HDAC9_HUMAN - dbPTM
HDAC9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HDAC9_HUMAN
UniProt AC Q9UKV0
Protein Name Histone deacetylase 9
Gene Name HDAC9
Organism Homo sapiens (Human).
Sequence Length 1011
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. Represses MEF2-dependent transcription.; Isoform 3 lacks active site residues and therefore is catalytically inactive. Represses MEF2-dependent transcription by recruiting HDAC1 and/or HDAC3. Seems to inhibit skeletal myogenesis and to 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 MHSMISSVDVKSEVPVGLEPISPLDLRTDLRMMMPVVDPVVREKQLQQELLLIQQQQQIQKQLLIAEFQKQHENLTRQHQAQLQEHIKELLAIKQQQELLEKEQKLEQQRQEQEVERHRREQQLPPLRGKDRGRERAVASTEVKQKLQEFLLSKSATKDTPTNGKNHSVSRHPKLWYTAAHHTSLDQSSPPLSGTSPSYKYTLPGAQDAKDDFPLRKTASEPNLKVRSRLKQKVAERRSSPLLRRKDGNVVTSFKKRMFEVTESSVSSSSPGSGPSSPNNGPTGSVTENETSVLPPTPHAEQMVSQQRILIHEDSMNLLSLYTSPSLPNITLGLPAVPSQLNASNSLKEKQKCETQTLRQGVPLPGQYGGSIPASSSHPHVTLEGKPPNSSHQALLQHLLLKEQMRQQKLLVAGGVPLHPQSPLATKERISPGIRGTHKLPRHRPLNRTQSAPLPQSTLAQLVIQQQHQQFLEKQKQYQQQIHMNKLLSKSIEQLKQPGSHLEEAEEELQGDQAMQEDRAPSSGNSTRSDSSACVDDTLGQVGAVKVKEEPVDSDEDAQIQEMESGEQAAFMQQPFLEPTHTRALSVRQAPLAAVGMDGLEKHRLVSRTHSSPAASVLPHPAMDRPLQPGSATGIAYDPLMLKHQCVCGNSTTHPEHAGRIQSIWSRLQETGLLNKCERIQGRKASLEEIQLVHSEHHSLLYGTNPLDGQKLDPRILLGDDSQKFFSSLPCGGLGVDSDTIWNELHSSGAARMAVGCVIELASKVASGELKNGFAVVRPPGHHAEESTAMGFCFFNSVAITAKYLRDQLNISKILIVDLDVHHGNGTQQAFYADPSILYISLHRYDEGNFFPGSGAPNEVGTGLGEGYNINIAWTGGLDPPMGDVEYLEAFRTIVKPVAKEFDPDMVLVSAGFDALEGHTPPLGGYKVTAKCFGHLTKQLMTLADGRVVLALEGGHDLTAICDASEACVNALLGNELEPLAEDILHQSPNMNAVISLQKIIEIQSMSLKFS
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
3Phosphorylation-----MHSMISSVDV
-----CCCCCCCCEE		29.6624043423
6Phosphorylation--MHSMISSVDVKSE
--CCCCCCCCEECCC		18.7024043423
7Phosphorylation-MHSMISSVDVKSEV
-CCCCCCCCEECCCC		16.0624043423
12PhosphorylationISSVDVKSEVPVGLE
CCCCEECCCCCCCCC		43.6124043423
22PhosphorylationPVGLEPISPLDLRTD
CCCCCCCCCCCHHHC		30.0828674151
44UbiquitinationVDPVVREKQLQQELL
CCHHHCHHHHHHHHH		45.82-
140PhosphorylationGRERAVASTEVKQKL
CCHHHHCCHHHHHHH		20.6427794612
141PhosphorylationRERAVASTEVKQKLQ
CHHHHCCHHHHHHHH		34.7527794612
177PhosphorylationSRHPKLWYTAAHHTS
CCCCCCEEEECCCCC		9.2727080861
178PhosphorylationRHPKLWYTAAHHTSL
CCCCCEEEECCCCCC		13.0423898821
183PhosphorylationWYTAAHHTSLDQSSP
EEEECCCCCCCCCCC		22.5527080861
184PhosphorylationYTAAHHTSLDQSSPP
EEECCCCCCCCCCCC		26.1223898821
188PhosphorylationHHTSLDQSSPPLSGT
CCCCCCCCCCCCCCC		44.4723898821
189PhosphorylationHTSLDQSSPPLSGTS
CCCCCCCCCCCCCCC		25.5527080861
191 (in isoform 11)Phosphorylation-40.90-
217UbiquitinationKDDFPLRKTASEPNL
CCCCCCCCCCCCCCH		57.01-
218PhosphorylationDDFPLRKTASEPNLK
CCCCCCCCCCCCCHH		29.0530183078
220PhosphorylationFPLRKTASEPNLKVR
CCCCCCCCCCCHHHH		59.8425159151
224 (in isoform 9)Phosphorylation-8.74-
227 (in isoform 6)Phosphorylation-17.93-
239PhosphorylationQKVAERRSSPLLRRK
HHHHHHCCCCCCCCC		42.3925159151
240PhosphorylationKVAERRSSPLLRRKD
HHHHHCCCCCCCCCC		20.1126846344
253PhosphorylationKDGNVVTSFKKRMFE
CCCCEEECEEHHHEE		24.3720188095
266 (in isoform 8)Phosphorylation-10.03-
409UbiquitinationKEQMRQQKLLVAGGV
HHHHHHCCCHHCCCC		35.14-
422PhosphorylationGVPLHPQSPLATKER
CCCCCCCCCCCCCCC		26.7428450419
426PhosphorylationHPQSPLATKERISPG
CCCCCCCCCCCCCCC		40.9128450419
449PhosphorylationRHRPLNRTQSAPLPQ
CCCCCCCCCCCCCCH		26.2930108239
451PhosphorylationRPLNRTQSAPLPQST
CCCCCCCCCCCCHHH		31.1022617229
457PhosphorylationQSAPLPQSTLAQLVI
CCCCCCHHHHHHHHH		24.3728450419
458PhosphorylationSAPLPQSTLAQLVIQ
CCCCCHHHHHHHHHH		22.3627080861
477 (in isoform 11)Phosphorylation-38.4825954137
488 (in isoform 11)Phosphorylation-6.9129523821
491PhosphorylationMNKLLSKSIEQLKQP
HHHHHHHHHHHHHCC		28.1628787133
510 (in isoform 9)Phosphorylation-57.6125954137
521 (in isoform 9)Phosphorylation-29.8929523821
526 (in isoform 10)Phosphorylation-28.8225954137
537 (in isoform 10)Phosphorylation-24.3529523821
552 (in isoform 8)Phosphorylation-14.4025954137
554PhosphorylationVKEEPVDSDEDAQIQ
EEECCCCCCHHHHHH		43.0326434776
554 (in isoform 3)Phosphorylation-43.0325954137
563 (in isoform 8)Phosphorylation-2.5929523821
565 (in isoform 3)Phosphorylation-46.4429523821
607PhosphorylationLEKHRLVSRTHSSPA
HHHHCCCCCCCCCCC		35.7323286773
609PhosphorylationKHRLVSRTHSSPAAS
HHCCCCCCCCCCCHH		20.7126434776
611PhosphorylationRLVSRTHSSPAASVL
CCCCCCCCCCCHHCC		37.0926434776
612PhosphorylationLVSRTHSSPAASVLP
CCCCCCCCCCHHCCC		15.7926434776
616PhosphorylationTHSSPAASVLPHPAM
CCCCCCHHCCCCCCC		26.7126434776
631PhosphorylationDRPLQPGSATGIAYD
CCCCCCCCCCCCCCC		29.3723286773
633PhosphorylationPLQPGSATGIAYDPL
CCCCCCCCCCCCCCC		30.7123286773
637PhosphorylationGSATGIAYDPLMLKH
CCCCCCCCCCCCCCE		19.0423286773
663PhosphorylationEHAGRIQSIWSRLQE
HHHHHHHHHHHHHHH		24.5328857561
767PhosphorylationELASKVASGELKNGF
HHHHHHHCCCCCCCE		35.4729396449
966 (in isoform 6)Phosphorylation-48.0517081983
996PhosphorylationPNMNAVISLQKIIEI
CCHHHEEEHHHHHHH		20.3924719451
1007 (in isoform 5)Phosphorylation-33.3817081983
1010 (in isoform 7)Phosphorylation-14.7217081983
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
220SPhosphorylationKinaseCAMK1Q14012
GPS
253SPhosphorylationKinasePKN1Q16512
PSP
451SPhosphorylationKinaseCAMK1Q14012
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
220SPhosphorylation

20188095
240SPhosphorylation

20188095
450SPhosphorylation

20188095
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTBP1_HUMANCTBP1physical
11022042
HDAC3_HUMANHDAC3physical
12590135
SIN3A_HUMANSIN3Aphysical
12590135
SIN3B_HUMANSIN3Bphysical
12590135
NCOR1_HUMANNCOR1physical
12590135
ETV6_HUMANETV6physical
12590135
HDAC4_HUMANHDAC4physical
12590135
MEF2A_HUMANMEF2Aphysical
10487761
HDAC1_HUMANHDAC1physical
10655483
HDAC3_HUMANHDAC3physical
10655483
NU214_HUMANNUP214physical
16356933
RFXK_HUMANRFXANKphysical
15964851
ANRA2_HUMANANKRA2physical
15964851
PKD1_HUMANPKD1physical
15738054
PKD1_HUMANPKD1physical
15623513
HDAC9_HUMANHDAC9physical
18332106
1433E_HUMANYWHAEphysical
15166223
KCC1A_HUMANCAMK1physical
15166223
HDAC1_HUMANHDAC1physical
10487760
PARP1_HUMANPARP1physical
20596014
SMCA4_HUMANSMARCA4physical
20596014
MAML1_HUMANMAML1physical
20203086
TRI29_HUMANTRIM29physical
20947501
P53_HUMANTP53physical
20947501
KI67_HUMANMKI67physical
23752268
TOP1_HUMANTOP1physical
23752268
DSRAD_HUMANADARphysical
23752268
IF6_HUMANEIF6physical
23752268
HDAC9_HUMANHDAC9physical
23752268
H1X_HUMANH1FXphysical
23752268
LAP2A_HUMANTMPOphysical
23752268
LAP2B_HUMANTMPOphysical
23752268
NUP93_HUMANNUP93physical
23752268
TPR_HUMANTPRphysical
23752268
FIP1_HUMANFIP1L1physical
23752268
CCAR2_HUMANCCAR2physical
23752268
NOP2_HUMANNOP2physical
23752268
RCC1_HUMANRCC1physical
23752268
RBM14_HUMANRBM14physical
23752268
SMC3_HUMANSMC3physical
23752268
TPX2_HUMANTPX2physical
23752268
ZC11A_HUMANZC3H11Aphysical
23752268
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00313Valproic Acid
Regulatory Network of HDAC9_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22, AND MASSSPECTROMETRY.

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