dbPTM

TDA7_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TDA7_YEAST
UniProt AC	P53882
Protein Name	Topoisomerase I damage affected protein 7
Gene Name	TDA7
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	636
Subcellular Localization	Vacuole membrane Single-pass membrane protein .
Protein Description
Protein Sequence	MNSNSTIGRTTLGESDTISLSFSEPSSSLNSRSTDVVFASTSTLVPQQGSLTSLPPVSSTATPTYYSTSLTYDETLHTSIDVSSTSTLVSSTDSSSSSEQDTYSSQYDPATSSYSIITPSMSIFSSTSPMSSSSSITSEWSSLTSTTPTLSSSATSLSSSWSSLSSPSSLLVSSSLSLSLSSSYSDTKLFSFDSRSSIFSPSTPTVISPSYTYLSSISATSFQISTTSELSSSWFSTISSPSTISNKDTTFPSSSRNTSTSFYSSSLSSTNDFSTISKSSKLSPSASSSTVSISTISVPTSSSVSSSSSKVPSNRPSSSSSSDDTTSAYSSTYTFQSLQSTTSSSIPPTTQTPSTSTISTSPIPTSSQVFNTVAISSSEDSKTIYYFYTQTYDITDSSTTFVTGLPTTIAVAKSEVTSFSAPSSTITADMSFYQHWLDGSLDNNKNQGTSKTNTGTIVGSVVGSVGGILICVLVVWFMLVRKRKAKRHFKENDSFCHEIGRRTGFPTTAQAKEASLQAQDSGSQQRNTETASANNPFSNEFNFKARGNPPPVPPPRNVTAMNGSFQNMRSNFMDQENRFSYGSSFTYSSLGSSTQGGFSTLSSNSIRLGRGLDNDISHDERNTVQNNSQGFLREII

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	N-linked_Glycosylation	----MNSNSTIGRTT ----CCCCCCCCCCC	37.86	-
257	N-linked_Glycosylation	TFPSSSRNTSTSFYS CCCCCCCCCCCCEEE	40.09	-
492	N-linked_Glycosylation	AKRHFKENDSFCHEI HHHHHHHCCCHHHHH	51.31	-
494	Phosphorylation	RHFKENDSFCHEIGR HHHHHCCCHHHHHHH	41.16	28889911
503	Phosphorylation	CHEIGRRTGFPTTAQ HHHHHHHHCCCCHHH	41.64	28132839
512	Ubiquitination	FPTTAQAKEASLQAQ CCCHHHHHHHHHHHH	41.55	23749301
515	Phosphorylation	TAQAKEASLQAQDSG HHHHHHHHHHHHCCC	23.31	27214570
521	Phosphorylation	ASLQAQDSGSQQRNT HHHHHHCCCCCCCCC	28.41	23749301
523	Phosphorylation	LQAQDSGSQQRNTET HHHHCCCCCCCCCCC	27.39	23749301
530	Phosphorylation	SQQRNTETASANNPF CCCCCCCCCCCCCCC	24.71	19779198
532	Phosphorylation	QRNTETASANNPFSN CCCCCCCCCCCCCCC	38.66	27214570
544	Ubiquitination	FSNEFNFKARGNPPP CCCCCCCCCCCCCCC	37.97	23749301
557	N-linked_Glycosylation	PPVPPPRNVTAMNGS CCCCCCCCCEECCCC	41.06	-
562	N-linked_Glycosylation	PRNVTAMNGSFQNMR CCCCEECCCCHHHHH	40.26	-
564	Phosphorylation	NVTAMNGSFQNMRSN CCEECCCCHHHHHHH	20.75	23749301
617	Phosphorylation	RGLDNDISHDERNTV CCCCCCCCHHHHHHH	27.96	27214570
626	N-linked_Glycosylation	DERNTVQNNSQGFLR HHHHHHHHCCCCCHH	45.87	-
628	Phosphorylation	RNTVQNNSQGFLREI HHHHHHCCCCCHHHC	38.95	22369663

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 TDA7_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TDA7_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 TDA7_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of TDA7_YEAST !!

Drug and Disease Associations

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

Regulatory Network of TDA7_YEAST

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-628, AND MASSSPECTROMETRY.	18407956 [Abstract]