UBP1_YEAST - dbPTM
UBP1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP1_YEAST
UniProt AC P25037
Protein Name Ubiquitin carboxyl-terminal hydrolase 1
Gene Name UBP1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 809
Subcellular Localization
Protein Description Has an ATP-independent isopeptidase activity, cleaving at the C-terminus of the ubiquitin moiety in natural or engineered linear fusion proteins, irrespective of their size or the presence of an N-terminal extension to ubiquitin..
Protein Sequence MDLFIESKINSLLQFLFGSRQDFLRNFKTWSNNNNNLSIYLLIFGIVVFFYKKPDHLNYIVESVSEMTTNFRNNNSLSRWLPRSKFTHLDEEILKRGGFIAGLVNDGNTCFMNSVLQSLASSRELMEFLDNNVIRTYEEIEQNEHNEEGNGQESAQDEATHKKNTRKGGKVYGKHKKKLNRKSSSKEDEEKSQEPDITFSVALRDLLSALNAKYYRDKPYFKTNSLLKAMSKSPRKNILLGYDQEDAQEFFQNILAELESNVKSLNTEKLDTTPVAKSELPDDALVGQLNLGEVGTVYIPTEQIDPNSILHDKSIQNFTPFKLMTPLDGITAERIGCLQCGENGGIRYSVFSGLSLNLPNENIGSTLKLSQLLSDWSKPEIIEGVECNRCALTAAHSHLFGQLKEFEKKPEGSIPEKLINAVKDRVHQIEEVLAKPVIDDEDYKKLHTANMVRKCSKSKQILISRPPPLLSIHINRSVFDPRTYMIRKNNSKVLFKSRLNLAPWCCDINEINLDARLPMSKKEKAAQQDSSEDENIGGEYYTKLHERFEQEFEDSEEEKEYDDAEGNYASHYNHTKDISNYDPLNGEVDGVTSDDEDEYIEETDALGNTIKKRIIEHSDVENENVKDNEELQEIDNVSLDEPKINVEDQLETSSDEEDVIPAPPINYARSFSTVPATPLTYSLRSVIVHYGTHNYGHYIAFRKYRGCWWRISDETVYVVDEAEVLSTPGVFMLFYEYDFDEETGKMKDDLEAIQSNNEEDDEKEQEQKGVQEPKESQEQGEGEEQEEGQEQMKFERTEDHRDISGKDVN
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
76PhosphorylationTNFRNNNSLSRWLPR
HCCCCCCCHHHCCCH		29.8230377154
85AcetylationSRWLPRSKFTHLDEE
HHCCCHHHCCCCCHH		56.4124489116
95UbiquitinationHLDEEILKRGGFIAG
CCCHHHHHCCCCEEE		55.4424961812
95AcetylationHLDEEILKRGGFIAG
CCCHHHHHCCCCEEE		55.4424489116
154PhosphorylationEEGNGQESAQDEATH
CCCCCCCCHHHHHHH		24.2825704821
160PhosphorylationESAQDEATHKKNTRK
CCHHHHHHHHHHCCC		31.9825005228
170AcetylationKNTRKGGKVYGKHKK
HHCCCCCCCCHHHHH		40.7425381059
184PhosphorylationKKLNRKSSSKEDEEK
HHCCCCCCCHHHHHH		48.7628889911
185PhosphorylationKLNRKSSSKEDEEKS
HCCCCCCCHHHHHHH		47.3428889911
213UbiquitinationLLSALNAKYYRDKPY
HHHHHHCHHHCCCCC		41.5624961812
213AcetylationLLSALNAKYYRDKPY
HHHHHHCHHHCCCCC		41.5624489116
269AcetylationVKSLNTEKLDTTPVA
HHHCCCCCCCCCCCC		50.0124489116
272PhosphorylationLNTEKLDTTPVAKSE
CCCCCCCCCCCCCCC		43.3619684113
314PhosphorylationNSILHDKSIQNFTPF
CCCCCCCCCCCCCCC		35.1521440633
378UbiquitinationQLLSDWSKPEIIEGV
HHHCCCCCCHHHCCC		42.2723749301
417AcetylationPEGSIPEKLINAVKD
CCCCCCHHHHHHHHH		49.6824489116
423UbiquitinationEKLINAVKDRVHQIE
HHHHHHHHHHHHHHH		37.0923749301
444AcetylationVIDDEDYKKLHTANM
CCCHHHHHHHHHHHH		62.2724489116
524UbiquitinationLPMSKKEKAAQQDSS
CCCCHHHHHHHCCCC		58.8823749301
530PhosphorylationEKAAQQDSSEDENIG
HHHHHCCCCCCCCCC		31.1522369663
531PhosphorylationKAAQQDSSEDENIGG
HHHHCCCCCCCCCCH		58.3122369663
540PhosphorylationDENIGGEYYTKLHER
CCCCCHHHHHHHHHH		21.5122890988
541PhosphorylationENIGGEYYTKLHERF
CCCCHHHHHHHHHHH		7.9722890988
542PhosphorylationNIGGEYYTKLHERFE
CCCHHHHHHHHHHHH		26.6522890988
555PhosphorylationFEQEFEDSEEEKEYD
HHHHCCCCHHHHCCC		39.4422369663
561PhosphorylationDSEEEKEYDDAEGNY
CCHHHHCCCCCCCCC		30.1429136822
568PhosphorylationYDDAEGNYASHYNHT
CCCCCCCCHHHCCCC		21.9729136822
579PhosphorylationYNHTKDISNYDPLNG
CCCCCCCCCCCCCCC		39.2023749301
581PhosphorylationHTKDISNYDPLNGEV
CCCCCCCCCCCCCCC		16.4922369663
592PhosphorylationNGEVDGVTSDDEDEY
CCCCCCCCCCCHHHH		31.7822369663
593PhosphorylationGEVDGVTSDDEDEYI
CCCCCCCCCCHHHHH		40.4322369663
599PhosphorylationTSDDEDEYIEETDAL
CCCCHHHHHHHHHHC		26.4220377248
603PhosphorylationEDEYIEETDALGNTI
HHHHHHHHHHCCHHH		17.4922369663
609PhosphorylationETDALGNTIKKRIIE
HHHHCCHHHHHHHHH		32.1621440633
618PhosphorylationKKRIIEHSDVENENV
HHHHHHCCCCCCCCC		30.4822369663
638PhosphorylationLQEIDNVSLDEPKIN
HHHHCCCCCCCCCCC		36.0422369663
652PhosphorylationNVEDQLETSSDEEDV
CHHHHCCCCCCCCCC		41.9722369663
653PhosphorylationVEDQLETSSDEEDVI
HHHHCCCCCCCCCCC		26.8122369663
654PhosphorylationEDQLETSSDEEDVIP
HHHCCCCCCCCCCCC		57.3622369663
667PhosphorylationIPAPPINYARSFSTV
CCCCCCCCCCCCCCC		12.2419779198
670PhosphorylationPPINYARSFSTVPAT
CCCCCCCCCCCCCCC		18.5122369663
672PhosphorylationINYARSFSTVPATPL
CCCCCCCCCCCCCCC		29.7322369663
673PhosphorylationNYARSFSTVPATPLT
CCCCCCCCCCCCCCE		28.6222369663
677PhosphorylationSFSTVPATPLTYSLR
CCCCCCCCCCEEEEE		16.8622369663
680PhosphorylationTVPATPLTYSLRSVI
CCCCCCCEEEEEEEE		16.5622369663
681PhosphorylationVPATPLTYSLRSVIV
CCCCCCEEEEEEEEE		17.2522369663
682PhosphorylationPATPLTYSLRSVIVH
CCCCCEEEEEEEEEE		16.4522369663
755PhosphorylationDDLEAIQSNNEEDDE
HHHHHHHHCCCCCHH		35.1922369663
776PhosphorylationGVQEPKESQEQGEGE
HCCCCHHHHCCCCCC		45.1817563356
804PhosphorylationTEDHRDISGKDVN--
CCCCCCCCCCCCC--		44.0427717283
806AcetylationDHRDISGKDVN----
CCCCCCCCCCC----		52.2722865919
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 UBP1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBP1_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 UBP1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RL40A_YEASTRPL40Bphysical
2050695
RL40B_YEASTRPL40Bphysical
2050695
RS31_YEASTRPS31physical
2050695
RL40A_YEASTRPL40Bphysical
1429680
RL40B_YEASTRPL40Bphysical
1429680
RS31_YEASTRPS31physical
1429680
UBP2_YEASTUBP2genetic
1429680
HRQ1_YEASTHRQ1physical
16554755
PRP22_YEASTPRP22physical
16554755
RLM1_YEASTRLM1physical
16554755
MKT1_YEASTMKT1physical
16554755
DEP1_YEASTDEP1genetic
20093466
KMO_YEASTBNA4genetic
20093466
SEC66_YEASTSEC66genetic
20093466
BEM1_YEASTBEM1genetic
20093466
YB75_YEASTYBR225Wgenetic
20093466
STE50_YEASTSTE50genetic
20093466
RV161_YEASTRVS161genetic
20093466
ELO2_YEASTELO2genetic
20093466
THRC_YEASTTHR4genetic
20093466
TPS2_YEASTTPS2genetic
20093466
SWF1_YEASTSWF1genetic
20093466
PMP3_YEASTPMP3genetic
20093466
YPQ2_YEASTYPQ2genetic
20093466
SEM1_YEASTSEM1genetic
20093466
RLA4_YEASTRPP2Bgenetic
20093466
RV167_YEASTRVS167genetic
20093466
FCY2_YEASTFCY2genetic
20093466
IES5_YEASTIES5genetic
20093466
BEM2_YEASTBEM2genetic
20093466
RPOM_YEASTRPO41genetic
20093466
TAN1_YEASTTAN1genetic
20093466
DBP3_YEASTDBP3genetic
20093466
ERV14_YEASTERV14genetic
20093466
PSA3_YEASTPRE9genetic
20093466
BTN2_YEASTBTN2genetic
20093466
CHO2_YEASTCHO2genetic
20093466
PHB2_YEASTPHB2genetic
20093466
ERV29_YEASTERV29genetic
20093466
MAL12_YEASTMAL12genetic
20093466
NPR3_YEASTNPR3genetic
20093466
ATG7_YEASTATG7genetic
20093466
TPM2_YEASTTPM2genetic
20093466
MET28_YEASTMET28genetic
20093466
HS150_YEASTHSP150genetic
20093466
DOHH_YEASTLIA1genetic
20093466
PLMT_YEASTOPI3genetic
20093466
SSH4_YEASTSSH4genetic
20093466
KTI12_YEASTKTI12genetic
20093466
SRN2_YEASTSRN2genetic
20093466
ECI1_YEASTECI1genetic
20093466
VRP1_YEASTVRP1genetic
20093466
ELO3_YEASTELO3genetic
20093466
SRR1L_YEASTBER1genetic
20093466
YL422_YEASTYLR422Wgenetic
20093466
SAM37_YEASTSAM37genetic
20093466
GBLP_YEASTASC1genetic
20093466
PKR1_YEASTPKR1genetic
20093466
YM24_YEASTYMR147Wgenetic
20093466
RAD14_YEASTRAD14genetic
20093466
COA6_YEASTCOA6genetic
20093466
UBP15_YEASTUBP15genetic
20093466
ADE_YEASTAAH1genetic
20093466
YNL5_YEASTYNL115Cgenetic
20093466
EOS1_YEASTEOS1genetic
20093466
VPS27_YEASTVPS27genetic
20093466
MED9_YEASTCSE2genetic
20093466
TM115_YEASTYOL107Wgenetic
20093466
MDM12_YEASTMDM12genetic
20093466
CY1_YEASTCYT1genetic
20093466
NAT5_YEASTNAT5genetic
20093466
ELP4_YEASTELP4genetic
20093466
ECM23_YEASTECM23genetic
20093466
SRO7_YEASTSRO7genetic
20093466
MED1_YEASTMED1genetic
20093466
AXL1_YEASTAXL1genetic
20093466
ATG13_YEASTATG13genetic
20093466
SMF1_YEASTSMF1genetic
15166140
SECU_YEASTPDS1physical
22072716
AP3B_YEASTAPL6genetic
27708008
SSP1_YEASTSSP1genetic
27708008
FIS1_YEASTFIS1genetic
27708008
NNK1_YEASTNNK1genetic
27708008
EOS1_YEASTEOS1genetic
27708008
CND2_YEASTBRN1genetic
27708008
CDS1_YEASTCDS1genetic
27708008
GPI11_YEASTGPI11genetic
27708008
RSC3_YEASTRSC3genetic
27708008
GPI8_YEASTGPI8genetic
27708008
GPI17_YEASTGPI17genetic
27708008
TSC11_YEASTTSC11genetic
27708008
PSB3_YEASTPUP3genetic
27708008
RPN11_YEASTRPN11genetic
27708008
PSB7_YEASTPRE4genetic
27708008
STT3_YEASTSTT3genetic
27708008
SWC4_YEASTSWC4genetic
27708008
SMD1_YEASTSMD1genetic
27708008
GPI16_YEASTGPI16genetic
27708008
SWD2_YEASTSWD2genetic
27708008
PRP19_YEASTPRP19genetic
27708008
SEC22_YEASTSEC22genetic
27708008
TAD3_YEASTTAD3genetic
27708008
CDC91_YEASTGAB1genetic
27708008
ERO1_YEASTERO1genetic
27708008
VTI1_YEASTVTI1genetic
27708008
LCB1_YEASTLCB1genetic
27708008
TOA1_YEASTTOA1genetic
27708008
SEC63_YEASTSEC63genetic
27708008
SEC62_YEASTSEC62genetic
27708008
MED10_YEASTNUT2genetic
27708008
VPS8_YEASTVPS8genetic
27708008
SEC66_YEASTSEC66genetic
27708008
STE50_YEASTSTE50genetic
27708008
RV161_YEASTRVS161genetic
27708008
ELO2_YEASTELO2genetic
27708008
SWF1_YEASTSWF1genetic
27708008
WDR59_YEASTMTC5genetic
27708008
MSC2_YEASTMSC2genetic
27708008
YPQ2_YEASTYPQ2genetic
27708008
SEM1_YEASTSEM1genetic
27708008
RLA4_YEASTRPP2Bgenetic
27708008
RV167_YEASTRVS167genetic
27708008
SAC7_YEASTSAC7genetic
27708008
SDC1_YEASTSDC1genetic
27708008
YD514_YEASTYDR514Cgenetic
27708008
AK_YEASTHOM3genetic
27708008
IES5_YEASTIES5genetic
27708008
YGB5_YEASTYGL015Cgenetic
27708008
DBP3_YEASTDBP3genetic
27708008
ATG1_YEASTATG1genetic
27708008
TAN1_YEASTTAN1genetic
27708008
PSA3_YEASTPRE9genetic
27708008
CHO2_YEASTCHO2genetic
27708008
BUB1_YEASTBUB1genetic
27708008
FHP_YEASTYHB1genetic
27708008
ERV29_YEASTERV29genetic
27708008
NPR3_YEASTNPR3genetic
27708008
ATG7_YEASTATG7genetic
27708008
SPO22_YEASTSPO22genetic
27708008
YIT6_YEASTYIR016Wgenetic
27708008
MET28_YEASTMET28genetic
27708008
DAL81_YEASTDAL81genetic
27708008
VPS53_YEASTVPS53genetic
27708008
BCK1_YEASTBCK1genetic
27708008
HS150_YEASTHSP150genetic
27708008
IXR1_YEASTIXR1genetic
27708008
VPS24_YEASTVPS24genetic
27708008
FABG_YEASTOAR1genetic
27708008
KTI12_YEASTKTI12genetic
27708008
SSH4_YEASTSSH4genetic
27708008
UBI4P_YEASTUBI4genetic
27708008
BRE2_YEASTBRE2genetic
27708008
SRN2_YEASTSRN2genetic
27708008
ARV1_YEASTARV1genetic
27708008
VRP1_YEASTVRP1genetic
27708008
ELO3_YEASTELO3genetic
27708008
YL422_YEASTYLR422Wgenetic
27708008
VPS9_YEASTVPS9genetic
27708008
SAM37_YEASTSAM37genetic
27708008
UBX4_YEASTUBX4genetic
27708008
GBLP_YEASTASC1genetic
27708008
PKR1_YEASTPKR1genetic
27708008
UBP15_YEASTUBP15genetic
27708008
ELP6_YEASTELP6genetic
27708008
SPO1_YEASTSPO1genetic
27708008
YNL5_YEASTYNL115Cgenetic
27708008
ARE2_YEASTARE2genetic
27708008
RTC1_YEASTRTC1genetic
27708008
CY1_YEASTCYT1genetic
27708008
MSA1_YEASTMSA1genetic
27708008
VAM10_YEASTVAM10genetic
27708008
VPS17_YEASTVPS17genetic
27708008
ELP4_YEASTELP4genetic
27708008
FUMH_YEASTFUM1genetic
27708008
HDA3_YEASTHDA3genetic
27708008
ATG13_YEASTATG13genetic
27708008
QCR2_YEASTQCR2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBP1_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-530; SER-531; SER-555;TYR-561; SER-618; SER-638 AND SER-755, 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-618 AND SER-776, ANDMASS SPECTROMETRY.
"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-555 AND SER-618, ANDMASS SPECTROMETRY.
"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-530; SER-531; SER-555;SER-618; SER-638; SER-670 AND SER-755, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672, AND MASSSPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-530 AND SER-531, ANDMASS SPECTROMETRY.

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