VTNC_HUMAN - dbPTM
VTNC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VTNC_HUMAN
UniProt AC P04004
Protein Name Vitronectin
Gene Name VTN
Organism Homo sapiens (Human).
Sequence Length 478
Subcellular Localization Secreted, extracellular space.
Protein Description Vitronectin is a cell adhesion and spreading factor found in serum and tissues. Vitronectin interact with glycosaminoglycans and proteoglycans. Is recognized by certain members of the integrin family and serves as a cell-to-substrate adhesion molecule. Inhibitor of the membrane-damaging effect of the terminal cytolytic complement pathway.; Somatomedin-B is a growth hormone-dependent serum factor with protease-inhibiting activity..
Protein Sequence MAPLRPLLILALLAWVALADQESCKGRCTEGFNVDKKCQCDELCSYYQSCCTDYTAECKPQVTRGDVFTMPEDEYTVYDDGEEKNNATVHEQVGGPSLTSDLQAQSKGNPEQTPVLKPEEEAPAPEVGASKPEGIDSRPETLHPGRPQPPAEEELCSGKPFDAFTDLKNGSLFAFRGQYCYELDEKAVRPGYPKLIRDVWGIEGPIDAAFTRINCQGKTYLFKGSQYWRFEDGVLDPDYPRNISDGFDGIPDNVDAALALPAHSYSGRERVYFFKGKQYWEYQFQHQPSQEECEGSSLSAVFEHFAMMQRDSWEDIFELLFWGRTSAGTRQPQFISRDWHGVPGQVDAAMAGRIYISGMAPRPSLAKKQRFRHRNRKGYRSQRGHSRGRNQNSRRPSRATWLSLFSSEESNLGANNYDDYRMDWLVPATCEPIQSVFFFSGDKYYRVNLRTRRVDTVDPPYPRSIAQYWLGCPAPGHL
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
69PhosphorylationVTRGDVFTMPEDEYT
CCCCCCEECCCCEEE		31.5026657352
75SulfationFTMPEDEYTVYDDGE
EECCCCEEEEECCCC		17.52-
75SulfationFTMPEDEYTVYDDGE
EECCCCEEEEECCCC		17.5217558413
75PhosphorylationFTMPEDEYTVYDDGE
EECCCCEEEEECCCC		17.5226657352
76PhosphorylationTMPEDEYTVYDDGEE
ECCCCEEEEECCCCC		15.5626657352
78SulfationPEDEYTVYDDGEEKN
CCCEEEEECCCCCCC		10.66-
78PhosphorylationPEDEYTVYDDGEEKN
CCCEEEEECCCCCCC		10.6626657352
78SulfationPEDEYTVYDDGEEKN
CCCEEEEECCCCCCC		10.6617558413
86N-linked_GlycosylationDDGEEKNNATVHEQV
CCCCCCCCCCCEEEC		48.3218638581
86N-linked_GlycosylationDDGEEKNNATVHEQV
CCCCCCCCCCCEEEC		48.3217623646
88PhosphorylationGEEKNNATVHEQVGG
CCCCCCCCCEEECCC		25.2326657352
88O-linked_GlycosylationGEEKNNATVHEQVGG
CCCCCCCCCEEECCC		25.23OGP
97O-linked_GlycosylationHEQVGGPSLTSDLQA
EEECCCCCHHHHHHH		47.78OGP
99O-linked_GlycosylationQVGGPSLTSDLQAQS
ECCCCCHHHHHHHHH		25.24OGP
100O-linked_GlycosylationVGGPSLTSDLQAQSK
CCCCCHHHHHHHHHC		41.43OGP
106PhosphorylationTSDLQAQSKGNPEQT
HHHHHHHHCCCCCCC		45.6129759185
130O-linked_GlycosylationPAPEVGASKPEGIDS
CCCCCCCCCCCCCCC		42.70OGP
130PhosphorylationPAPEVGASKPEGIDS
CCCCCCCCCCCCCCC		42.7026657352
137PhosphorylationSKPEGIDSRPETLHP
CCCCCCCCCCCCCCC		48.0627130503
141O-linked_GlycosylationGIDSRPETLHPGRPQ
CCCCCCCCCCCCCCC		32.80OGP
141PhosphorylationGIDSRPETLHPGRPQ
CCCCCCCCCCCCCCC		32.8027130503
157PhosphorylationPAEEELCSGKPFDAF
CCHHHHHCCCCCCCC		63.5824505115
169N-linked_GlycosylationDAFTDLKNGSLFAFR
CCCEECCCCCEEEEE		53.2117623646
169N-linked_GlycosylationDAFTDLKNGSLFAFR
CCCEECCCCCEEEEE		53.2117623646
171PhosphorylationFTDLKNGSLFAFRGQ
CEECCCCCEEEEECC		29.7022817900
179PhosphorylationLFAFRGQYCYELDEK
EEEEECCEEEEECHH		10.38-
218AcetylationTRINCQGKTYLFKGS
EEEECCCCEEEECCC		14.2327178108
219PhosphorylationRINCQGKTYLFKGSQ
EEECCCCEEEECCCE		32.0824505115
220PhosphorylationINCQGKTYLFKGSQY
EECCCCEEEECCCEE		17.3924505115
225PhosphorylationKTYLFKGSQYWRFED
CEEEECCCEEEEEEC		22.2324505115
227PhosphorylationYLFKGSQYWRFEDGV
EEECCCEEEEEECCC		10.5524505115
239PhosphorylationDGVLDPDYPRNISDG
CCCCCCCCCCCCCCC		14.9624505115
242N-linked_GlycosylationLDPDYPRNISDGFDG
CCCCCCCCCCCCCCC		33.3417623646
242N-linked_GlycosylationLDPDYPRNISDGFDG
CCCCCCCCCCCCCCC		33.3417623646
244PhosphorylationPDYPRNISDGFDGIP
CCCCCCCCCCCCCCC		34.9224505115
275AcetylationRERVYFFKGKQYWEY
CCEEEEEECCEEEEE		56.1327178108
282SulfationKGKQYWEYQFQHQPS
ECCEEEEEEECCCCC		10.65-
282SulfationKGKQYWEYQFQHQPS
ECCEEEEEEECCCCC		10.65-
312PhosphorylationFAMMQRDSWEDIFEL
HHHHHCCCHHHHHHH		34.2625072903
325PhosphorylationELLFWGRTSAGTRQP
HHHHCCCCCCCCCCC		20.9927251275
355PhosphorylationAAMAGRIYISGMAPR
HHHCCCEEEECCCCC		6.4129691806
357PhosphorylationMAGRIYISGMAPRPS
HCCCEEEECCCCCCC		12.9228270605
364PhosphorylationSGMAPRPSLAKKQRF
ECCCCCCCHHHHHHH		42.0929691806
381PhosphorylationRNRKGYRSQRGHSRG
HCCCCCHHHCCCCCC		18.7522817900
386PhosphorylationYRSQRGHSRGRNQNS
CHHHCCCCCCCCCCC		38.9722817900
393PhosphorylationSRGRNQNSRRPSRAT
CCCCCCCCCCCCHHH		21.6522817900
397PhosphorylationNQNSRRPSRATWLSL
CCCCCCCCHHHHHHH		32.511696913
400PhosphorylationSRRPSRATWLSLFSS
CCCCCHHHHHHHHCC		26.3128270605
403PhosphorylationPSRATWLSLFSSEES
CCHHHHHHHHCCCCC		20.9429691806
406PhosphorylationATWLSLFSSEESNLG
HHHHHHHCCCCCCCC		41.9826657352
407PhosphorylationTWLSLFSSEESNLGA
HHHHHHCCCCCCCCC		37.7426657352
410PhosphorylationSLFSSEESNLGANNY
HHHCCCCCCCCCCCC		33.0526657352
417SulfationSNLGANNYDDYRMDW
CCCCCCCCCCCCCEE		15.25-
417SulfationSNLGANNYDDYRMDW
CCCCCCCCCCCCCEE		15.25-
420PhosphorylationGANNYDDYRMDWLVP
CCCCCCCCCCEEECC		12.63-
420SulfationGANNYDDYRMDWLVP
CCCCCCCCCCEEECC		12.63-
420SulfationGANNYDDYRMDWLVP
CCCCCCCCCCEEECC		12.63-
429O-linked_GlycosylationMDWLVPATCEPIQSV
CEEECCCCCCCEEEE		16.01OGP
456PhosphorylationLRTRRVDTVDPPYPR
CCCCCCCCCCCCCCC		24.7723403867
461PhosphorylationVDTVDPPYPRSIAQY
CCCCCCCCCCCHHHH		19.3723403867
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
69TPhosphorylationKinaseCSNK2A1P68400
GPS
69TPhosphorylationKinaseCK2_GROUP-PhosphoELM
69TPhosphorylationKinaseCK2-Uniprot
69TPhosphorylationKinaseCK2-FAMILY-GPS
76TPhosphorylationKinaseCK2-FAMILY-GPS
76TPhosphorylationKinaseCK2-Uniprot
76TPhosphorylationKinaseCK2_GROUP-PhosphoELM
76TPhosphorylationKinaseCSNK2A1P68400
GPS
381SPhosphorylationKinasePRKCAP17252
GPS
381SPhosphorylationKinasePKC-FAMILY-GPS
386SPhosphorylationKinasePRKCAP17252
GPS
393SPhosphorylationKinasePRKCAP17252
GPS
393SPhosphorylationKinasePKC-FAMILY-GPS
397SPhosphorylationKinasePRKCAP17252
GPS
397SPhosphorylationKinasePKA-FAMILY-GPS
397SPhosphorylationKinasePKC-FAMILY-GPS
397SPhosphorylationKinasePRKACAP17612
GPS
397SPhosphorylationKinasePKA-Uniprot
397SPhosphorylationKinasePKA_GROUP-PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
69TPhosphorylation

9733784
76TPhosphorylation

9733784
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
393Phosphorylation400 (7)T ⇒ Mrs704
  • Osteoprotegerin levels
25080503
397Phosphorylation400 (3)T ⇒ Mrs704
  • Osteoprotegerin levels
25080503
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PAI1_HUMANSERPINE1physical
11113116
IGF2_HUMANIGF2physical
10342887
TGFB1_HUMANTGFB1physical
11796824
TGFB2_HUMANTGFB2physical
11796824
VEGFA_HUMANVEGFAphysical
11796824
EGF_HUMANEGFphysical
11796824
FGF2_HUMANFGF2physical
11796824
KNG1_HUMANKNG1physical
10887113
PVR_HUMANPVRphysical
11437656
COLI_HUMANPOMCphysical
2475499
A4_HUMANAPPphysical
21832049
WDR18_HUMANWDR18physical
22939629
GOPC_HUMANGOPCphysical
25416956
UACA_HUMANUACAphysical
28514442
TARA_HUMANTRIOBPphysical
28514442
GLI4_HUMANGLI4physical
28514442
RAI14_HUMANRAI14physical
28514442
OTUD4_HUMANOTUD4physical
28514442
CU002_HUMANC21orf2physical
28514442
ZN483_HUMANZNF483physical
28514442
GRIN1_HUMANGPRIN1physical
28514442
ZN696_HUMANZNF696physical
28514442
MPRIP_HUMANMPRIPphysical
28514442
RNF14_HUMANRNF14physical
28514442
MBOA5_HUMANLPCAT3physical
28514442
RPP40_HUMANRPP40physical
28514442
ZN777_HUMANZNF777physical
28514442
ITB5_HUMANITGB5physical
28514442
PTCD2_HUMANPTCD2physical
28514442
FBX33_HUMANFBXO33physical
28514442
RPP29_HUMANPOP4physical
28514442
WDR33_HUMANWDR33physical
28514442
RTN2_HUMANRTN2physical
28514442
RRP1_HUMANRRP1physical
28514442
MRS2_HUMANMRS2physical
28514442
TTLL4_HUMANTTLL4physical
28514442
HAT1_HUMANHAT1physical
28514442
HXB9_HUMANHOXB9physical
28514442
ISOC1_HUMANISOC1physical
28514442
KTN1_HUMANKTN1physical
28514442
HACD2_HUMANPTPLBphysical
28514442
NP1L1_HUMANNAP1L1physical
28514442
FAKD3_HUMANFASTKD3physical
28514442
CUL7_HUMANCUL7physical
28514442
ARMX3_HUMANARMCX3physical
28514442
NEK1_HUMANNEK1physical
28514442
RBM5_HUMANRBM5physical
28514442
POP1_HUMANPOP1physical
28514442
RHGBA_HUMANARHGAP11Aphysical
28514442
LEMD2_HUMANLEMD2physical
28514442
TRM11_HUMANTRMT11physical
28514442
CDK4_HUMANCDK4physical
28514442
DCAF1_HUMANVPRBPphysical
28514442
C1QBP_HUMANC1QBPphysical
28514442
SIA7D_HUMANST6GALNAC4physical
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 VTNC_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-86; ASN-169 AND ASN-242,AND MASS SPECTROMETRY.
"Determination of the sites of tyrosine O-sulfation in peptides andproteins.";
Yu Y., Hoffhines A.J., Moore K.L., Leary J.A.;
Nat. Methods 4:583-588(2007).
Cited for: SULFATION AT TYR-75 AND TYR-78, PHOSPHORYLATION AT SER-312,GLYCOSYLATION AT ASN-86, AND MASS SPECTROMETRY.
"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-86; ASN-169 AND ASN-242,AND MASS SPECTROMETRY.
"Screening for N-glycosylated proteins by liquid chromatography massspectrometry.";
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
Proteomics 4:454-465(2004).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-86; ASN-169 AND ASN-242,AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"An initial characterization of the serum phosphoproteome.";
Zhou W., Ross M.M., Tessitore A., Ornstein D., Vanmeter A.,Liotta L.A., Petricoin E.F. III;
J. Proteome Res. 8:5523-5531(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312, TISSUE SPECIFICITY,AND MASS SPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312, AND MASSSPECTROMETRY.
"Determination of the sites of tyrosine O-sulfation in peptides andproteins.";
Yu Y., Hoffhines A.J., Moore K.L., Leary J.A.;
Nat. Methods 4:583-588(2007).
Cited for: SULFATION AT TYR-75 AND TYR-78, PHOSPHORYLATION AT SER-312,GLYCOSYLATION AT ASN-86, AND MASS SPECTROMETRY.
"Phosphoproteomic analysis of the human pituitary.";
Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
Pituitary 9:109-120(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-312, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171, AND MASSSPECTROMETRY.
"The phosphorylation of the two-chain form of vitronectin by proteinkinase A is heparin dependent.";
Chain D., Korc-Grodzicki B., Kreizman T., Shaltiel S.;
FEBS Lett. 269:221-225(1990).
Cited for: PHOSPHORYLATION AT SER-397.
"Phosphorylation of vitronectin by a protein kinase in human plasma.Identification of a unique phosphorylation site in the heparin-bindingdomain.";
McGuire E.A., Peacock M.E., Inhorn R.C., Siegel N.R., Tollefsen D.M.;
J. Biol. Chem. 263:1942-1945(1988).
Cited for: PROTEIN SEQUENCE OF 393-400, AND PHOSPHORYLATION AT SER-397.
"Phosphorylation of vitronectin by casein kinase II. Identification ofthe sites and their promotion of cell adhesion and spreading.";
Seger D., Gechtman Z., Shaltiel S.;
J. Biol. Chem. 273:24805-24813(1998).
Cited for: PHOSPHORYLATION AT THR-69 AND THR-76, AND MUTAGENESIS OF THR-69 ANDTHR-76.
Sulfation
ReferencePubMed
"Determination of the sites of tyrosine O-sulfation in peptides andproteins.";
Yu Y., Hoffhines A.J., Moore K.L., Leary J.A.;
Nat. Methods 4:583-588(2007).
Cited for: SULFATION AT TYR-75 AND TYR-78, PHOSPHORYLATION AT SER-312,GLYCOSYLATION AT ASN-86, AND MASS SPECTROMETRY.

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