LYVE1_HUMAN - dbPTM
LYVE1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LYVE1_HUMAN
UniProt AC Q9Y5Y7
Protein Name Lymphatic vessel endothelial hyaluronic acid receptor 1
Gene Name LYVE1
Organism Homo sapiens (Human).
Sequence Length 322
Subcellular Localization Membrane
Single-pass type I membrane protein . Localized to the plasma membrane and in vesicles near extranuclear membranes which may represent trans-Golgi network (TGN) and endosomes/prelysosomeal compartments. Undergoes ligand-dependent internali
Protein Description Ligand-specific transporter trafficking between intracellular organelles (TGN) and the plasma membrane. Plays a role in autocrine regulation of cell growth mediated by growth regulators containing cell surface retention sequence binding (CRS). May act as a hyaluronan (HA) transporter, either mediating its uptake for catabolism within lymphatic endothelial cells themselves, or its transport into the lumen of afferent lymphatic vessels for subsequent re-uptake and degradation in lymph nodes..
Protein Sequence MARCFSLVLLLTSIWTTRLLVQGSLRAEELSIQVSCRIMGITLVSKKANQQLNFTEAKEACRLLGLSLAGKDQVETALKASFETCSYGWVGDGFVVISRISPNPKCGKNGVGVLIWKVPVSRQFAAYCYNSSDTWTNSCIPEIITTKDPIFNTQTATQTTEFIVSDSTYSVASPYSTIPAPTTTPPAPASTSIPRRKKLICVTEVFMETSTMSTETEPFVENKAAFKNEAAGFGGVPTALLVLALLFFGAAAGLGFCYVKRYVKAFPFTNKNQQKEMIETKVVKEEKANDSNPNEESKKTDKNPEESKSPSKTTVRCLEAEV
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
42PhosphorylationSCRIMGITLVSKKAN
HHEEECEEEEEHHHH
18.51-
53N-linked_GlycosylationKKANQQLNFTEAKEA
HHHHCCCCHHHHHHH
37.1416335952
55PhosphorylationANQQLNFTEAKEACR
HHCCCCHHHHHHHHH
33.6828842319
67PhosphorylationACRLLGLSLAGKDQV
HHHHHCCHHCCHHHH
17.86-
76PhosphorylationAGKDQVETALKASFE
CCHHHHHHHHHHHEE
38.1329083192
130N-linked_GlycosylationQFAAYCYNSSDTWTN
HEHHHHCCCCCCCCC
31.32UniProtKB CARBOHYD
146PhosphorylationCIPEIITTKDPIFNT
CCCEECCCCCCCCCC
24.04-
216O-linked_GlycosylationTSTMSTETEPFVENK
CCCCCCCCCCCCCCH
49.39OGP
280PhosphorylationQQKEMIETKVVKEEK
HHHHHEEEHHHHHHH
20.4322817900
297PhosphorylationDSNPNEESKKTDKNP
CCCCCHHHHCCCCCH
33.0217693683
298MethylationSNPNEESKKTDKNPE
CCCCHHHHCCCCCHH
64.0723644510
308UbiquitinationDKNPEESKSPSKTTV
CCCHHHCCCCCHHHE
70.44-

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 LYVE1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LYVE1_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 LYVE1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KR108_HUMANKRTAP10-8physical
25416956
KR103_HUMANKRTAP10-3physical
25416956

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 LYVE1_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-53, 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-53, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteome profiling of Wnt3a-mediated signalingnetwork: indicating the involvement of ribonucleoside-diphosphatereductase M2 subunit phosphorylation at residue serine 20 in canonicalWnt signal transduction.";
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S.,Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.;
Mol. Cell. Proteomics 6:1952-1967(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-297, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-280, AND MASSSPECTROMETRY.

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