UTP23_YEAST - dbPTM
UTP23_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UTP23_YEAST
UniProt AC Q12339
Protein Name rRNA-processing protein UTP23
Gene Name UTP23
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 254
Subcellular Localization Mitochondrion . Nucleus, nucleolus .
Protein Description Involved in rRNA-processing and ribosome biogenesis..
Protein Sequence MRQKRAKSYRKQLLVYSHTFKFREPYQVLVDNQLVLECNNSNFNLPSGLKRTLQADVKVMITQCCIQALYETRNDGAINLAKQFERRRCNHSFKDPKSPAECIESVVNISGANKHRYVVASQDIDLRRKLRTVPGVPLIHLTRSVMVMEPLSTASAKASKITEEQKLYKGLNDPNIEKLQESGDGSGKESITKKRKLGPKAPNPLSVKKKKKVNSPSDEVKDKEDTSKEKKKRRRRKHKSNTNVPVSNGTTAAQ
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
82AcetylationDGAINLAKQFERRRC
CCHHHHHHHHHHHHC		59.7024489116
117PhosphorylationSGANKHRYVVASQDI
CCCCCCCEEEECCCH		10.0527017623
144PhosphorylationPLIHLTRSVMVMEPL
EEEEEECCEEECCCC		14.8827017623
152PhosphorylationVMVMEPLSTASAKAS
EEECCCCCCCCHHHH		32.4227017623
178AcetylationLNDPNIEKLQESGDG
CCCCCHHHHHHHCCC		52.2322865919
182PhosphorylationNIEKLQESGDGSGKE
CHHHHHHHCCCCCCH		29.2628889911
186PhosphorylationLQESGDGSGKESITK
HHHHCCCCCCHHHCC		51.9723749301
188AcetylationESGDGSGKESITKKR
HHCCCCCCHHHCCCH		50.4125381059
190PhosphorylationGDGSGKESITKKRKL
CCCCCCHHHCCCHHC		38.7627017623
192PhosphorylationGSGKESITKKRKLGP
CCCCHHHCCCHHCCC		39.5327017623
215PhosphorylationKKKKKVNSPSDEVKD
CCCCCCCCCCHHCCC		28.8625521595
217PhosphorylationKKKVNSPSDEVKDKE
CCCCCCCCHHCCCHH		46.3427214570
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 UTP23_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UTP23_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 UTP23_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UTP23_YEASTUTP23physical
24152547
COPA_YEASTCOP1genetic
27708008
SLX5_YEASTSLX5genetic
27708008
OCA5_YEASTOCA5genetic
27708008
SRO7_YEASTSRO7genetic
27708008
NHP2_YEASTNHP2genetic
27708008
RRP1_YEASTRRP1genetic
27708008
CDC1_YEASTCDC1genetic
27708008
TCPZ_YEASTCCT6genetic
27708008
GPI11_YEASTGPI11genetic
27708008
UTP5_YEASTUTP5genetic
27708008
ACT_YEASTACT1genetic
27708008
UTP9_YEASTUTP9genetic
27708008
MET30_YEASTMET30genetic
27708008
SHQ1_YEASTSHQ1genetic
27708008
DCA13_YEASTSOF1genetic
27708008
NEP1_YEASTEMG1genetic
27708008
RRP5_YEASTRRP5genetic
27708008
RPC6_YEASTRPC34genetic
27708008
ASA1_YEASTASA1genetic
27708008
PFF1_YEASTPFF1genetic
27708008
SNT1_YEASTSNT1genetic
27708008
BUD31_YEASTBUD31genetic
27708008
TPS2_YEASTTPS2genetic
27708008
DAL81_YEASTDAL81genetic
27708008
YJQ3_YEASTYJL163Cgenetic
27708008
IMDH4_YEASTIMD4genetic
27708008
MBF1_YEASTMBF1genetic
27708008
THP3_YEASTTHP3genetic
27708008
UBA3_YEASTUBA3genetic
27708008
KAR3_YEASTKAR3genetic
27708008
AQY1_YEASTAQY1genetic
27708008
UTP23_YEASTUTP23physical
28082392
ROK1_YEASTROK1physical
28082392
FCF1_YEASTFCF1physical
28082392
RRP7_YEASTRRP7physical
28082392
KRI1_YEASTKRI1physical
28082392
NHP2_YEASTNHP2physical
28082392
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UTP23_YEAST

loading...

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-182 AND SER-215, ANDMASS SPECTROMETRY.

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