UBP2_YEAST - dbPTM
UBP2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UBP2_YEAST
UniProt AC Q01476
Protein Name Ubiquitin carboxyl-terminal hydrolase 2
Gene Name UBP2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1272
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. Removes ubiquitin chains that initiate proteolysis of FZO1 and inhibit mitochondrial fusion..
Protein Sequence MPNEDNELQKAIENHHNQLLNQDKENADRNGSVIEDLPLYGTSINQQSTPGDVDDGKHLLYPDIATNLPLKTSDRLLDDILCDTIFLNSTDPKVMQKGLQSRGILKESMLSYSTFRSSIRPNCLGSLTDQVVFQTKSEYDSISCPKYNKIHVFQAVIFNPSLAEQQISTFDDIVKIPIYHLKVSVKVRQELERLKKHVGVTQFHSLDHLHEYDRVDLSTFDSSDPNLLDYGIYVSDDTNKLILIEIFKPEFNSPEEHESFTADAIKKRYNAMCVKNESLDKSETPSQVDCFYTLFKIFKGPLTRKSKAEPTKTIDSGNLALNTHLNPEWLTSKYGFQASSEIDEETNEIFTEYVPPDMVDYVNDLETRKIRESFVRKCLQLIFWGQLSTSLLAPNSPLKNTKSVKGMSSLQTSFSTLPWFHLLGESRARILLNSNEQTHSPLDAEPHFINLSVSHYYTDRDIIRNYESLSSLDPENIGLYFDALTYIANRKGAYQLIAYCGKQDIIGQEALENALLMFKINPKECNISELNEATLLSIYKYETSNKSQVTSNHLTNLKNALRLLAKYTKSDKLKFYVDHEPYRALSQAYDTLSIDESVDEDIIKTAYSVKINDSPGLKLDCDRALYTIAISKRSLDLFNFLTEECPQFSNYYGPEKLDYQEALKLLQVNENASDETILKIFKQKWFDENVYEPDQFLILRAALTKISIERNSTLITNFLLTGTIDPNSLPPENWPTGINNIGNTCYLNSLLQYYFSIAPLRRYVLEYQKTVENFNDHLSNSGHIRRIGGREISRGEVERSIQFIYQLRNLFYAMVHTRERCVTPSKELAYLAFAPSNVEVEFEVEGNKVVDQTGVLSDSKKETTDDAFTTKIKDTSLIDLEMEDGLNGDVGTDANRKKNESNDAEVSENEDTTGLTSPTRVAKISSDQLENALEMGRQQDVTECIGNVLFQIESGSEPIRYDEDNEQYDLVKQLFYGTTKQSIVPLSATNKVRTKVERFLSLLINIGDHPKDIYDAFDSYFKDEYLTMEEYGDVIRTVAVTTFPTILQVQIQRVYYDRERLMPFKSIEPLPFKEVIYMDRYADTENPLLLAKKKETEEMKQKLKVMKNRQRELLSRDDSGLTRKDAFLESIKLLESDTIKKTPLKIEAANDVIKTLRNNVQNIDNELMKLYNDINSLEEKISHQFDDFKEYGYSLFSVFIHRGEASYGHYWIYIKDRNRNGIWRKYNDETISEVQEEEVFNFNEGNTATPYFLVYVKQGQEGDIEPLKRILK
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
32PhosphorylationENADRNGSVIEDLPL
CCCCCCCCEECCCCC		24.3820377248
40PhosphorylationVIEDLPLYGTSINQQ
EECCCCCCCCCCCCC		19.2022369663
42PhosphorylationEDLPLYGTSINQQST
CCCCCCCCCCCCCCC		16.9322369663
43PhosphorylationDLPLYGTSINQQSTP
CCCCCCCCCCCCCCC		18.3822369663
48PhosphorylationGTSINQQSTPGDVDD
CCCCCCCCCCCCCCC		27.1422369663
49PhosphorylationTSINQQSTPGDVDDG
CCCCCCCCCCCCCCC		27.2722369663
201PhosphorylationLKKHVGVTQFHSLDH
HHHHHCCCEEECCCC		21.4227017623
313PhosphorylationSKAEPTKTIDSGNLA
CCCCCCCEECCCCEE		32.2820377248
316PhosphorylationEPTKTIDSGNLALNT
CCCCEECCCCEEECC		26.2320377248
574AcetylationYTKSDKLKFYVDHEP
CCCCCCCEEEECCHH		40.1524489116
582PhosphorylationFYVDHEPYRALSQAY
EEECCHHHHHHHHHH		12.9224930733
608PhosphorylationDIIKTAYSVKINDSP
HHHHHHEEEECCCCC		17.9221440633
614PhosphorylationYSVKINDSPGLKLDC
EEEECCCCCCCEEEC		19.1723749301
664UbiquitinationLDYQEALKLLQVNEN
CCHHHHHHHHCCCCC		54.9524961812
857PhosphorylationVDQTGVLSDSKKETT
EECCCCCCCCCCCCC		37.1128889911
859PhosphorylationQTGVLSDSKKETTDD
CCCCCCCCCCCCCCC		42.1021440633
863PhosphorylationLSDSKKETTDDAFTT
CCCCCCCCCCCCCCC		44.3924961812
864PhosphorylationSDSKKETTDDAFTTK
CCCCCCCCCCCCCCC		32.7324961812
869PhosphorylationETTDDAFTTKIKDTS
CCCCCCCCCCCCCCC		28.9724961812
875PhosphorylationFTTKIKDTSLIDLEM
CCCCCCCCCEEEEEC		22.0422369663
876PhosphorylationTTKIKDTSLIDLEME
CCCCCCCCEEEEECC		33.2025521595
901PhosphorylationANRKKNESNDAEVSE
HCHHCCCCCCCCCCC		49.7822369663
907PhosphorylationESNDAEVSENEDTTG
CCCCCCCCCCCCCCC		26.6422369663
912PhosphorylationEVSENEDTTGLTSPT
CCCCCCCCCCCCCCC		19.3125521595
913PhosphorylationVSENEDTTGLTSPTR
CCCCCCCCCCCCCCC		42.3822369663
916PhosphorylationNEDTTGLTSPTRVAK
CCCCCCCCCCCCEEE		33.7220377248
917PhosphorylationEDTTGLTSPTRVAKI
CCCCCCCCCCCEEEC		29.3522369663
919PhosphorylationTTGLTSPTRVAKISS
CCCCCCCCCEEECCH		37.2322369663
923UbiquitinationTSPTRVAKISSDQLE
CCCCCEEECCHHHHH		40.0224961812
980UbiquitinationQLFYGTTKQSIVPLS
HHHCCCCCCCEEECC		41.7223749301
991UbiquitinationVPLSATNKVRTKVER
EECCCCCCHHHHHHH		28.8323749301
1065UbiquitinationRERLMPFKSIEPLPF
HHHCCCCCCCCCCCC		44.6523749301
1081PhosphorylationEVIYMDRYADTENPL
EEEEECCCCCCCCCC		12.4530377154
1104AcetylationEEMKQKLKVMKNRQR
HHHHHHHHHHHHHHH		47.5225381059
1107AcetylationKQKLKVMKNRQRELL
HHHHHHHHHHHHHHH		52.5525381059
1130PhosphorylationRKDAFLESIKLLESD
HHHHHHHHHHHHCCC		27.4628889911
1142PhosphorylationESDTIKKTPLKIEAA
CCCCCCCCCCHHHHH		28.9320377248
1145AcetylationTIKKTPLKIEAANDV
CCCCCCCHHHHHHHH		39.4424489116
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 UBP2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UBP2_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 UBP2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RUP1_YEASTRUP1physical
15933713
RL40A_YEASTRPL40Bphysical
1429680
RL40B_YEASTRPL40Bphysical
1429680
RS31_YEASTRPS31physical
1429680
SPT23_YEASTSPT23physical
15933713
RSP5_YEASTRSP5physical
16554755
PUR4_YEASTADE6physical
16554755
IMB1_YEASTKAP95physical
16554755
CORO_YEASTCRN1physical
16554755
IMA1_YEASTSRP1physical
16554755
RUP1_YEASTRUP1physical
16554755
RSP5_YEASTRSP5physical
16429126
RUP1_YEASTRUP1physical
16429126
CSR2_YEASTCSR2physical
17028178
ECM21_YEASTECM21physical
17028178
MMR1_YEASTMMR1genetic
17314980
CDC73_YEASTCDC73genetic
17314980
YPT6_YEASTYPT6genetic
17314980
INO4_YEASTINO4genetic
17314980
RGP1_YEASTRGP1genetic
17314980
NUP84_YEASTNUP84genetic
17314980
SLX5_YEASTSLX5genetic
17314980
VPS21_YEASTVPS21genetic
17314980
SLX8_YEASTSLX8genetic
17314980
ARD1_YEASTARD1genetic
17314980
RFA2_YEASTRFA2genetic
17314980
PFD2_YEASTGIM4genetic
17314980
SRB8_YEASTSRB8genetic
17314980
RPD3_YEASTRPD3genetic
17314980
ORM2_YEASTORM2genetic
17314980
HUA1_YEASTHUA1physical
11283351
HUA1_YEASTHUA1physical
18719252
RUP1_YEASTRUP1physical
18719252
CSM3_YEASTCSM3physical
18719252
HSP71_YEASTSSA1physical
19536198
SSB1_YEASTSSB1physical
19536198
RSP5_YEASTRSP5physical
19165343
RUP1_YEASTRUP1physical
19165343
RUP1_YEASTRUP1genetic
19165343
MUM2_YEASTMUM2genetic
20093466
UBP14_YEASTUBP14genetic
20093466
PP2C1_YEASTPTC1genetic
20093466
CLG1_YEASTCLG1genetic
20093466
RAV1_YEASTRAV1genetic
20093466
YJ24_YEASTKCH1genetic
20093466
ELF1_YEASTELF1genetic
20093466
COX12_YEASTCOX12genetic
20093466
MMR1_YEASTMMR1genetic
20093466
LIPB_YEASTLIP2genetic
20093466
VPS9_YEASTVPS9genetic
20093466
AF9_YEASTYAF9genetic
20093466
CRZ1_YEASTCRZ1genetic
20093466
COT1_YEASTCOT1genetic
20093466
NEW1_YEASTNEW1genetic
20093466
RUP1_YEASTRUP1physical
20826334
RSP5_YEASTRSP5physical
19920177
RPB1_YEASTRPO21physical
19920177
FIN1_YEASTFIN1physical
22875988
YAP6_YEASTYAP6physical
22875988
MPD2_YEASTMPD2physical
22875988
FZO1_YEASTFZO1physical
23317502
SECU_YEASTPDS1physical
22072716
UBC4_YEASTUBC4physical
24069405
RL40_HUMANUBA52physical
10527495
UBI4P_YEASTUBI4physical
25622294
VPS8_YEASTVPS8genetic
27708008
MUM2_YEASTMUM2genetic
27708008
PP2C1_YEASTPTC1genetic
27708008
VAM6_YEASTVAM6genetic
27708008
INO2_YEASTINO2genetic
27708008
SAC3_YEASTSAC3genetic
27708008
UME6_YEASTUME6genetic
27708008
YFAS1_YEASTYDR262Wgenetic
27708008
RLA4_YEASTRPP2Bgenetic
27708008
VMA21_YEASTVMA21genetic
27708008
RAV1_YEASTRAV1genetic
27708008
YJ24_YEASTKCH1genetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
DBR1_YEASTDBR1genetic
27708008
ELF1_YEASTELF1genetic
27708008
COX12_YEASTCOX12genetic
27708008
RL22A_YEASTRPL22Agenetic
27708008
MMR1_YEASTMMR1genetic
27708008
VPS9_YEASTVPS9genetic
27708008
CRZ1_YEASTCRZ1genetic
27708008
COG6_YEASTCOG6genetic
27708008
AF9_YEASTYAF9genetic
27708008
VPH1_YEASTVPH1genetic
27708008
COT1_YEASTCOT1genetic
27708008
ELP3_YEASTELP3genetic
27708008
MDM30_YEASTMDM30genetic
29309037
CDC48_YEASTCDC48physical
29309037
UBP15_YEASTUBP15genetic
28298493
UBP4_YEASTDOA4genetic
28298493
UBP3_YEASTUBP3genetic
28298493
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UBP2_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-875; SER-876 ANDSER-907, 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 THR-875 AND SER-907, 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-907, AND MASSSPECTROMETRY.

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