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histone acetyltransferase MYST3; MYST protein 3; MOZ, YBF2/SAS3, SAS2 & TIP60 protein 3; Runt-related transcription factor-binding protein 2; monocytic leukemia zinc finger protein; zinc finger protein 220 (MYST3, MOZ, RUNXBP2, ZNF220, KAT6A)

Function: - histone acetyltransferase - may act as a transcriptional coactivator for RUNX1 & RUNX2 - interacts with RUNX1 & RUNX2 - autoacetylated - phosphorylated upon DNA damage, probably by ATM or ATR acetyl-CoA + histone CoA + acetylhistone Structure: - N-terminus is involved in transcriptional activation - C-terminus is involved in transcriptional repression - belongs to the MYST (SAS/MOZ) family - contains 1 C2HC-type Zn+2 finger - contains 2 PHD-type Zn+2 fingers Compartment: - nucleus - partially concentrated in subnuclear foci distinct from PML bodies, & excluded from the nucleoli Pathology: - chromosomal aberrations involving MYST3 may be a cause of acute myeloid leukemias a) translocation t(8;16)(p11;p13) with CREBBP; fusion protein MYST3-CREBBP may induce leukemia by inhibiting RUNX1-mediated transcription b) translocation t(8;22)(p11;q13) with EP300 c) inversion inv(8)(p11;q13) generates the MYST3-NCOA2 oncogene, which consists of the N-terminus part of MYST3 & the C-terminus part of NCOA2; MYST3-NCOA2 binds to CREBBP & disrupts its function in transcription activation - chromosomal translocation t(2;8)(p23;p11.2) involving MYST3 with ASXL2 is a cause of therapy-related myelodysplastic syndrome; translocation generates a MYST3-ASXL2 fusion protein

Related

MOZ gene

General

acetyltransferase phosphoprotein transcription factor (TF) zinc finger protein

Properties

SIZE: entity length = 2004 aa MW = 225 kD COMPARTMENT: cell nucleus MOTIF: activation of RUNX1-1 {1-144} nuclear localization {52-166} Zn finger PHD-type NAME: Zn finger PHD-type SITE: 206-265 EFFECTOR-BOUND: Zn+2 Zn finger PHD-type NAME: Zn finger PHD-type SITE: 259-313 EFFECTOR-BOUND: Zn+2 RUNX1-1 interaction {312-664} MOTIF: serine-rich region {371-379} MOTIF: serine residue (SEVERAL) Ser phosphorylation site {S473} active site SITE: 488-778 MOTIF: Zn finger C2HC-type SITE: 538-560 EFFECTOR-BOUND: Zn+2 binding site SITE: 635-668 FOR-BINDING-OF: ACETYLCOENZYME-A cysteine residue {C646} glutamate-rich region {788-801} MOTIF: glutamate residue (SEVERAL) breakpoint {813-814} Thr phosphorylation site {T909} Ser phosphorylation site {S941} glutamate-rich region {989-995} MOTIF: glutamate residue (SEVERAL) arginine-rich region {1019-1026} MOTIF: arginine residue (SEVERAL) glutamate-rich region {1069-1078} MOTIF: glutamate residue (SEVERAL) Ser phosphorylation site {S1113} breakpoint {1117-1118} lysine-rich region {1147-1150} MOTIF: lysine residue (SEVERAL) glutamate-rich region {1221-1242} MOTIF: glutamate residue (SEVERAL) glutamate-rich region {1267-1302} MOTIF: glutamate residue (SEVERAL) glutamate-rich region {1411-1414} MOTIF: glutamate residue (SEVERAL) RUNX1-2 interaction {1517-1642} MOTIF: breakpoint {1546-1547} serine-rich region {1593-1597} MOTIF: serine residue (SEVERAL) proline-rich region SITE: 1643-1704 MOTIF: proline residue (SEVERAL) activation of RUNX1-2 {1913-1948}

Database Correlations

OMIM 601408 UniProt Q92794 PFAM correlations ENZYME 2.3.1.48

References

  1. UniProt :accession Q92794
  2. Atlas of genetics & cytogenetics in oncology & haematology http://atlasgeneticsoncology.org/genes/MYST3ID25ch8p11.html
  3. Marks P, Rifkind RA, Richon VM, Breslow R, Miller T, Kelly WK. Histone deacetylases and cancer: causes and therapies. Nat Rev Cancer. 2001 Dec;1(3):194-202. Review. PMID: 11902574