQQFGNDISPEIGERVRTLVLGLVNSTLTIEEFHSKLQEATNFPLRPFVIPFLKANLPLLQRELLHCARLAKQNPAQYLAQHEQL LLDASTTSPVDSSELLLDVNENGKRRTPDRTKENGFDREPLHSEHPSKRPCTISPGQRYSPNNGLSYQPNGLPHPTPPPPQHYRLDDMAI AHHYRDSYRHPSHRDLRDRNRPMGLHGTRQEEMIDHRLTDREWAEEWKHLDHLLNCIMDMVEKTRRSLTVLRRCQEADREELNYWIRRYS DAEDLKKGGGSSSSHSRQQSPVNPDPVALDAHREFLHRPASGYVPEEIWKKAEEAVNEVKRQAMTELQKAVSEAERKAHDMITTERAKME RTVAEAKRQAAEDALAVINQQEDSSESCWNCGRKASETCSGCNTARYCGSFCQHKDWEKHHHICGQTLQAQQQGDTPAVSSSVTPNSGAG
Q06455-5	MISVKRNTWRALSLVIGDCRKKGNFEYCQDRTEKHSTMPDSPVDVKTQSRLTPPTMPPPPTTQGAPRTSSFTPTTLTNGTSHSPTALNGA PSPPNGFSNGPSSSSSSSLANQQLPPACGARQLSKLKRFLTTLQQFGNDISPEIGERVRTLVLGLVNSTLTIEEFHSKLQEATNFPLRPF VIPFLKANLPLLQRELLHCARLAKQNPAQYLAQHEQLLLDASTTSPVDSSELLLDVNENGKRRTPDRTKENGFDREPLHSEHPSKRPCTI SPGQRYSPNNGLSYQPNGLPHPTPPPPQHYRLDDMAIAHHYRDSYRHPSHRDLRDRNRPMGLHGTRQEEMIDHRLTDREWAEEWKHLDHL
Q06455-6	MPDRTEKHSTMPDSPVDVKTQSRLTPPTMPPPPTTQGAPRTSSFTPTTLTNGTSHSPTALNGAPSPPNGFSNGPSSSSSSSLANQQLPPA CGARQLSKLKRFLTTLQQFGNDISPEIGERVRTLVLGLVNSTLTIEEFHSKLQEATNFPLRPFVIPFLKANLPLLQRELLHCARLAKQNP AQYLAQHEQLLLDASTTSPVDSSELLLDVNENGKRRTPDRTKENGFDREPLHSEHPSKRPCTISPGQRYSPNNGLSYQPNGLPHPTPPPP QHYRLDDMAIAHHYRDSYRHPSHRDLRDRNRPMGLHGTRQEEMIDHRLTDREWAEEWKHLDHLLNCIMDMVEKTRRSLTVLRRCQEADRE

Protein Functional Features

Main function of this protein. (from UniProt)

RUNX1T1 (go to UniProt):Q06455

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
Q06455	Zinc finger	515	551	Note=MYND-type;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00134	Type=Deletion;Start=428;End=604
Q06455	Zinc finger	515	551	Note=MYND-type;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU00134	Type=Deletion;Start=428;End=604
Q06455	Region	32	114	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=1;End=37
Q06455	Region	443	492	Note=Nervy homology region 3 (NHR3);Ontology_term=ECO:0000303;evidence=ECO:0000303\|PubMed:12559562;Dbxref=PMID:12559562	Type=Deletion;Start=428;End=604
Q06455	Region	443	492	Note=Nervy homology region 3 (NHR3);Ontology_term=ECO:0000303;evidence=ECO:0000303\|PubMed:12559562;Dbxref=PMID:12559562	Type=Deletion;Start=428;End=604
Q06455	Region	557	604	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=428;End=604
Q06455	Region	557	604	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=428;End=604

Gene Isoform Structures and Expression Levels for RUNX1T1

Gene structures of our canonical and alternative spliced genes of RUNX1T1
* 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 Q06455-1

3D view using mol* of Q06455-2

3D view using mol* of Q06455-3

3D view using mol* of Q06455-4

3D view using mol* of Q06455-5

3D view using mol* of Q06455-6

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 Q06455-1

pLDDT distribution across the protein length of Q06455-2

pLDDT distribution across the protein length of Q06455-3

pLDDT distribution across the protein length of Q06455-4

pLDDT distribution across the protein length of Q06455-5

pLDDT distribution across the protein length of Q06455-6

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 Q06455-1

Ramachandran plot of Q06455-2

Ramachandran plot of Q06455-3

Ramachandran plot of Q06455-4

Ramachandran plot of Q06455-6

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
Q06455-1	1.053	126	1.131	369.068	0.635	0.656	0.859	1.36	0.622	2.188	1.357	4,5,7,8,9,11,12,13,15,16,17,18,19,125,128,129,131, 132,133,135,136,139,140,175,180,181,184,221
Q06455-2	0.846	41	0.863	74.088	0.474	0.706	0.922	2.213	0.499	4.438	3.225	100,165,168,169,172,183,184,187,190,191
Q06455-3	1.024	96	1.081	237.013	0.464	0.672	0.953	1.312	0.747	1.756	1.645	125,126,127,128,130,131,134,138,202,203,205,206,20 7,209,210,221,222,225,228,229
Q06455-4	0.743	30	0.749	95.011	0.634	0.643	0.891	1.245	0.466	2.674	1.893	78,80,81,84,348,351,352,355
Q06455-5	1.033	113	1.078	412.286	0.612	0.694	0.874	0.868	0.854	1.015	1.337	16,18,19,20,22,23,24,25,117,118,120,121,122,125,18 0,183,184,187,188,381,384,385,388,389,392
Q06455-6	0.92	83	0.945	247.303	0.661	0.635	0.865	0.63	0.897	0.702	1.031	83,84,85,86,87,88,89,91,92,93,95,96,160,161,164,16 7,168,365,369

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 Q06455-1_Q06455-1_4jol_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 Q06455-1_4jol_A_Q06455-2.pdb

3D view using mol* of Q06455-1_4jol_A_Q06455-3.pdb

3D view using mol* of Q06455-1_4jol_A_Q06455-4.pdb

3D view using mol* of Q06455-1_4jol_A_Q06455-5.pdb

3D view using mol* of Q06455-1_4jol_A_Q06455-6.pdb

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

3D view using mol* of Q06455-1_Q06455-2.pdb

3D view using mol* of Q06455-1_Q06455-3.pdb

3D view using mol* of Q06455-1_Q06455-4.pdb

3D view using mol* of Q06455-1_Q06455-5.pdb

3D view using mol* of Q06455-1_Q06455-6.pdb

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

./stats/secondary_structure/figure/Q06455-1_vs_Q06455-2.png

./stats/secondary_structure/figure/Q06455-1_vs_Q06455-3.png

./stats/secondary_structure/figure/Q06455-1_vs_Q06455-4.png

./stats/secondary_structure/figure/Q06455-1_vs_Q06455-5.png

./stats/secondary_structure/figure/Q06455-1_vs_Q06455-6.png

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

./stats/relative_asa/Q06455-1_vs_Q06455-2.png

./stats/relative_asa/Q06455-1_vs_Q06455-3.png

./stats/relative_asa/Q06455-1_vs_Q06455-4.png

./stats/relative_asa/Q06455-1_vs_Q06455-5.png

./stats/relative_asa/Q06455-1_vs_Q06455-6.png

Protein-Protein Interaction

Interactors from UniProt.

Accession_id

Subsection

Start

End

Funcitonal feature

Splicing information

Interactors from STRING.

Gene name

Interactors

Related Drugs to RUNX1T1

Drugs targeting this gene/protein.
(DrugBank)

UniProt accession

Gene name

DrugBank ID

Drug name

Drug group

Actions

Related Diseases to RUNX1T1

Previous studies relating to the alternative splicing of RUNX1T1 and disease information from the MeSH term (PubMed)

Gene	PMID	Title	Abstract	MeSH ID	MeSH term
RUNX1T1	9790752	CBFA2T1, a gene rearranged in human leukemia, is a member of a multigene family.	MTG8 (HGMW-approved symbol CBFA2T1) was originally identified as one of the loci involved in the t(8;21)(q22;q22) of acute myeloid leukemia. We characterize two human MTG8-related genes, MTGR1 and MTGR2 (HGMW-approved symbols CBFA2T2 and CBFA2T3). The former is duplicated in mouse, one locus possibly being a retroposon. Multiple MTG8-related sequences are found in several vertebrate species, from fish to mammals, albeit not in a urodele. MTGR2 maps to 16q24 and, like MTG8 and MTGR1, is close to one of three loci encoding a syntrophin (dystrophin-associated proteins). Moreover, an alternative MTGR1 promoter/5' exon is contained within the alpha1-syntrophin locus. Thus, the two classes of genes may define novel paralogous groups. MTGR1 is expressed mainly in brain, while MTGR2 is expressed in the thymus and possibly in monocytes. Like MTG8, MTGR1 is transcribed into a number of isoforms due to alternative splicing of different 5' exons onto a common splice acceptor site. Comparison of the three predicted human MTG8-related polypeptides to their Drosophila counterpart (nervy) highlights four separate regions of sequence conservation that may correspond to distinct domains. The most NH2-terminal of these is proportionately more conserved among the human polypeptides, presumably due to specific structural/functional constraints.	D007938	Leukemia
RUNX1T1	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
RUNX1T1	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

Clinically important variants in RUNX1T1

(ClinVar, 04/20/2024)

accession_id

uniprot_id

gene_name

Type

Variant

Clinical_significance