UIP3_YEAST - dbPTM
UIP3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UIP3_YEAST
UniProt AC P39547
Protein Name ULP1-interacting protein 3
Gene Name UIP3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 235
Subcellular Localization Nucleus membrane
Multi-pass membrane protein . Cell membrane
Multi-pass membrane protein .
Protein Description
Protein Sequence MQTPSENTDVKLDTLDEPSAHLIEENVALPEDTFNSYWSYILNEIARCKPLMIMFLIPVCLVLLITFFHDIKGILVFLVISLILSIIILLIGITAFVSETLNKGFIIKLLVEVITRKPAVGGKEWRIIAYNMNQYLFDHGIWHTPYYFFCEHRCHKFFKSLIKQTRSNAHLSSPTNGAENTQSNTPAKEVSNEMVKPYIFSSDPVLEAYLIKAAEIHKEAEFEYWRKQYPEVDLP
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
3Phosphorylation-----MQTPSENTDV
-----CCCCCCCCCC
27.7325752575
5Phosphorylation---MQTPSENTDVKL
---CCCCCCCCCCCC
47.0328889911
8PhosphorylationMQTPSENTDVKLDTL
CCCCCCCCCCCCCCC
37.8127717283
11UbiquitinationPSENTDVKLDTLDEP
CCCCCCCCCCCCCCC
43.3812872131
167PhosphorylationSLIKQTRSNAHLSSP
HHHHHHHHCCCCCCC
41.5821440633
173PhosphorylationRSNAHLSSPTNGAEN
HHCCCCCCCCCCCCC
41.9523749301
188UbiquitinationTQSNTPAKEVSNEMV
CCCCCCHHHHCHHHC
60.9124961812
218UbiquitinationIKAAEIHKEAEFEYW
HHHHHHHHHHHHHHH
65.3723749301
227UbiquitinationAEFEYWRKQYPEVDL
HHHHHHHHHCCCCCC
39.7823749301

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 UIP3_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UIP3_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 UIP3_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UIP3_YEASTUIP3physical
18719252
PMT2_YEASTPMT2physical
16093310
PHO88_YEASTPHO88physical
16093310
MKAR_YEASTIFA38physical
16093310
GEX1_YEASTGEX1physical
16093310
GGC1_YEASTGGC1physical
16093310
PDR15_YEASTPDR15physical
16093310
YEF1_YEASTYEF1physical
16093310
RT23_YEASTRSM23physical
16093310
MSB2_YEASTMSB2physical
16093310
ERV29_YEASTERV29physical
16093310
YHK8_YEASTYHK8physical
16093310
BET1_YEASTBET1physical
16093310
SNL1_YEASTSNL1physical
16093310
COX5B_YEASTCOX5Bphysical
16093310
MGA2_YEASTMGA2physical
16093310
OST1_YEASTOST1physical
16093310
TOK1_YEASTTOK1physical
16093310
GEF1_YEASTGEF1physical
16093310
YKT6_YEASTYKT6physical
16093310
VBA5_YEASTVBA5physical
16093310
U5072_YEASTYML002Wphysical
16093310
YMD8_YEASTYMD8physical
16093310
OSTD_YEASTSWP1physical
16093310
CUE1_YEASTCUE1physical
16093310
YM8M_YEASTYMR279Cphysical
16093310
ESBP6_YEASTESBP6physical
16093310
GAS5_YEASTGAS5physical
16093310
HXT11_YEASTHXT11physical
16093310
TPO4_YEASTTPO4physical
16093310
SEC62_YEASTSEC62physical
16093310
ANT1_YEASTANT1physical
16093310
UIP3_YEASTUIP3physical
16093310
HSP71_YEASTSSA1physical
22940862
TR130_YEASTTRS130genetic
23891562
MKK2_YEASTMKK2genetic
23891562
COAD_YEASTCAB4genetic
27708008
DPOA2_YEASTPOL12genetic
27708008
TAF6_YEASTTAF6genetic
27708008
PRP18_YEASTPRP18genetic
27708008
ORC6_YEASTORC6genetic
27708008
CYAA_YEASTCYR1genetic
27708008
TAD3_YEASTTAD3genetic
27708008
POB3_YEASTPOB3genetic
27708008
MCM1_YEASTMCM1genetic
27708008
SEC23_YEASTSEC23genetic
27708008
TMM79_HUMANTMEM79physical
27107014

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UIP3_YEAST

loading...

Related Literatures of Post-Translational Modification
Ubiquitylation
ReferencePubMed
"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: PROTEIN SEQUENCE OF 1-21 AND 213-226, MASS SPECTROMETRY, ANDUBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-11 AND LYS-218.

TOP