SETD1A Histone methyltransferase that specifically methylates 'Lys-4' of histone H3, when part of the SET1 histone methyltransferase (HMT) complex, but not if the neighboring 'Lys-9' residue is already methylated. H3 'Lys-4' methylation represents a specific tag for epigenetic transcriptional activation. The non-overlapping localization with SETD1B suggests that SETD1A and SETD1B make non-redundant contributions to the epigenetic control of chromatin structure and gene expression. Belongs to the class V-like SAM-binding methyltransferase superfamily. Note: This description may include information from UniProtKB.
Protein type: Amino Acid Metabolism - lysine degradation; EC 2.1.1.43; Methyltransferase; Methyltransferase, protein lysine
Chromosomal Location of Human Ortholog: 16p11.2
Cellular Component:  histone methyltransferase complex; nuclear chromatin; nuclear speck; nucleoplasm; nucleus; Set1C/COMPASS complex
Molecular Function:  beta-catenin binding; histone methyltransferase activity (H3-K4 specific); protein binding; RNA binding; transcription factor binding
Biological Process:  histone H3-K4 methylation; regulation of chromatin organization; regulation of hematopoietic stem cell differentiation; regulation of megakaryocyte differentiation
Disease: Epilepsy, Early-onset, With Or Without Developmental Delay; Neurodevelopmental Disorder With Speech Impairment And Dysmorphic Facies
Reference #:  O15047 (UniProtKB)
Alt. Names/Synonyms: EPEDD; Histone-lysine N-methyltransferase SETD1A; hSET1A; KIAA0339; KMT2F; Lysine N-methyltransferase 2F; SET domain containing 1A; SET domain containing 1A, histone lysine methyltransferase; SET domain-containing protein 1A; SET1; Set1/Ash2 histone methyltransferase complex subunit SET1; SET1A; SETD1A
Gene Symbols: SETD1A
Molecular weight: 186,034 Da
Basal Isoelectric point: 5.07  Predict pI for various phosphorylation states
CST Pathways:  Histone Methylation
Protein-Specific Antibodies, siRNAs or Recombinant Proteins from Cell Signaling Technology® Total Proteins
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SETD1A

Protein Structure Not Found.


Cross-references to other databases:  STRING  |  cBioPortal  |  Wikipedia  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene