PBP1_YEAST - dbPTM
PBP1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PBP1_YEAST
UniProt AC P53297
Protein Name PAB1-binding protein 1
Gene Name PBP1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 722
Subcellular Localization Cytoplasm . Nucleus . Mitochondrion .
Protein Description Appears to promote proper polyadenylation. In the absence of PBP1, the 3'termini of pre-mRNAs are properly cleaved but lack full-length poly(A) tails. May act to repress the ability of PAB1 to negatively regulate polyadenylation. Negative regulator of poly(A) nuclease (PAN) activity..
Protein Sequence MKGNFRKRDSSTNSRKGGNSDSNYTNGGVPNQNNSSMFYENPEITRNFDDRQDYLLANSIGSDVTVTVTSGVKYTGLLVSCNLESTNGIDVVLRFPRVADSGVSDSVDDLAKTLGETLLIHGEDVAELELKNIDLSLDEKWENSKAQETTPARTNIEKERVNGESNEVTKFRTDVDISGSGREIKERKLEKWTPEEGAEHFDINKGKALEDDSASWDQFAVNEKKFGVKSTFDEHLYTTKINKDDPNYSKRLQEAERIAKEIESQGTSGNIHIAEDRGIIIDDSGLDEEDLYSGVDRRGDELLAALKSNSKPNSNKGNRYVPPTLRQQPHHMDPAIISSSNSNKNENAVSTDTSTPAAAGAPEGKPPQKTSKNKKSLSSKEAQIEELKKFSEKFKVPYDIPKDMLEVLKRSSSTLKSNSSLPPKPISKTPSAKTVSPTTQISAGKSESRRSGSNISQGQSSTGHTTRSSTSLRRRNHGSFFGAKNPHTNDAKRVLFGKSFNMFIKSKEAHDEKKKGDDASENMEPFFIEKPYFTAPTWLNTIEESYKTFFPDEDTAIQEAQTRFQQRQLNSMGNAVPGMNPAMGMNMGGMMGFPMGGPSASPNPMMNGFAAGSMGMYMPFQPQPMFYHPSMPQMMPVMGSNGAEEGGGNISPHVPAGFMAAGPGAPMGAFGYPGGIPFQGMMGSGPSGMPANGSAMHSHGHSRNYHQTSHHGHHNSSTSGHK
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
101PhosphorylationRFPRVADSGVSDSVD
ECCCHHCCCCCCCHH		31.2121126336
104PhosphorylationRVADSGVSDSVDDLA
CHHCCCCCCCHHHHH		27.9122890988
106PhosphorylationADSGVSDSVDDLAKT
HCCCCCCCHHHHHHH		21.6822369663
112UbiquitinationDSVDDLAKTLGETLL
CCHHHHHHHHCCEEE		52.1317644757
149PhosphorylationENSKAQETTPARTNI
HCCCCCCCCCCCCHH		26.4621551504
150PhosphorylationNSKAQETTPARTNIE
CCCCCCCCCCCCHHH		17.7525521595
154PhosphorylationQETTPARTNIEKERV
CCCCCCCCHHHHHHH		42.5327717283
165PhosphorylationKERVNGESNEVTKFR
HHHHCCCCCCEEEEE		39.4219779198
169PhosphorylationNGESNEVTKFRTDVD
CCCCCCEEEEEEECC		20.4919779198
170AcetylationGESNEVTKFRTDVDI
CCCCCEEEEEEECCC		37.7222865919
178PhosphorylationFRTDVDISGSGREIK
EEEECCCCCCCHHHH		23.5730377154
180PhosphorylationTDVDISGSGREIKER
EECCCCCCCHHHHHH		28.0830377154
188AcetylationGREIKERKLEKWTPE
CHHHHHHHHHCCCCC		63.1924489116
191UbiquitinationIKERKLEKWTPEEGA
HHHHHHHCCCCCCCC		67.8017644757
191AcetylationIKERKLEKWTPEEGA
HHHHHHHCCCCCCCC		67.8024489116
193PhosphorylationERKLEKWTPEEGAEH
HHHHHCCCCCCCCCC		31.7129136822
205UbiquitinationAEHFDINKGKALEDD
CCCCCCCCCCCCCCC		63.2217644757
205AcetylationAEHFDINKGKALEDD
CCCCCCCCCCCCCCC		63.2224489116
207UbiquitinationHFDINKGKALEDDSA
CCCCCCCCCCCCCCC		51.9417644757
213PhosphorylationGKALEDDSASWDQFA
CCCCCCCCCCHHHHH		36.2022369663
215PhosphorylationALEDDSASWDQFAVN
CCCCCCCCHHHHHHC		34.8322369663
224AcetylationDQFAVNEKKFGVKST
HHHHHCHHHHCCCCC		48.4724489116
224UbiquitinationDQFAVNEKKFGVKST
HHHHHCHHHHCCCCC		48.4717644757
225UbiquitinationQFAVNEKKFGVKSTF
HHHHCHHHHCCCCCC		40.9717644757
229UbiquitinationNEKKFGVKSTFDEHL
CHHHHCCCCCCCCCE		44.1217644757
230PhosphorylationEKKFGVKSTFDEHLY
HHHHCCCCCCCCCEE		31.7229734811
231PhosphorylationKKFGVKSTFDEHLYT
HHHCCCCCCCCCEEE		29.4120377248
240UbiquitinationDEHLYTTKINKDDPN
CCCEEEEECCCCCCC		36.1617644757
243UbiquitinationLYTTKINKDDPNYSK
EEEEECCCCCCCHHH		67.9617644757
243AcetylationLYTTKINKDDPNYSK
EEEEECCCCCCCHHH		67.9625381059
250UbiquitinationKDDPNYSKRLQEAER
CCCCCHHHHHHHHHH		46.9317644757
260AcetylationQEAERIAKEIESQGT
HHHHHHHHHHHHCCC		57.7824489116
284PhosphorylationRGIIIDDSGLDEEDL
CCEEECCCCCCHHHH		37.1929688323
292PhosphorylationGLDEEDLYSGVDRRG
CCCHHHHHCCCCCCH		18.7229688323
344UbiquitinationISSSNSNKNENAVST
HCCCCCCCCCCCCCC		66.5122106047
350PhosphorylationNKNENAVSTDTSTPA
CCCCCCCCCCCCCCH		20.3921551504
351PhosphorylationKNENAVSTDTSTPAA
CCCCCCCCCCCCCHH		36.3821551504
353PhosphorylationENAVSTDTSTPAAAG
CCCCCCCCCCCHHCC		34.2928132839
354PhosphorylationNAVSTDTSTPAAAGA
CCCCCCCCCCHHCCC		34.8922369663
355PhosphorylationAVSTDTSTPAAAGAP
CCCCCCCCCHHCCCC		21.0222369663
379PhosphorylationKNKKSLSSKEAQIEE
CCCCCCCHHHHHHHH		39.5528889911
389AcetylationAQIEELKKFSEKFKV
HHHHHHHHHHHHCCC		67.7424489116
413PhosphorylationEVLKRSSSTLKSNSS
HHHHHCCCCCCCCCC		38.7221440633
416UbiquitinationKRSSSTLKSNSSLPP
HHCCCCCCCCCCCCC		47.9117644757
424UbiquitinationSNSSLPPKPISKTPS
CCCCCCCCCCCCCCC		53.7117644757
428UbiquitinationLPPKPISKTPSAKTV
CCCCCCCCCCCCCEE		66.2417644757
429PhosphorylationPPKPISKTPSAKTVS
CCCCCCCCCCCCEEC		18.7119779198
433AcetylationISKTPSAKTVSPTTQ
CCCCCCCCEECCCCC		54.5223572591
433UbiquitinationISKTPSAKTVSPTTQ
CCCCCCCCEECCCCC		54.5223749301
434PhosphorylationSKTPSAKTVSPTTQI
CCCCCCCEECCCCCC		26.4022890988
436PhosphorylationTPSAKTVSPTTQISA
CCCCCEECCCCCCCC		23.0422369663
438PhosphorylationSAKTVSPTTQISAGK
CCCEECCCCCCCCCC		24.6722890988
439PhosphorylationAKTVSPTTQISAGKS
CCEECCCCCCCCCCC		27.5622890988
442PhosphorylationVSPTTQISAGKSESR
ECCCCCCCCCCCCCC		22.5822890988
445UbiquitinationTTQISAGKSESRRSG
CCCCCCCCCCCCCCC		51.2523749301
451PhosphorylationGKSESRRSGSNISQG
CCCCCCCCCCCCCCC		45.5222369663
453PhosphorylationSESRRSGSNISQGQS
CCCCCCCCCCCCCCC		32.0322369663
456PhosphorylationRRSGSNISQGQSSTG
CCCCCCCCCCCCCCC		32.2922890988
460PhosphorylationSNISQGQSSTGHTTR
CCCCCCCCCCCCCCC		36.3722890988
461PhosphorylationNISQGQSSTGHTTRS
CCCCCCCCCCCCCCC		30.4422890988
462PhosphorylationISQGQSSTGHTTRSS
CCCCCCCCCCCCCCC		37.9222890988
465PhosphorylationGQSSTGHTTRSSTSL
CCCCCCCCCCCCCCC		25.8322890988
466PhosphorylationQSSTGHTTRSSTSLR
CCCCCCCCCCCCCCC		23.9122890988
479PhosphorylationLRRRNHGSFFGAKNP
CCCCCCCCCCCCCCC		15.1728889911
484AcetylationHGSFFGAKNPHTNDA
CCCCCCCCCCCCCHH		71.9722865919
484UbiquitinationHGSFFGAKNPHTNDA
CCCCCCCCCCCCCHH		71.9717644757
492AcetylationNPHTNDAKRVLFGKS
CCCCCHHHHHHHCHH		46.0025381059
498UbiquitinationAKRVLFGKSFNMFIK
HHHHHHCHHHHHHHH		44.5315699485
498AcetylationAKRVLFGKSFNMFIK
HHHHHHCHHHHHHHH		44.5325381059
499PhosphorylationKRVLFGKSFNMFIKS
HHHHHCHHHHHHHHC		23.4121440633
505UbiquitinationKSFNMFIKSKEAHDE
HHHHHHHHCHHHHCH		44.1815699485
507AcetylationFNMFIKSKEAHDEKK
HHHHHHCHHHHCHHH		54.6525381059
520PhosphorylationKKKGDDASENMEPFF
HHCCCCCHHCCCCEE		36.1827717283
547UbiquitinationNTIEESYKTFFPDED
HHHHHHHHHHCCCHH		48.4017644757
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 PBP1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PBP1_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 PBP1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FIR1_YEASTFIR1physical
15121841
UFD1_YEASTUFD1physical
15121841
PBP4_YEASTPBP4physical
15121841
DIG1_YEASTDIG1physical
15121841
PBP1_YEASTPBP1physical
15121841
PBP1_YEASTPBP1physical
15169912
LSM12_YEASTLSM12physical
16429126
RLA0_YEASTRPP0physical
16429126
LSM12_YEASTLSM12physical
11283351
DEF1_YEASTDEF1physical
18467557
PPID_YEASTCPR6physical
18467557
LSM12_YEASTLSM12physical
18467557
EDC3_YEASTEDC3genetic
18408161
LRS4_YEASTLRS4genetic
19061648
LSM1_YEASTLSM1genetic
19061648
LTV1_YEASTLTV1genetic
19061648
NU120_YEASTNUP120genetic
19061648
ELP5_YEASTIKI1genetic
19061648
RIC1_YEASTRIC1genetic
19061648
YPT6_YEASTYPT6genetic
19061648
NU170_YEASTNUP170genetic
19061648
HOS2_YEASTHOS2genetic
19061648
CWC26_YEASTBUD13genetic
19061648
PFD5_YEASTGIM5genetic
19061648
NUP53_YEASTNUP53genetic
19061648
BRR1_YEASTBRR1genetic
19061648
FHL1_YEASTFHL1genetic
19061648
CHD1_YEASTCHD1genetic
19061648
RS8A_YEASTRPS8Agenetic
20093466
RS8B_YEASTRPS8Agenetic
20093466
SKT5_YEASTSKT5genetic
20093466
SNF5_YEASTSNF5genetic
20093466
RV161_YEASTRVS161genetic
20093466
THRC_YEASTTHR4genetic
20093466
RL35A_YEASTRPL35Agenetic
20093466
RL35B_YEASTRPL35Agenetic
20093466
MTU1_YEASTSLM3genetic
20093466
SLX5_YEASTSLX5genetic
20093466
VPS41_YEASTVPS41genetic
20093466
SWF1_YEASTSWF1genetic
20093466
UBP3_YEASTUBP3genetic
20093466
CHD1_YEASTCHD1genetic
20093466
BLM10_YEASTBLM10genetic
20093466
MTO1_YEASTMTO1genetic
20093466
YGY5_YEASTYGL235Wgenetic
20093466
XRN1_YEASTXRN1genetic
20093466
CGR1_YEASTCGR1genetic
20093466
RS27B_YEASTRPS27Bgenetic
20093466
COX23_YEASTCOX23genetic
20093466
PTH_YEASTPTH1genetic
20093466
LHS1_YEASTLHS1genetic
20093466
FRMSR_YEASTYKL069Wgenetic
20093466
IXR1_YEASTIXR1genetic
20093466
NU133_YEASTNUP133genetic
20093466
MDL1_YEASTMDL1genetic
20093466
COA4_YEASTCOA4genetic
20093466
VRP1_YEASTVRP1genetic
20093466
FKS1_YEASTFKS1genetic
20093466
CIK1_YEASTCIK1genetic
20093466
EOS1_YEASTEOS1genetic
20093466
MAS5_YEASTYDJ1genetic
20093466
ATP23_YEASTATP23genetic
20093466
BRE5_YEASTBRE5genetic
20093466
INO4_YEASTINO4genetic
20093466
MDM12_YEASTMDM12genetic
20093466
TOP1_YEASTTOP1genetic
20093466
NCBP2_YEASTCBC2genetic
20093466
YP066_YEASTRGL1genetic
20093466
QCR2_YEASTQCR2genetic
20093466
IGO1_YEASTIGO1physical
20471941
KOG1_YEASTKOG1physical
22727621
TOR1_YEASTTOR1physical
22727621
LSM12_YEASTLSM12physical
23563484
RL12A_YEASTRPL12Bphysical
23563484
RL12B_YEASTRPL12Bphysical
23563484
PSK1_YEASTPSK1genetic
25428989
PSK2_YEASTPSK2genetic
25428989
PIF1_YEASTPIF1genetic
27574117
RNH1_YEASTRNH1genetic
27574117
RNH2A_YEASTRNH201genetic
27574117
PABP_YEASTPAB1physical
25073155
LSM12_YEASTLSM12physical
25073155
PBP4_YEASTPBP4physical
25073155
STM1_YEASTSTM1physical
25073155
YRA1_YEASTYRA1physical
25073155
H4_YEASTHHF1physical
25073155
STM1_YEASTSTM1genetic
25073155
PIF1_YEASTPIF1genetic
25073155
FOB1_YEASTFOB1genetic
25073155
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PBP1_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-106; SER-215; SER-436AND SER-442, AND MASS SPECTROMETRY.
"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-451, 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 SER-106 AND SER-436, ANDMASS SPECTROMETRY.

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