PBP2_YEAST - dbPTM
PBP2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PBP2_YEAST
UniProt AC P38151
Protein Name PAB1-binding protein 2
Gene Name PBP2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 413
Subcellular Localization Nucleus .
Protein Description
Protein Sequence MSTETTKPSITTTPTTVLVSPNTLKRKKGEDTSEEQLEAEIKRVALKDADSHSDNDHDSPDNVPSDVHLRMLCLVKHASLIVGHKGATISRIKSETSARINISNNIRGVPERIVYVRGTCDDVAKAYGMIVRALLEEHGNEDNGEDIEISINLLIPHHLMGCIIGKRGSRLREIEDLSAAKLFASPNQLLLSNDRILTINGVPDAIHIATFYISQTLLNFQMESPQKNVKRSIYYQPTQFNSVLIDHSQPNTIFHQRNHQYHPSDKLLSYKPNKNLPISSTLLSMATPQYTTASVANATAFQPNFVIPNVTVLDGPVISPAPGNHLLMNFVQQEIFIDEKFVGNVIGKDGKHINSVKESTGCSIIIQDPVEGSSERRLTIRGTFMASQAAIMLISNKIEIDRSNAERKRRSPL
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
12PhosphorylationTTKPSITTTPTTVLV
CCCCCCCCCCCEEEE
29.1624961812
15PhosphorylationPSITTTPTTVLVSPN
CCCCCCCCEEEECCC
27.6921551504
16PhosphorylationSITTTPTTVLVSPNT
CCCCCCCEEEECCCC
17.0424961812
20PhosphorylationTPTTVLVSPNTLKRK
CCCEEEECCCCCCCC
14.3119823750
23PhosphorylationTVLVSPNTLKRKKGE
EEEECCCCCCCCCCC
36.7223607784
33PhosphorylationRKKGEDTSEEQLEAE
CCCCCCCCHHHHHHH
52.0027214570
51PhosphorylationVALKDADSHSDNDHD
HHHHCCCCCCCCCCC
26.9822369663
53PhosphorylationLKDADSHSDNDHDSP
HHCCCCCCCCCCCCC
41.9022369663
59PhosphorylationHSDNDHDSPDNVPSD
CCCCCCCCCCCCCCH
30.6322369663
65PhosphorylationDSPDNVPSDVHLRML
CCCCCCCCHHHHHHH
48.2422369663
90PhosphorylationGHKGATISRIKSETS
CCCCCCEEEECCCCC
24.4928889911
94PhosphorylationATISRIKSETSARIN
CCEEEECCCCCCCEE
43.6728889911
224PhosphorylationLLNFQMESPQKNVKR
HHHCCCCCCCCCCCC
27.5623749301
264PhosphorylationRNHQYHPSDKLLSYK
CCCCCCCCCCCCCCC
33.7827017623

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 PBP2_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PBP2_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 PBP2_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HMO1_YEASTHMO1physical
11805826
EF3A_YEASTYEF3physical
11805826
YRA1_YEASTYRA1physical
11805826
PBP2_YEASTPBP2physical
18719252
GPR1_YEASTGPR1genetic
27708008
GNTK_YEASTYDR248Cgenetic
27708008
YJ24_YEASTKCH1genetic
27708008
FEN1_YEASTRAD27genetic
27708008
RAD14_YEASTRAD14genetic
27708008
PPAL_YEASTLTP1genetic
27708008
ASNS1_YEASTASN1genetic
27708008
QKI_HUMANQKIphysical
27107014
BEND7_HUMANBEND7physical
27107014
NMNA1_HUMANNMNAT1physical
27107014
TRI39_HUMANTRIM39physical
27107014
SNRPA_HUMANSNRPAphysical
27107014
GOGA2_HUMANGOLGA2physical
27107014

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PBP2_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-53 AND SER-224, AND MASSSPECTROMETRY.
"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-51 AND SER-53, AND MASSSPECTROMETRY.

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