ASH1_YEAST - dbPTM
ASH1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ASH1_YEAST
UniProt AC P34233
Protein Name Transcriptional regulatory protein ASH1
Gene Name ASH1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 588
Subcellular Localization Nucleus . Preferentially accumulates in daughter cell nuclei at the end of anaphase.
Protein Description Component of the RPD3C(L) histone deacetylase complex (HDAC). 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. ASH1 is necessary to repress HO in daughter cells to block mating-type switching through its binding to HO promoter 5'-YTGAT-3' sites. Also involved in pseudohyphal growth..
Protein Sequence MSSLYIKTPLHALSAGPDSHANSSYYDNLLLPSFSNLSSNISRNNITTDNNINSASPRKYSFHSLNVSPILSPISLANEILGKKSNTAPASPHHMDYNPISSLTPGNSPEFNKASLSQISFTNPLNYGSGLGFSSNSQPRLPLLDRLSSVSLSKRPERPQQSLPSLRHLQLLPSPLLQENAARFPDTSKRTSNWKTDLTHWCKDTNYQDYVKIREEVAHFKPLSIPNLTNNQNNDSFNYGKELESTRSSKFHSPSKESFDRTKLIPSILEAKDQFKDLSNNAWSITPPVTPPMSPPTNRTMERTTLRGVEASFFEGKSSNNDSIFNPIISEKLVQEVKHQRQLRGNSFPMPNASHKKTNSFKALQIKKLLANRDILSNNSKSNVRKPSKNKISKQASNVFGNTARQLVMKLDNASYSSVSASSSPSPSTPTKSGKMRSRSSSPVRPKAYTPSPRSPNYHRFALDSPPQSPRRSSNSSITKKGSRRSSGSSPTRHTTRVCVSCHSSDSPCWRPSWSPRKQDQLCNSCGLRYKKTHTRCLNDLCRKIPTKGEINIMKSNGIDKEFVPERNCEIEGYRCLFCNYITETVEN
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
7Ubiquitination-MSSLYIKTPLHALS
-CCCCEECCCHHHHH		30.4517644757
47PhosphorylationNISRNNITTDNNINS
CCCCCCCCCCCCCCC		30.1622369663
48PhosphorylationISRNNITTDNNINSA
CCCCCCCCCCCCCCC		32.6922369663
54PhosphorylationTTDNNINSASPRKYS
CCCCCCCCCCCCEEE		26.7322369663
56PhosphorylationDNNINSASPRKYSFH
CCCCCCCCCCEEEEE		25.6722369663
59UbiquitinationINSASPRKYSFHSLN
CCCCCCCEEEEECCC		48.9417644757
60PhosphorylationNSASPRKYSFHSLNV
CCCCCCEEEEECCCC		20.1819795423
61PhosphorylationSASPRKYSFHSLNVS
CCCCCEEEEECCCCC		21.3722369663
64PhosphorylationPRKYSFHSLNVSPIL
CCEEEEECCCCCCCC		21.4522369663
68PhosphorylationSFHSLNVSPILSPIS
EEECCCCCCCCCHHH		12.7322369663
72PhosphorylationLNVSPILSPISLANE
CCCCCCCCHHHHHHH		22.4022369663
75PhosphorylationSPILSPISLANEILG
CCCCCHHHHHHHHHC		25.4722369663
85PhosphorylationNEILGKKSNTAPASP
HHHHCCCCCCCCCCC		42.7920377248
87PhosphorylationILGKKSNTAPASPHH
HHCCCCCCCCCCCCC		40.9020377248
91PhosphorylationKSNTAPASPHHMDYN
CCCCCCCCCCCCCCC		24.5722369663
97PhosphorylationASPHHMDYNPISSLT
CCCCCCCCCCCHHCC		18.4420377248
101PhosphorylationHMDYNPISSLTPGNS
CCCCCCCHHCCCCCC		22.1322369663
102PhosphorylationMDYNPISSLTPGNSP
CCCCCCHHCCCCCCC		36.6622369663
104PhosphorylationYNPISSLTPGNSPEF
CCCCHHCCCCCCCCC		30.9720377248
108PhosphorylationSSLTPGNSPEFNKAS
HHCCCCCCCCCCCCC		31.5520377248
113UbiquitinationGNSPEFNKASLSQIS
CCCCCCCCCCHHHCC		44.6817644757
148PhosphorylationLPLLDRLSSVSLSKR
CCCHHHHHHCCCCCC		29.5922369663
149PhosphorylationPLLDRLSSVSLSKRP
CCHHHHHHCCCCCCC		21.9522369663
151PhosphorylationLDRLSSVSLSKRPER
HHHHHHCCCCCCCCC		28.9522369663
153PhosphorylationRLSSVSLSKRPERPQ
HHHHCCCCCCCCCCC		21.0722369663
236PhosphorylationTNNQNNDSFNYGKEL
CCCCCCCCCCCCHHH		19.9521551504
253PhosphorylationTRSSKFHSPSKESFD
CCCCCCCCCCHHHCC		33.7225704821
263AcetylationKESFDRTKLIPSILE
HHHCCCHHCHHHHHH		45.3624489116
272UbiquitinationIPSILEAKDQFKDLS
HHHHHHHHHHHHHCC		42.5623749301
276UbiquitinationLEAKDQFKDLSNNAW
HHHHHHHHHCCCCCE		52.7222817900
279PhosphorylationKDQFKDLSNNAWSIT
HHHHHHCCCCCEECC		37.8722369663
284PhosphorylationDLSNNAWSITPPVTP
HCCCCCEECCCCCCC		17.7421440633
286PhosphorylationSNNAWSITPPVTPPM
CCCCEECCCCCCCCC		18.9422369663
290PhosphorylationWSITPPVTPPMSPPT
EECCCCCCCCCCCCC		27.7022369663
294PhosphorylationPPVTPPMSPPTNRTM
CCCCCCCCCCCCCCC		33.2422369663
297PhosphorylationTPPMSPPTNRTMERT
CCCCCCCCCCCCCCC		40.4922369663
312PhosphorylationTLRGVEASFFEGKSS
EECCCHHHCCCCCCC		19.5729688323
317UbiquitinationEASFFEGKSSNNDSI
HHHCCCCCCCCCCCC		43.4417644757
318PhosphorylationASFFEGKSSNNDSIF
HHCCCCCCCCCCCCC		49.5129688323
319PhosphorylationSFFEGKSSNNDSIFN
HCCCCCCCCCCCCCH		43.0429688323
323PhosphorylationGKSSNNDSIFNPIIS
CCCCCCCCCCHHHHC		31.0729688323
332UbiquitinationFNPIISEKLVQEVKH
CHHHHCHHHHHHHHH		47.3617644757
338AcetylationEKLVQEVKHQRQLRG
HHHHHHHHHHHHHCC		33.0122865919
347PhosphorylationQRQLRGNSFPMPNAS
HHHHCCCCCCCCCCC		33.2930377154
360PhosphorylationASHKKTNSFKALQIK
CCCCCCCCHHHHHHH		33.1021440633
397PhosphorylationNKISKQASNVFGNTA
CHHHHHHHHHHHHHH		30.9122369663
410UbiquitinationTARQLVMKLDNASYS
HHHHHHHHHHCCCCC		45.2517644757
415PhosphorylationVMKLDNASYSSVSAS
HHHHHCCCCCCCCCC		31.6323749301
418PhosphorylationLDNASYSSVSASSSP
HHCCCCCCCCCCCCC		16.3227017623
423PhosphorylationYSSVSASSSPSPSTP
CCCCCCCCCCCCCCC		46.0820377248
426PhosphorylationVSASSSPSPSTPTKS
CCCCCCCCCCCCCCC		33.1720377248
428PhosphorylationASSSPSPSTPTKSGK
CCCCCCCCCCCCCCC		51.8929734811
429PhosphorylationSSSPSPSTPTKSGKM
CCCCCCCCCCCCCCC		38.0627017623
431PhosphorylationSPSPSTPTKSGKMRS
CCCCCCCCCCCCCCC		37.6227017623
432UbiquitinationPSPSTPTKSGKMRSR
CCCCCCCCCCCCCCC		59.4217644757
438PhosphorylationTKSGKMRSRSSSPVR
CCCCCCCCCCCCCCC		32.7728889911
440PhosphorylationSGKMRSRSSSPVRPK
CCCCCCCCCCCCCCC		36.0919795423
441PhosphorylationGKMRSRSSSPVRPKA
CCCCCCCCCCCCCCC		37.2419795423
442PhosphorylationKMRSRSSSPVRPKAY
CCCCCCCCCCCCCCC		28.7619795423
447UbiquitinationSSSPVRPKAYTPSPR
CCCCCCCCCCCCCCC		43.3822817900
449PhosphorylationSPVRPKAYTPSPRSP
CCCCCCCCCCCCCCC		25.8822369663
450PhosphorylationPVRPKAYTPSPRSPN
CCCCCCCCCCCCCCC		23.3422369663
452PhosphorylationRPKAYTPSPRSPNYH
CCCCCCCCCCCCCCC		25.7522369663
455PhosphorylationAYTPSPRSPNYHRFA
CCCCCCCCCCCCCCC		22.3822369663
458PhosphorylationPSPRSPNYHRFALDS
CCCCCCCCCCCCCCC		9.5822369663
465PhosphorylationYHRFALDSPPQSPRR
CCCCCCCCCCCCCCC		39.0522369663
469PhosphorylationALDSPPQSPRRSSNS
CCCCCCCCCCCCCCC		26.5822369663
474PhosphorylationPQSPRRSSNSSITKK
CCCCCCCCCCCCCCC		38.6328889911
477PhosphorylationPRRSSNSSITKKGSR
CCCCCCCCCCCCCCC		38.2328889911
505PhosphorylationVCVSCHSSDSPCWRP
EEEEECCCCCCCCCC		20.6019779198
518UbiquitinationRPSWSPRKQDQLCNS
CCCCCHHHHHHCCHH		62.7017644757
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 ASH1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ASH1_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 ASH1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PHO23_YEASTPHO23physical
16554755
RPD3_YEASTRPD3physical
16314178
SIN3_YEASTSIN3physical
16314178
UME1_YEASTUME1physical
16314178
PHO23_YEASTPHO23physical
16314178
SAP30_YEASTSAP30physical
16314178
SDS3_YEASTSDS3physical
16314178
CTI6_YEASTCTI6physical
16314178
RXT2_YEASTRXT2physical
16314178
RXT3_YEASTRXT3physical
16314178
DEP1_YEASTDEP1physical
16314178
UME6_YEASTUME6physical
16314178
ASH1_YEASTASH1physical
16314178
ACE2_YEASTACE2genetic
19841732
CDC4_YEASTCDC4physical
21098119
SWI6_YEASTSWI6genetic
20831804
INO4_YEASTINO4genetic
20831804
SOK2_YEASTSOK2genetic
20831804
SWI4_YEASTSWI4genetic
20831804
SWI5_YEASTSWI5genetic
20831804
SHE2_YEASTSHE2physical
20876833
MYO4_YEASTMYO4physical
20876833
ARP8_YEASTARP8genetic
20959818
AFT1_YEASTAFT1genetic
20959818
SUT2_YEASTSUT2genetic
20959818
LSM6_YEASTLSM6genetic
20959818
AF9_YEASTYAF9genetic
20959818
DOA1_YEASTDOA1genetic
20959818
SWR1_YEASTSWR1genetic
20959818
LEO1_YEASTLEO1genetic
20959818
ELP2_YEASTELP2genetic
20959818
JHD2_YEASTJHD2genetic
20959818
HAL4_YEASTSAT4genetic
21127252
PACC_YEASTRIM101genetic
21127252
FUS3_YEASTFUS3genetic
21127252
CTF8_YEASTCTF8genetic
21127252
CTK1_YEASTCTK1genetic
21127252
ATM_YEASTTEL1genetic
21127252
KDX1_YEASTKDX1genetic
21127252
INO2_YEASTINO2genetic
21127252
CDC53_YEASTCDC53genetic
27708008
ORC6_YEASTORC6genetic
27708008
CND2_YEASTBRN1genetic
27708008
PRP5_YEASTPRP5genetic
27708008
TRS20_YEASTTRS20genetic
27708008
PRP11_YEASTPRP11genetic
27708008
CDC1_YEASTCDC1genetic
27708008
TRS23_YEASTTRS23genetic
27708008
TFB1_YEASTTFB1genetic
27708008
GPI8_YEASTGPI8genetic
27708008
COG3_YEASTCOG3genetic
27708008
MOB2_YEASTMOB2genetic
27708008
YPT1_YEASTYPT1genetic
27708008
SAD1_YEASTSAD1genetic
27708008
BRL1_YEASTBRL1genetic
27708008
MED6_YEASTMED6genetic
27708008
EXO70_YEASTEXO70genetic
27708008
SEC39_YEASTSEC39genetic
27708008
BET5_YEASTBET5genetic
27708008
TAF13_YEASTTAF13genetic
27708008
SMC5_YEASTSMC5genetic
27708008
SYA_YEASTALA1genetic
27708008
TIM50_YEASTTIM50genetic
27708008
IPL1_YEASTIPL1genetic
27708008
PGTB2_YEASTBET2genetic
27708008
PP2C3_YEASTPTC3genetic
27708008
SWC5_YEASTSWC5genetic
27708008
VBA2_YEASTVBA2genetic
27708008
LSM6_YEASTLSM6genetic
27708008
AIM11_YEASTAIM11genetic
27708008
YGZ2_YEASTYGL242Cgenetic
27708008
RME1_YEASTRME1genetic
27708008
YG1X_YEASTYGR050Cgenetic
27708008
PHB2_YEASTPHB2genetic
27708008
TBP7_YEASTYTA7genetic
27708008
YJY1_YEASTYJR011Cgenetic
27708008
ELO3_YEASTELO3genetic
27708008
HAT1_YEASTHAT1genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
NEW1_YEASTNEW1genetic
27708008
SUE1_YEASTSUE1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ASH1_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-54 AND SER-465, AND MASSSPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-452, AND MASSSPECTROMETRY.

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