NAF1_SCHPO - dbPTM
NAF1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NAF1_SCHPO
UniProt AC O14360
Protein Name H/ACA ribonucleoprotein complex non-core subunit NAF1
Gene Name naf1
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 516
Subcellular Localization Nucleus. Absent from the nucleolus..
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 to yield mature H/ACA snoRNPs complex (By similarity)..
Protein Sequence MYPHLPCKIPGLSLIYDDESKVEKSKQLSTNASSSNFVKEDQIPSNLSIDNINTPQGDPIDKNNLNTNTENNLPNIVNFQNISSANSGEIKQKDNEILFSSTEDINQHKENYQDENKIDLLDVALANPKDCVVPSSGLLMPKEEFISNEEVGIPATNSSEKSNVKIADEIAEVTHSNSSIGKSSADLSSDSSSDSESNTSFSETDVEEEKAEEKSDAESMAPSTPPKTVNELPEQIYEKPEIVLQPNSLIEPLGKIIQVLKREVVVKSDIDDEKIVFDEKTVLCFEDRSIIGYIHETFGPVSSPYYIVRFSTEEECSAINACMGRPVFYVPTMANKIDPEPLKYIKGSDASNVYDEEINPSEQEFSDDEAEVAAKQLKKKRKRKAKSMVSGNQALPGEANFQSLNQNNVRNYPFYQTNQGSNPPAKRFTQEPPSSSLYSLSESSINYSTQSPMYYNYNYPQPSFPPFHPIYNDSIGYYSQANPQMYYANQVSAPPPQGSFDPNSKFYRNSSDSYRK
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
45PhosphorylationVKEDQIPSNLSIDNI
CCHHCCCCCCCCCCC
52.6229996109
48PhosphorylationDQIPSNLSIDNINTP
HCCCCCCCCCCCCCC
31.9521712547
100PhosphorylationKDNEILFSSTEDINQ
CCCEEEECCHHHHHH
32.6724763107
101PhosphorylationDNEILFSSTEDINQH
CCEEEECCHHHHHHH
28.6021712547
102PhosphorylationNEILFSSTEDINQHK
CEEEECCHHHHHHHH
36.1624763107
176PhosphorylationEIAEVTHSNSSIGKS
HHHHHCCCCCCCCCC
29.1019547744
215PhosphorylationEEKAEEKSDAESMAP
HHHHHHHCHHHHHCC
45.3824763107
219PhosphorylationEEKSDAESMAPSTPP
HHHCHHHHHCCCCCC
23.2024763107
223PhosphorylationDAESMAPSTPPKTVN
HHHHHCCCCCCCCHH
43.9724763107
224PhosphorylationAESMAPSTPPKTVNE
HHHHCCCCCCCCHHH
42.4228889911
361PhosphorylationYDEEINPSEQEFSDD
CCCCCCCCCCCCCHH
47.6328889911
366PhosphorylationNPSEQEFSDDEAEVA
CCCCCCCCHHHHHHH
43.3228889911

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_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NAF1_SCHPO !!

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_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of NAF1_SCHPO !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NAF1_SCHPO

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361 AND SER-366, ANDMASS SPECTROMETRY.

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