dbPTM

KAD6_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	KAD6_YEAST
UniProt AC	Q12055
Protein Name	Adenylate kinase isoenzyme 6 homolog FAP7 {ECO:0000255\|HAMAP-Rule:MF_03173}
Gene Name	FAP7
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	197
Subcellular Localization	Cytoplasm. Nucleus.
Protein Description	Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Has also ATPase activity (By similarity). Involved in 18S rRNA maturation. Required for cleavage of the 20S pre-rRNA at site D in the cytoplasm. Involved in oxidative stress response. Required for POS9-dependent target gene transcription upon oxidative stress..
Protein Sequence	MEARRYGPNIIVTGTPGCGKSSTCEFLKNKLKDYKYYNISDFAKDNDCFEGYDEGRKSHIVDEDKLLDMLEPLLRQGNSIVDWHVNDVFPERLIDLVVVLRCDNSNLYSRLHARGYHDSKIEENLDAEIMGVVKQDAVESYEPHIVVELQSDTKEDMVSNVSRIVAWEKMWLEQHPDGVTNEYQGPRSDDEDDEDSE

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
22	Phosphorylation	TPGCGKSSTCEFLKN CCCCCCHHHHHHHHH	40.33	21440633
32	Acetylation	EFLKNKLKDYKYYNI HHHHHHHCCCCEECH	61.70	24489116
35	Succinylation	KNKLKDYKYYNISDF HHHHCCCCEECHHHH	51.93	23954790
40	Phosphorylation	DYKYYNISDFAKDND CCCEECHHHHHCCCC	24.04	22369663
58	Phosphorylation	GYDEGRKSHIVDEDK CCCCCCHHHCCCHHH	19.65	21440633
180	Phosphorylation	EQHPDGVTNEYQGPR HHCCCCCCCCCCCCC	28.06	22890988
183	Phosphorylation	PDGVTNEYQGPRSDD CCCCCCCCCCCCCCC	22.34	22890988
188	Phosphorylation	NEYQGPRSDDEDDED CCCCCCCCCCCCCCC	53.17	22369663
196	Phosphorylation	DDEDDEDSE------ CCCCCCCCC------	43.06	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 KAD6_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of KAD6_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 KAD6_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RS14A_YEAST	RPS14A	physical	16429126
RS14B_YEAST	RPS14B	physical	16429126
SAP1_YEAST	SAP1	physical	18719252
GBLP_YEAST	ASC1	physical	22770215
RSSA1_YEAST	RPS0A	physical	22770215
RS7A_YEAST	RPS7A	physical	22770215
RS12_YEAST	RPS12	physical	22770215
RS14A_YEAST	RPS14A	physical	22770215
RS18A_YEAST	RPS18A	physical	22770215
RS18B_YEAST	RPS18A	physical	22770215
RS19A_YEAST	RPS19A	physical	22770215
RS22A_YEAST	RPS22A	physical	22770215
RLA0_YEAST	RPP0	physical	22770215
RL5_YEAST	RPL5	physical	22770215
RL6A_YEAST	RPL6A	physical	22770215
RLP7_YEAST	RLP7	physical	22770215
RL11A_YEAST	RPL11A	physical	22770215
RL14A_YEAST	RPL14A	physical	22770215
RL23A_YEAST	RPL23A	physical	22770215
RL23B_YEAST	RPL23A	physical	22770215
RL26A_YEAST	RPL26A	physical	22770215
DIM1_YEAST	DIM1	physical	22770215
EF3A_YEAST	YEF3	physical	22770215
IF5A1_YEAST	HYP2	physical	22770215
TSA1_YEAST	TSA1	physical	22770215
BMH2_YEAST	BMH2	physical	22770215
OLA1_YEAST	OLA1	physical	22770215
VATE_YEAST	VMA4	physical	22770215
METK1_YEAST	SAM1	physical	22770215
RS14A_YEAST	RPS14A	physical	24823650
MK07_HUMAN	MAPK7	physical	27107014
BEND7_HUMAN	BEND7	physical	27107014
LDOC1_HUMAN	LDOC1	physical	27107014

Drug and Disease Associations

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

Regulatory Network of KAD6_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-188 AND SER-196, ANDMASS SPECTROMETRY.	18407956 [Abstract]
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-196, ANDMASS SPECTROMETRY.	11875433 [Abstract]