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:MLLT10

Protein Summary

Gene summary

Gene name: MLLT10
ASpdb.0 ID: 8028
	Gene
Gene symbol	MLLT10
Gene ID	8028
Gene name	MLLT10 histone lysine methyltransferase DOT1L cofactor
Synonyms	AF10
Cytomap	10p12.31
Type of gene	protein-coding
Description	protein AF-10ALL1-fused gene from chromosome 10 proteinmyeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila); translocated to, 10myeloid/lymphoid or mixed-lineage leukemia; translocated to, 10type I AF10 proteintype III AF10 prot
Modification date	20240305
UniProtAcc	P55197

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

Partner	Gene	GO ID	GO term	PubMed ID
Gene	MLLT10	GO:0003682	chromatin binding	26439302
Gene	MLLT10	GO:0005634	nucleus	15851025
Gene	MLLT10	GO:0005654	nucleoplasm	-
Gene	MLLT10	GO:0031491	nucleosome binding	26439302
Gene	MLLT10	GO:0032991	protein-containing complex	15851025
Gene	MLLT10	GO:0045944	positive regulation of transcription by RNA polymerase II	17868029

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
P55197-4	P55197-4_5dah_B.pdb	5DAH	X-ray	2.61	B	20	203

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
P55197	MLLT10	P55197-4	P55197-1	1068	1027	566	566	Substitution	N	NDRGDSSTLTKQELKFI	566	582
P55197	MLLT10	P55197-4	P55197-1	1068	1027	986	1011	Substitution	EQHQAFLYQLMQHHHQQHHQPELQQL	VHRHPHFTQLPPTHFSPSMEIMQVRK	1002	1027
P55197	MLLT10	P55197-4	P55197-1	1068	1027	1012	1068	Deletion	none	none	1027	1027
P55197	MLLT10	P55197-4	P55197-2	1068	126	81	126	Substitution	RCELCPHKDGALKRTDNGGWAHVVCALYIPEVQFANVSTMEPIVLQ	AESRSVAQAKVQWCDLSPLQPLLPGFKRFSCLSLPNGMQFLLVSLI	81	126
P55197	MLLT10	P55197-4	P55197-2	1068	126	127	1068	Deletion	none	none	126	126
P55197	MLLT10	P55197-4	P55197-3	1068	179	81	179	Substitution	RCELCPHKDGALKRTDNGGWAHVVCALYIPEVQFANVSTMEPIVLQSVPHDRYNKTCYICDEQGRESKAATGACMTCNKHGCRQAFHVTCAQFAGLLCE	MVCNSCWLASSENVTPGYIEHHCACASPHPRCLVSNVPPVSGALMHCFWACLTTAAFFGPQSFTTCHMSFLVSRDILFYIYGFMPFISVVIWRFKKERW	81	179
P55197	MLLT10	P55197-4	P55197-3	1068	179	180	1068	Deletion	none	none	179	179

Multiple sequence alignment of our canonical and alternatively spliced MLLT10

Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of MLLT10

UniProt-id	ENSG	ENST	ENSP
P55197-4	ENSG00000078403.17	ENST00000307729.12	ENSP00000307411.7
P55197-4	ENSG00000078403.17	ENST00000377059.7	ENSP00000366258.4
P55197-4	ENSG00000078403.17	ENST00000631589.1	ENSP00000488569.1
P55197-1	ENSG00000078403.17	ENST00000377072.8	ENSP00000366272.3
P55197-2	ENSG00000078403.17	ENST00000377091.7	ENSP00000366295.2
P55197-2	ENSG00000078403.17	ENST00000621220.4	ENSP00000484335.1
P55197-3	ENSG00000078403.17	ENST00000377100.8	ENSP00000366304.3
P55197-3	ENSG00000078403.17	ENST00000652497.1	ENSP00000498595.1

UniProt-id	NM ID	NP ID
P55197-4	NM_001195626.1	NP_001182555.1
P55197-1	NM_004641.3	NP_004632.1
P55197-2	NM_001195627.1	NP_001182556.1
P55197-3	NM_001195628.1	NP_001182557.1
P55197-3	NM_001195630.1	NP_001182559.1
P55197-3	NM_001324296.1	NP_001311225.1

Amino acid sequences of our canonical and alternatively spliced MLLT10

accession_id	Protein sequence
P55197-4	MVSSDRPVSLEDEVSHSMKEMIGGCCVCSDERGWAENPLVYCDGHGCSVAVHQACYGIVQVPTGPWFCRKCESQERAARVRCELCPHKDG ALKRTDNGGWAHVVCALYIPEVQFANVSTMEPIVLQSVPHDRYNKTCYICDEQGRESKAATGACMTCNKHGCRQAFHVTCAQFAGLLCEE EGNGADNVQYCGYCKYHFSKLKKSKRGSNRSYDQSLSDSSSHSQDKHHEKEKKKYKEKDKHKQKHKKQPEPSPALVPSLTVTTEKTYTST SNNSISGSLKRLEDTTARFTNANFQEVSAHTSSGKDVSETRGSEGKGKKSSAHSSGQRGRKPGGGRNPGTTVSAASPFPQGSFSGTPGSV KSSSGSSVQSPQDFLSFTDSDLRNDSYSHSQQSSATKDVHKGESGSQEGGVNSFSTLIGLPSTSAVTSQPKSFENSPGDLGNSSLPTAGY KRAQTSGIEEETVKEKKRKGNKQSKHGPGRPKGNKNQENVSHLSVSSASPTSSVASAAGSITSSSLQKSPTLLRNGSLQSLSVGSSPVGS EISMQYRHDGACPTTTFSELLNAIHNGIYNSNDVAVSFPNVVSGSGSSTPVSSSHLPQQSSGHLQQVGALSPSAVSSAAPAVATTQANTL SGSSLSQAPSHMYGNRSNSSMAALIAQSENNQTDQDLGDNSRNLVGRGSSPRGSLSPRSPVSSLQIRYDQPGNSSLENLPPVAASIEQLL ERQWSEGQQFLLEQGTPSDILGMLKSLHQLQVENRRLEEQIKNLTAKKERLQLLNAQLSVPFPTITANPSPSHQIHTFSAQTAPTTDSLN SSKSPHIGNSFLPDNSLPVLNQDLTSSGQSTSSSSALSTPPPAGQSPAQQGSGVSGVQQVNGVTVGALASGMQPVTSTIPAVSAVGGIIG ALPGNQLAINGIVGALNGVMQTPVTMSQNPTPLTHTTVPPNATHPMPATLTNSASGLGLLSDQQRQILIHQQQFQQLLNSQQLTPEQHQA
P55197-1	MVSSDRPVSLEDEVSHSMKEMIGGCCVCSDERGWAENPLVYCDGHGCSVAVHQACYGIVQVPTGPWFCRKCESQERAARVRCELCPHKDG ALKRTDNGGWAHVVCALYIPEVQFANVSTMEPIVLQSVPHDRYNKTCYICDEQGRESKAATGACMTCNKHGCRQAFHVTCAQFAGLLCEE EGNGADNVQYCGYCKYHFSKLKKSKRGSNRSYDQSLSDSSSHSQDKHHEKEKKKYKEKDKHKQKHKKQPEPSPALVPSLTVTTEKTYTST SNNSISGSLKRLEDTTARFTNANFQEVSAHTSSGKDVSETRGSEGKGKKSSAHSSGQRGRKPGGGRNPGTTVSAASPFPQGSFSGTPGSV KSSSGSSVQSPQDFLSFTDSDLRNDSYSHSQQSSATKDVHKGESGSQEGGVNSFSTLIGLPSTSAVTSQPKSFENSPGDLGNSSLPTAGY KRAQTSGIEEETVKEKKRKGNKQSKHGPGRPKGNKNQENVSHLSVSSASPTSSVASAAGSITSSSLQKSPTLLRNGSLQSLSVGSSPVGS EISMQYRHDGACPTTTFSELLNAIHNDRGDSSTLTKQELKFIGIYNSNDVAVSFPNVVSGSGSSTPVSSSHLPQQSSGHLQQVGALSPSA VSSAAPAVATTQANTLSGSSLSQAPSHMYGNRSNSSMAALIAQSENNQTDQDLGDNSRNLVGRGSSPRGSLSPRSPVSSLQIRYDQPGNS SLENLPPVAASIEQLLERQWSEGQQFLLEQGTPSDILGMLKSLHQLQVENRRLEEQIKNLTAKKERLQLLNAQLSVPFPTITANPSPSHQ IHTFSAQTAPTTDSLNSSKSPHIGNSFLPDNSLPVLNQDLTSSGQSTSSSSALSTPPPAGQSPAQQGSGVSGVQQVNGVTVGALASGMQP VTSTIPAVSAVGGIIGALPGNQLAINGIVGALNGVMQTPVTMSQNPTPLTHTTVPPNATHPMPATLTNSASGLGLLSDQQRQILIHQQQF
P55197-2	MVSSDRPVSLEDEVSHSMKEMIGGCCVCSDERGWAENPLVYCDGHGCSVAVHQACYGIVQVPTGPWFCRKCESQERAARVAESRSVAQAK
P55197-3	MVSSDRPVSLEDEVSHSMKEMIGGCCVCSDERGWAENPLVYCDGHGCSVAVHQACYGIVQVPTGPWFCRKCESQERAARVMVCNSCWLAS

Protein Functional Features

Main function of this protein. (from UniProt)

MLLT10 (go to UniProt):P55197

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
P55197	Zinc finger	79	112	Note=C2HC pre-PHD-type;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU01146	Type=Substitution;Start=81;End=126
P55197	Zinc finger	79	112	Note=C2HC pre-PHD-type;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU01146	Type=Substitution;Start=81;End=179
P55197	Zinc finger	135	198	Note=PHD-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU01146	Type=Deletion;Start=127;End=1068
P55197	Zinc finger	135	198	Note=PHD-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU01146	Type=Substitution;Start=81;End=179
P55197	Zinc finger	135	198	Note=PHD-type 2;Ontology_term=ECO:0000255;evidence=ECO:0000255\|PROSITE-ProRule:PRU01146	Type=Deletion;Start=180;End=1068
P55197	Region	80	287	Note=Self-association	Type=Substitution;Start=81;End=126
P55197	Region	80	287	Note=Self-association	Type=Deletion;Start=127;End=1068
P55197	Region	80	287	Note=Self-association	Type=Substitution;Start=81;End=179
P55197	Region	80	287	Note=Self-association	Type=Deletion;Start=180;End=1068
P55197	Region	106	190	Note=Required for interaction with histone H3;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:26439302;Dbxref=PMID:26439302	Type=Substitution;Start=81;End=126
P55197	Region	106	190	Note=Required for interaction with histone H3;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:26439302;Dbxref=PMID:26439302	Type=Deletion;Start=127;End=1068
P55197	Region	106	190	Note=Required for interaction with histone H3;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:26439302;Dbxref=PMID:26439302	Type=Substitution;Start=81;End=179
P55197	Region	106	190	Note=Required for interaction with histone H3;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:26439302;Dbxref=PMID:26439302	Type=Deletion;Start=180;End=1068
P55197	Region	141	233	Note=Interaction with FSTL3;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:17868029;Dbxref=PMID:17868029	Type=Deletion;Start=127;End=1068
P55197	Region	141	233	Note=Interaction with FSTL3;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:17868029;Dbxref=PMID:17868029	Type=Substitution;Start=81;End=179
P55197	Region	141	233	Note=Interaction with FSTL3;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:17868029;Dbxref=PMID:17868029	Type=Deletion;Start=180;End=1068
P55197	Region	206	260	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=127;End=1068
P55197	Region	206	260	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=180;End=1068
P55197	Region	291	505	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=127;End=1068
P55197	Region	291	505	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=180;End=1068
P55197	Region	311	674	Note=DNA-binding	Type=Substitution;Start=566;End=566
P55197	Region	311	674	Note=DNA-binding	Type=Deletion;Start=127;End=1068
P55197	Region	311	674	Note=DNA-binding	Type=Deletion;Start=180;End=1068
P55197	Region	583	612	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=127;End=1068
P55197	Region	583	612	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=180;End=1068
P55197	Region	660	708	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=127;End=1068
P55197	Region	660	708	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=180;End=1068
P55197	Region	703	784	Note=Transactivation domain%3B required for DOT1L-binding	Type=Deletion;Start=127;End=1068
P55197	Region	703	784	Note=Transactivation domain%3B required for DOT1L-binding	Type=Deletion;Start=180;End=1068
P55197	Region	750	778	Note=Leucine-zipper	Type=Deletion;Start=127;End=1068
P55197	Region	750	778	Note=Leucine-zipper	Type=Deletion;Start=180;End=1068
P55197	Region	800	865	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=127;End=1068
P55197	Region	800	865	Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=180;End=1068
P55197	Compositional bias	291	306	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=127;End=1068
P55197	Compositional bias	291	306	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=180;End=1068
P55197	Compositional bias	339	451	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=127;End=1068
P55197	Compositional bias	339	451	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=180;End=1068
P55197	Compositional bias	484	505	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=127;End=1068
P55197	Compositional bias	484	505	Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256\|SAM:MobiDB-lite	Type=Deletion;Start=180;End=1068

Gene Isoform Structures and Expression Levels for MLLT10

Gene structures of our canonical and alternative spliced genes of MLLT10
* 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 P55197-4

3D view using mol* of P55197-1

3D view using mol* of P55197-2

3D view using mol* of P55197-3

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 P55197-4

pLDDT distribution across the protein length of P55197-1

pLDDT distribution across the protein length of P55197-2

pLDDT distribution across the protein length of P55197-3

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 P55197-4

Ramachandran plot of P55197-1

Ramachandran plot of P55197-2

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
P55197-4	1.016	131	1.074	384.16	0.7	0.646	0.779	0.42	0.778	0.54	1.232	19,20,21,22,23,24,26,27,28,29,31,41,42,43,44,45,46 ,47,48,49,50,70,89,90,91,102,104,108,169,172,173,1 75,177,178,179
P55197-1	0.961	151	1.001	396.165	0.682	0.609	0.779	0.452	0.935	0.483	1.349	19,20,21,22,23,24,26,27,29,31,41,42,43,45,46,47,48 ,49,50,70,71,73,75,76,77,78,80,81,87,88,89,90,91,1 02,103,104,169,172,173
P55197-2	0.629	28	0.604	129.311	0.836	0.565	0.749	0.707	0.713	0.992	0.877	89,90,93,94,96,111,117,118,119,120,121
P55197-3	1.085	159	1.175	415.373	0.517	0.678	0.917	1.391	0.528	2.635	1.282	123,124,125,127,128,131,132,135,140,141,142,143,14 4,145,146,148,150,160,161,162,163,164,167

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 P55197-4_P55197-4_5dah_B.pdb

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

3D view using mol* of P55197-4_5dah_B_P55197-1.pdb

3D view using mol* of P55197-4_5dah_B_P55197-2.pdb

3D view using mol* of P55197-4_5dah_B_P55197-3.pdb

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

3D view using mol* of P55197-4_P55197-1.pdb

3D view using mol* of P55197-4_P55197-2.pdb

3D view using mol* of P55197-4_P55197-3.pdb

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

./stats/secondary_structure/figure/P55197-4_vs_P55197-1.png

./stats/secondary_structure/figure/P55197-4_vs_P55197-2.png

./stats/secondary_structure/figure/P55197-4_vs_P55197-3.png

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

./stats/relative_asa/P55197-4_vs_P55197-1.png

./stats/relative_asa/P55197-4_vs_P55197-2.png

./stats/relative_asa/P55197-4_vs_P55197-3.png

Protein-Protein Interaction

Interactors from UniProt.

Accession_id	Subsection	Start	End	Funcitonal feature	Splicing information
P55197	Region	106	190	Note=Required for interaction with histone H3;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:26439302;Dbxref=PMID:26439302	Type=Substitution;Start=81;End=126
P55197	Region	106	190	Note=Required for interaction with histone H3;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:26439302;Dbxref=PMID:26439302	Type=Deletion;Start=127;End=1068
P55197	Region	106	190	Note=Required for interaction with histone H3;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:26439302;Dbxref=PMID:26439302	Type=Substitution;Start=81;End=179
P55197	Region	106	190	Note=Required for interaction with histone H3;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:26439302;Dbxref=PMID:26439302	Type=Deletion;Start=180;End=1068
P55197	Region	141	233	Note=Interaction with FSTL3;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:17868029;Dbxref=PMID:17868029	Type=Deletion;Start=127;End=1068
P55197	Region	141	233	Note=Interaction with FSTL3;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:17868029;Dbxref=PMID:17868029	Type=Substitution;Start=81;End=179
P55197	Region	141	233	Note=Interaction with FSTL3;Ontology_term=ECO:0000269;evidence=ECO:0000269\|PubMed:17868029;Dbxref=PMID:17868029	Type=Deletion;Start=180;End=1068

Interactors from STRING.

Gene name

Interactors

Related Drugs to MLLT10

Drugs targeting this gene/protein.
(DrugBank)

UniProt accession

Gene name

DrugBank ID

Drug name

Drug group

Actions

Related Diseases to MLLT10

Previous studies relating to the alternative splicing of MLLT10 and disease information from the MeSH term (PubMed)

Gene	PMID	Title	Abstract	MeSH ID	MeSH term
MLLT10	9737689	Alternative splicing in wild-type AF10 and CALM cDNAs and in AF10-CALM and CALM-AF10 fusion cDNAs produced by the t(10;11)(p13-14;q14-q21) suggests a potential role for truncated AF10 polypeptides.	The t(10;11)(p13;q14-21) is a non-random translocation that occurs primarily in T cell acute lymphoblastic leukemias (T-ALL), but has also been observed in leukemias and lymphomas of diverse lineages. In U937, a cell line established from a diffuse histiocytic lymphoma, a t(10;11)(p13;q14-21) fuses AF10 to CALM. AF10 is also fused to MLL by a translocation that appears quite similar at the cytogenetic level, the t(10;11)(p12;q23). Fluorescence in situ hybridization studies have demonstrated that AF10 and CALM are also involved in other hematological malignancies containing t(10;11)(p13;q21), but no data are available concerning the molecular details of AF10-CALM fusion in primary leukemias. Using RT-PCR, we amplified multiple different isoforms of AF10-CALM and CALM-AF10 fusion cDNAs from a primary T cell ALL containing a t(10;11)(p13-14;q14-21). These cDNAs arose via alternative splicing of exons from both AF10 and CALM, which we demonstrated can also occur in the native genes. We identified at least two novel AF10 exons that can be included in wild-type and fusion cDNAs. The majority of the AF10 and AF10-CALM cDNA isoforms that we identified are predicted to encode for truncated AF10 polypeptides, raising the possibility that these might have important cellular functions in normal and malignant cells, perhaps by acting as dominant negative inhibitors of full-length AF10 or related proteins.	D001932	Brain Neoplasms
MLLT10	9737689	Alternative splicing in wild-type AF10 and CALM cDNAs and in AF10-CALM and CALM-AF10 fusion cDNAs produced by the t(10;11)(p13-14;q14-q21) suggests a potential role for truncated AF10 polypeptides.	The t(10;11)(p13;q14-21) is a non-random translocation that occurs primarily in T cell acute lymphoblastic leukemias (T-ALL), but has also been observed in leukemias and lymphomas of diverse lineages. In U937, a cell line established from a diffuse histiocytic lymphoma, a t(10;11)(p13;q14-21) fuses AF10 to CALM. AF10 is also fused to MLL by a translocation that appears quite similar at the cytogenetic level, the t(10;11)(p12;q23). Fluorescence in situ hybridization studies have demonstrated that AF10 and CALM are also involved in other hematological malignancies containing t(10;11)(p13;q21), but no data are available concerning the molecular details of AF10-CALM fusion in primary leukemias. Using RT-PCR, we amplified multiple different isoforms of AF10-CALM and CALM-AF10 fusion cDNAs from a primary T cell ALL containing a t(10;11)(p13-14;q14-21). These cDNAs arose via alternative splicing of exons from both AF10 and CALM, which we demonstrated can also occur in the native genes. We identified at least two novel AF10 exons that can be included in wild-type and fusion cDNAs. The majority of the AF10 and AF10-CALM cDNA isoforms that we identified are predicted to encode for truncated AF10 polypeptides, raising the possibility that these might have important cellular functions in normal and malignant cells, perhaps by acting as dominant negative inhibitors of full-length AF10 or related proteins.	D015459	Leukemia-Lymphoma, Adult T-Cell
MLLT10	9737689	Alternative splicing in wild-type AF10 and CALM cDNAs and in AF10-CALM and CALM-AF10 fusion cDNAs produced by the t(10;11)(p13-14;q14-q21) suggests a potential role for truncated AF10 polypeptides.	The t(10;11)(p13;q14-21) is a non-random translocation that occurs primarily in T cell acute lymphoblastic leukemias (T-ALL), but has also been observed in leukemias and lymphomas of diverse lineages. In U937, a cell line established from a diffuse histiocytic lymphoma, a t(10;11)(p13;q14-21) fuses AF10 to CALM. AF10 is also fused to MLL by a translocation that appears quite similar at the cytogenetic level, the t(10;11)(p12;q23). Fluorescence in situ hybridization studies have demonstrated that AF10 and CALM are also involved in other hematological malignancies containing t(10;11)(p13;q21), but no data are available concerning the molecular details of AF10-CALM fusion in primary leukemias. Using RT-PCR, we amplified multiple different isoforms of AF10-CALM and CALM-AF10 fusion cDNAs from a primary T cell ALL containing a t(10;11)(p13-14;q14-21). These cDNAs arose via alternative splicing of exons from both AF10 and CALM, which we demonstrated can also occur in the native genes. We identified at least two novel AF10 exons that can be included in wild-type and fusion cDNAs. The majority of the AF10 and AF10-CALM cDNA isoforms that we identified are predicted to encode for truncated AF10 polypeptides, raising the possibility that these might have important cellular functions in normal and malignant cells, perhaps by acting as dominant negative inhibitors of full-length AF10 or related proteins.	D014178	Translocation, Genetic

Clinically important variants in MLLT10

(ClinVar, 04/20/2024)

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