UniProt ID | LYVE1_HUMAN | |
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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 |
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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 | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
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42 | Phosphorylation | SCRIMGITLVSKKAN HHEEECEEEEEHHHH | 18.51 | - | |
53 | N-linked_Glycosylation | KKANQQLNFTEAKEA HHHHCCCCHHHHHHH | 37.14 | 16335952 | |
55 | Phosphorylation | ANQQLNFTEAKEACR HHCCCCHHHHHHHHH | 33.68 | 28842319 | |
67 | Phosphorylation | ACRLLGLSLAGKDQV HHHHHCCHHCCHHHH | 17.86 | - | |
76 | Phosphorylation | AGKDQVETALKASFE CCHHHHHHHHHHHEE | 38.13 | 29083192 | |
130 | N-linked_Glycosylation | QFAAYCYNSSDTWTN HEHHHHCCCCCCCCC | 31.32 | UniProtKB CARBOHYD | |
146 | Phosphorylation | CIPEIITTKDPIFNT CCCEECCCCCCCCCC | 24.04 | - | |
216 | O-linked_Glycosylation | TSTMSTETEPFVENK CCCCCCCCCCCCCCH | 49.39 | OGP | |
280 | Phosphorylation | QQKEMIETKVVKEEK HHHHHEEEHHHHHHH | 20.43 | 22817900 | |
297 | Phosphorylation | DSNPNEESKKTDKNP CCCCCHHHHCCCCCH | 33.02 | 17693683 | |
298 | Methylation | SNPNEESKKTDKNPE CCCCHHHHCCCCCHH | 64.07 | 23644510 | |
308 | Ubiquitination | DKNPEESKSPSKTTV CCCHHHCCCCCHHHE | 70.44 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of LYVE1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of LYVE1_HUMAN !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
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Oops, there are no SNP-PTM records of LYVE1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
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KR108_HUMAN | KRTAP10-8 | physical | 25416956 | |
KR103_HUMAN | KRTAP10-3 | physical | 25416956 |
Kegg Disease | ||||||
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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. |
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N-linked Glycosylation | |
Reference | PubMed |
"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 | |
Reference | PubMed |
"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. |