| UniProt ID | JAM3_HUMAN | |
|---|---|---|
| UniProt AC | Q9BX67 | |
| Protein Name | Junctional adhesion molecule C | |
| Gene Name | JAM3 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 310 | |
| Subcellular Localization |
Cell membrane Single-pass type I membrane protein . Cell junction, desmosome . Secreted, extracellular space . In epithelial cells, it is expressed at desmosomes but not at tight junctions (PubMed:15194813). Localizes at the cell surface of endothe |
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| Protein Description | Participates in cell-cell adhesion. It is a counter-receptor for ITGAM, mediating leukocyte-platelet interactions and is involved in the regulation of transepithelial migration of polymorphonuclear neutrophils (PMN). The soluble form is a mediator of angiogenesis.. | |
| Protein Sequence | MALRRPPRLRLCARLPDFFLLLLFRGCLIGAVNLKSSNRTPVVQEFESVELSCIITDSQTSDPRIEWKKIQDEQTTYVFFDNKIQGDLAGRAEILGKTSLKIWNVTRRDSALYRCEVVARNDRKEIDEIVIELTVQVKPVTPVCRVPKAVPVGKMATLHCQESEGHPRPHYSWYRNDVPLPTDSRANPRFRNSSFHLNSETGTLVFTAVHKDDSGQYYCIASNDAGSARCEEQEMEVYDLNIGGIIGGVLVVLAVLALITLGICCAYRRGYFINNKQDGESYKNPGKPDGVNYIRTDEEGDFRHKSSFVI | |
| 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 |
|---|---|---|---|---|---|
| 53 | Glutathionylation | FESVELSCIITDSQT EEEEEEEEEEECCCC | 4.00 | 22555962 | |
| 75 | O-linked_Glycosylation | KKIQDEQTTYVFFDN EECCCCEEEEEEECC | 20.32 | OGP | |
| 97 | Ubiquitination | GRAEILGKTSLKIWN CCCEECCCCEEEEEE | 31.34 | - | |
| 104 | N-linked_Glycosylation | KTSLKIWNVTRRDSA CCEEEEEEEECCCCH | 28.84 | UniProtKB CARBOHYD | |
| 124 | Acetylation | VVARNDRKEIDEIVI EEECCCHHHCCEEEE | 62.98 | 19818981 | |
| 138 | Acetylation | IELTVQVKPVTPVCR EEEEEEEECCCCCEE | 19.38 | 19818989 | |
| 148 | Ubiquitination | TPVCRVPKAVPVGKM CCCEECCCCEECCCE | 60.19 | - | |
| 192 | N-linked_Glycosylation | RANPRFRNSSFHLNS CCCCCCCCCCEEEEC | 39.02 | 19349973 | |
| 192 | N-linked_Glycosylation | RANPRFRNSSFHLNS CCCCCCCCCCEEEEC | 39.02 | 19349973 | |
| 198 | N-linked_Glycosylation | RNSSFHLNSETGTLV CCCCEEEECCCCEEE | 29.27 | 19349973 | |
| 198 | N-linked_Glycosylation | RNSSFHLNSETGTLV CCCCEEEECCCCEEE | 29.27 | 19349973 | |
| 225 | Ubiquitination | YCIASNDAGSARCEE EEEEECCCCCCCCCC | 20.35 | 32142685 | |
| 232 | Ubiquitination | AGSARCEEQEMEVYD CCCCCCCCCEEEEEE | 56.31 | 21890473 | |
| 232 | Ubiquitination | AGSARCEEQEMEVYD CCCCCCCCCEEEEEE | 56.31 | 22053931 | |
| 236 | Ubiquitination | RCEEQEMEVYDLNIG CCCCCEEEEEECCCC | 36.85 | 33845483 | |
| 264 | S-palmitoylation | ALITLGICCAYRRGY HHHHHHHHHHHHCCC | 0.74 | 28196865 | |
| 265 | S-palmitoylation | LITLGICCAYRRGYF HHHHHHHHHHHCCCC | 3.35 | 28196865 | |
| 276 | Ubiquitination | RGYFINNKQDGESYK CCCCCCCCCCCCCCC | 45.32 | 32142685 | |
| 281 | Phosphorylation | NNKQDGESYKNPGKP CCCCCCCCCCCCCCC | 47.11 | 26657352 | |
| 282 | Phosphorylation | NKQDGESYKNPGKPD CCCCCCCCCCCCCCC | 15.52 | 26657352 | |
| 283 | Ubiquitination | KQDGESYKNPGKPDG CCCCCCCCCCCCCCC | 66.98 | 22053931 | |
| 287 | Ubiquitination | ESYKNPGKPDGVNYI CCCCCCCCCCCCCEE | 40.99 | 33845483 | |
| 293 | Phosphorylation | GKPDGVNYIRTDEEG CCCCCCCEEECCCCC | 6.86 | 25884760 | |
| 305 | Ubiquitination | EEGDFRHKSSFVI-- CCCCCCCCCCCCC-- | 43.47 | - | |
| 306 | Phosphorylation | EGDFRHKSSFVI--- CCCCCCCCCCCC--- | 23.92 | 30266825 | |
| 307 | Phosphorylation | GDFRHKSSFVI---- CCCCCCCCCCC---- | 28.47 | 30266825 | |
| 328 | Ubiquitination | ------------------------- ------------------------- | 21890473 |
| 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 JAM3_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of JAM3_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 JAM3_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| PARD3_HUMAN | PARD3 | physical | 12953056 | |
| JAM2_HUMAN | JAM2 | physical | 21982860 | |
| JAM3_HUMAN | JAM3 | physical | 21982860 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| H01301 | Hemorrhagic destruction of the brain, subependymal calcification, and cataracts | |||||
| OMIM Disease | ||||||
| 613730 | Hemorrhagic destruction of the brain with subependymal calcification and cataracts (HDBSCC) | |||||
| 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 |
| "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-192 AND ASN-198, AND MASSSPECTROMETRY. | |
