VNN1_HUMAN - dbPTM
VNN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VNN1_HUMAN
UniProt AC O95497
Protein Name Pantetheinase
Gene Name VNN1
Organism Homo sapiens (Human).
Sequence Length 513
Subcellular Localization Cell membrane
Lipid-anchor, GPI-anchor .
Protein Description Amidohydrolase that hydrolyzes specifically one of the carboamide linkages in D-pantetheine thus recycling pantothenic acid (vitamin B5) and releasing cysteamine..
Protein Sequence MTTQLPAYVAILLFYVSRASCQDTFTAAVYEHAAILPNATLTPVSREEALALMNRNLDILEGAITSAADQGAHIIVTPEDAIYGWNFNRDSLYPYLEDIPDPEVNWIPCNNRNRFGQTPVQERLSCLAKNNSIYVVANIGDKKPCDTSDPQCPPDGRYQYNTDVVFDSQGKLVARYHKQNLFMGENQFNVPKEPEIVTFNTTFGSFGIFTCFDILFHDPAVTLVKDFHVDTIVFPTAWMNVLPHLSAVEFHSAWAMGMRVNFLASNIHYPSKKMTGSGIYAPNSSRAFHYDMKTEEGKLLLSQLDSHPSHSAVVNWTSYASSIEALSSGNKEFKGTVFFDEFTFVKLTGVAGNYTVCQKDLCCHLSYKMSENIPNEVYALGAFDGLHTVEGRYYLQICTLLKCKTTNLNTCGDSAETASTRFEMFSLSGTFGTQYVFPEVLLSENQLAPGEFQVSTDGRLFSLKPTSGPVLTVTLFGRLYEKDWASNASSGLTAQARIIMLIVIAPIVCSLSW
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
8PhosphorylationMTTQLPAYVAILLFY
CCCHHHHHHHHHHHH		6.6224043423
15PhosphorylationYVAILLFYVSRASCQ
HHHHHHHHHHHHCCC		9.4824043423
17PhosphorylationAILLFYVSRASCQDT
HHHHHHHHHHCCCCH		15.6824043423
38N-linked_GlycosylationEHAAILPNATLTPVS
HHHHCCCCCCCCCCC		41.9515084671
83PhosphorylationVTPEDAIYGWNFNRD
ECCHHHCCCCCCCCH		20.1522468782
130N-linked_GlycosylationRLSCLAKNNSIYVVA
HHHHHHHCCCEEEEE		41.7016335952
134PhosphorylationLAKNNSIYVVANIGD
HHHCCCEEEEEEECC		6.68-
200N-linked_GlycosylationEPEIVTFNTTFGSFG
CCCEEEEECCCCCCC		28.92UniProtKB CARBOHYD
265PhosphorylationMRVNFLASNIHYPSK
HCCCHHHHCCCCCCC		38.1629978859
269PhosphorylationFLASNIHYPSKKMTG
HHHHCCCCCCCCCCC		12.8529978859
271PhosphorylationASNIHYPSKKMTGSG
HHCCCCCCCCCCCCC		37.4329978859
275PhosphorylationHYPSKKMTGSGIYAP
CCCCCCCCCCCEECC		36.7629978859
277PhosphorylationPSKKMTGSGIYAPNS
CCCCCCCCCEECCCC		16.9229978859
280PhosphorylationKMTGSGIYAPNSSRA
CCCCCCEECCCCCCC		21.3829978859
283N-linked_GlycosylationGSGIYAPNSSRAFHY
CCCEECCCCCCCEEE		44.4316335952
283N-linked_GlycosylationGSGIYAPNSSRAFHY
CCCEECCCCCCCEEE		44.4317623646
284PhosphorylationSGIYAPNSSRAFHYD
CCEECCCCCCCEEEE		21.8329978859
285PhosphorylationGIYAPNSSRAFHYDM
CEECCCCCCCEEEEC		33.9829978859
293AcetylationRAFHYDMKTEEGKLL
CCEEEECCCCCCCCH		50.3011642129
302PhosphorylationEEGKLLLSQLDSHPS
CCCCCHHHHHHCCCC		28.7726074081
306PhosphorylationLLLSQLDSHPSHSAV
CHHHHHHCCCCCCEE		45.9826074081
309PhosphorylationSQLDSHPSHSAVVNW
HHHHCCCCCCEEECC		25.3426074081
311PhosphorylationLDSHPSHSAVVNWTS
HHCCCCCCEEECCHH		27.3926074081
315N-linked_GlycosylationPSHSAVVNWTSYASS
CCCCEEECCHHHHHH		29.7016335952
317PhosphorylationHSAVVNWTSYASSIE
CCEEECCHHHHHHHH		13.4726074081
318PhosphorylationSAVVNWTSYASSIEA
CEEECCHHHHHHHHH		15.4326074081
319PhosphorylationAVVNWTSYASSIEAL
EEECCHHHHHHHHHH		11.7926074081
321PhosphorylationVNWTSYASSIEALSS
ECCHHHHHHHHHHHC		24.5026074081
322PhosphorylationNWTSYASSIEALSSG
CCHHHHHHHHHHHCC		19.1026074081
327PhosphorylationASSIEALSSGNKEFK
HHHHHHHHCCCCEEE		43.1626074081
328PhosphorylationSSIEALSSGNKEFKG
HHHHHHHCCCCEEEE		47.4326074081
353N-linked_GlycosylationKLTGVAGNYTVCQKD
EECEECCCCEEECHH		21.4015084671
462PhosphorylationSTDGRLFSLKPTSGP
CCCCCEEEECCCCCC		39.8224719451
491GPI-anchorWASNASSGLTAQARI
HHCCCCCCCCHHHHH		25.26-
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 VNN1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VNN1_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 VNN1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of VNN1_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VNN1_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-353, AND MASSSPECTROMETRY.
"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.
"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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