PBP4_YEAST - dbPTM
PBP4_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PBP4_YEAST
UniProt AC Q07362
Protein Name Protein PBP4
Gene Name PBP4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 185
Subcellular Localization Cytoplasm . Nucleus .
Protein Description
Protein Sequence MTTTSTTSVDGRTSSTLKATLSASGPNSNGPTPAVLPQKPKLTGWAQAAAKALPRQQQQQQQARKDDSVAVQPANTKTKTIASTAPPANIKGSSTANGSSTNKKFKRANKQPYNREEVRSYMHKLFQSYTAGEKSHSMKTYKQVLSETASGRVSTATDWGTVSSSKNKNKKYGCLSDIAKVLRNQ
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
2Phosphorylation------MTTTSTTSV
------CCCCEEEEE
38.4922369663
3Phosphorylation-----MTTTSTTSVD
-----CCCCEEEEEC
19.9022369663
4Phosphorylation----MTTTSTTSVDG
----CCCCEEEEECC
18.2122369663
5Phosphorylation---MTTTSTTSVDGR
---CCCCEEEEECCC
27.8222369663
6Phosphorylation--MTTTSTTSVDGRT
--CCCCEEEEECCCC
22.4622369663
7Phosphorylation-MTTTSTTSVDGRTS
-CCCCEEEEECCCCC
26.9022369663
8PhosphorylationMTTTSTTSVDGRTSS
CCCCEEEEECCCCCC
20.4922369663
13PhosphorylationTTSVDGRTSSTLKAT
EEEECCCCCCEEEEE
32.3424961812
14PhosphorylationTSVDGRTSSTLKATL
EEECCCCCCEEEEEE
21.6917563356
15PhosphorylationSVDGRTSSTLKATLS
EECCCCCCEEEEEEC
36.8324961812
16PhosphorylationVDGRTSSTLKATLSA
ECCCCCCEEEEEECC
31.8524961812
20PhosphorylationTSSTLKATLSASGPN
CCCEEEEEECCCCCC
21.4723749301
22PhosphorylationSTLKATLSASGPNSN
CEEEEEECCCCCCCC
18.9429136822
24PhosphorylationLKATLSASGPNSNGP
EEEEECCCCCCCCCC
51.9429136822
28PhosphorylationLSASGPNSNGPTPAV
ECCCCCCCCCCCCCC
46.4221440633
32PhosphorylationGPNSNGPTPAVLPQK
CCCCCCCCCCCCCCC
25.8629136822
39AcetylationTPAVLPQKPKLTGWA
CCCCCCCCCCCCHHH
42.0324489116
51AcetylationGWAQAAAKALPRQQQ
HHHHHHHHHCHHHHH
45.8124489116
68PhosphorylationQQARKDDSVAVQPAN
HHHHHCCCEEEECCC
23.3130377154
80PhosphorylationPANTKTKTIASTAPP
CCCCCCCEEECCCCC
27.3229136822
83PhosphorylationTKTKTIASTAPPANI
CCCCEEECCCCCCCC
22.6629136822
84PhosphorylationKTKTIASTAPPANIK
CCCEEECCCCCCCCC
33.8729136822
93PhosphorylationPPANIKGSSTANGSS
CCCCCCCCCCCCCCC
21.3629136822
94PhosphorylationPANIKGSSTANGSST
CCCCCCCCCCCCCCC
39.9629136822
95PhosphorylationANIKGSSTANGSSTN
CCCCCCCCCCCCCCH
26.3229136822
99PhosphorylationGSSTANGSSTNKKFK
CCCCCCCCCCHHHHH
33.5229136822
100PhosphorylationSSTANGSSTNKKFKR
CCCCCCCCCHHHHHH
37.0829136822
101PhosphorylationSTANGSSTNKKFKRA
CCCCCCCCHHHHHHH
53.4029136822
124AcetylationEVRSYMHKLFQSYTA
HHHHHHHHHHHHHCC
34.1724489116
134AcetylationQSYTAGEKSHSMKTY
HHHCCCCCCCCHHHH
53.1824489116
142AcetylationSHSMKTYKQVLSETA
CCCHHHHHHHHHHHC
38.8824489116
146PhosphorylationKTYKQVLSETASGRV
HHHHHHHHHHCCCCC
33.7629688323
148PhosphorylationYKQVLSETASGRVST
HHHHHHHHCCCCCEE
23.8130377154
150PhosphorylationQVLSETASGRVSTAT
HHHHHHCCCCCEECC
34.2524909858
154PhosphorylationETASGRVSTATDWGT
HHCCCCCEECCCCCC
15.8029688323
155PhosphorylationTASGRVSTATDWGTV
HCCCCCEECCCCCCC
30.6227017623
157PhosphorylationSGRVSTATDWGTVSS
CCCCEECCCCCCCCC
32.1627017623
161PhosphorylationSTATDWGTVSSSKNK
EECCCCCCCCCCCCC
16.9827017623
163PhosphorylationATDWGTVSSSKNKNK
CCCCCCCCCCCCCCC
28.8230377154
164PhosphorylationTDWGTVSSSKNKNKK
CCCCCCCCCCCCCCC
40.7827017623
165PhosphorylationDWGTVSSSKNKNKKY
CCCCCCCCCCCCCCE
32.5129688323
180AcetylationGCLSDIAKVLRNQ--
ECHHHHHHHHHCC--
41.9824489116

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 PBP4_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PBP4_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 PBP4_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LSM12_YEASTLSM12physical
16554755
LSM12_YEASTLSM12physical
16702403
PBP1_YEASTPBP1physical
16702403
SUS1_YEASTSUS1genetic
17314980
SNF5_YEASTSNF5genetic
17314980
EDC3_YEASTEDC3genetic
18408161
PBP1_YEASTPBP1physical
18719252
VID30_YEASTVID30genetic
18408161
IGO1_YEASTIGO1physical
20471941
MRM2_YEASTMRM2genetic
27708008
YHI2_YEASTYHR022Cgenetic
27708008
GRE2_YEASTGRE2genetic
27708008
ARO1_YEASTARO1genetic
27708008
YSP2_YEASTYSP2genetic
27708008
MSH4_YEASTMSH4genetic
27708008
RL24A_YEASTRPL24Agenetic
27708008
YG036_YEASTYGL036Wgenetic
27708008
YG4I_YEASTYGR210Cgenetic
27708008
ERC1_YEASTERC1genetic
27708008
PIH1_YEASTPIH1genetic
27708008
MED20_YEASTSRB2genetic
27708008
DSE2_YEASTDSE2genetic
27708008
MNT3_YEASTMNT3genetic
27708008
YIC9_YEASTYIL029Cgenetic
27708008
VHR1_YEASTVHR1genetic
27708008
RPA34_YEASTRPA34genetic
27708008
MSN4_YEASTMSN4genetic
27708008
PRY2_YEASTPRY2genetic
27708008
DBP7_YEASTDBP7genetic
27708008
UBR2_YEASTUBR2genetic
27708008
SPO1_YEASTSPO1genetic
27708008
PUB1_YEASTPUB1genetic
27708008
RNH2A_YEASTRNH201genetic
27708008
APP1_YEASTAPP1genetic
27708008
NRK1_YEASTNRK1genetic
27708008
NTH2_YEASTNTG2genetic
27708008
HMI1_YEASTHMI1genetic
27708008
PT127_YEASTPET127genetic
27708008
MTHR1_YEASTMET12genetic
27708008
AP1G1_YEASTAPL4genetic
27708008
LSM12_YEASTLSM12physical
25073155
PBP1_YEASTPBP1physical
25073155
PABP_YEASTPAB1physical
25073155
YRA1_YEASTYRA1physical
25073155

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PBP4_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-2; SER-5 AND SER-14, ANDMASS SPECTROMETRY.

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