ETP1_YEAST - dbPTM
ETP1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ETP1_YEAST
UniProt AC P38748
Protein Name RING finger protein ETP1
Gene Name ETP1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 585
Subcellular Localization Cytoplasm.
Protein Description May act as a cytoplasmic retention protein with a role in regulating nuclear transport. Binds nuclear localization sequences in vitro. Needed to adapt efficiently to ethanol, either as sole carbon source or as cell stressor. Involved in ethanol-dependent transcriptional activation of several genes and ethanol-induced protein turnover of some proteins..
Protein Sequence MDQFEYIITLEFGNQNQVESAYQIFKSIPKKLKAKSIGEESIKSNNQDWQDWRVCDLEIDMITDFKNQTSKEEESDLITSQYLGHGIIRLFKLSNANNTLNEKEILTIPGDDTMICILFVPTYFTVHDLLHFYIGDDIVNKQVSNFRILRNQQKGMGFNFTVLIKFRNALDAKNFKEEFNGKSFSRMDPETCHVISVKEIVFQKKLFQRPAANEDFPYLLTDPFTVKKKKELVKVELPTCPVCLERMDSETTGLVTIPCQHTFHCQCLNKWKNSRCPVCRHSSLRLSRESLLKQAGDSAHCATCGSTDNLWICLICGNVGCGRYNSKHAIKHYEETLHCFAMDIRTQRVWDYAGDNYVHRLVQNEVDGKLVEVGGSGDDDNNDIGNSDELQNVVYGNRSKNGEKSNSNKKDGELAANFLRHREYHLEYVQVLISQLESQREYYELKLQEKDQTASDSSNVESLKKSMEDLKLQFQVTQKEWQKREMAQKSKLEEDMLVIEGLQANLDHLSKKQEQLERENKALEESKQDLEEQVKDLMFYLDSQEKFKDADESVKEGTILIQQPHGAAQASKSKKKRNKNKKAGK
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
36PhosphorylationPKKLKAKSIGEESIK
CHHHCCCCCCHHHHH		40.4623749301
43UbiquitinationSIGEESIKSNNQDWQ
CCCHHHHHHCCCCHH		57.3123749301
66UbiquitinationIDMITDFKNQTSKEE
EEEEECCCCCCCHHH		51.4617644757
71UbiquitinationDFKNQTSKEEESDLI
CCCCCCCHHHHHHHH		72.9617644757
198UbiquitinationTCHVISVKEIVFQKK
HCEEEEEEHHHHCHH		34.6317644757
204UbiquitinationVKEIVFQKKLFQRPA
EEHHHHCHHHHCCCC		39.7217644757
205UbiquitinationKEIVFQKKLFQRPAA
EHHHHCHHHHCCCCC		43.6917644757
227UbiquitinationLTDPFTVKKKKELVK
CCCCCCCCCCHHHEE		56.6817644757
228UbiquitinationTDPFTVKKKKELVKV
CCCCCCCCCHHHEEE		65.8217644757
229UbiquitinationDPFTVKKKKELVKVE
CCCCCCCCHHHEEEE		45.8417644757
230UbiquitinationPFTVKKKKELVKVEL
CCCCCCCHHHEEEEC		66.2217644757
234UbiquitinationKKKKELVKVELPTCP
CCCHHHEEEECCCCC		42.4917644757
270UbiquitinationFHCQCLNKWKNSRCP
EECCCCCCCCCCCCC		46.7417644757
369UbiquitinationVQNEVDGKLVEVGGS
HHCCCCCCEEEECCC		44.9123749301
376PhosphorylationKLVEVGGSGDDDNND
CEEEECCCCCCCCCC		32.8720377248
409UbiquitinationGEKSNSNKKDGELAA
CCCCCCCCCCHHHHH		52.6524961812
410UbiquitinationEKSNSNKKDGELAAN
CCCCCCCCCHHHHHH		75.1923749301
446UbiquitinationQREYYELKLQEKDQT
HHHHHHEEHHHCCCC		35.8617644757
450UbiquitinationYELKLQEKDQTASDS
HHEEHHHCCCCCCCC		42.0223749301
464UbiquitinationSSNVESLKKSMEDLK
CCCHHHHHHHHHHHH		52.6717644757
465UbiquitinationSNVESLKKSMEDLKL
CCHHHHHHHHHHHHH		61.4017644757
489UbiquitinationQKREMAQKSKLEEDM
HHHHHHHHCCCHHHH		39.7717644757
491UbiquitinationREMAQKSKLEEDMLV
HHHHHHCCCHHHHHH		67.9417644757
511UbiquitinationANLDHLSKKQEQLER
HHHHHHHHHHHHHHH		65.9117644757
512UbiquitinationNLDHLSKKQEQLERE
HHHHHHHHHHHHHHH		56.5417644757
527UbiquitinationNKALEESKQDLEEQV
HHHHHHHHHHHHHHH		51.6223749301
540PhosphorylationQVKDLMFYLDSQEKF
HHHHHHHHHCCHHHH		8.8127017623
543PhosphorylationDLMFYLDSQEKFKDA
HHHHHHCCHHHHCCC		37.3327017623
546UbiquitinationFYLDSQEKFKDADES
HHHCCHHHHCCCCHH		50.5017644757
548UbiquitinationLDSQEKFKDADESVK
HCCHHHHCCCCHHHH		64.1717644757
555UbiquitinationKDADESVKEGTILIQ
CCCCHHHHCCCEEEE		60.7617644757
572UbiquitinationHGAAQASKSKKKRNK
CHHHHHHHHHHHHHC		70.1217644757
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 ETP1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ETP1_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 ETP1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NAH1_YEASTNHA1physical
11805837
HEL1_YEASTHEL1physical
11805837
MOH1_YEASTMOH1physical
11805837
NNF2_YEASTNNF2physical
11087867
ETP1_YEASTETP1physical
11967834
NAH1_YEASTNHA1genetic
19416103
NRG1_YEASTNRG1genetic
19416103
SPC72_YEASTSPC72physical
22875988
HSP73_YEASTSSA3physical
22875988
ARE1_YEASTARE1physical
22875988
NHP10_YEASTNHP10physical
22875988
SIR4_YEASTSIR4physical
22875988
HSP78_YEASTHSP78physical
22875988
SPC25_YEASTSPC25physical
22875988
TSC11_YEASTTSC11physical
22875988
FMP32_YEASTFMP32physical
22875988
NIC96_YEASTNIC96physical
22875988
SEC9_YEASTSEC9physical
22875988
SPR3_YEASTSPR3physical
22875988
ETP1_YEASTETP1physical
22875988
SKN7_YEASTSKN7physical
22875988
YJE9_YEASTYJL049Wphysical
22875988
NNF1_YEASTNNF1physical
22875988
SGM1_YEASTSGM1physical
22875988
LHS1_YEASTLHS1physical
22875988
NTR2_YEASTNTR2physical
22875988
DID2_YEASTDID2physical
22875988
FAR10_YEASTFAR10physical
22875988
AP1_YEASTYAP1physical
22875988
RNA1_YEASTRNA1physical
22875988
NST1_YEASTNST1physical
22875988
ULP1_YEASTULP1physical
22875988
RLF2_YEASTRLF2physical
22875988
KAR3_YEASTKAR3physical
22875988
YAP8_YEASTARR1physical
22875988
UBI4P_YEASTUBI4physical
16564012
PP2C4_YEASTPTC4genetic
27708008
SEC66_YEASTSEC66genetic
27708008
FTR1_YEASTFTR1genetic
27708008
MSP1_YEASTMSP1genetic
27708008
MNN11_YEASTMNN11genetic
27708008
YKE44_YEASTYKL044Wgenetic
27708008
RIC1_YEASTRIC1genetic
27708008
AIM34_YEASTAIM34genetic
27708008
PFKA2_YEASTPFK2genetic
27708008
ZRC1_YEASTZRC1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ETP1_YEAST

loading...

Related Literatures of Post-Translational Modification
Ubiquitylation
ReferencePubMed
"A subset of membrane-associated proteins is ubiquitinated in responseto mutations in the endoplasmic reticulum degradation machinery.";
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-410, AND MASSSPECTROMETRY.
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-369 AND LYS-410, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory