ADY3_YEAST - dbPTM
ADY3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ADY3_YEAST
UniProt AC Q07732
Protein Name Accumulates dyads protein 3
Gene Name ADY3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 790
Subcellular Localization Prospore membrane. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Localizes to the leading edge, which cover the ring-shape opening of the PSMs during meiosis II. Colocalizes with DON1 to dots in the cytoplasm and at the S
Protein Description Involved in the pathway that organizes the prospore membrane (PSM) during sporulation. Mediates the assembly of the DON1 ring structure at the leading edge of PSM during meiosis II. May constitute a physical link between SSP1-containing PSM precursors and the spindle pole body (SPB) and may facilitate the recruitment of other factors that are required to promote spore wall formation..
Protein Sequence MNHWLAFLNKPESLKEQNSDCDQQGEMRHVTDGTLTKSPESKPFRERRSQTWIDSEVPTSTEKSNVQESISSDIISKLSNRRSRRNRSESWAGSEASSPSGNISTLENATEKNTLKSPNKFLQRGGLPTVGIGSQALSPAGKPSTLGNVSPGKFTTYKVHNSIEVNRFSSTPTKLLTNPHKVAAISNDEHYVVSNESLEENIEVAHLENVFRSSKTPDEEQSEYMKLGEIRLSSSSYGGSISKENSLPKVLDELQSQNEEIKALRQKLEEKDDRIQELEELNSMNDAKLQRIEDLQKEFHNERKAASKRLNIVQDRFRKEIKKIREEKITDFQNKNASKKEKNEVTSAKTKCKAFSQRNILVSELYRKQKQILNLQQENDKFLKDINESNNSIVKLRSEVEILKSNLQLSQDENKKLHDNGSFYEKRLNDVYSYMQNLSLFEKDLGKFILEEMKCGHSPSMFQNGFAKLYPDFQDIKNLENMEQYKQLKGKIELLEKNDRIRLEKIISVFKLINERLHFMQQQHSHKIKYLQKEALTKEQQFRLEKRRWHDILNLKEENFQKLKSELKEKLILSEKIQKNAEDKLNDYMNEHQEIVEKLQNQALIASRWSTQIQESENTHKKITDELAGKQSEILKLEETILSLKEDVFQEKLNLKKLYGDPSTELNFETVGKSFPHITKEKYDSLGLDILTDLTYVQSQNLIKNLLIVLDIPLKTFLKIVPTIVIQLRCELTLLTKFANDLNLKVFGKQLDFKSRRKVAMNEFLNNHDIAEVKHPLEYDLQALFKYFFS
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
117PhosphorylationTEKNTLKSPNKFLQR
CHHCCCCCCCHHHHC		36.5027214570
129PhosphorylationLQRGGLPTVGIGSQA
HHCCCCCCCCCCCCC		36.0929734811
138PhosphorylationGIGSQALSPAGKPST
CCCCCCCCCCCCCCC		18.7329734811
150PhosphorylationPSTLGNVSPGKFTTY
CCCCCCCCCCCCCEE		31.7527214570
216PhosphorylationNVFRSSKTPDEEQSE
HHHHCCCCCCHHHHH		37.6127214570
234PhosphorylationLGEIRLSSSSYGGSI
HCEEECCCCCCCCCC		28.0927214570
235PhosphorylationGEIRLSSSSYGGSIS
CEEECCCCCCCCCCC		24.9727214570
256PhosphorylationKVLDELQSQNEEIKA
HHHHHHHHCHHHHHH		47.8227214570
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 ADY3_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ADY3_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 ADY3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CHA4_YEASTCHA4physical
10688190
MPC70_YEASTSPO21physical
10688190
SSP1_YEASTSSP1physical
10688190
CNM67_YEASTCNM67physical
11973299
MPC70_YEASTSPO21physical
11973299
SPC42_YEASTSPC42physical
11973299
NUD1_YEASTNUD1physical
11973299
MPC54_YEASTMPC54physical
11742972
MPC70_YEASTSPO21physical
11742972
CNM67_YEASTCNM67physical
11742972
SSP1_YEASTSSP1physical
11742972
NUD1_YEASTNUD1physical
11742972
HPH2_YEASTFRT2physical
11283351
HSP26_YEASTHSP26physical
11283351
ODO2_YEASTKGD2physical
11283351
DON1_YEASTDON1physical
11283351
HUA1_YEASTHUA1physical
11283351
SSP1_YEASTSSP1physical
11283351
AMPL_YEASTAPE1physical
11283351
LAM6_YEASTYLR072Wphysical
11283351
ATG17_YEASTATG17physical
11283351
CACP_YEASTCAT2physical
11283351
HPH1_YEASTFRT1physical
11283351
MUK1_YEASTMUK1physical
11283351
SPC29_YEASTSPC29physical
11283351
BBP1_YEASTBBP1physical
11283351
GIP1_YEASTGIP1genetic
17905927
CHA4_YEASTCHA4physical
18719252
RDR1_YEASTRDR1physical
18719252
ATG17_YEASTATG17physical
18719252
PEX14_YEASTPEX14physical
18719252
MUK1_YEASTMUK1physical
18719252
AMPL_YEASTAPE1physical
18719252
DIG1_YEASTDIG1physical
18719252
URC2_YEASTURC2physical
18719252
URK1_YEASTURK1physical
18719252
DAL80_YEASTDAL80physical
18719252
ENO2_YEASTENO2physical
22940862
HSP71_YEASTSSA1physical
22940862
HSP72_YEASTSSA2physical
22940862
NGG1_YEASTNGG1physical
22875988
KEL2_YEASTKEL2physical
22875988
SKN7_YEASTSKN7physical
22875988
SPC42_YEASTSPC42physical
22875988
ENT2_YEASTENT2physical
22875988
VPS20_YEASTVPS20physical
22875988
YM11_YEASTEPO1physical
22875988
HPH1_YEASTFRT1physical
22875988
SPC29_YEASTSPC29physical
22875988
BBP1_YEASTBBP1physical
22875988
VPS64_YEASTVPS64physical
22875988
RGA1_YEASTRGA1physical
22875988
STU1_YEASTSTU1genetic
27708008
MED8_YEASTMED8genetic
27708008
LIP1_YEASTLIP1genetic
27708008
DON1_YEASTDON1physical
27477278
GMCL1_HUMANGMCL1physical
27107014
SPERT_HUMANSPERTphysical
27107014
GCC1_HUMANGCC1physical
27107014
CEP55_HUMANCEP55physical
27107014
AMOL2_HUMANAMOTL2physical
27107014
ZBT8A_HUMANZBTB8Aphysical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ADY3_YEAST

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Related Literatures of Post-Translational Modification

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