NAF1_DROME - dbPTM
NAF1_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NAF1_DROME
UniProt AC Q9VJ62
Protein Name H/ACA ribonucleoprotein complex non-core subunit NAF1
Gene Name CG10341
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 564
Subcellular Localization Nucleus.
Protein Description RNA-binding protein required for the maturation of box H/ACA snoRNPs complex and ribosome biogenesis. During assembly of the H/ACA snoRNPs complex, it associates with the complex and disappears during maturation of the complex and is replaced by GAR1/CG4038 to yield mature H/ACA snoRNPs complex (By similarity)..
Protein Sequence MESEQPAAVKASAPIEEPQSTETAVELGKHSTLKADLSIDKLETATTEATNAVVEPVEMEQQVENELVNESTQAMTSTTTQEKVVGSVNNLVEEQQCVEMEFETSSDLVVQGSPSEESKKVASDASATVTAPQVQPAPHVDSSPQASGLSLLAAYSSDDSDDEKVTPVQNGDNDVIEVPVTDPASSTTAYRPVVAVSSDDESSKSSSSSSDSDSDSEGEYLTVLRKKIDKRINTVDCDEDDEDFDEDGATGDRSRRRQPPKVRGEMLLDDLPPIHQLEITVPEDECVELGKVQSIVDQLVLVSVLPNSMLFDLDTVLFLEKGRKVLGEVFDVLGQVSDPLYCVRFNSNKQILDRGIKIGDVVYCAPKTEHTQFVILSKLMQVRGSDASWEHDVEPPARYVDHSDDEEEREARAEQRKRRQRDRTNSTDSVDTVTSVATTATKASSVAPPPRQRGRRGQRESFRQSQRPSINQHNQNQPQDEQYNFHPSYNPGSWHSNYYQNYHQAAANFNMAQQHPGMPFPVPNYGYGMPYAMPPMYPHMYPPPPPFAPPPPNNQSHQGQPPPS
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
38PhosphorylationSTLKADLSIDKLETA
CCCCCCCCCCCHHHH
29.3219429919
234PhosphorylationKIDKRINTVDCDEDD
HCCCCCCCCCCCCCC
18.4921082442
250PhosphorylationDFDEDGATGDRSRRR
CCCCCCCCCCHHHCC
45.1818327897
254PhosphorylationDGATGDRSRRRQPPK
CCCCCCHHHCCCCCC
34.5718327897
385PhosphorylationKLMQVRGSDASWEHD
HHHHHCCCCCCCCCC
21.3119429919
388PhosphorylationQVRGSDASWEHDVEP
HHCCCCCCCCCCCCC
37.6819429919
399PhosphorylationDVEPPARYVDHSDDE
CCCCCCCCCCCCCCH
16.6119060867
403PhosphorylationPARYVDHSDDEEERE
CCCCCCCCCCHHHHH
42.1521082442
424PhosphorylationKRRQRDRTNSTDSVD
HHHHHHCCCCCCCCH
37.5019429919
426PhosphorylationRQRDRTNSTDSVDTV
HHHHCCCCCCCCHHH
32.7419429919
427PhosphorylationQRDRTNSTDSVDTVT
HHHCCCCCCCCHHHH
34.0719429919
429PhosphorylationDRTNSTDSVDTVTSV
HCCCCCCCCHHHHHH
23.2119429919
432PhosphorylationNSTDSVDTVTSVATT
CCCCCCHHHHHHHHC
24.4319429919
434PhosphorylationTDSVDTVTSVATTAT
CCCCHHHHHHHHCCC
21.4119429919
435PhosphorylationDSVDTVTSVATTATK
CCCHHHHHHHHCCCH
12.8619429919
438PhosphorylationDTVTSVATTATKASS
HHHHHHHHCCCHHHH
18.1419429919
439PhosphorylationTVTSVATTATKASSV
HHHHHHHCCCHHHHC
23.6919429919
441PhosphorylationTSVATTATKASSVAP
HHHHHCCCHHHHCCC
25.6719429919

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 NAF1_DROME !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NAF1_DROME !!

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 NAF1_DROME !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NUP58_DROMENup58physical
14605208
POXM_DROMEPoxmphysical
14605208

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NAF1_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-250; SER-254; SER-403;THR-427; SER-429 AND THR-432, AND MASS SPECTROMETRY.

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