UTP5_YEAST - dbPTM
UTP5_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UTP5_YEAST
UniProt AC Q04177
Protein Name U3 small nucleolar RNA-associated protein 5
Gene Name UTP5
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 643
Subcellular Localization Nucleus, nucleolus . Associated with ribosomal chromatin, even in the absence of transcription.
Protein Description Involved in nucleolar processing of pre-18S ribosomal RNA. Required for optimal pre-ribosomal RNA transcription by RNA polymerase I together with a subset of U3 proteins required for transcription (t-UTPs)..
Protein Sequence MDSPVLQSAYDPSGQYLCYVTVALDKQRVGVQPTQRATSSGVDTVWNENFLYLEDSKLKVTCLKWVNLASSDTVAIILGMNNGEIWLYSVLANEVTYKFTTGNSYEIKDIDLMGNQLWCIDSSDAFYQFDLLQFKLLQHFRINNCVQLNKLTIVPAGDSVAQLLVASHSISLIDIEEKKVVMTFPGHVSPVSTLQVITNEFFISGAEGDRFLNVYDIHSGMTKCVLVAESDIKELSHSGQADSIAVTTEDGSLEIFVDPLVSSSTKKRGNKSKKSSKKIQIVSKDGRKVPIYNAFINKDLLNVSWLQNATMPYFKNLQWREIPNEYTVEISLNWNNKNKSADRDLHGKDLASATNYVEGNARVTSGDNFKHVDDAIKSWERELTSLEQEQAKPPQANELLTETFGDKLESSTVARISGKKTNLKGSNLKTATTTGTVTVILSQALQSNDHSLLETVLNNRDERVIRDTIFRLKPALAVILLERLAERIARQTHRQGPLNVWVKWCLIIHGGYLVSIPNLMSTLSSLHSTLKRRSDLLPRLLALDARLDCTINKFKTLNYEAGDIHSSEPVVEEDEDDVEYNEELDDAGLIEDGEESYGSEEEEEGDSDNEEEQKHTSSKQDGRLETEQSDGEEEAGYSDVEME
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
16PhosphorylationAYDPSGQYLCYVTVA
CCCCCCCEEEEEEEE		11.4128889911
348AcetylationADRDLHGKDLASATN
CCCCCCCCHHHHHCC		38.5322865919
352PhosphorylationLHGKDLASATNYVEG
CCCCHHHHHCCCEEC		42.8128889911
354PhosphorylationGKDLASATNYVEGNA
CCHHHHHCCCEECCE		25.2930377154
364PhosphorylationVEGNARVTSGDNFKH
EECCEEECCCCCCCC		22.8020377248
365PhosphorylationEGNARVTSGDNFKHV
ECCEEECCCCCCCCH		41.0921440633
370AcetylationVTSGDNFKHVDDAIK
ECCCCCCCCHHHHHH		49.3124489116
384PhosphorylationKSWERELTSLEQEQA
HHHHHHHHHHHHHHC		26.8927214570
426PhosphorylationKKTNLKGSNLKTATT
CCCCCCCCCCCCCCC		37.0830377154
553AcetylationRLDCTINKFKTLNYE
HCCCEECCCCCCCCC		44.3724489116
626PhosphorylationKQDGRLETEQSDGEE
CCCCCEEECCCCCCC		43.8722890988
629PhosphorylationGRLETEQSDGEEEAG
CCEEECCCCCCCCCC		41.1522369663
637PhosphorylationDGEEEAGYSDVEME-
CCCCCCCCCCCCCC-		14.5622890988
638PhosphorylationGEEEAGYSDVEME--
CCCCCCCCCCCCC--		33.9722369663
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 UTP5_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UTP5_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 UTP5_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PRS10_YEASTRPT4physical
11805837
PPID_YEASTCPR6physical
11805837
OLA1_YEASTOLA1physical
11805837
DOHH_YEASTLIA1physical
11805837
YE11B_YEASTYER138Cphysical
11805837
PMM_YEASTSEC53physical
11805837
ACAC_YEASTACC1physical
11805837
LCF4_YEASTFAA4physical
11805837
RIR2_YEASTRNR2physical
11805837
SGD1_YEASTSGD1physical
11805837
MPP10_YEASTMPP10physical
12068309
YC16_YEASTYCR087C-Aphysical
16554755
YRA1_YEASTYRA1physical
16554755
UTP8_YEASTUTP8physical
16554755
UTP9_YEASTUTP9physical
16554755
SRP40_YEASTSRP40physical
16554755
UTP15_YEASTUTP15physical
16554755
BRE5_YEASTBRE5physical
16554755
UTP17_YEASTNAN1physical
16554755
UTP8_YEASTUTP8physical
18467557
UTP15_YEASTUTP15physical
18467557
RRT14_YEASTRRT14physical
18467557
UTP9_YEASTUTP9physical
18467557
STE12_YEASTSTE12physical
18467557
UTP10_YEASTUTP10physical
18467557
MPP10_YEASTMPP10physical
15489292
UTP17_YEASTNAN1physical
15489292
UTP4_YEASTUTP4physical
20385600
UTP15_YEASTUTP15physical
20385600
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UTP5_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-352, AND MASSSPECTROMETRY.

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