dbPTM

SCY1_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	SCY1_YEAST
UniProt AC	P53009
Protein Name	Protein kinase-like protein SCY1
Gene Name	SCY1
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	804
Subcellular Localization
Protein Description
Protein Sequence	MMFWSSKTGITSKYSFSSSPTFTAEPWSIYTGRPKSSSSSSPSKVSIFMFDKKQFENYLLHYGIIKSKSGSRDKVLIQEAYEILRNQANNLAKLKHPNILTLIEPLEEHSKNFMFVTEFVTSSLETVFRETDDEEQNFLQGHVKDNIVVQRGILQLVNALDFVHNRASFVHLNIQPRAIFINENSDWKISGLGYLVKIPPGTNTSEYFLPQYDPRVPPFMHLQLNYTAPEIVFENTLTFKNDYFSLGLLIYFLYTGKDLFRSENSTSEYKLEYNKFESKISTMSWDNIFSKVPQKLRHCIPKLINRDIYSRYDNITLILDSEFFQDPLVKTLNFLDDLPTKNNEEKYVFLEGLVNLLPEFPPALLQKKFLPILLELLSQFCAEKVVSDKCVGKSLDLIIKIGSTLSQLSFQEKVYPVLLSDANFPVLLKKATICLIDNLDTLKQKVKRSDFLENILKPLFNYVLHDSESDITVVCQEKLLSQIPLALEVLDFPTVKQFLLPLLSNLFTKTTSLTVKNTCVTCFQIMIEHKSIDSYTCSETVLPLFKSMKTRDPRILSKLLKLFETVPLIITDEIVLVDQVLPLMWNYSMASTLTKSQYSGYTKAINKMSSDIQKHHIAKLDDKVNDIGEDAFHKVIEPTIMKKEDPETVAAKNIEVAAMQPVKKKTGSSYGETLPQSKSILNSKPLNPKNALATRGFPTRILNSPPQTPSSRTGSKVMTKGGSNDASSTKVEEEFNEFQSFSSTGSIRQTSAPSDVWMNSTPSPTPTSASSTNLPPGFSISLQPNKRKDGSSDIPRSNVYGSLI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MMFWSSKTGITSK --CCCCCCCCCCCCC	25.49	28889911
8	Phosphorylation	MMFWSSKTGITSKYS CCCCCCCCCCCCCCC	35.45	28889911
37	Phosphorylation	YTGRPKSSSSSSPSK EECCCCCCCCCCCCE	40.12	27214570
312	Phosphorylation	NRDIYSRYDNITLIL CCCHHHHCCCEEEEE	13.85	27214570
321	Phosphorylation	NITLILDSEFFQDPL CEEEEECCHHHCCCH	32.62	27214570
648	Phosphorylation	MKKEDPETVAAKNIE CCCCCHHHHHHCCEE	22.34	28889911
684	Acetylation	SKSILNSKPLNPKNA CHHHHCCCCCCHHHH	53.07	24489116
694	Phosphorylation	NPKNALATRGFPTRI CHHHHHHCCCCCCHH	31.98	21440633
699	Phosphorylation	LATRGFPTRILNSPP HHCCCCCCHHCCCCC	28.25	21440633
704	Phosphorylation	FPTRILNSPPQTPSS CCCHHCCCCCCCCCC	34.22	25533186
708	Phosphorylation	ILNSPPQTPSSRTGS HCCCCCCCCCCCCCC	30.80	28889911
710	Phosphorylation	NSPPQTPSSRTGSKV CCCCCCCCCCCCCCE	35.52	29688323
711	Phosphorylation	SPPQTPSSRTGSKVM CCCCCCCCCCCCCEE	34.76	29734811
740	Phosphorylation	EEFNEFQSFSSTGSI HHHHHHHHCCCCCCC	32.20	30377154
743	Phosphorylation	NEFQSFSSTGSIRQT HHHHHCCCCCCCCCC	34.47	30377154
791	Phosphorylation	PNKRKDGSSDIPRSN CCCCCCCCCCCCHHH	34.66	19823750
792	Phosphorylation	NKRKDGSSDIPRSNV CCCCCCCCCCCHHHC	45.12	19823750
797	Phosphorylation	GSSDIPRSNVYGSLI CCCCCCHHHCCCCCC	25.87	19823750
800	Phosphorylation	DIPRSNVYGSLI--- CCCHHHCCCCCC---	12.78	19823750
802	Phosphorylation	PRSNVYGSLI----- CHHHCCCCCC-----	12.76	24961812

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 SCY1_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of SCY1_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 SCY1_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PP11_YEAST	SIT4	genetic	19269370
DPP1_YEAST	DPP1	genetic	19269370
LSM6_YEAST	LSM6	genetic	19269370
GET2_YEAST	GET2	genetic	19269370
UBP3_YEAST	UBP3	genetic	19269370
CAX4_YEAST	CAX4	genetic	19269370
TCPZ_YEAST	CCT6	physical	21460040
NOB1_YEAST	NOB1	physical	21460040
RBG2_YEAST	RBG2	physical	21460040
SEC2_YEAST	SEC2	physical	21460040
YP12B_YEAST	YPR137C-B	physical	21460040
SLF1_YEAST	SLF1	genetic	25887987

Drug and Disease Associations

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

Regulatory Network of SCY1_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-704 AND SER-791, ANDMASS SPECTROMETRY.	18407956 [Abstract]
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-791, AND MASSSPECTROMETRY.	17563356 [Abstract]
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-704, AND MASSSPECTROMETRY.	15665377 [Abstract]