Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Pantetheinase  

UniProtKB / Swiss-Prot ID :  VNN1_HUMAN

Gene Name (Synonyms) : 
VNN1  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cell membrane; Lipid-anchor, GPI-anchor (Potential). 

Protein Function :  Amidohydrolase that hydrolyzes specifically one of the carboamide linkages in D-pantetheine thus recycling pantothenic acid (vitamin B5) and releasing cysteamine. 

Protein Sequence MTTQLPAYVAILLFYVSRASCQDTFTAAVYEHAAILPNATLTPVSREEALALMNRNLDILEGAITSAADQ...
Predicted Secondary Structure CCCCHHHHHHHHHHHHHHHCCCCEEEEEEEEECCCCCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHHHHC...
Protein Variant
LocationDescription
26T -> I (in dbSNP:rs2294757). VAR_023529
63A -> T. VAR_023967
131N -> S (in dbSNP:rs2272996). VAR_023968
136V -> L (in dbSNP:rs45610032). VAR_023969
146D -> N. VAR_023970
296E -> D (in dbSNP:rs45523444). VAR_023971
325A -> E (in dbSNP:rs34535050). VAR_023972
336T -> A (in dbSNP:rs45562238). VAR_023973
373I -> T (in dbSNP:rs35938565). VAR_023974
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
38N-linked (GlcNAc...).AILPNATLT
CCCCCCCHH
41.95UniProtKB
Link-
130N-linked (GlcNAc...).CLAKNNSIY
HHHHHCCEE
41.70UniProtKB
Link-
283N-linked (Glc...)IYAPNSSRA
EEECCCCEE
44.43HPRD
Link-
283N-linked (GlcNAc...)IYAPNSSRA
EEECCCCEE
44.43SysPTM
Link-
283N-linked (GlcNAc...).IYAPNSSRA
EEECCCCEE
44.43UniProtKB
Link-
315N-linked (GlcNAc...).SAVVNWTSY
CCCCCCCCC
29.70UniProtKB
Link-
353N-linked (GlcNAc...)GVAGNYTVC
CCCCEEEEE
21.40SysPTM
Link-
353N-linked (GlcNAc...).GVAGNYTVC
CCCCEEEEE
21.40UniProtKB
Link-
486GPI-anchor amidated serineKDWASNASS
CCCCCCCCC
28.77HPRD
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-130; ASN-283; ASN-315 ANDASN-353, AND MASS SPECTROMETRY.
"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-353, AND MASSSPECTROMETRY.
"A proteomic analysis of human bile.";
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.;
Mol. Cell. Proteomics 3:715-728(2004).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-38 AND ASN-353, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures