UTP17_YEAST - dbPTM
UTP17_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID UTP17_YEAST
UniProt AC Q02931
Protein Name NET1-associated nuclear protein 1
Gene Name NAN1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 896
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 MTQSLGIEQYKLSVVSGGKPALNNLSSVTGNKNIARLSQDQRNYIIPFNNQIKVYSVETRQCVKTLKFANNSLLSGIFLQEEENNESIVKILLGDITVPQQEDAHLITVFTNNGHVIVLNYKGKLVESPKHFKISLADEKLANVFHSEGNYRILTTFKDPSQKAHNSLQSYRLYALTFDDAKKQFEVAHQAEWHNVILSNISSNGKLLAHMCKDVSTKDHEHKSISVVSLFDDSVNLSFPLGSILSSQTQSLSYNTRYVSSMAIDNMGQQLAVGFASGVISIVSLADLQIRLLKWHIDSVLSLSFSHDGSYLLSGGWEKVMSLWQLETNSQQFLPRLNGIIIDCQVLGPQGNYYSLILQMTENNSNSDYQFLLLNASDLTSKLSINGPLPVFNSTIKHIQQPISAMNTKNSNSITSLNHSKKKQSRKLIKSRRQDFTTNVEINPINKNLYFPHISAVQIFDFYKNEQVNYQYLTSGVNNSMGKVRFELNLQDPIITDLKFTKDGQWMITYEIEYPPNDLLSSKDLTHILKFWTKNDNETNWNLKTKVINPHGISVPITKILPSPRSVNNSQGCLTADNNGGLKFWSFDSHESNWCLKKISLPNFNHFSNSVSLAWSQDGSLIFHGFDDKLQILDFDTFKKFESLENTKTVSEFTLDSEIQTVKLINDTNLIVATRTTLNAINLLRGQVINSFDLYPFVNGVYKNGHMDRLITCDERTGNIALVINQQLTDLDGVPTINYKSRIIIFDSDLSTKLGNFTHHEYISWIGWNYDTDFIFLDIESTLGVVGTTVNTQLSDEVNNEGILDGLVSNTITTSASNSDIFAEQLHKLSSRGKKSDTRDKNTNDNDEDEEDIALEFINGEKKDKLVNMNSFTSMFDNIQNVQMDTFFDRVMKVLT
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
2Phosphorylation------MTQSLGIEQ
------CCCCCCCEE
27.1923749301
4Phosphorylation----MTQSLGIEQYK
----CCCCCCCEEEE
21.2828152593
10PhosphorylationQSLGIEQYKLSVVSG
CCCCCEEEEEEEEEC
10.9125533186
140UbiquitinationKISLADEKLANVFHS
EEEECCHHHHHHCCC
54.1417644757
158AcetylationYRILTTFKDPSQKAH
EEEEEEECCHHHHHH
67.6424489116
163UbiquitinationTFKDPSQKAHNSLQS
EECCHHHHHHHCHHH
56.8217644757
177PhosphorylationSYRLYALTFDDAKKQ
HEEEEEEEHHHHHHH
19.4927017623
409UbiquitinationPISAMNTKNSNSITS
CHHHCCCCCCCCCCC
54.0717644757
411PhosphorylationSAMNTKNSNSITSLN
HHCCCCCCCCCCCCC
33.2530377154
413PhosphorylationMNTKNSNSITSLNHS
CCCCCCCCCCCCCCC
27.3723749301
421UbiquitinationITSLNHSKKKQSRKL
CCCCCCCCHHHHHHH
57.3417644757
422UbiquitinationTSLNHSKKKQSRKLI
CCCCCCCHHHHHHHH
60.0917644757
483UbiquitinationGVNNSMGKVRFELNL
CCCCCCCEEEEEEEC
22.9223749301
530AcetylationKDLTHILKFWTKNDN
CCHHHHHHHHCCCCC
37.9524489116
817PhosphorylationNTITTSASNSDIFAE
CCEECCCCCCHHHHH
36.3128889911

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 UTP17_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UTP17_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 UTP17_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SAP1_YEASTSAP1physical
11805837
6PGD2_YEASTGND2physical
11805837
6PGD1_YEASTGND1physical
11805837
IMP3_YEASTIMP3physical
12150911
RRP5_YEASTRRP5physical
12150911
UTP4_YEASTUTP4physical
12150911
UTP8_YEASTUTP8physical
12150911
UTP9_YEASTUTP9physical
12150911
UTP10_YEASTUTP10physical
12150911
UTP15_YEASTUTP15physical
12150911
PNO1_YEASTPNO1physical
12150911
MPP10_YEASTMPP10physical
12068309
DPO5_YEASTPOL5physical
16554755
EIF3B_YEASTPRT1physical
16554755
PNO1_YEASTPNO1physical
16429126
UTP10_YEASTUTP10physical
16429126
UTP15_YEASTUTP15physical
16429126
UTP4_YEASTUTP4physical
16429126
UTP8_YEASTUTP8physical
16429126
UTP9_YEASTUTP9physical
16429126
IMP3_YEASTIMP3physical
16429126
RRP5_YEASTRRP5physical
16429126
SSB1_YEASTSSB1physical
19536198
PWP2_YEASTPWP2physical
17515605
UTP8_YEASTUTP8physical
20385600
UTP10_YEASTUTP10physical
20385600
UTP17_YEASTNAN1physical
20385600

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of UTP17_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-4 AND SER-817, AND MASSSPECTROMETRY.

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