UniProt ID | HAVR2_HUMAN | |
---|---|---|
UniProt AC | Q8TDQ0 | |
Protein Name | Hepatitis A virus cellular receptor 2 | |
Gene Name | HAVCR2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 301 | |
Subcellular Localization |
Membrane Single-pass type I membrane protein . Cell junction . Localizes to the immunological synapse between CD8+ T-cells and target cells. |
|
Protein Description | Cell surface receptor implicated in modulating innate and adaptive immune responses. Generally accepted to have an inhibiting function. Reports on stimulating functions suggest that the activity may be influenced by the cellular context and/or the respective ligand. [PubMed: 24825777 Regulates macrophage activation] | |
Protein Sequence | MFSHLPFDCVLLLLLLLLTRSSEVEYRAEVGQNAYLPCFYTPAAPGNLVPVCWGKGACPVFECGNVVLRTDERDVNYWTSRYWLNGDFRKGDVSLTIENVTLADSGIYCCRIQIPGIMNDEKFNLKLVIKPAKVTPAPTRQRDFTAAFPRMLTTRGHGPAETQTLGSLPDINLTQISTLANELRDSRLANDLRDSGATIRIGIYIGAGICAGLALALIFGALIFKWYSHSKEKIQNLSLISLANLPPSGLANAVAEGIRSEENIYTIEENVYEVEEPNEYYCYVSSRQQPSQPLGCRFAMP | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
105 | Phosphorylation | ENVTLADSGIYCCRI ECEEECCCCEEEEEE | 22.83 | 30377224 | |
108 | Phosphorylation | TLADSGIYCCRIQIP EECCCCEEEEEEECC | 6.77 | 30377224 | |
126 | Acetylation | NDEKFNLKLVIKPAK CCCCCCEEEEEECCC | 41.64 | 7370233 | |
145 | O-linked_Glycosylation | PTRQRDFTAAFPRML CCCCCCHHHHHCCHH | 22.74 | 22171320 | |
153 | Phosphorylation | AAFPRMLTTRGHGPA HHHCCHHHCCCCCCC | 12.71 | - | |
154 | Phosphorylation | AFPRMLTTRGHGPAE HHCCHHHCCCCCCCC | 30.60 | - | |
172 | N-linked_Glycosylation | LGSLPDINLTQISTL CCCCCCCCHHHHHHH | 44.40 | UniProtKB CARBOHYD | |
174 | O-linked_Glycosylation | SLPDINLTQISTLAN CCCCCCHHHHHHHHH | 21.26 | OGP | |
178 | O-linked_Glycosylation | INLTQISTLANELRD CCHHHHHHHHHHHHH | 31.36 | OGP | |
238 | Phosphorylation | KEKIQNLSLISLANL HHHHHCEEEEECCCC | 31.07 | 28857561 | |
241 | Phosphorylation | IQNLSLISLANLPPS HHCEEEEECCCCCCC | 27.07 | 28857561 | |
265 | Phosphorylation | IRSEENIYTIEENVY CCCCCCEEEEECCEE | 17.16 | 17069754 | |
272 | Phosphorylation | YTIEENVYEVEEPNE EEEECCEEECCCCCC | 26.32 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
265 | Y | Phosphorylation | Kinase | ITK | Q08881 | Uniprot |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HAVR2_HUMAN !! |
* 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 HAVR2_HUMAN !! |
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. |
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O-linked Glycosylation | |
Reference | PubMed |
"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 THR-145, STRUCTURE OF CARBOHYDRATES, AND MASSSPECTROMETRY. |