SAS4_YEAST - dbPTM
SAS4_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SAS4_YEAST
UniProt AC Q04003
Protein Name Something about silencing protein 4
Gene Name SAS4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 481
Subcellular Localization Nucleus .
Protein Description Component of the SAS complex, a multiprotein complex that acetylates 'Lys-16' of histone H4 and 'Lys-14' of histone H3. The SAS complex is however unable to acetylate nucleosomal histones. The complex is involved in transcriptional silencing at telomeres and at HML locus. Also involved in rDNA silencing. In the complex, SAS4 is essential for histone acetyltransferase (HAT) activity of the complex..
Protein Sequence MGIFQSIEEANNTSERLLRSEIKNSHGEFEKFDFDTEEYEINPKRKLRLVSRINPNAGHLRKSKSCFTVDEHVDETRCQKPVMKSPFMSNVDDEIKKKRETITKMTLEIEHHELSQNIRKPTDDLLPDSTYQPYHKKMLKQENRMIQSDIVNGENEADRLSLISDRLGMLNWEVTLQKVTKINDPTDENEMETKRYQTKELIDSMLHKFESMKKKSRNLARRPASSDSLLKLVSGKDWPKIYTRIDRTFIPDYASSSDEEEEKITVEEIRERRLKKREQQCGGSIIVLLSDHQSQKGMTRFAIVAEPLRKPYLIKTSTKERNSWKNKVPTNPKKFKKAPRISTQIAVKRRREVIPLTMEVEPEVIRDIRQDTQKSMKLNVKAEEISVTETVKSKEMNALRNNAASISPTLSEKAPLGSISSCTASQISQRSSENVGAIINNINPNLAIVPSCNEKTFVKTHNGMKTNSGINILPVRKKKKV
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
23AcetylationRLLRSEIKNSHGEFE
HHHHHHHHHCCCCCC		48.6322865919
85PhosphorylationCQKPVMKSPFMSNVD
CCCCCCCCCCCCCCC		12.7921551504
180PhosphorylationEVTLQKVTKINDPTD
EEEEEEEECCCCCCC		32.9928889911
181AcetylationVTLQKVTKINDPTDE
EEEEEEECCCCCCCC		42.3622865919
186PhosphorylationVTKINDPTDENEMET
EECCCCCCCCCHHHH		59.8328889911
225PhosphorylationNLARRPASSDSLLKL
HHHHCCCCCHHHHHH		37.0423749301
226PhosphorylationLARRPASSDSLLKLV
HHHCCCCCHHHHHHH		33.0727214570
228PhosphorylationRRPASSDSLLKLVSG
HCCCCCHHHHHHHHC		37.2330377154
253PhosphorylationDRTFIPDYASSSDEE
CCCCCCCCCCCCHHH		11.7424961812
255PhosphorylationTFIPDYASSSDEEEE
CCCCCCCCCCHHHHH		24.9321440633
256PhosphorylationFIPDYASSSDEEEEK
CCCCCCCCCHHHHHC		33.3721440633
257PhosphorylationIPDYASSSDEEEEKI
CCCCCCCCHHHHHCC		46.6921440633
377AcetylationQDTQKSMKLNVKAEE
HHHHHHCCCCEEHEE		43.9624489116
405PhosphorylationALRNNAASISPTLSE
HHHHCCCCCCCCCCC		22.6123749301
407PhosphorylationRNNAASISPTLSEKA
HHCCCCCCCCCCCCC		14.8821082442
409PhosphorylationNAASISPTLSEKAPL
CCCCCCCCCCCCCCC		35.8025005228
411PhosphorylationASISPTLSEKAPLGS
CCCCCCCCCCCCCCC		39.2624909858
413AcetylationISPTLSEKAPLGSIS
CCCCCCCCCCCCCHH		52.5124489116
431PhosphorylationASQISQRSSENVGAI
HHHHHHHCCCCHHHH		34.0730377154
432PhosphorylationSQISQRSSENVGAII
HHHHHHCCCCHHHHH		35.0728889911
456PhosphorylationVPSCNEKTFVKTHNG
CCCCCCCEEEEECCC		27.7328889911
460PhosphorylationNEKTFVKTHNGMKTN
CCCEEEEECCCCCCC		18.4428889911
468PhosphorylationHNGMKTNSGINILPV
CCCCCCCCCCCEEEC		46.4028889911
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 SAS4_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SAS4_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 SAS4_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ASF1_YEASTASF1physical
11731480
SAS2_YEASTSAS2physical
11731480
SAS5_YEASTSAS5physical
11731480
RLF2_YEASTRLF2physical
11731480
SAS4_YEASTSAS4physical
11731480
SAS5_YEASTSAS5physical
11731479
SIR4_YEASTSIR4genetic
10471696
SAS5_YEASTSAS5physical
15788653
SAS2_YEASTSAS2physical
15788653
TAF12_YEASTTAF12genetic
17314980
SAC3_YEASTSAC3genetic
17314980
NOT2_YEASTCDC36genetic
17314980
DEP1_YEASTDEP1genetic
17314980
SAN1_YEASTSAN1genetic
17314980
CYPH_YEASTCPR1genetic
17314980
UMP1_YEASTUMP1genetic
17314980
RGP1_YEASTRGP1genetic
17314980
PLPHP_YEASTYBL036Cgenetic
17314980
ARO1_YEASTARO1genetic
17314980
PAT1_YEASTPAT1genetic
17314980
IWR1_YEASTIWR1genetic
17314980
MED2_YEASTMED2genetic
17314980
ORC2_YEASTORC2genetic
18682530
DEP1_YEASTDEP1genetic
20093466
YAJ9_YEASTYAR029Wgenetic
20093466
ATG8_YEASTATG8genetic
20093466
PP2C4_YEASTPTC4genetic
20093466
APE3_YEASTAPE3genetic
20093466
VBA3_YEASTVBA3genetic
20093466
PAT1_YEASTPAT1genetic
20093466
YD114_YEASTYDL114Wgenetic
20093466
RL13A_YEASTRPL13Agenetic
20093466
RLA1_YEASTRPP1Agenetic
20093466
BRE1_YEASTBRE1genetic
20093466
YFF1_YEASTYFL051Cgenetic
20093466
RTF1_YEASTRTF1genetic
20093466
DBF2_YEASTDBF2genetic
20093466
RS27B_YEASTRPS27Bgenetic
20093466
ICE2_YEASTICE2genetic
20093466
SDS3_YEASTSDS3genetic
20093466
CYP7_YEASTCPR7genetic
20093466
MOG1_YEASTMOG1genetic
20093466
DBP7_YEASTDBP7genetic
20093466
APC9_YEASTAPC9genetic
20093466
SMA2_YEASTSMA2genetic
20093466
RAD14_YEASTRAD14genetic
20093466
ESC1_YEASTESC1genetic
20093466
SAP30_YEASTSAP30genetic
20093466
RL9B_YEASTRPL9Bgenetic
20093466
PET8_YEASTPET8genetic
20093466
SIN3_YEASTSIN3genetic
20093466
SHE4_YEASTSHE4genetic
20093466
RS10A_YEASTRPS10Agenetic
20093466
CTI6_YEASTCTI6genetic
20093466
AIM44_YEASTAIM44genetic
20093466
UME1_YEASTUME1genetic
20093466
YP109_YEASTYPL109Cgenetic
20093466
LGE1_YEASTLGE1genetic
20093466
RAD1_YEASTRAD1genetic
20093466
CTF4_YEASTCTF4genetic
20093466
QCR2_YEASTQCR2genetic
20093466
RPD3_YEASTRPD3genetic
20133733
NPL4_YEASTNPL4genetic
27708008
ORC1_YEASTORC1genetic
27708008
ORC4_YEASTORC4genetic
27708008
DEP1_YEASTDEP1genetic
27708008
STE50_YEASTSTE50genetic
27708008
MRC1_YEASTMRC1genetic
27708008
SNT1_YEASTSNT1genetic
27708008
RTF1_YEASTRTF1genetic
27708008
AP18A_YEASTYAP1801genetic
27708008
PTH_YEASTPTH1genetic
27708008
SDS3_YEASTSDS3genetic
27708008
CYP7_YEASTCPR7genetic
27708008
CBF1_YEASTCBF1genetic
27708008
MDM35_YEASTMDM35genetic
27708008
DBP7_YEASTDBP7genetic
27708008
SA190_YEASTSAP190genetic
27708008
SET3_YEASTSET3genetic
27708008
SKG1_YEASTSKG1genetic
27708008
RT109_YEASTRTT109genetic
27708008
BPT1_YEASTBPT1genetic
27708008
TSL1_YEASTTSL1genetic
27708008
SAP30_YEASTSAP30genetic
27708008
IZH2_YEASTIZH2genetic
27708008
SIN3_YEASTSIN3genetic
27708008
LGE1_YEASTLGE1genetic
27708008
CTF4_YEASTCTF4genetic
27708008
QCR2_YEASTQCR2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SAS4_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225; SER-407 ANDSER-432, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, AND MASSSPECTROMETRY.

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