HDAC1_MOUSE - dbPTM
HDAC1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HDAC1_MOUSE
UniProt AC O09106
Protein Name Histone deacetylase 1
Gene Name Hdac1
Organism Mus musculus (Mouse).
Sequence Length 482
Subcellular Localization Nucleus .
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. Deacetylates SP proteins, SP1 and SP3, and regulates their function. Component of the BRG1-RB1-HDAC1 complex, which negatively regulates the CREST-mediated transcription in resting neurons. Upon calcium stimulation, HDAC1 is released from the complex and CREBBP is recruited, which facilitates transcriptional activation. Deacetylates TSHZ3 and regulates its transcriptional repressor activity. Deacetylates 'Lys-310' in RELA and thereby inhibits the transcriptional activity of NF-kappa-B. Deacetylates NR1D2 and abrogates the effect of KAT5-mediated relieving of NR1D2 transcription repression 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. Involved in CIART-mediated transcriptional repression of the circadian transcriptional activator: CLOCK-ARNTL/BMAL1 heterodimer. Required for the transcriptional repression of circadian target genes, such as PER1, mediated by the large PER complex or CRY1 through histone deacetylation..
Protein Sequence MAQTQGTKRKVCYYYDGDVGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKANAEEMTKYHSDDYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVASAVKLNKQQTDIAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNYPLRDGIDDESYEAIFKPVMSKVMEMFQPSAVVLQCGSDSLSGDRLGCFNLTIKGHAKCVEFVKSFNLPMLMLGGGGYTIRNVARCWTYETAVALDTEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTNEYLEKIKQRLFENLRMLPHAPGVQMQAIPEDAIPEESGDEDEEDPDKRISICSSDKRIACEEEFSDSDEEGEGGRKNSSNFKKAKRVKTEDEKEKDPEEKKEVTEEEKTKEEKPEAKGVKEEVKLA
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
7Phosphorylation-MAQTQGTKRKVCYY
-CCCCCCCCEEEEEE		20.19-
45PhosphorylationTHNLLLNYGLYRKME
HHHHHHHHHHHHCCE		14.4224759943
74AcetylationYHSDDYIKFLRSIRP
HCCHHHHHHHHHHCC		31.9222826441
74UbiquitinationYHSDDYIKFLRSIRP
HCCHHHHHHHHHHCC		31.9222790023
87PhosphorylationRPDNMSEYSKQMQRF
CCCCHHHHHHHHHHC		17.54-
89UbiquitinationDNMSEYSKQMQRFNV
CCHHHHHHHHHHCCC		49.2222790023
89AcetylationDNMSEYSKQMQRFNV
CCHHHHHHHHHHCCC		49.2223806337
220AcetylationDIGAGKGKYYAVNYP
ECCCCCCCEEEEECC		38.2823806337
221PhosphorylationIGAGKGKYYAVNYPL
CCCCCCCEEEEECCC		12.82-
261S-nitrosylationPSAVVLQCGSDSLSG
CCEEEEECCCCCCCC		5.01-
261S-nitrosocysteinePSAVVLQCGSDSLSG
CCEEEEECCCCCCCC		5.01-
263PhosphorylationAVVLQCGSDSLSGDR
EEEEECCCCCCCCCC		31.4925521595
265PhosphorylationVLQCGSDSLSGDRLG
EEECCCCCCCCCCEE		26.5725521595
273S-nitrosocysteineLSGDRLGCFNLTIKG
CCCCCEECEEEEECC		2.12-
273S-nitrosylationLSGDRLGCFNLTIKG
CCCCCEECEEEEECC		2.12-
346PhosphorylationPDFKLHISPSNMTNQ
CCCEEEECCCCCCCC		16.1326643407
348PhosphorylationFKLHISPSNMTNQNT
CEEEECCCCCCCCCH		32.2326643407
351PhosphorylationHISPSNMTNQNTNEY
EECCCCCCCCCHHHH		37.5926643407
355PhosphorylationSNMTNQNTNEYLEKI
CCCCCCCHHHHHHHH		21.47-
361UbiquitinationNTNEYLEKIKQRLFE
CHHHHHHHHHHHHHH		53.2422790023
393PhosphorylationEDAIPEESGDEDEED
CCCCCCCCCCCCCCC		50.2924925903
406PhosphorylationEDPDKRISICSSDKR
CCCCCCEEEECCCCE		22.9023684622
408GlutathionylationPDKRISICSSDKRIA
CCCCEEEECCCCEEE		2.2524333276
409PhosphorylationDKRISICSSDKRIAC
CCCEEEECCCCEEEE		39.6426824392
410PhosphorylationKRISICSSDKRIACE
CCEEEECCCCEEEEE		42.6223684622
412UbiquitinationISICSSDKRIACEEE
EEEECCCCEEEEECC		47.88-
412AcetylationISICSSDKRIACEEE
EEEECCCCEEEEECC		47.8823806337
421PhosphorylationIACEEEFSDSDEEGE
EEEECCCCCCCCCCC		39.2127087446
423PhosphorylationCEEEFSDSDEEGEGG
EECCCCCCCCCCCCC		45.8027087446
432MethylationEEGEGGRKNSSNFKK
CCCCCCCCCCHHHHC		65.54-
432AcetylationEEGEGGRKNSSNFKK
CCCCCCCCCCHHHHC		65.548439425
434PhosphorylationGEGGRKNSSNFKKAK
CCCCCCCCHHHHCHH		29.6923684622
435PhosphorylationEGGRKNSSNFKKAKR
CCCCCCCHHHHCHHC		56.5324759943
445PhosphorylationKKAKRVKTEDEKEKD
HCHHCCCCHHHHCCC		45.90-
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
-KUbiquitinationE3 ubiquitin ligaseChfrQ810L3
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
421SPhosphorylation

-
423SPhosphorylation

-
444KSumoylation

-
476KSumoylation

-
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 HDAC1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RB_MOUSERb1physical
11684023
MYOD1_MOUSEMyod1physical
11684023
TF65_MOUSERelaphysical
11931769
NFKB1_MOUSENfkb1physical
11931769
TF65_HUMANRELAphysical
11564889
XPO1_MOUSEXpo1physical
20037577
KIF2A_MOUSEKif2aphysical
20037577
SMAD4_MOUSESmad4physical
17226765
TYY1_MOUSEYy1physical
17220375
NANOG_MOUSENanogphysical
18454139
SIN3A_MOUSESin3aphysical
16109738
HDAC2_MOUSEHdac2physical
16109738
SP3_MOUSESp3physical
16109738
SIN3B_MOUSESin3bphysical
16103876
BRMS1_MOUSEBrms1physical
15978719
CCNE1_MOUSECcne1physical
15722557
MD1L1_MOUSEMad1l1physical
15722557
CCND1_MOUSECcnd1physical
15713663
HDAC9_MOUSEHdac9physical
15711539
PDX1_MOUSEPdx1physical
15496408
SP1_MOUSESp1physical
10409740
PHB2_HUMANPHB2physical
15140878
PHB2_MOUSEPhb2physical
15140878
MYOD1_MOUSEMyod1physical
14749395
SOX2_MOUSESox2physical
21321941
CEBPB_MOUSECebpbphysical
21521687
SIN3A_MOUSESin3aphysical
21448134
KDM5B_MOUSEKdm5bphysical
21448134
ZN431_MOUSEZfp932physical
21177534
SATB2_MOUSESatb2physical
22334647
ETS1_MOUSEEts1physical
22266280
HDAC2_MOUSEHdac2genetic
22223663
SIN3A_MOUSESin3aphysical
11302704
SIN3B_MOUSESin3bphysical
11302704
RBBP4_MOUSERbbp4physical
11302704
HDAC1_MOUSEHdac1physical
11302704
MTA2_MOUSEMta2physical
16462733
MTA1_MOUSEMta1physical
16462733
GSC_MOUSEGscphysical
17568773
TLE1_MOUSETle1physical
22439931
EZH2_MOUSEEzh2physical
22439931
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HDAC1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-393; SER-421 ANDSER-423, AND MASS SPECTROMETRY.
"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-393; SER-421 ANDSER-423, AND MASS SPECTROMETRY.
"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-393; SER-421 ANDSER-423, AND MASS SPECTROMETRY.

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