MLLT10

MLLT10
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 5DAG, 5DAH
Identifiers
Aliases	MLLT10, AF10, myeloid/lymphoid or mixed-lineage leukemia; translocated to, 10, histone lysine methyltransferase DOT1L cofactor, MLLT10 histone lysine methyltransferase DOT1L cofactor
External IDs	OMIM: 602409 MGI: 1329038 HomoloGene: 20973 GeneCards: MLLT10
Gene location (Human) Chr. Chromosome 10 (human) Band 10p12.31 Start 21,524,646 bp End 21,743,630 bp
Gene location (Mouse) Chr. Chromosome 2 (mouse) Band 2|2 A3 Start 18,055,237 bp End 18,212,388 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in Achilles tendon secondary oocyte sperm tibia superficial temporal artery sural nerve skin of abdomen gastric mucosa ganglionic eminence canal of the cervix Top expressed in spermatocyte secondary oocyte seminiferous tubule spermatid thymus abdominal wall ganglionic eminence Paneth cell atrioventricular valve ciliary body More reference expression data BioGPS More reference expression data
Gene ontology Molecular function DNA-binding transcription factor activity DNA binding protein binding metal ion binding chromatin binding nucleosome binding histone binding Cellular component nucleoplasm nucleus cytosol protein-containing complex Biological process regulation of transcription, DNA-templated transcription, DNA-templated positive regulation of transcription by RNA polymerase II Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8028 17354 Ensembl ENSG00000078403 ENSMUSG00000026743 UniProt P55197 O54826 RefSeq (mRNA) NM_001009569 NM_001195626 NM_001195627 NM_001195628 NM_001195630 NM_004641 NM_001324296 NM_001324297 NM_001252560 NM_001252561 NM_010804 RefSeq (protein) NP_001182555 NP_001182556 NP_001182557 NP_001182559 NP_001311225 NP_001311226 NP_004632 NP_001239489 NP_001239490 NP_034934 Location (UCSC) Chr 10: 21.52 – 21.74 Mb Chr 2: 18.06 – 18.21 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Protein AF-10 is a protein that in humans is encoded by the MLLT10 gene.

Interactions

MLLT10 has been shown to interact with SS18.

Further reading

• Silliman CC, McGavran L, Wei Q, Miller LA, Li S, Hunger SP (1998). "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". Leukemia. 12 (9): 1404–10. doi:10.1038/sj.leu.2401109. PMID 9737689. S2CID 5821466.
• Linder B, Newman R, Jones LK, Debernardi S, Young BD, Freemont P, Verrijzer CP, Saha V (2000). "Biochemical analyses of the AF10 protein: the extended LAP/PHD-finger mediates oligomerisation". J. Mol. Biol. 299 (2): 369–78. doi:10.1006/jmbi.2000.3766. PMID 10860745.
• Lillington DM, Jaju RJ, Shankar AG, Neat M, Kearney L, Young BD, Saha V (2000). "Cytogenetic and molecular evidence of marrow involvement in extramedullary acute myeloid leukaemia". Br. J. Haematol. 110 (3): 547–51. doi:10.1046/j.1365-2141.2000.02212.x. PMID 10997963. S2CID 45898713.
• de Bruijn DR, dos Santos NR, Thijssen J, Balemans M, Debernardi S, Linder B, Young BD, Geurts van Kessel A (2001). "The synovial sarcoma associated protein SYT interacts with the acute leukemia associated protein AF10". Oncogene. 20 (25): 3281–9. doi:10.1038/sj.onc.1204419. PMID 11423977. S2CID 2364045.
• Debernardi S, Bassini A, Jones LK, Chaplin T, Linder B, de Bruijn DR, Meese E, Young BD (2002). "The MLL fusion partner AF10 binds GAS41, a protein that interacts with the human SWI/SNF complex". Blood. 99 (1): 275–81. doi:10.1182/blood.V99.1.275. PMID 11756182.
• Cai Y, Gao Y, Sheng Q, Miao S, Cui X, Wang L, Zong S, Koide SS (2002). "Characterization and potential function of a novel testis-specific nucleoporin BS-63". Mol. Reprod. Dev. 61 (1): 126–34. doi:10.1002/mrd.1139. PMID 11774384. S2CID 23631919.
• Roll P, Zattara-Cannoni H, Bustos-Bernard MC, Curtillet C, Michel G, Vagner-Capodano AM (2002). "Molecular and fluorescence in situ hybridization analysis of a 10;11 rearrangement in a case of infant acute monocytic leukemia". Cancer Genet. Cytogenet. 135 (2): 187–91. doi:10.1016/S0165-4608(01)00644-6. PMID 12127405.
• Nakamura T, Mori T, Tada S, Krajewski W, Rozovskaia T, Wassell R, Dubois G, Mazo A, Croce CM, Canaani E (2002). "ALL-1 is a histone methyltransferase that assembles a supercomplex of proteins involved in transcriptional regulation". Mol. Cell. 10 (5): 1119–28. doi:10.1016/S1097-2765(02)00740-2. PMID 12453419.
• Perrin L, Bloyer S, Ferraz C, Agrawal N, Sinha P, Dura JM (2003). "The leucine zipper motif of the Drosophila AF10 homologue can inhibit PRE-mediated repression: implications for leukemogenic activity of human MLL-AF10 fusions". Mol. Cell. Biol. 23 (1): 119–30. doi:10.1128/MCB.23.1.119-130.2003. PMC 140655. PMID 12482966.
• Okada Y, Feng Q, Lin Y, Jiang Q, Li Y, Coffield VM, Su L, Xu G, Zhang Y (2005). "hDOT1L links histone methylation to leukemogenesis". Cell. 121 (2): 167–78. doi:10.1016/j.cell.2005.02.020. PMID 15851025. S2CID 15638573.