UniProt ID | WDR43_MOUSE | |
---|---|---|
UniProt AC | Q6ZQL4 | |
Protein Name | WD repeat-containing protein 43 | |
Gene Name | Wdr43 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 677 | |
Subcellular Localization | Nucleus, nucleolus . Found predominantly at the fibrillar center. | |
Protein Description | Ribosome biogenesis factor. Involved in nucleolar processing of pre-18S ribosomal RNA. Required for optimal pre-ribosomal RNA transcription by RNA polymerase I.. | |
Protein Sequence | MAAGGGGSYDPLAPAGVPCAFSPDSQAYFALASSDGQLRVWETANNRLHQEYVPSAHLSGTCTCLAWAPARLQAKESHQRKKRKSEVTGTKDQADLLALGTAVGSILLYSTVRGELHSKLTSGGHENRVNCIQWHQDNDCLYSCSDDKYIVEWSTQTCKVKCKWKGDNSSVSSLCISPDGKMLLSAGRTIKLWVLETKEVYRHFTGHATPVSSLRFTTIRPNESQPSDGITGLYFLSGAVHDRLLNVWQVRSENKEKSAVMSFTVTDEPVYVDLTLSENKEEPVKLAVVCRDGQVHLFEHILNGHCKKPLTSNCTIQIATPGKGKKVTPKPIPILAASFCLDKMSLLLVYGNWFQPTIERVALNSKDTHICLERDISNCWAPTVETAITKVKTPVMNSEAKVLVPGIPGHHAPIKLPPAQPKEAENKRKLGSTEATIEERLGAMDLDRKGRKDDLQTNSFAVLLTQGLESNDFEILNKVLQTKNVNLIKRTVLRIPLRVVIPLLQELTKRLQGHPNSAALMIQWLKCVLTIHASYLSTLPDLVEQLGTLYQLMESRVKTFQKLSNLHGKLILLVTQVTASEKSKKMTSPGQKAKLVYEEESSEEESDDEVPEKDSDDNWDEDEDKDSEKDEGVDEDNEEEDEDMEDKEENEEDREVSSEKELNGDSDLDPENESEEE | |
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 |
---|---|---|---|---|---|
77 | Phosphorylation | ARLQAKESHQRKKRK HHHHHHHHHHHHHHH | 24.98 | - | |
85 | Phosphorylation | HQRKKRKSEVTGTKD HHHHHHHHHCCCCHH | 41.13 | 26824392 | |
320 | Phosphorylation | NCTIQIATPGKGKKV CCEEEEECCCCCCCC | 33.91 | 26643407 | |
393 | Phosphorylation | TAITKVKTPVMNSEA HHHHCCCCCCCCCCC | 24.89 | 25159016 | |
398 | Phosphorylation | VKTPVMNSEAKVLVP CCCCCCCCCCEEECC | 22.34 | - | |
432 | Phosphorylation | ENKRKLGSTEATIEE HHHHCCCCCHHHHHH | 33.25 | 26824392 | |
433 | Phosphorylation | NKRKLGSTEATIEER HHHCCCCCHHHHHHH | 28.04 | 28833060 | |
436 | Phosphorylation | KLGSTEATIEERLGA CCCCCHHHHHHHHCC | 23.77 | 28833060 | |
587 | Phosphorylation | SEKSKKMTSPGQKAK CHHHCCCCCCCCEEE | 40.42 | 28066266 | |
588 | Phosphorylation | EKSKKMTSPGQKAKL HHHCCCCCCCCEEEE | 24.43 | 26824392 | |
597 | Phosphorylation | GQKAKLVYEEESSEE CCEEEEEEECCCCCC | 28.23 | 25195567 | |
601 | Phosphorylation | KLVYEEESSEEESDD EEEEECCCCCCCCCC | 46.45 | 22817900 | |
602 | Phosphorylation | LVYEEESSEEESDDE EEEECCCCCCCCCCC | 52.92 | 22817900 | |
606 | Phosphorylation | EESSEEESDDEVPEK CCCCCCCCCCCCCCC | 54.35 | 22817900 | |
615 | Phosphorylation | DEVPEKDSDDNWDED CCCCCCCCCCCCCCC | 58.91 | 22817900 | |
627 | Phosphorylation | DEDEDKDSEKDEGVD CCCCCCCCCCCCCCC | 52.89 | 25195567 | |
657 | Phosphorylation | NEEDREVSSEKELNG CHHHHHHHHHHHHCC | 28.20 | 25521595 | |
658 | Phosphorylation | EEDREVSSEKELNGD HHHHHHHHHHHHCCC | 58.84 | 25521595 | |
666 | Phosphorylation | EKELNGDSDLDPENE HHHHCCCCCCCCCCC | 41.28 | 25521595 | |
674 | Phosphorylation | DLDPENESEEE---- CCCCCCCCCCC---- | 62.99 | 25521595 |
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 WDR43_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of WDR43_MOUSE !! |
* 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 WDR43_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of WDR43_MOUSE !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-657 AND SER-658, ANDMASS SPECTROMETRY. |