NEUR1_HUMAN - dbPTM
NEUR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NEUR1_HUMAN
UniProt AC Q99519
Protein Name Sialidase-1
Gene Name NEU1
Organism Homo sapiens (Human).
Sequence Length 415
Subcellular Localization Lysosome membrane
Peripheral membrane protein
Lumenal side. Lysosome lumen. Cell membrane. Cytoplasmic vesicle. Lysosome . Localized not only on the inner side of the lysosomal membrane and in the lysosomal lumen, but also on the plasma membrane an
Protein Description Catalyzes the removal of sialic acid (N-acetylneuraminic acid) moities from glycoproteins and glycolipids. To be active, it is strictly dependent on its presence in the multienzyme complex. Appears to have a preference for alpha 2-3 and alpha 2-6 sialyl linkage..
Protein Sequence MTGERPSTALPDRRWGPRILGFWGGCRVWVFAAIFLLLSLAASWSKAENDFGLVQPLVTMEQLLWVSGRQIGSVDTFRIPLITATPRGTLLAFAEARKMSSSDEGAKFIALRRSMDQGSTWSPTAFIVNDGDVPDGLNLGAVVSDVETGVVFLFYSLCAHKAGCQVASTMLVWSKDDGVSWSTPRNLSLDIGTEVFAPGPGSGIQKQREPRKGRLIVCGHGTLERDGVFCLLSDDHGASWRYGSGVSGIPYGQPKQENDFNPDECQPYELPDGSVVINARNQNNYHCHCRIVLRSYDACDTLRPRDVTFDPELVDPVVAAGAVVTSSGIVFFSNPAHPEFRVNLTLRWSFSNGTSWRKETVQLWPGPSGYSSLATLEGSMDGEEQAPQLYVLYEKGRNHYTESISVAKISVYGTL
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
2Phosphorylation------MTGERPSTA
------CCCCCCCCC
47.9924043423
7Phosphorylation-MTGERPSTALPDRR
-CCCCCCCCCCCCCC
32.3124043423
8PhosphorylationMTGERPSTALPDRRW
CCCCCCCCCCCCCCC
34.5924043423
100PhosphorylationFAEARKMSSSDEGAK
HHHHHHCCCCHHHHH
29.71-
107UbiquitinationSSSDEGAKFIALRRS
CCCHHHHHHEEEEEC
48.43-
169PhosphorylationAGCQVASTMLVWSKD
HCCEEEEEEEEEECC
12.5625332170
174PhosphorylationASTMLVWSKDDGVSW
EEEEEEEECCCCCCC
20.8025332170
183PhosphorylationDDGVSWSTPRNLSLD
CCCCCCCCCCCEEEE
21.7325332170
186N-linked_GlycosylationVSWSTPRNLSLDIGT
CCCCCCCCEEEEECC
34.87UniProtKB CARBOHYD
206UbiquitinationGPGSGIQKQREPRKG
CCCCCCHHCCCCCCC
49.7721906983
233PhosphorylationDGVFCLLSDDHGASW
CCEEEEEECCCCCCC
28.2230576142
239PhosphorylationLSDDHGASWRYGSGV
EECCCCCCCCCCCCC
19.3730576142
242PhosphorylationDHGASWRYGSGVSGI
CCCCCCCCCCCCCCC
14.9116094384
244PhosphorylationGASWRYGSGVSGIPY
CCCCCCCCCCCCCCC
27.3816094384
247PhosphorylationWRYGSGVSGIPYGQP
CCCCCCCCCCCCCCC
34.2330174305
251PhosphorylationSGVSGIPYGQPKQEN
CCCCCCCCCCCCCCC
26.8616094384
343N-linked_GlycosylationAHPEFRVNLTLRWSF
CCCCEEEEEEEEEEE
24.05UniProtKB CARBOHYD
345PhosphorylationPEFRVNLTLRWSFSN
CCEEEEEEEEEEECC
14.7424719451
352N-linked_GlycosylationTLRWSFSNGTSWRKE
EEEEEECCCCCEEEE
56.6119159218

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 NEUR1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NEUR1_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 NEUR1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EF1A1_HUMANEEF1A1physical
16169070
GALNS_HUMANGALNSphysical
8910459
BGAL_HUMANGLB1physical
3102233
PPGB_HUMANCTSAphysical
9501080
KCNA2_HUMANKCNA2physical
10896669
KCNA4_HUMANKCNA4physical
10896669

Drug and Disease Associations
Kegg Disease
H00142 Sialidosis; Mucolipidosis I
H00276 Galactosialidosis
H00810 Progressive myoclonic epilepsy (PME), including: Lafora disease (LBD); Unverricht-Lundborg disease (
OMIM Disease
256550Sialidosis (SIALIDOSIS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00198Oseltamivir
Regulatory Network of NEUR1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-352, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry.";
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
Nat. Methods 2:591-598(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-242; SER-244 ANDTYR-251, AND MASS SPECTROMETRY.

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