NEP1_HUMAN - dbPTM
NEP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NEP1_HUMAN
UniProt AC Q92979
Protein Name Ribosomal RNA small subunit methyltransferase NEP1 {ECO:0000305|PubMed:20047967}
Gene Name EMG1 {ECO:0000303|PubMed:19463982}
Organism Homo sapiens (Human).
Sequence Length 244
Subcellular Localization Nucleus, nucleolus .
Protein Description S-adenosyl-L-methionine-dependent pseudouridine N(1)-methyltransferase that methylates pseudouridine at position 1248 (Psi1248) in 18S rRNA. Involved the biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA. Is not able to methylate uridine at this position. [PubMed: 20047967 Has also an essential role in 40S ribosomal subunit biogenesis independent on its methyltransferase activity, facilitating the incorporation of ribosomal protein S19 during the formation of pre-ribosomes (By similarity]
Protein Sequence MAAPSDGFKPRERSGGEQAQDWDALPPKRPRLGAGNKIGGRRLIVVLEGASLETVKVGKTYELLNCDKHKSILLKNGRDPGEARPDITHQSLLMLMDSPLNRAGLLQVYIHTQKNVLIEVNPQTRIPRTFDRFCGLMVQLLHKLSVRAADGPQKLLKVIKNPVSDHFPVGCMKVGTSFSIPVVSDVRELVPSSDPIVFVVGAFAHGKVSVEYTEKMVSISNYPLSAALTCAKLTTAFEEVWGVI
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
2Acetylation------MAAPSDGFK
------CCCCCCCCC
28.2522814378
5Phosphorylation---MAAPSDGFKPRE
---CCCCCCCCCCCC
45.7129255136
9AcetylationAAPSDGFKPRERSGG
CCCCCCCCCCCCCCC
49.0123954790
9UbiquitinationAAPSDGFKPRERSGG
CCCCCCCCCCCCCCC
49.0124816145
14PhosphorylationGFKPRERSGGEQAQD
CCCCCCCCCCCCCCC
46.5325159151
28AcetylationDWDALPPKRPRLGAG
CCCCCCCCCCCCCCC
73.4326051181
28UbiquitinationDWDALPPKRPRLGAG
CCCCCCCCCCCCCCC
73.4329967540
37AcetylationPRLGAGNKIGGRRLI
CCCCCCCCCCCEEEE
41.6425953088
37UbiquitinationPRLGAGNKIGGRRLI
CCCCCCCCCCCEEEE
41.6424816145
51PhosphorylationIVVLEGASLETVKVG
EEEEECCCEEEEECC
37.2820068231
54PhosphorylationLEGASLETVKVGKTY
EECCCEEEEECCCEE
30.8120068231
56UbiquitinationGASLETVKVGKTYEL
CCCEEEEECCCEEEE
53.3323000965
59UbiquitinationLETVKVGKTYELLNC
EEEEECCCEEEEECC
51.4223000965
592-HydroxyisobutyrylationLETVKVGKTYELLNC
EEEEECCCEEEEECC
51.42-
59AcetylationLETVKVGKTYELLNC
EEEEECCCEEEEECC
51.4223954790
60PhosphorylationETVKVGKTYELLNCD
EEEECCCEEEEECCC
19.1221815630
61PhosphorylationTVKVGKTYELLNCDK
EEECCCEEEEECCCC
14.2028152594
68UbiquitinationYELLNCDKHKSILLK
EEEECCCCCCEEEEE
55.9529967540
68AcetylationYELLNCDKHKSILLK
EEEECCCCCCEEEEE
55.9523749302
70AcetylationLLNCDKHKSILLKNG
EECCCCCCEEEEECC
44.9526051181
70UbiquitinationLLNCDKHKSILLKNG
EECCCCCCEEEEECC
44.9529967540
75AcetylationKHKSILLKNGRDPGE
CCCEEEEECCCCCCC
54.6425953088
75UbiquitinationKHKSILLKNGRDPGE
CCCEEEEECCCCCCC
54.6421890473
91PhosphorylationRPDITHQSLLMLMDS
CCCCCHHHHHHHHCC
18.83-
154UbiquitinationRAADGPQKLLKVIKN
HCCCCHHHHHHHHCC
59.9423000965
154AcetylationRAADGPQKLLKVIKN
HCCCCHHHHHHHHCC
59.9425953088
157UbiquitinationDGPQKLLKVIKNPVS
CCHHHHHHHHCCCCC
52.9623000965
157AcetylationDGPQKLLKVIKNPVS
CCHHHHHHHHCCCCC
52.9626051181
160AcetylationQKLLKVIKNPVSDHF
HHHHHHHCCCCCCCC
59.1826051181
160UbiquitinationQKLLKVIKNPVSDHF
HHHHHHHCCCCCCCC
59.1823000965
176PhosphorylationVGCMKVGTSFSIPVV
CCCEEECCCEEEEEE
29.5923186163
177PhosphorylationGCMKVGTSFSIPVVS
CCEEECCCEEEEEEC
15.8623186163
179PhosphorylationMKVGTSFSIPVVSDV
EEECCCEEEEEECCH
26.2523186163
218PhosphorylationEYTEKMVSISNYPLS
EEEEEEEECCCCCHH
19.4628152594
220PhosphorylationTEKMVSISNYPLSAA
EEEEEECCCCCHHHH
23.8628442448
222PhosphorylationKMVSISNYPLSAALT
EEEECCCCCHHHHHH
9.9628152594
225PhosphorylationSISNYPLSAALTCAK
ECCCCCHHHHHHHHH
13.6428442448
229PhosphorylationYPLSAALTCAKLTTA
CCHHHHHHHHHHHHH
12.9928442448
234PhosphorylationALTCAKLTTAFEEVW
HHHHHHHHHHHHHHH
18.5128122231
235PhosphorylationLTCAKLTTAFEEVWG
HHHHHHHHHHHHHHC
39.5228122231

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 NEP1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NEP1_HUMAN !!

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 NEP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
S2538_HUMANSLC25A38physical
16169070
KHDR1_HUMANKHDRBS1physical
16169070
A4_HUMANAPPphysical
21832049
IL7RA_HUMANIL7Rphysical
23151878

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
211180Bowen-Conradi syndrome (BWCNS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NEP1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5 AND SER-14, AND MASSSPECTROMETRY.

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