UniProt ID | UTP9_YEAST | |
---|---|---|
UniProt AC | P38882 | |
Protein Name | U3 small nucleolar RNA-associated protein 9 | |
Gene Name | UTP9 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 575 | |
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 | MGSSLDLVASFSHDSTRFAFQASVAQKNNVDIYPLNETKDYVVNSSLVSHIDYETNDMKVSDVIFFGWCSDLIDTQSSNIKRKLDEDEGTGESSEQRCENFFVNGFPDGRIVVYSSNGKDIVNIIKNKKEILGADTDESDIWILDSDKVVKKLQYNNSKPLKTFTLVDGKDDEIVHFQILHQNGTLLVCIITKQMVYIVDPSKRRPSTKYSFEISDAVACEFSSDGKYLLIANNEELIAYDLKEDSKLIQSWPVQVKTLKTLDDLIMALTTDGKINNYKIGEADKVCSIVVNEDLEIIDFTPINSKQQVLISWLNVNEPNFESISLKEIETQGYITINKNEKNNADEADQKKLEEKEEEAQPEVQHEKKETETKINKKVSKSDQVEIANILSSHLEANSTEILDDLMSGSWTEPEIKKFILTKINTVDHLSKIFLTISKSITQNPWNEENLLPLWLKWLLTLKSGELNSIKDKHTKKNCKHLKSALRSSEEILPVLLGIQGRLEMLRRQAKLREDLAQLSMQEGEDDEIEVIEHSNVISNPLQDQASPVEKLEPDSIVYANGESDEFVDASEYKD | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
3 | Phosphorylation | -----MGSSLDLVAS -----CCCCCEEEEE | 26.82 | 30377154 | |
12 | Phosphorylation | LDLVASFSHDSTRFA CEEEEECCCCCHHHE | 24.72 | 30377154 | |
15 | Phosphorylation | VASFSHDSTRFAFQA EEECCCCCHHHEEEE | 18.96 | 30377154 | |
38 | Phosphorylation | DIYPLNETKDYVVNS EEEECCCCCCEEEEH | 28.30 | 27017623 | |
41 | Phosphorylation | PLNETKDYVVNSSLV ECCCCCCEEEEHHHH | 14.09 | 27017623 | |
45 | Phosphorylation | TKDYVVNSSLVSHID CCCEEEEHHHHCCCC | 17.28 | 21440633 | |
46 | Phosphorylation | KDYVVNSSLVSHIDY CCEEEEHHHHCCCCC | 27.82 | 27017623 | |
49 | Phosphorylation | VVNSSLVSHIDYETN EEEHHHHCCCCCCCC | 21.73 | 27017623 | |
55 | Phosphorylation | VSHIDYETNDMKVSD HCCCCCCCCCCCHHH | 30.23 | 27017623 | |
83 | Ubiquitination | QSSNIKRKLDEDEGT CCHHHHHHCCCCCCC | 56.11 | 23749301 | |
93 | Phosphorylation | EDEGTGESSEQRCEN CCCCCCCCHHHHHHH | 40.29 | 30377154 | |
203 | Acetylation | VYIVDPSKRRPSTKY EEEECHHHCCCCCEE | 58.79 | 24489116 | |
520 | Phosphorylation | REDLAQLSMQEGEDD HHHHHHHHHHCCCCC | 13.31 | 21440633 | |
539 | Phosphorylation | IEHSNVISNPLQDQA EEECCCCCCCCCCCC | 28.28 | 24961812 | |
547 | Phosphorylation | NPLQDQASPVEKLEP CCCCCCCCCCHHCCC | 24.68 | 27214570 | |
556 | Phosphorylation | VEKLEPDSIVYANGE CHHCCCCCEEEECCC | 25.35 | 22369663 | |
559 | Phosphorylation | LEPDSIVYANGESDE CCCCCEEEECCCCCC | 7.84 | 22369663 | |
564 | Phosphorylation | IVYANGESDEFVDAS EEEECCCCCCCCCHH | 43.78 | 22369663 | |
571 | Phosphorylation | SDEFVDASEYKD--- CCCCCCHHHCCC--- | 36.67 | 22369663 | |
573 | Phosphorylation | EFVDASEYKD----- CCCCHHHCCC----- | 20.26 | 22369663 |
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 UTP9_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of UTP9_YEAST !! |
* 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 UTP9_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"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-547 AND SER-564, ANDMASS SPECTROMETRY. |