HDAC8_HUMAN - dbPTM
HDAC8_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HDAC8_HUMAN
UniProt AC Q9BY41
Protein Name Histone deacetylase 8
Gene Name HDAC8
Organism Homo sapiens (Human).
Sequence Length 377
Subcellular Localization Nucleus. Cytoplasm. Excluded from the nucleoli. Found in the cytoplasm of cells showing smooth muscle differentiation.
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. Also involved in the deacetylation of cohesin complex protein SMC3 regulating release of cohesin complexes from chromatin. May play a role in smooth muscle cell contractility..
Protein Sequence MEEPEEPADSGQSLVPVYIYSPEYVSMCDSLAKIPKRASMVHSLIEAYALHKQMRIVKPKVASMEEMATFHTDAYLQHLQKVSQEGDDDHPDSIEYGLGYDCPATEGIFDYAAAIGGATITAAQCLIDGMCKVAINWSGGWHHAKKDEASGFCYLNDAVLGILRLRRKFERILYVDLDLHHGDGVEDAFSFTSKVMTVSLHKFSPGFFPGTGDVSDVGLGKGRYYSVNVPIQDGIQDEKYYQICESVLKEVYQAFNPKAVVLQLGADTIAGDPMCSFNMTPVGIGKCLKYILQWQLATLILGGGGYNLANTARCWTYLTGVILGKTLSSEIPDHEFFTAYGPDYVLEITPSCRPDRNEPHRIQQILNYIKGNLKHVV
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
39PhosphorylationAKIPKRASMVHSLIE
HCCCHHHHHHHHHHH		25.9310926844
43PhosphorylationKRASMVHSLIEAYAL
HHHHHHHHHHHHHHH		21.45-
48PhosphorylationVHSLIEAYALHKQMR
HHHHHHHHHHHHHHC		9.26-
63PhosphorylationIVKPKVASMEEMATF
CCCCCCCCHHHHHHH		29.70-
92UbiquitinationEGDDDHPDSIEYGLG
CCCCCCCCCCCCCCC		59.8522817900
104UbiquitinationGLGYDCPATEGIFDY
CCCCCCCCCCCHHHH		25.3122817900
122UbiquitinationIGGATITAAQCLIDG
HCCCCEEHHHHHHHC		7.5329967540
130UbiquitinationAQCLIDGMCKVAINW
HHHHHHCCCEEEEEE		1.4522817900
142UbiquitinationINWSGGWHHAKKDEA
EEECCCCCCCCCCCC		17.8222817900
168UbiquitinationGILRLRRKFERILYV
HHHHHHHCCCEEEEE		45.1822817900
221 (in isoform 1)Ubiquitination-45.3021890473
221AcetylationVSDVGLGKGRYYSVN
CCCCCCCCCCEEEEE		45.3025953088
221UbiquitinationVSDVGLGKGRYYSVN
CCCCCCCCCCEEEEE		45.3021906983
233UbiquitinationSVNVPIQDGIQDEKY
EEECCCCCCCCCHHH		57.8122817900
239UbiquitinationQDGIQDEKYYQICES
CCCCCCHHHHHHHHH		58.5129967540
252PhosphorylationESVLKEVYQAFNPKA
HHHHHHHHHHHCCCC		8.67-
259UbiquitinationYQAFNPKAVVLQLGA
HHHHCCCCEEEECCC		9.6322817900
279UbiquitinationDPMCSFNMTPVGIGK
CCCCCCCCCCCCHHH		4.1721890473
279UbiquitinationDPMCSFNMTPVGIGK
CCCCCCCCCCCCHHH		4.1721890473
283UbiquitinationSFNMTPVGIGKCLKY
CCCCCCCCHHHHHHH		24.9222817900
308UbiquitinationLGGGGYNLANTARCW
HCCCCCHHHHHHHHH		2.6821890473
312UbiquitinationGYNLANTARCWTYLT
CCHHHHHHHHHHHHH		12.3922817900
368PhosphorylationRIQQILNYIKGNLKH
HHHHHHHHHHCCCCC		10.6823612710
370 (in isoform 1)Ubiquitination-31.2421890473
370UbiquitinationQQILNYIKGNLKHVV
HHHHHHHHCCCCCCC		31.2422817900
374UbiquitinationNYIKGNLKHVV----
HHHHCCCCCCC----		38.0522817900
382UbiquitinationHVV------------
CCC------------		21890473
386Ubiquitination----------------
----------------		22817900
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
39SPhosphorylationKinasePRKACAP17612
GPS
39SPhosphorylationKinasePKA-FAMILY-GPS
39SPhosphorylationKinasePKA_GROUP-PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HDAC8_HUMAN !!
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 HDAC8_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MTG8_HUMANRUNX1T1physical
11533236
MTG16_HUMANCBFA2T3physical
11533236
CREB1_HUMANCREB1physical
19070599
PP1G_HUMANPPP1CCphysical
19070599
ERR1_HUMANESRRAphysical
20484414
H31_HUMANHIST1H3Aphysical
10926844
H31T_HUMANHIST3H3physical
21499270
HSP74_HUMANHSPA4physical
16809764
HS90A_HUMANHSP90AA1physical
16809764
STAG2_HUMANSTAG2physical
23752268
MIC19_HUMANCHCHD3physical
23752268
CPNE3_HUMANCPNE3physical
23752268
ADDG_HUMANADD3physical
23752268
NEP_HUMANMMEphysical
23752268
NUP98_HUMANNUP98physical
23752268
MDM1_HUMANMDM1physical
23752268
SC16A_HUMANSEC16Aphysical
23752268
CROCC_HUMANCROCCphysical
23752268
SMC1A_HUMANSMC1Aphysical
23752268
SMC3_HUMANSMC3physical
23752268
SVIL_HUMANSVILphysical
23752268
TPM3_HUMANTPM3physical
23752268
TPM4_HUMANTPM4physical
23752268
ZSCA2_HUMANZSCAN2physical
23752268
DCAF1_HUMANVPRBPphysical
26679995
DDB1_HUMANDDB1physical
26679995
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
300882Cornelia de Lange syndrome 5 (CDLS5)
309585Wilson-Turner X-linked mental retardation syndrome (WTS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB02546Vorinostat
Regulatory Network of HDAC8_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Structural snapshots of human HDAC8 provide insights into the class Ihistone deacetylases.";
Somoza J.R., Skene R.J., Katz B.A., Mol C., Ho J.D., Jennings A.J.,Luong C., Arvai A., Buggy J.J., Chi E., Tang J., Sang B.-C.,Verner E., Wynands R., Leahy E.M., Dougan D.R., Snell G., Navre M.,Knuth M.W., Swanson R.V., McRee D.E., Tari L.W.;
Structure 12:1325-1334(2004).
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH TSA; SAHA;MS-344; CRA-A AND DIVALENT METAL CATION, ENZYME REGULATION, ANDPHOSPHORYLATION AT SER-39.

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