STE13_YEAST - dbPTM
STE13_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STE13_YEAST
UniProt AC P33894
Protein Name Dipeptidyl aminopeptidase A
Gene Name STE13
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 931
Subcellular Localization Vacuole membrane
Single-pass type II membrane protein. Lysosome-like vacuoles.
Protein Description Responsible for the proteolytic maturation of the alpha-factor precursor..
Protein Sequence MSASTHSHKRKNSHLFPQRKSSNSSMDKPFFPNNDSVANTDPQSNENGHTINEIRPTEATIDVTDVPQTPFLQEQYSMRPRRESFQFNDIENQHHTHSFFSVNKFNRRWGEWSLPEKRSYVLVFTLIALSVLVLLVILIPSKLLPTKITRPKTSAGDSSLGKRSFSIENVLNGDFAIPEDTFHFIDPPQRLLGQDSDPGLYFTTKEIDGHTNFIAKQLFDETFEVNLGGNRFLYEGVEFTVSTVQINYKLDKLIFGTNLESEFRHSSKGFYWIKDLNTGNIEPILPPEKSDDNYELGLSKLSYAHFSPAYNYIYFVYENNLFLQQVNSGVAKKVTEDGSKDIFNAKPDWIYEEEVLASDQAIWWAPDDSKAVFARFNDTSVDDIRLNRYTNMNEAYLSDTKIKYPKPGFQNPQFDLFLVNLQNGIIYSINTGGQKDSILYNGKWISPDTFRFEITDRNSKILDVKVYDIPSSQMLTVRNTNSNLFNGWIEKTKDILSIPPKPELKRMDYGYIDIHADSRGFSHLFYYPTVFAKEPIQLTKGNWEVTGNGIVGYEYETDTIFFTANEIGVMSQHLYSISLTDSTTQNTFQSLQNPSDKYDFYDFELSSSARYAISKKLGPDTPIKVAGPLTRVLNVAEIHDDSILQLTKDEKFKEKIKNYDLPITSYKTMVLDDGVEINYIEIKPANLNPKKKYPILVNIYGGPGSQTFTTKSSLAFEQAVVSGLDVIVLQIEPRGTGGKGWSFRSWAREKLGYWEPRDITEVTKKFIQRNSQHIDESKIAIWGWSYGGFTSLKTVELDNGDTFKYAMAVAPVTNWTLYDSVYTERYMNQPSENHEGYFEVSTIQNFKSFESLKRLFIVHGTFDDNVHIQNTFRLVDQLNLLGLTNYDMHIFPDSDHSIRYHNAQRIVFQKLYYWLRDAFAERFDNTEVLHL
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
4Phosphorylation----MSASTHSHKRK
----CCCCCCCCCCC
21.2430377154
13PhosphorylationHSHKRKNSHLFPQRK
CCCCCCCCCCCCCCC
25.3021440633
21PhosphorylationHLFPQRKSSNSSMDK
CCCCCCCCCCCCCCC
36.6217287358
22PhosphorylationLFPQRKSSNSSMDKP
CCCCCCCCCCCCCCC
43.7121440633
24PhosphorylationPQRKSSNSSMDKPFF
CCCCCCCCCCCCCCC
29.0519823750
25PhosphorylationQRKSSNSSMDKPFFP
CCCCCCCCCCCCCCC
34.9424961812
153PhosphorylationTKITRPKTSAGDSSL
CCCCCCCCCCCCCCC
26.8827017623
154PhosphorylationKITRPKTSAGDSSLG
CCCCCCCCCCCCCCC
36.0627017623
377N-linked_GlycosylationKAVFARFNDTSVDDI
CEEEEECCCCCHHHH
46.20-
390PhosphorylationDIRLNRYTNMNEAYL
HHHECCCCCCCHHHH
25.4227214570
398PhosphorylationNMNEAYLSDTKIKYP
CCCHHHHCCCCCCCC
30.4727214570
437PhosphorylationNTGGQKDSILYNGKW
ECCCCCCEEEECCEE
22.8727017623
467PhosphorylationKILDVKVYDIPSSQM
CEEEEEEEECCCHHE
11.4819684113
471PhosphorylationVKVYDIPSSQMLTVR
EEEEECCCHHEEEEE
33.2728889911
472PhosphorylationKVYDIPSSQMLTVRN
EEEECCCHHEEEEEE
17.7928889911
814N-linked_GlycosylationMAVAPVTNWTLYDSV
EEECCCCCCEECCCC
29.93-
848PhosphorylationSTIQNFKSFESLKRL
EEEECCCCHHHHHEE
30.0628889911

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 STE13_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STE13_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 STE13_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SNX3_YEASTSNX3physical
17420293
SNX3_YEASTSNX3physical
24344282

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STE13_YEAST

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASSSPECTROMETRY.

TOP