VASN_HUMAN - dbPTM
VASN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VASN_HUMAN
UniProt AC Q6EMK4
Protein Name Vasorin
Gene Name VASN
Organism Homo sapiens (Human).
Sequence Length 673
Subcellular Localization Membrane
Single-pass type I membrane protein . Secreted .
Protein Description May act as an inhibitor of TGF-beta signaling..
Protein Sequence MCSRVPLLLPLLLLLALGPGVQGCPSGCQCSQPQTVFCTARQGTTVPRDVPPDTVGLYVFENGITMLDAGSFAGLPGLQLLDLSQNQIASLPSGVFQPLANLSNLDLTANRLHEITNETFRGLRRLERLYLGKNRIRHIQPGAFDTLDRLLELKLQDNELRALPPLRLPRLLLLDLSHNSLLALEPGILDTANVEALRLAGLGLQQLDEGLFSRLRNLHDLDVSDNQLERVPPVIRGLRGLTRLRLAGNTRIAQLRPEDLAGLAALQELDVSNLSLQALPGDLSGLFPRLRLLAAARNPFNCVCPLSWFGPWVRESHVTLASPEETRCHFPPKNAGRLLLELDYADFGCPATTTTATVPTTRPVVREPTALSSSLAPTWLSPTEPATEAPSPPSTAPPTVGPVPQPQDCPPSTCLNGGTCHLGTRHHLACLCPEGFTGLYCESQMGQGTRPSPTPVTPRPPRSLTLGIEPVSPTSLRVGLQRYLQGSSVQLRSLRLTYRNLSGPDKRLVTLRLPASLAEYTVTQLRPNATYSVCVMPLGPGRVPEGEEACGEAHTPPAVHSNHAPVTQAREGNLPLLIAPALAAVLLAALAAVGAAYCVRRGRAMAAAAQDKGQVGPGAGPLELEGVKVPLEPGPKATEGGGEALPSGSECEVPLMGFPGPGLQSPLHAKPYI
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
45PhosphorylationCTARQGTTVPRDVPP
EECCCCCCCCCCCCC		35.0228857561
101N-linked_GlycosylationGVFQPLANLSNLDLT
CCHHHCCCCCCCCCC		52.2419159218
117N-linked_GlycosylationNRLHEITNETFRGLR
HHHHHHHHHHHHHHH		52.5522171320
224PhosphorylationNLHDLDVSDNQLERV
CCCCCCCCCCHHHCC		30.43-
273N-linked_GlycosylationLQELDVSNLSLQALP
HHHCCCCCCCCCCCC		33.2316335952
284PhosphorylationQALPGDLSGLFPRLR
CCCCCCHHCHHHHHH		37.8829496963
319O-linked_GlycosylationWVRESHVTLASPEET
CCEECCEEECCCCCC		15.9355830571
378PhosphorylationLSSSLAPTWLSPTEP
CCCCCCCCCCCCCCC		33.1725332170
454O-linked_GlycosylationQGTRPSPTPVTPRPP
CCCCCCCCCCCCCCC		34.43OGP
454PhosphorylationQGTRPSPTPVTPRPP
CCCCCCCCCCCCCCC		34.4323684312
457PhosphorylationRPSPTPVTPRPPRSL
CCCCCCCCCCCCCCE		18.1325332170
463O-linked_GlycosylationVTPRPPRSLTLGIEP
CCCCCCCCEEECCEE		31.32OGP
463PhosphorylationVTPRPPRSLTLGIEP
CCCCCCCCEEECCEE		31.3229396449
465O-linked_GlycosylationPRPPRSLTLGIEPVS
CCCCCCEEECCEECC		24.96OGP
465PhosphorylationPRPPRSLTLGIEPVS
CCCCCCEEECCEECC		24.9629396449
472O-linked_GlycosylationTLGIEPVSPTSLRVG
EECCEECCCCHHHHH		32.93OGP
474O-linked_GlycosylationGIEPVSPTSLRVGLQ
CCEECCCCHHHHHHH		32.65OGP
475O-linked_GlycosylationIEPVSPTSLRVGLQR
CEECCCCHHHHHHHH		19.98OGP
487O-linked_GlycosylationLQRYLQGSSVQLRSL
HHHHHCCCCEEEEEE		17.8655832923
493PhosphorylationGSSVQLRSLRLTYRN
CCCEEEEEEEEEEEC		26.8322210691
498PhosphorylationLRSLRLTYRNLSGPD
EEEEEEEEECCCCCC		11.33-
500N-linked_GlycosylationSLRLTYRNLSGPDKR
EEEEEEECCCCCCCE		28.30UniProtKB CARBOHYD
510PhosphorylationGPDKRLVTLRLPASL
CCCCEEEEEECCHHH		15.6821712546
516O-linked_GlycosylationVTLRLPASLAEYTVT
EEEECCHHHHEEEEH		26.6055829943
520PhosphorylationLPASLAEYTVTQLRP
CCHHHHEEEEHHCCC		10.8225332170
521PhosphorylationPASLAEYTVTQLRPN
CHHHHEEEEHHCCCC		14.4725332170
528N-linked_GlycosylationTVTQLRPNATYSVCV
EEHHCCCCCEEEEEE		38.18UniProtKB CARBOHYD
530O-linked_GlycosylationTQLRPNATYSVCVMP
HHCCCCCEEEEEEEE		23.99OGP
532O-linked_GlycosylationLRPNATYSVCVMPLG
CCCCCEEEEEEEECC		12.51OGP
555O-linked_GlycosylationEACGEAHTPPAVHSN
HCCCCCCCCCCCCCC		37.71OGP
567O-linked_GlycosylationHSNHAPVTQAREGNL
CCCCCCCCCCCCCCC		18.5655829627
612UbiquitinationMAAAAQDKGQVGPGA
HHHHHHCCCCCCCCC		38.8821906983
628UbiquitinationPLELEGVKVPLEPGP
CCEEECEEEECCCCC		49.3321963094
636UbiquitinationVPLEPGPKATEGGGE
EECCCCCCCCCCCCC		74.0729967540
638PhosphorylationLEPGPKATEGGGEAL
CCCCCCCCCCCCCCC		41.0929514088
647PhosphorylationGGGEALPSGSECEVP
CCCCCCCCCCEEEEE		56.6627050516
649PhosphorylationGEALPSGSECEVPLM
CCCCCCCCEEEEEEC		43.3329514088
665PhosphorylationFPGPGLQSPLHAKPY
CCCCCCCCCCCCCCC		34.1822199227
670UbiquitinationLQSPLHAKPYI----
CCCCCCCCCCC----		27.8329967540
672PhosphorylationSPLHAKPYI------
CCCCCCCCC------		20.6818669648
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 VASN_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VASN_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 VASN_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TGFB1_HUMANTGFB1physical
15247411
TGFB2_HUMANTGFB2physical
15247411
TGFB3_HUMANTGFB3physical
15247411
ZCH18_HUMANZC3H18physical
22939629
PACN2_HUMANPACSIN2physical
22863883
JAG2_HUMANJAG2physical
28514442
ABCD1_HUMANABCD1physical
28514442
TAF12_HUMANTAF12physical
28514442
CNPY3_HUMANCNPY3physical
28514442
THADA_HUMANTHADAphysical
28514442
NOTC2_HUMANNOTCH2physical
28514442
XPO4_HUMANXPO4physical
28514442
TMX4_HUMANTMX4physical
28514442
AP3B1_HUMANAP3B1physical
28514442
S11IP_HUMANSTK11IPphysical
28514442
DIAP3_HUMANDIAPH3physical
28514442
LRC40_HUMANLRRC40physical
28514442
XPO7_HUMANXPO7physical
28514442
MON2_HUMANMON2physical
28514442
CIP2A_HUMANKIAA1524physical
28514442
SAAL1_HUMANSAAL1physical
28514442
TNPO3_HUMANTNPO3physical
28514442
TNPO2_HUMANTNPO2physical
28514442
GLMN_HUMANGLMNphysical
28514442
ATR_HUMANATRphysical
28514442
NUP85_HUMANNUP85physical
28514442
TBA4A_HUMANTUBA4Aphysical
28514442
NU160_HUMANNUP160physical
28514442
LTN1_HUMANLTN1physical
28514442
LEG1_HUMANLGALS1physical
28514442
STAT3_HUMANSTAT3physical
28514442
JIP4_HUMANSPAG9physical
28514442
AP3M1_HUMANAP3M1physical
28514442
FBX2_HUMANFBXO2physical
28514442
UFSP2_HUMANUFSP2physical
28514442
CHPT1_HUMANCHPT1physical
28514442
TBB8_HUMANTUBB8physical
28514442
S39AB_HUMANSLC39A11physical
28514442
BIG2_HUMANARFGEF2physical
28514442
CNO6L_HUMANCNOT6Lphysical
28514442
NUP98_HUMANNUP98physical
28514442
CNOT9_HUMANRQCD1physical
28514442
CARM1_HUMANCARM1physical
28514442
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 VASN_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD.";
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
Mol. Cell. Proteomics 0:0-0(2011).
Cited for: GLYCOSYLATION AT ASN-117, STRUCTURE OF CARBOHYDRATES, AND MASSSPECTROMETRY.
"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-101 AND ASN-273, 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-117 AND ASN-273, AND MASSSPECTROMETRY.

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