dbPTM

HDAC9_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	HDAC9_MOUSE
UniProt AC	Q99N13
Protein Name	Histone deacetylase 9
Gene Name	Hdac9
Organism	Mus musculus (Mouse).
Sequence Length	588
Subcellular Localization	Nucleus .
Protein Description	Devoided of intrinsic deacetylase activity, promotes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) by recruiting HDAC1 and HDAC3. Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Represses MEF2-dependent transcription, inhibits skeletal myogenesis and may be involved in heart development. Protects neurons from apoptosis, both by inhibiting JUN phosphorylation by MAPK10 and by repressing JUN transcription via HDAC1 recruitment to JUN promoter..
Protein Sequence	MHSMISSVDVKSEVPMGLEPISPLDLRTDLRMMMPVVDPVVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHIKELLAIKQQQELLEKEQKLEQQRQEQEVERHRREQQLPPLRGKDRGRERAVASTEVKQKLQEFLLSKSATKDTPTNGKNHSVGRHPKLWYTAAHHTSLDQSSPPLSGTSPSYKYTLPGAQDSKDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGNLVTSFKKRVFEVAESSVSSSSPGSGPSSPNNGPAGNVTENEASALPPTPHPEQLVPQQRILIHEDSMNLLSLYTSPSLPNITLGLPAVPSPLNASNSLKDKQKCETQMLRQGVPLPSQYGSSIAASSSHVHVAMEGKPNSSHQALLQHLLLKEQMRQQKLLVAGGVPLHPQSPLATKERISPGIRGTHKLPRHRPLNRTQSAPLPQSTLAQLVIQQQHQQFLEKQKQYQQQIHMNKLLSKSIEQLKQPGSHLEEAEEELQGDQSMEDRAASKDNSARSDSSACVEDTLGQVGAVKVKEEPVDSDEDAQIQEMECGEQAAFMQQVIGKDLAPGFVIKVII

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MHSMISSVDVKSEV -CCCCCCCCEECCCC	16.06	29895711
22	Phosphorylation	PMGLEPISPLDLRTD CCCCCCCCCCCHHHC	30.08	22942356
157	Phosphorylation	FLLSKSATKDTPTNG HHHCCCCCCCCCCCC	36.22	28576409
160	Phosphorylation	SKSATKDTPTNGKNH CCCCCCCCCCCCCCC	33.30	28576409
162	Phosphorylation	SATKDTPTNGKNHSV CCCCCCCCCCCCCCC	59.71	28576409
178	Phosphorylation	RHPKLWYTAAHHTSL CCCCCEEEECCCCCC	13.04	22807455
183	Phosphorylation	WYTAAHHTSLDQSSP EEEECCCCCCCCCCC	22.55	22807455
184	Phosphorylation	YTAAHHTSLDQSSPP EEECCCCCCCCCCCC	26.12	21082442
218	Phosphorylation	DDFPLRKTASEPNLK CCCCCCCCCCCCCHH	29.05	28833060
220	Phosphorylation	FPLRKTASEPNLKVR CCCCCCCCCCCHHHH	59.84	27087446
239	Phosphorylation	QKVAERRSSPLLRRK HHHHHHCCCCCHHCC	42.39	22942356
240	Phosphorylation	KVAERRSSPLLRRKD HHHHHCCCCCHHCCC	20.11	22942356
421	Phosphorylation	GVPLHPQSPLATKER CCCCCCCCCCCCCCC	26.74	22942356
425	Phosphorylation	HPQSPLATKERISPG CCCCCCCCCCCCCCC	40.91	28725479
448	Phosphorylation	RHRPLNRTQSAPLPQ CCCCCCCCCCCCCCH	26.29	30635358
450	Phosphorylation	RPLNRTQSAPLPQST CCCCCCCCCCCCHHH	31.10	25521595
490	Phosphorylation	MNKLLSKSIEQLKQP HHHHHHHHHHHHHCC	28.16	29899451
552	Phosphorylation	VKEEPVDSDEDAQIQ EEECCCCCCHHHHHH	43.03	11022042

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
240	S	Phosphorylation	Kinase	DYRK1B	Q9Z188	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
220	S	Phosphorylation	11390982
Phosphorylated on Ser-220 and Ser-450; which promotes 14-3-3-binding, impairs interaction with MEF2, and antagonizes antimyogenic activity.
240	S	Phosphorylation	15546868
Phosphorylated on Ser-240 by DYRK1B; which impairs nuclear accumulation.
450	S	Phosphorylation	11390982
Phosphorylated on Ser-220 and Ser-450; which promotes 14-3-3-binding, impairs interaction with MEF2, and antagonizes antimyogenic activity.

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 HDAC9_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CBX5_MOUSE	Cbx5	physical	12242305
SUV91_HUMAN	SUV39H1	physical	12242305
BTG2_RAT	Btg2	physical	27333946

Drug and Disease Associations

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

Regulatory Network of HDAC9_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Mirk/dyrk1B decreases the nuclear accumulation of class II histonedeacetylases during skeletal muscle differentiation."; Deng X., Ewton D.Z., Mercer S.E., Friedman E.; J. Biol. Chem. 280:4894-4905(2005). Cited for: PHOSPHORYLATION AT SER-240, AND SUBCELLULAR LOCATION.	15546868 [Abstract]
"Class II histone deacetylases act as signal-responsive repressors ofcardiac hypertrophy."; Zhang C.L., McKinsey T.A., Chang S., Antos C.L., Hill J.A.,Olson E.N.; Cell 110:479-488(2002). Cited for: PHOSPHORYLATION AT SER-220 AND SER-450, FUNCTION, AND DISRUPTIONPHENOTYPE.	12202037 [Abstract]
"The transcriptional corepressor MITR is a signal-responsive inhibitorof myogenesis."; Zhang C.L., McKinsey T.A., Olson E.N.; Proc. Natl. Acad. Sci. U.S.A. 98:7354-7359(2001). Cited for: FUNCTION, PHOSPHORYLATION AT SER-220 AND SER-450, TISSUE SPECIFICITY,DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.	11390982 [Abstract]