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HDAC1 (human)

Overview HDAC1 a transcriptional regulator of the histone deacetylase family, subfamily 1. Deacetylates lysine residues on the N-terminal part of the core histones H2A, H2B, H3 AND H4. Plays an important role in transcriptional regulation, cell cycle progression and developmental events. Note: This description may include information from UniProtKB. Protein type: EC 3.5.1.98; Hydrolase; Nuclear receptor co-regulator Cellular Component: nucleoplasm; Sin3 complex; histone deacetylase complex; cytoplasm; nucleolus; NuRD complex; cytosol; nucleus Molecular Function: identical protein binding; NAD-dependent histone deacetylase activity (H3-K9 specific); protein binding; enzyme binding; transcription activator binding; NAD-dependent histone deacetylase activity (H3-K14 specific); histone deacetylase binding; protein deacetylase activity; NAD-dependent histone deacetylase activity (H4-K16 specific); histone deacetylase activity; transcription factor activity; transcription factor binding Biological Process: transcription initiation from RNA polymerase II promoter; Notch signaling pathway; transcription, DNA-dependent; nerve growth factor receptor signaling pathway; positive regulation of transcription, DNA-dependent; histone deacetylation; negative regulation of transcription from RNA polymerase II promoter; chromatin modification; odontogenesis of dentine-containing teeth; negative regulation of cell cycle; chromatin remodeling; protein amino acid deacetylation; virus-host interaction; transforming growth factor beta receptor signaling pathway; positive regulation of cell proliferation; epidermal cell differentiation; positive regulation of transcription from RNA polymerase II promoter; gene expression; embryonic digit morphogenesis; mitotic cell cycle; blood coagulation; negative regulation of transcription, DNA-dependent; negative regulation of apoptosis Reference #:  Q13547 (UniProtKB) Alt. Names/Synonyms: DKFZp686H12203; GON-10; HD1; HDAC1; Histone deacetylase 1; reduced potassium dependency, yeast homolog-like 1; RPD3; RPD3L1 Gene Symbols: HDAC1 Molecular weight: 55,103 Da Basal Isoelectric point: 5.31  Predict pI for various phosphorylation states CST Pathways:  Cell Cycle: G1/S Checkpoint  |  Crosstalk between PTMs  |  NF-kB Signaling  |  Protein Acetylation  |  Wnt/ß-Catenin Signaling Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below HDAC1 1TYI - A=1-482 (human)

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	Sites Implicated In
enzymatic activity, induced: S421‑p, S423‑p molecular association, regulation: S421‑p, S423‑p

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	1		K10-u	QTQGTRRkVCYYYDG
0	1		T7	_MAQTQGTRRkVCYY
0	1		Y48-p	LLLNYGLyRKMEIYR
0	4		K66-u	ANAEEMTkYHSDDYI
0	1		K74-a	YHSDDYIkFLRSIRP
0	6		K74-u	YHSDDYIkFLRSIRP
0	8		Y87-p	RPDNMSEySkQMQRF
0	75		K89-u	DNMSEySkQMQRFNV
0	4		K126-u	ASAVKLNkQQTDIAV
1	0		K218-a	LRDIGAGkGkyYAVN
1	3		K220-a	DIGAGkGkyYAVNyP
0	5		Y221-p	IGAGkGkyYAVNyPL
0	1		Y226-p	GkyYAVNyPLRDGID
0	1		K242-u	ESYEAIFkPVMSKVM
0	1		S290-p	KCVEFVKsFNLPMLM
0	4		K361-u	NTNEYLEkIkQRLFE
0	2		K363-u	NEYLEkIkQRLFENL
0	296		S393-p	EDAIPEEsGDEDEDD
0	1		S409-p	DKRISICsSDkRIAC
0	28		K412-a	ISICsSDkRIACEEE
0	1		K412	ISICsSDKRIACEEE
1	64		S421-p	IACEEEFsDsEEEGE
1	62		S423-p	CEEEFsDsEEEGEGG
2	0		K432-a	EEGEGGRkNssNFkk
0	1		K432-m	EEGEGGRkNssNFkk
0	5		S434-p	GEGGRkNssNFkkAk
0	1		S435-p	EGGRkNssNFkkAkR
1	0		K438-a	RkNssNFkkAkRVkt
1	0		K439-a	kNssNFkkAkRVktE
1	0		K441-a	ssNFkkAkRVktEDE
2	0		K444-s	FkkAkRVktEDEKEK
0	3		T445-p	kkAkRVktEDEKEKD
2	0		K476-s	KPEAKGVkEEVKLA_

	mouse
K10	QTQGtKRKVCYYYDG
T7-p	_MAQTQGtKRKVCYY
Y48	LLLNYGLYRKMEIYR
K66	ANAEEMTKYHSDDYI
K74	YHSDDYIKFLRSIRP
K74-u	YHSDDYIkFLRSIRP
Y87-p	RPDNMSEySkQMQRF
K89-u	DNMSEySkQMQRFNV
K126	ASAVKLNKQQTDIAV
K218	LRDIGAGKGKyYAVN
K220	DIGAGKGKyYAVNYP
Y221-p	IGAGKGKyYAVNYPL
Y226	GKyYAVNYPLRDGID
K242	ESYEAIFKPVMSKVM
S290	KCVEFVKSFNLPMLM
K361-u	NTNEYLEkIKQRLFE
K363	NEYLEkIKQRLFENL
S393-p	EDAIPEEsGDEDEED
S409-p	DKRISICsSDkRIAC
K412-a	ISICsSDkRIACEEE
K412-u	ISICsSDkRIACEEE
S421-p	IACEEEFsDsDEEGE
S423-p	CEEEFsDsDEEGEGG
K432-a	EEGEGGRkNSSNFKK
K432	EEGEGGRKNSSNFKK
S434	GEGGRkNSSNFKKAK
S435	EGGRkNSSNFKKAKR
K438	RkNSSNFKKAKRVKt
K439	kNSSNFKKAKRVKtE
K441	SSNFKKAKRVKtEDE
K444	FKKAKRVKtEDEKEK
T445-p	KKAKRVKtEDEKEKD
K476	KPEAKGVKEEVKLA_

	rat
K10	QTQGTKRKVCYYYDG
T7	_MAQTQGTKRKVCYY
Y48	LLLNYGLYRKMEIYR
K66	ANAEEMTKYHSDDYI
K74	YHSDDYIKFLRSIRP
K74	YHSDDYIKFLRSIRP
Y87	RPDNMSEYSKQMQRF
K89	DNMSEYSKQMQRFNV
K126	ASAVKLNKQQTDIAV
K218	LRDIGAGKGKYYAVN
K220	DIGAGKGKYYAVNYP
Y221	IGAGKGKYYAVNYPL
Y226	GKYYAVNYPLRDGID
K242	ESYEAIFKPVMSKVM
S290	KCVEFVKSFNLPMLM
K361	NTNEYLEKIKQRLFE
K363	NEYLEKIKQRLFENL
S393-p	EDAIPEEsGDEDEED
S409	DKRISICSSDKRIAC
K412	ISICSSDKRIACEEE
K412	ISICSSDKRIACEEE
S421-p	IACEEEFsDsDEEGE
S423-p	CEEEFsDsDEEGEGG
K432	EEGEGGRKNSSNFKK
K432	EEGEGGRKNSSNFKK
S434	GEGGRKNSSNFKKAK
S435	EGGRKNSSNFKKAKR
K438	RKNSSNFKKAKRVKT
K439	KNSSNFKKAKRVKTE
K441	SSNFKKAKRVKTEDE
K444	FKKAKRVKTEDEKEK
T445	KKAKRVKTEDEKEKD
K476	KPEAKGVKEEVKMA_

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