IPB2_YEAST - dbPTM
IPB2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IPB2_YEAST
UniProt AC P0CT04
Protein Name Protease B inhibitor 2
Gene Name PBI2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 75
Subcellular Localization Cytoplasm .
Protein Description Cytosolic inhibitor of vacuolar proteinase B (yscB), probably regulating protease B activity during limited proteolysis. PBI2 is a component of the LMA1 complex, which is involved in the facilitation of vesicle fusion such as homotypic vacuole and ER-derived COPII vesicle fusion with the Golgi..
Protein Sequence MTKNFIVTLKKNTPDVEAKKFLDSVHHAGGSIVHEFDIIKGYTIKVPDVLHLNKLKEKHNDVIENVEEDKEVHTN
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
10UbiquitinationKNFIVTLKKNTPDVE
CCEEEEECCCCCCHH		34.3122817900
11UbiquitinationNFIVTLKKNTPDVEA
CEEEEECCCCCCHHH		69.9923749301
13PhosphorylationIVTLKKNTPDVEAKK
EEEECCCCCCHHHHH		29.7323749301
20UbiquitinationTPDVEAKKFLDSVHH
CCCHHHHHHHHHHHH		59.2024961812
24PhosphorylationEAKKFLDSVHHAGGS
HHHHHHHHHHHCCCC		26.0422369663
31PhosphorylationSVHHAGGSIVHEFDI
HHHHCCCCEEEEEEE		22.1122369663
45AcetylationIIKGYTIKVPDVLHL
EECCEEEECCCEECH		39.6624489116
54AcetylationPDVLHLNKLKEKHND
CCEECHHHHHHHCCH		68.2624489116
58AcetylationHLNKLKEKHNDVIEN
CHHHHHHHCCHHHHC		46.2324489116
70AcetylationIENVEEDKEVHTN--
HHCHHHHCCCCCC--		65.9924489116
74PhosphorylationEEDKEVHTN------
HHHCCCCCC------		48.0422369663
74PhosphorylationEEDKEVHTN------
HHHCCCCCC------		48.0417330950
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 IPB2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IPB2_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 IPB2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SLX5_YEASTSLX5genetic
27708008
TPS1_YEASTTPS1genetic
27708008
MGR1_YEASTMGR1genetic
27708008
BRE1_YEASTBRE1genetic
27708008
MDHP_YEASTMDH3genetic
27708008
SAC3_YEASTSAC3genetic
27708008
UME6_YEASTUME6genetic
27708008
PEX10_YEASTPEX10genetic
27708008
CYPD_YEASTCPR5genetic
27708008
ASK10_YEASTASK10genetic
27708008
SDS3_YEASTSDS3genetic
27708008
OSM1_YEASTOSM1genetic
27708008
PTK2_YEASTPTK2genetic
27708008
PAM17_YEASTPAM17genetic
27708008
BRE2_YEASTBRE2genetic
27708008
MGR3_YEASTMGR3genetic
27708008
SCS7_YEASTSCS7genetic
27708008
SIN3_YEASTSIN3genetic
27708008
IDH2_YEASTIDH2genetic
27708008
SFL1_YEASTSFL1genetic
27708008
PALA_YEASTRIM20genetic
27708008
MSC6_YEASTMSC6genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IPB2_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 THR-74, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-74, AND MASSSPECTROMETRY.

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