TRE1_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TRE1_YEAST
• UniProt AC: Q08919
• Protein Name: Uncharacterized protein TRE1
• Gene Name: TRE1
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 783
• Subcellular Localization: Cell membrane ; Single-pass type II membrane protein .
• Protein Sequence: MVNTRGYTTLPNVEEPANNSQDELNSQDFEQAIGMPSEPPVYVEEMGMEEPQAPEAFSEKVQRFRMCFENNVVIPVKKNVVDPLAQMISLASEKFDLFLSKIGNVMVMRRIFYIMMMSIIAALIIASDRLPNGKARGSNGSFSDHDLLLQYARKSIDLSKIERDLEYISSMPHMSGTSGDAAIRHYIKESFDKNGIRLAGEEEFMAYSNYPGNVSLRVYSKDDTEGFDIPLNEENFNPMSHNGQLNNIPVIYANKASLDDMASMQDQGLLNGDFILLVHYGDYVFQQMLTAQEYGAKAIIFISEPYQDNKDVIQMKSVALPQYGTGDALTPEWEGSIRDPIDATEAKCLPKIPSIPISANQGDKILAILSDTGVKFSNNLFSGSLNDCRLDLLVQTAIRERHPVHDIVGKIEGSEQAGRAIVIAAPRNSASYGTMYPSFGTVVLLSLIQLYQEMVYKFDWKPLRNIYFISFGGSEFNEAGATELMEKRTEALKSEIYTIIDVGQIGIWDDSNNLEIQCHPLLVDLFQKNMTSRKFNVKVDNVHQFGDWTPYLAQGIPVAIISSPGVMNREHPIYTVEDKFDFIKDKLRDKKKGEVLSEIMLYLVEKSLELIDDPFIPFSISNYVDFLSTTLKDLQKECPDTVNFDEVFLGTTLWENTKLQFEKWKSEWTELMYGAGTYIEPTIIAINRWSWNYLLSLIGVTQCLEEGLMDRTFYKNVIFGPKLWVDKGDPLRSWTFPEIRDTIAIKDWSSVQVQANTLGTILQNTARYFLENKNLHGINTNEF

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
139	N-linked_Glycosylation	NGKARGSNGSFSDHD CCCCCCCCCCCCCHH	53.61	-
213	N-linked_Glycosylation	AYSNYPGNVSLRVYS EECCCCCCEEEEEEE	18.72	-
377	Phosphorylation	SDTGVKFSNNLFSGS ECCCCCCCCCCCCCC	21.06	27017623
410	Ubiquitination	PVHDIVGKIEGSEQA CCCCCEEEEECCHHH	27.04	17644757
529	N-linked_Glycosylation	LVDLFQKNMTSRKFN HHHHHHCCCCCCCCC	28.34	-
597	Phosphorylation	KKKGEVLSEIMLYLV CCCCHHHHHHHHHHH	30.19	17287358

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
-	K	Ubiquitination	E3 ubiquitin ligase	RSP5	P39940	PMID:22199232

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TRE1_YEAST !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of TRE1_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRE2_YEAST	TRE2	genetic	16456538
BSD2_YEAST	BSD2	physical	16456538
YPR71_YEAST	YPR071W	physical	18719252
ATG21_YEAST	ATG21	genetic	19547744
SLA1_YEAST	SLA1	genetic	20093466
ATC1_YEAST	PMR1	genetic	20093466
SPA2_YEAST	SPA2	genetic	20093466
UBR2_YEAST	UBR2	genetic	20093466
CSF1_YEAST	CSF1	genetic	20093466
GYL1_YEAST	GYL1	genetic	20093466
PFKA2_YEAST	PFK2	genetic	20093466
AIM39_YEAST	AIM39	genetic	20093466
NOP12_YEAST	NOP12	genetic	20093466
SHE4_YEAST	SHE4	genetic	20093466
DIA2_YEAST	DIA2	genetic	20093466
BSD2_YEAST	BSD2	physical	17429078
HSP71_YEAST	SSA1	physical	22940862
FCY2_YEAST	FCY2	genetic	27708008
HUR1_YEAST	HUR1	genetic	27708008
UPS1_YEAST	UPS1	genetic	27708008

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"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-597, AND MASSSPECTROMETRY.
PubMed: 17287358