HDAC1_DROME - dbPTM
HDAC1_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HDAC1_DROME
UniProt AC Q94517
Protein Name Histone deacetylase Rpd3
Gene Name Rpd3
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 521
Subcellular Localization Nucleus .
Protein Description Catalyzes the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). [PubMed: 11571273]
Protein Sequence MQSHSKKRVCYYYDSDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATADEMTKFHSDEYVRFLRSIRPDNMSEYNKQMQRFNVGEDCPVFDGLYEFCQLSAGGSVAAAVKLNKQASEICINWGGGLHHAKKSEASGFCYVNDIVLGILELLKYHQRVLYIDIDVHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNIPLRDGMDDDAYESIFVPIISKVMETFQPAAVVLQCGADSLTGDRLGCFNLTVKGHGKCVEFVKKYNLPFLMVGGGGYTIRNVSRCWTYETSVALAVEIANELPYNDYFEYFGPDFKLHISPSNMTNQNTSEYLEKIKNRLFENLRMLPHAPGVQIQAIPEDAINDESDDEDKVDKDDRLPQSDKDKRIVPENEYSDSEDEGEGGRRDNRSYKGQRKRPRLDKDTNSNKASSETSSEIKDEKEKGDGADGEESTASNTNSNNNSNNKSDNDAGATANAGSGSGSGSGAGAKGAKENNI
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
87UbiquitinationDNMSEYNKQMQRFNV
CCHHHHHHHHHHCCC
46.3631113955
391PhosphorylationEDAINDESDDEDKVD
HHHCCCCCCCCCCCC
53.9021082442
406PhosphorylationKDDRLPQSDKDKRIV
CCCCCCCCHHCCCCC
44.6919429919
418PhosphorylationRIVPENEYSDSEDEG
CCCCCCCCCCCCCCC
29.3819429919
419PhosphorylationIVPENEYSDSEDEGE
CCCCCCCCCCCCCCC
28.6021082442
421PhosphorylationPENEYSDSEDEGEGG
CCCCCCCCCCCCCCC
40.7921082442
448PhosphorylationRPRLDKDTNSNKASS
CCCCCCCCCCCCCCC
46.4129892262
450PhosphorylationRLDKDTNSNKASSET
CCCCCCCCCCCCCCC
41.6329892262
454PhosphorylationDTNSNKASSETSSEI
CCCCCCCCCCCHHHH
30.2519429919
455PhosphorylationTNSNKASSETSSEIK
CCCCCCCCCCHHHHH
50.1519429919
457PhosphorylationSNKASSETSSEIKDE
CCCCCCCCHHHHHHH
39.2319429919
458PhosphorylationNKASSETSSEIKDEK
CCCCCCCHHHHHHHH
23.1729892262
462AcetylationSETSSEIKDEKEKGD
CCCHHHHHHHHHCCC
56.6421791702
491PhosphorylationNNNSNNKSDNDAGAT
CCCCCCCCCCCCCCC
43.7119429919
507PhosphorylationNAGSGSGSGSGAGAK
CCCCCCCCCCCCCCC
31.3327794539

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

Oops, there are no upstream regulatory protein records of HDAC1_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HDAC1_DROME !!

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_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PCL_DROMEPclphysical
12697833
EZ_DROMEE(z)physical
12697833
EZ_DROMEE(z)physical
11124122
ESC_DROMEescphysical
11124122
PC_DROMEPcphysical
11493709
CAF1_DROMECaf1physical
15516265
RBF_DROMERbfphysical
15456884
AN32A_DROMEMapmodulinphysical
22036573
AGT2L_DROMECG8745physical
22036573
SIR2_DROMESir2genetic
15520384
PROS_DROMEprosgenetic
20660276
RCOR_DROMECoRestphysical
22036573
ESC_DROMEescphysical
11581156
ESC_DROMEescphysical
12697833
ESC_DROMEescphysical
12408863
FOSLD_DROMEkayphysical
16391236
FOSLA_DROMEkayphysical
16391236
EZ_DROMEE(z)physical
12408863
PC_DROMEPcphysical
11581156
CAF1_DROMECaf1physical
11124122
CAF1_DROMECaf1physical
12697833
GROU_DROMEgrophysical
10485845
SUZ12_DROMESu(z)12physical
12408863

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HDAC1_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391; SER-419; SER-421;SER-455 AND THR-457, AND MASS SPECTROMETRY.

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