LYP1_YEAST - dbPTM
LYP1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LYP1_YEAST
UniProt AC P32487
Protein Name Lysine-specific permease
Gene Name LYP1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 611
Subcellular Localization Membrane
Multi-pass membrane protein.
Protein Description High-affinity permease for lysine..
Protein Sequence MGRFSNIITSNKWDEKQNNIGEQSMQELPEDQIEHEMEAIDPSNKTTPYSIDEKQYNTKKKHGSLQGGAIADVNSITNSLTRLQVVSHETDINEDEEEAHYEDKHVKRALKQRHIGMIALGGTIGTGLFVGISTPLSNAGPVGSLIAYIFMGTIVYFVTQSLGEMATFIPVTSSITVFSKRFLSPAFGVSNGYMYWFNWAITYAVEVSVIGQVIEYWTDKVPLAAWIAIFWVIITLMNFFPVKVYGEFEFWVASVKVLAIMGYLIYALIIVCGGSHQGPIGFRYWRNPGAWGPGIISSDKSEGRFLGWVSSLINAAFTYQGTELVGITAGEAANPRKTVPRAINKVVFRIVLFYIMSLFFIGLLVPYNDSRLSASSAVIASSPFVISIQNAGTYALPDIFNAVVLITVVSAANSNVYVGSRVLYSLARTGNAPKQFGYVTRQGVPYLGVVCTAALGLLAFLVVNNNANTAFNWLINISTLAGLCAWLFISLAHIRFMQALKHRGISRDDLPFKAKLMPYGAYYAAFFVTVIIFIQGFQAFCPFKVSEFFTSYISLILLAVVFIGCQIYYKCRFIWKLEDIDIDSDRREIEAIIWEDDEPKNLWEKFWAAVA
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
5Phosphorylation---MGRFSNIITSNK
---CCCCCCCCCCCC		26.2628889911
9PhosphorylationGRFSNIITSNKWDEK
CCCCCCCCCCCCHHH		23.5819779198
10PhosphorylationRFSNIITSNKWDEKQ
CCCCCCCCCCCHHHH		26.4619779198
12UbiquitinationSNIITSNKWDEKQNN
CCCCCCCCCHHHHCC		56.6523749301
16UbiquitinationTSNKWDEKQNNIGEQ
CCCCCHHHHCCCCHH		56.7223749301
24PhosphorylationQNNIGEQSMQELPED
HCCCCHHHHHHCCHH		20.3820377248
45UbiquitinationEAIDPSNKTTPYSID
HHCCCCCCCCCCCCC		59.1023749301
49PhosphorylationPSNKTTPYSIDEKQY
CCCCCCCCCCCHHHH		19.0324961812
50PhosphorylationSNKTTPYSIDEKQYN
CCCCCCCCCCHHHHC		25.4321440633
54AcetylationTPYSIDEKQYNTKKK
CCCCCCHHHHCCCCC		55.1024489116
54UbiquitinationTPYSIDEKQYNTKKK
CCCCCCHHHHCCCCC		55.1023749301
59UbiquitinationDEKQYNTKKKHGSLQ
CHHHHCCCCCCCCCC		57.0722817900
60UbiquitinationEKQYNTKKKHGSLQG
HHHHCCCCCCCCCCC		48.2224961812
61UbiquitinationKQYNTKKKHGSLQGG
HHHCCCCCCCCCCCC		55.5423749301
64PhosphorylationNTKKKHGSLQGGAIA
CCCCCCCCCCCCCEE		19.7622369663
75PhosphorylationGAIADVNSITNSLTR
CCEECHHHHCCCCHH		30.5522369663
77PhosphorylationIADVNSITNSLTRLQ
EECHHHHCCCCHHEE		20.6922369663
79PhosphorylationDVNSITNSLTRLQVV
CHHHHCCCCHHEEEE		23.5922369663
81PhosphorylationNSITNSLTRLQVVSH
HHHCCCCHHEEEEEE		29.2022369663
87PhosphorylationLTRLQVVSHETDINE
CHHEEEEEEECCCCC		19.4222369663
90PhosphorylationLQVVSHETDINEDEE
EEEEEEECCCCCCHH		36.4322369663
104UbiquitinationEEAHYEDKHVKRALK
HHHHHCHHHHHHHHH		38.0623749301
104AcetylationEEAHYEDKHVKRALK
HHHHHCHHHHHHHHH		38.0624489116
300UbiquitinationPGIISSDKSEGRFLG
CCCCCCCCCCCCHHH		52.9723749301
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 LYP1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LYP1_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 LYP1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DIP5_YEASTDIP5physical
18467557
LYS1_YEASTLYS1genetic
16941010
LYS2_YEASTLYS2genetic
16941010
LYS9_YEASTLYS9genetic
16941010
LYS12_YEASTLYS12genetic
16941010
HOSC_YEASTLYS20genetic
16941010
LYS4_YEASTLYS4genetic
16941010
KMO_YEASTBNA4genetic
16941010
I23O_YEASTBNA2genetic
16941010
KYNU_YEASTBNA5genetic
16941010
HSP72_YEASTSSA2physical
22940862
HSP71_YEASTSSA1physical
22940862
SSB1_YEASTSSB1physical
22940862
VATB_YEASTVMA2physical
22940862
LDB19_YEASTLDB19genetic
23599894
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LYP1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-87 AND THR-90, AND MASSSPECTROMETRY.
"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-75 AND SER-79, AND MASSSPECTROMETRY.
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-90, AND MASSSPECTROMETRY.

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