HST1_YEAST - dbPTM
HST1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HST1_YEAST
UniProt AC P53685
Protein Name NAD-dependent protein deacetylase HST1
Gene Name HST1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 503
Subcellular Localization Nucleus . But not nucleolar, and cytoplasmic.
Protein Description NAD-dependent histone deacetylase involved in telomeric silencing. Histone deacetylase proteins act via the formation of large multiprotein complexes that are 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. Restores silencing at HMR in SIR2 mutants when overexpressed. Required to repress middle sporulation genes during vegetative growth. Acts as a sensor of NAD(+) levels and regulator of NAD(+) biosynthesis. Regulates the gene expression of de novo NAD(+) biosynthesis genes..
Protein Sequence MNILLMQRIVSFILVVSQGRYFHVGELTMTMLKRPQEEESDNNATKKLKTRLTYPCILGKDKVTGKFIFPAITKDDVMNARLFLKDNDLKTFLEYFLPVEVNSIYIYFMIKLLGFDVKDKELFMALNSNITSNKERSSAELSSIHAKAEDEDELTDPLEKKHAVKLIKDLQKAINKVLSTRLRLPNFNTIDHFTATLRNAKKILVLTGAGVSTSLGIPDFRSSEGFYSKIRHLGLEDPQDVFNLDIFLQDPSVFYNIAHMVLPPENMYSPLHSFIKMLQDKGKLLRNYTQNIDNLESYAGIDPDKLVQCHGSFATASCVTCHWQIPGEKIFENIRNLELPLCPYCYQKRKQYFPMSNGNNTVQTNINFNSPILKSYGVLKPDMTFFGEALPSRFHKTIRKDILECDLLICIGTSLKVAPVSEIVNMVPSHVPQILINRDMVTHAEFDLNLLGFCDDVASLVAKKCHWDIPHKKWQDLKKIDYNCTEIDKGTYKIKKQPRKKQQ
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
40PhosphorylationKRPQEEESDNNATKK
CCCCCCCCCCCCCHH
49.2528889911
91PhosphorylationLKDNDLKTFLEYFLP
EECCCHHHHHHHHCC
40.5228889911
95PhosphorylationDLKTFLEYFLPVEVN
CHHHHHHHHCCCCHH
16.7428889911
103PhosphorylationFLPVEVNSIYIYFMI
HCCCCHHHHHHHHHH
23.1928889911
105PhosphorylationPVEVNSIYIYFMIKL
CCCHHHHHHHHHHHH
6.8728889911
107PhosphorylationEVNSIYIYFMIKLLG
CHHHHHHHHHHHHHC
3.1028889911
137PhosphorylationITSNKERSSAELSSI
CCCCCCCCHHHHHHH
34.6822369663
138PhosphorylationTSNKERSSAELSSIH
CCCCCCCHHHHHHHH
31.8022369663
142PhosphorylationERSSAELSSIHAKAE
CCCHHHHHHHHHHCC
20.8221440633
143PhosphorylationRSSAELSSIHAKAED
CCHHHHHHHHHHCCC
30.9023749301

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 HST1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HST1_YEAST !!

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 HST1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SIF2_YEASTSIF2physical
11805826
HOS2_YEASTHOS2physical
11711434
SET3_YEASTSET3physical
11711434
SIF2_YEASTSIF2physical
11711434
SNT1_YEASTSNT1physical
11711434
SUM1_YEASTSUM1physical
11711434
CYPH_YEASTCPR1physical
11711434
HOS4_YEASTHOS4physical
11711434
SUM1_YEASTSUM1physical
12612074
AKL1_YEASTAKL1physical
16554755
SNT1_YEASTSNT1physical
16554755
SUM1_YEASTSUM1physical
16554755
HOS4_YEASTHOS4physical
16554755
SET3_YEASTSET3physical
16554755
STM1_YEASTSTM1physical
16554755
TPM1_YEASTTPM1physical
16554755
RFM1_YEASTRFM1physical
16554755
CSF1_YEASTCSF1genetic
17314980
RIC1_YEASTRIC1genetic
17314980
LSM7_YEASTLSM7genetic
17314980
VRP1_YEASTVRP1genetic
17314980
RGP1_YEASTRGP1genetic
17314980
RFA2_YEASTRFA2genetic
17314980
YPT6_YEASTYPT6genetic
17314980
ELP2_YEASTELP2genetic
17314980
PFD4_YEASTGIM3genetic
17314980
MMR1_YEASTMMR1genetic
17314980
PFD6_YEASTYKE2genetic
17314980
CDC73_YEASTCDC73genetic
17314980
SUM1_YEASTSUM1physical
17242192
SIR2_YEASTSIR2genetic
17676954
BDF1_YEASTBDF1genetic
18676811
LDB7_YEASTLDB7genetic
18676811
RSC1_YEASTRSC1genetic
18676811
ORC2_YEASTORC2genetic
18990212
AF9_YEASTYAF9genetic
19547744
SUB1_YEASTSUB1genetic
19547744
DAL81_YEASTDAL81genetic
19547744
BEM1_YEASTBEM1genetic
20093466
REI1_YEASTREI1genetic
20093466
HOSC_YEASTLYS20genetic
20093466
NRG1_YEASTNRG1genetic
20093466
FOLC_YEASTRMA1genetic
20093466
DYHC_YEASTDYN1genetic
20093466
SWI6_YEASTSWI6genetic
20093466
VRP1_YEASTVRP1genetic
20093466
SIR2_YEASTSIR2genetic
10562556
ESC2_YEASTESC2genetic
14764870
WHI2_YEASTWHI2genetic
14764870
CLA4_YEASTCLA4genetic
16487579
LTE1_YEASTLTE1genetic
16487579
SIN3_YEASTSIN3genetic
20959818
YPT6_YEASTYPT6genetic
20959818
RFM1_YEASTRFM1physical
21690292
SIR4_YEASTSIR4physical
21690292
SUM1_YEASTSUM1genetic
22285862
TOS4_YEASTTOS4physical
22333912
SIR2_YEASTSIR2genetic
21483810
HOS2_YEASTHOS2genetic
25132173
HST2_YEASTHST2genetic
25381059
ESA1_YEASTESA1genetic
25381059
PDC2_YEASTPDC2genetic
27708008
RAD61_YEASTRAD61genetic
27708008
KRR1_YEASTKRR1genetic
27708008
PSF2_YEASTPSF2genetic
27708008
BOS1_YEASTBOS1genetic
27708008
ORC1_YEASTORC1genetic
27708008
SEC65_YEASTSEC65genetic
27708008
SYH_YEASTHTS1genetic
27708008
ORC4_YEASTORC4genetic
27708008
NPL4_YEASTNPL4genetic
27708008
INO2_YEASTINO2genetic
27708008
RTG2_YEASTRTG2genetic
27708008
GPP1_YEASTGPP1genetic
27708008
DPOD3_YEASTPOL32genetic
27708008
MRT4_YEASTMRT4genetic
27708008
ELM1_YEASTELM1genetic
27708008
MEH1_YEASTMEH1genetic
27708008
VPS51_YEASTVPS51genetic
27708008
MSC1_YEASTMSC1genetic
27708008
YO385_YEASTYOR385Wgenetic
27708008
MED1_YEASTMED1genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HST1_YEAST

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Related Literatures of Post-Translational Modification

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