dbPTM

HDAC2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HDAC2_MOUSE
UniProt AC	P70288
Protein Name	Histone deacetylase 2
Gene Name	Hdac2
Organism	Mus musculus (Mouse).
Sequence Length	488
Subcellular Localization	Nucleus. Cytoplasm.
Protein Description	Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Forms transcriptional repressor complexes by associating with MAD, SIN3, YY1 and N-COR. Interacts in the late S-phase of DNA-replication with DNMT1 in the other transcriptional repressor complex composed of DNMT1, DMAP1, PCNA, CAF1. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Component of a RCOR/GFI/KDM1A/HDAC complex that suppresses, via histone deacetylase (HDAC) recruitment, a number of genes implicated in multilineage blood cell development. May be involved in the transcriptional repression of circadian target genes, such as PER1, mediated by CRY1 through histone deacetylation. Involved in MTA1-mediated transcriptional corepression of TFF1 and CDKN1A..
Protein Sequence	MAYSQGGGKKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVAKTFNLPLLMLGGGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYMEKIKQRLFENLRMLPHAPGVQMQAIPEDAVHEDSGDEDGEDPDKRISIRASDKRIACDEEFSDSEDEGEGGRRNVADHKKGAKKARIEEDKKETEDKKTDVKEEDKSKDNSGEKTDPKGAKSEQLSNP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MAYSQGGGKKK ----CCCCCCCCCCE	16.89	18779572
46	Phosphorylation	THNLLLNYGLYRKME HHHHHHHHHHHHCCE	14.42	24759943
75	Acetylation	YHSDEYIKFLRSIRP HCCHHHHHHHHHHCC	37.13	23954790
75	Ubiquitination	YHSDEYIKFLRSIRP HCCHHHHHHHHHHCC	37.13	22790023
88	Phosphorylation	RPDNMSEYSKQMQRF CCCCHHHHHHHHHHC	17.54	-
90	Ubiquitination	DNMSEYSKQMQRFNV CCHHHHHHHHHHCCC	49.22	-
221	Acetylation	DIGAGKGKYYAVNFP ECCCCCCCEEEEEEE	38.28	22826441
243	Ubiquitination	ESYGQIFKPIISKVM CCHHHHHHHHHHHHH	36.62	22790023
262	S-nitrosocysteine	PSAVVLQCGADSLSG CCEEEEECCCCCCCC	4.19	-
262	S-nitrosylation	PSAVVLQCGADSLSG CCEEEEECCCCCCCC	4.19	18754010
274	S-nitrosocysteine	LSGDRLGCFNLTVKG CCCCCEECEEEEECC	2.12	-
274	S-nitrosylation	LSGDRLGCFNLTVKG CCCCCEECEEEEECC	2.12	18754010
347	Phosphorylation	PDFKLHISPSNMTNQ CCCEEEECCCCCCCC	16.13	26745281
349	Phosphorylation	FKLHISPSNMTNQNT CEEEECCCCCCCCCC	32.23	26745281
352	Phosphorylation	HISPSNMTNQNTPEY EECCCCCCCCCCHHH	37.59	26745281
356	Phosphorylation	SNMTNQNTPEYMEKI CCCCCCCCHHHHHHH	14.03	26745281
359	Phosphorylation	TNQNTPEYMEKIKQR CCCCCHHHHHHHHHH	16.27	26745281
373	Oxidation	RLFENLRMLPHAPGV HHHHHHCCCCCCCCC	8.43	17242355
382	Oxidation	PHAPGVQMQAIPEDA CCCCCCCCEECCCCC	2.43	17242355
394	Phosphorylation	EDAVHEDSGDEDGED CCCCCCCCCCCCCCC	45.20	24925903
407	Phosphorylation	EDPDKRISIRASDKR CCCCCCEEEEECCCE	15.28	23984901
411	Phosphorylation	KRISIRASDKRIACD CCEEEEECCCEEECC	33.54	21576649
422	Phosphorylation	IACDEEFSDSEDEGE EECCCCCCCCCCCCC	43.43	27087446
424	Phosphorylation	CDEEFSDSEDEGEGG CCCCCCCCCCCCCCC	45.83	27087446
451	Acetylation	KARIEEDKKETEDKK HHHHHHHHHHCCHHC	56.65	23806337
481	Acetylation	KTDPKGAKSEQLSNP CCCCCCCCCHHCCCC	64.29	23806337

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
394	S	Phosphorylation	Kinase	CSNK2A1	Q60737	GPS
-	K	Ubiquitination	E3 ubiquitin ligase	Rlim	Q9WTV7	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
262	C	Acetylation	18754010
In neurons, S-Nitrosylation at Cys-262 and Cys-274 does not affect the enzyme activity but abolishes chromatin-binding, leading to increases acetylation of histones and activate genes that are associated with neuronal development.
262	C	S-nitrosylation	18754010
In neurons, S-Nitrosylation at Cys-262 and Cys-274 does not affect the enzyme activity but abolishes chromatin-binding, leading to increases acetylation of histones and activate genes that are associated with neuronal development.
274	C	Acetylation	18754010
In neurons, S-Nitrosylation at Cys-262 and Cys-274 does not affect the enzyme activity but abolishes chromatin-binding, leading to increases acetylation of histones and activate genes that are associated with neuronal development.
274	C	S-nitrosylation	18754010
In neurons, S-Nitrosylation at Cys-262 and Cys-274 does not affect the enzyme activity but abolishes chromatin-binding, leading to increases acetylation of histones and activate genes that are associated with neuronal development.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of HDAC2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
THB_HUMAN	THRB	physical	10508171
THA_HUMAN	THRA	physical	10508171
TYY1_MOUSE	Yy1	physical	17220375
HDAC9_MOUSE	Hdac9	physical	20211142
NANOG_MOUSE	Nanog	physical	18454139
PO5F1_MOUSE	Pou5f1	physical	18454139
SIN3A_MOUSE	Sin3a	physical	18454139
MTA1_MOUSE	Mta1	physical	18454139
MTA2_MOUSE	Mta2	physical	18454139
MBD3_MOUSE	Mbd3	physical	18454139
RBBP7_MOUSE	Rbbp7	physical	18454139
SIN3A_MOUSE	Sin3a	physical	16109738
SP3_MOUSE	Sp3	physical	16109738
PML_MOUSE	Pml	physical	18454139
PDX1_MOUSE	Pdx1	physical	15496408
ZN431_MOUSE	Zfp932	physical	21177534
LCLT1_MOUSE	Lclat1	physical	26604221
CAF1A_MOUSE	Chaf1a	physical	26365490

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of HDAC2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 ANDSER-424, AND MASS SPECTROMETRY.	19131326 [Abstract]
"The phagosomal proteome in interferon-gamma-activated macrophages."; Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.; Immunity 30:143-154(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, AND MASSSPECTROMETRY.	19144319 [Abstract]
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394; SER-422 ANDSER-424, AND MASS SPECTROMETRY.	19367708 [Abstract]
S-nitrosylation
Reference	PubMed
"S-Nitrosylation of histone deacetylase 2 induces chromatinremodelling in neurons."; Nott A., Watson P.M., Robinson J.D., Crepaldi L., Riccio A.; Nature 455:411-415(2008). Cited for: S-NITROSYLATION AT CYS-262 AND CYS-274, AND MUTAGENESIS OF CYS-152;CYS-262 AND CYS-274.	18754010 [Abstract]

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