VCAM1_MOUSE - dbPTM
VCAM1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VCAM1_MOUSE
UniProt AC P29533
Protein Name Vascular cell adhesion protein 1
Gene Name Vcam1
Organism Mus musculus (Mouse).
Sequence Length 739
Subcellular Localization Isoform 1: Cell membrane
Single-pass type I membrane protein.
Isoform 2: Cell membrane
Lipid-anchor, GPI-anchor.
Protein Description Important in cell-cell recognition. Appears to function in leukocyte-endothelial cell adhesion. Interacts with integrin alpha-4/beta-1 (ITGA4/ITGB1) on leukocytes, and mediates both adhesion and signal transduction. The VCAM1/ITGA4/ITGB1 interaction may play a pathophysiologic role both in immune responses and in leukocyte emigration to sites of inflammation..
Protein Sequence MPVKMVAVLGASTVLWILFAVSQAFKIEISPEYKTIAQIGDSMALTCSTTGCESPLFSWRTQIDSPLNAKVRTEGSKSVLTMEPVSFENEHSYLCTATCGSGKLERSIHVDIYSFPKDPEIQFSGPLEVGKPVTVKCLAPDIYPVYRLEIDLFKGDQLMNRQEFSSEEMTKSLETKSLEVTFTPVIEDIGKALVCRAKLHIDQIDSTLKERETVKELQVYISPRNTTISVHPSTRLQEGGAVTMTCSSEGLPAPEIFWGRKLDNEVLQLLSGNATLTLIAMRMEDSGVYVCEGVNLIGRDKAEVELVVQEKPFIVDISPGSQVAAQVGDSVVLTCAAIGCDSPSFSWRTQTDSPLNGVVRNEGAKSTLVLSSVGFEDEHSYLCAVTCLQRTLEKRTQVEVYSFPEDPVIKMSGPLVHGRPVTVNCTVPNVYPFDHLEIELLKGETTLMKKYFLEEMGIKSLETKILETTFIPTIEDTGKSLVCLARLHSGEMESEPKQRQSVQPLYVNVAPKETTIWVSPSPILEEGSPVNLTCSSDGIPAPKILWSRQLNNGELQPLSENTTLTFMSTKRDDSGIYVCEGINEAGISRKSVELIIQVSPKDIQLTVFPSKSVKEGDTVIISCTCGNVPETWIILKKKAKTGDMVLKSVDGSYTIRQAQLQDAGIYECESKTEVGSQLRSLTLDVKGKEHNKDYFSPELLALYCASSLVIPAIGMIVYFARKANMKGSYSLVEAQKSKV
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
165PhosphorylationLMNRQEFSSEEMTKS
HCCHHCCCHHHHHHH
35.7725521595
166PhosphorylationMNRQEFSSEEMTKSL
CCHHCCCHHHHHHHH
42.7825521595
170PhosphorylationEFSSEEMTKSLETKS
CCCHHHHHHHHHCCC
22.2927742792
225N-linked_GlycosylationQVYISPRNTTISVHP
EEEECCCCCEEEECC
44.9819656770
264N-linked_GlycosylationFWGRKLDNEVLQLLS
EECCCCCHHHHHHHC
52.2719656770
273N-linked_GlycosylationVLQLLSGNATLTLIA
HHHHHCCCCEEEEEE
26.7819656770
319 (in isoform 2)GPI-anchor-46.957687058
346PhosphorylationGCDSPSFSWRTQTDS
CCCCCCCCCCCCCCC
21.7128059163
424N-linked_GlycosylationHGRPVTVNCTVPNVY
CCCCEEEECCCCCEE
13.33-
494PhosphorylationLHSGEMESEPKQRQS
HHCCCCCCCCCCCCC
58.87-
531N-linked_GlycosylationLEEGSPVNLTCSSDG
CCCCCCCEEEECCCC
32.77-
552N-linked_GlycosylationLWSRQLNNGELQPLS
EEEEECCCCCCCCCC
54.6419656770
561N-linked_GlycosylationELQPLSENTTLTFMS
CCCCCCCCCEEEEEC
34.6819656770
680PhosphorylationEVGSQLRSLTLDVKG
CCCHHHEEEEEECCC
34.0128833060
729PhosphorylationKANMKGSYSLVEAQK
HCCCCCCCCHHHHHH
18.0729514104
730PhosphorylationANMKGSYSLVEAQKS
CCCCCCCCHHHHHHC
27.8620450229
736UbiquitinationYSLVEAQKSKV----
CCHHHHHHCCC----
60.33-

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 VCAM1_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VCAM1_MOUSE !!

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 VCAM1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of VCAM1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VCAM1_MOUSE

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:identification, glycosite occupancy, and membrane orientation.";
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,Wollscheid B.;
Mol. Cell. Proteomics 8:2555-2569(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-225; ASN-264; ASN-273;ASN-552 AND ASN-561, AND MASS SPECTROMETRY.

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