LSB1_YEAST - dbPTM
LSB1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LSB1_YEAST
UniProt AC P53281
Protein Name LAS seventeen-binding protein 1
Gene Name LSB1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 241
Subcellular Localization Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, actin patch.
Protein Description Involved in resistance to EDTA..
Protein Sequence MSASLVNRSLKNIRNELEFLKESNVISGDIFELINSKLPEKWDGNQRSPQNADTEEYVEALYDFEAQQDGDLSLKTGDKIQVLEKISPDWYRGKSNNKIGIFPANYVKPAFTRSASPKSAEAASSSTVSRPSVPPPSYEPAASQYPSQQVSAPYAPPAGYMQAPPPQQQQAPLPYPPPFTNYYQQPQQQYAPPSQQAPVEAQPQQSSGASSAFKSFGSKLGNAAIFGAGSAIGSDIVNSIF
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
2Acetylation------MSASLVNRS
------CCHHHHHHH
26.9422814378
2Phosphorylation------MSASLVNRS
------CCHHHHHHH
26.9424961812
4Phosphorylation----MSASLVNRSLK
----CCHHHHHHHHH
26.0824961812
11UbiquitinationSLVNRSLKNIRNELE
HHHHHHHHHHHHHHH
52.1317644757
21UbiquitinationRNELEFLKESNVISG
HHHHHHHHHCCCCCH
65.5017644757
37UbiquitinationIFELINSKLPEKWDG
HHHHHHHCCCCCCCC
64.6724961812
41UbiquitinationINSKLPEKWDGNQRS
HHHCCCCCCCCCCCC
48.9623749301
48PhosphorylationKWDGNQRSPQNADTE
CCCCCCCCCCCCCHH
22.5228889911
54PhosphorylationRSPQNADTEEYVEAL
CCCCCCCHHHHHHHH
28.4528132839
57PhosphorylationQNADTEEYVEALYDF
CCCCHHHHHHHHHCH
9.4321440633
75UbiquitinationQDGDLSLKTGDKIQV
CCCCCCCCCCCEEEE
47.2722817900
79UbiquitinationLSLKTGDKIQVLEKI
CCCCCCCEEEEEEEC
36.0623749301
87PhosphorylationIQVLEKISPDWYRGK
EEEEEECCCCCCCCC
28.0721440633
94UbiquitinationSPDWYRGKSNNKIGI
CCCCCCCCCCCEEEE
40.8022817900
98AcetylationYRGKSNNKIGIFPAN
CCCCCCCEEEEEEHH
46.7024489116
98UbiquitinationYRGKSNNKIGIFPAN
CCCCCCCEEEEEEHH
46.7022817900
106PhosphorylationIGIFPANYVKPAFTR
EEEEEHHHCCCCCCC
16.3822369663
108UbiquitinationIFPANYVKPAFTRSA
EEEHHHCCCCCCCCC
21.9217644757
108AcetylationIFPANYVKPAFTRSA
EEEHHHCCCCCCCCC
21.9224489116
112PhosphorylationNYVKPAFTRSASPKS
HHCCCCCCCCCCHHH
26.3122369663
114PhosphorylationVKPAFTRSASPKSAE
CCCCCCCCCCHHHHH
30.0019823750
116PhosphorylationPAFTRSASPKSAEAA
CCCCCCCCHHHHHHH
33.8219823750
118UbiquitinationFTRSASPKSAEAASS
CCCCCCHHHHHHHCC
60.8622106047
119PhosphorylationTRSASPKSAEAASSS
CCCCCHHHHHHHCCC
34.4228889911
124PhosphorylationPKSAEAASSSTVSRP
HHHHHHHCCCCCCCC
31.6928889911
219UbiquitinationAFKSFGSKLGNAAIF
HHHHHHHHHHCHHHC
61.8722106047

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
-KUbiquitinationE3 ubiquitin ligaseRSP5P39940
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LSB1_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 LSB1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LAS17_YEASTLAS17physical
11743162
APP1_YEASTAPP1physical
11743162
SGF73_YEASTSGF73genetic
18931302
ACBP_YEASTACB1physical
19841731
ENG2_YEASTACF2physical
19841731
SYG2_YEASTGRS2physical
19841731
MCA1_YEASTMCA1physical
19841731
MET31_YEASTMET31physical
19841731
GYP3_YEASTMSB3physical
19841731
LAS17_YEASTLAS17physical
21777813
UBI4P_YEASTUBI4physical
21777813
ERF3_YEASTSUP35physical
21777813
ACT_YEASTACT1physical
21777813
LAS17_YEASTLAS17physical
23577202
PIN3_YEASTPIN3physical
23577202
PIN3_YEASTPIN3genetic
25143386
PIN3_YEASTPIN3physical
25143386
GLE1_YEASTGLE1genetic
27708008
MOB1_YEASTMOB1genetic
27708008
SSL1_YEASTSSL1genetic
27708008
SEC22_YEASTSEC22genetic
27708008
IMB1_YEASTKAP95genetic
27708008
HAS1_YEASTHAS1genetic
27708008
PSB5_YEASTPRE2genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LSB1_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-48, AND MASSSPECTROMETRY.
"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-114 AND SER-116, ANDMASS SPECTROMETRY.
Ubiquitylation
ReferencePubMed
"A subset of membrane-associated proteins is ubiquitinated in responseto mutations in the endoplasmic reticulum degradation machinery.";
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-41 AND LYS-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: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-41 AND LYS-79, AND MASSSPECTROMETRY.

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