| UniProt ID | CD86_HUMAN | |
|---|---|---|
| UniProt AC | P42081 | |
| Protein Name | T-lymphocyte activation antigen CD86 | |
| Gene Name | CD86 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 329 | |
| Subcellular Localization |
Cell membrane Single-pass type I membrane protein. |
|
| Protein Description | Receptor involved in the costimulatory signal essential for T-lymphocyte proliferation and interleukin-2 production, by binding CD28 or CTLA-4. May play a critical role in the early events of T-cell activation and costimulation of naive T-cells, such as deciding between immunity and anergy that is made by T-cells within 24 hours after activation. Isoform 2 interferes with the formation of CD86 clusters, and thus acts as a negative regulator of T-cell activation.; (Microbial infection) Acts as a receptor for adenovirus subgroup B.. | |
| Protein Sequence | MDPQCTMGLSNILFVMAFLLSGAAPLKIQAYFNETADLPCQFANSQNQSLSELVVFWQDQENLVLNEVYLGKEKFDSVHSKYMGRTSFDSDSWTLRLHNLQIKDKGLYQCIIHHKKPTGMIRIHQMNSELSVLANFSQPEIVPISNITENVYINLTCSSIHGYPEPKKMSVLLRTKNSTIEYDGVMQKSQDNVTELYDVSISLSVSFPDVTSNMTIFCILETDKTRLLSSPFSIELEDPQPPPDHIPWITAVLPTVIICVMVFCLILWKWKKKKRPRNSYKCGTNTMEREESEQTKKREKIHIPERSDEAQRVFKSSKTSSCDKSDTCF | |
| 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 |
|---|---|---|---|---|---|
| 33 | N-linked_Glycosylation | LKIQAYFNETADLPC CEEHHHHCCCCCCCC | 32.79 | UniProtKB CARBOHYD | |
| 47 | N-linked_Glycosylation | CQFANSQNQSLSELV CCCCCCCCCCHHHEE | 32.98 | UniProtKB CARBOHYD | |
| 77 | Phosphorylation | LGKEKFDSVHSKYMG CCHHHCCCCCHHHCC | 25.51 | - | |
| 80 | Phosphorylation | EKFDSVHSKYMGRTS HHCCCCCHHHCCCCC | 24.27 | - | |
| 108 | Phosphorylation | QIKDKGLYQCIIHHK EECCCEEEEEEEECC | 15.26 | 25884760 | |
| 135 | N-linked_Glycosylation | SELSVLANFSQPEIV HHHEEEECCCCCEEE | 32.70 | UniProtKB CARBOHYD | |
| 146 | N-linked_Glycosylation | PEIVPISNITENVYI CEEEECCCCCCCEEE | 46.01 | UniProtKB CARBOHYD | |
| 154 | N-linked_Glycosylation | ITENVYINLTCSSIH CCCCEEEEEEEEHHC | 16.17 | UniProtKB CARBOHYD | |
| 175 | Phosphorylation | KMSVLLRTKNSTIEY EEEEEEECCCCEEEE | 34.25 | 22496350 | |
| 177 | N-linked_Glycosylation | SVLLRTKNSTIEYDG EEEEECCCCEEEECC | 43.71 | UniProtKB CARBOHYD | |
| 192 | N-linked_Glycosylation | VMQKSQDNVTELYDV EEECCCCCCEEEEEE | 34.67 | UniProtKB CARBOHYD | |
| 213 | N-linked_Glycosylation | SFPDVTSNMTIFCIL ECCCCCCCEEEEEEE | 23.42 | UniProtKB CARBOHYD | |
| 223 (in isoform 4) | Phosphorylation | - | 40.74 | - | |
| 224 (in isoform 4) | Phosphorylation | - | 42.86 | - | |
| 227 (in isoform 4) | Phosphorylation | - | 7.05 | - | |
| 230 (in isoform 4) | Phosphorylation | - | 29.90 | - | |
| 284 | Phosphorylation | RNSYKCGTNTMEREE CCCCCCCCCHHCHHH | 36.67 | 27486199 | |
| 286 | Phosphorylation | SYKCGTNTMEREESE CCCCCCCHHCHHHHH | 21.90 | 27486199 | |
| 292 | Phosphorylation | NTMEREESEQTKKRE CHHCHHHHHHHHHHH | 30.19 | 27486199 | |
| 295 | Phosphorylation | EREESEQTKKREKIH CHHHHHHHHHHHHCC | 34.19 | 27486199 | |
| 315 | Acetylation | DEAQRVFKSSKTSSC HHHHHHHHCCCCCCC | 51.46 | 7971967 | |
| 316 | Phosphorylation | EAQRVFKSSKTSSCD HHHHHHHCCCCCCCC | 26.13 | 30108239 | |
| 317 | Phosphorylation | AQRVFKSSKTSSCDK HHHHHHCCCCCCCCC | 40.31 | 30108239 | |
| 319 | Phosphorylation | RVFKSSKTSSCDKSD HHHHCCCCCCCCCCC | 28.02 | 30108239 | |
| 320 | Phosphorylation | VFKSSKTSSCDKSDT HHHCCCCCCCCCCCC | 32.48 | 30108239 | |
| 321 | Phosphorylation | FKSSKTSSCDKSDTC HHCCCCCCCCCCCCC | 31.41 | 30108239 | |
| 325 | Phosphorylation | KTSSCDKSDTCF--- CCCCCCCCCCCC--- | 25.54 | 30108239 | |
| 327 | Phosphorylation | SSCDKSDTCF----- CCCCCCCCCC----- | 23.93 | 30108239 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| - | K | Ubiquitination | E3 ubiquitin ligase | MARCHF1 | Q8TCQ1 | PMID:21220452 |
| - | K | Ubiquitination | E3 ubiquitin ligase | MARCHF8 | Q5T0T0 | PMID:12582153 |
| - | K | Ubiquitination | E3 ubiquitin ligase | MARCHF2 | Q9P0N8 | PMID:14722266 |
| - | K | Ubiquitination | E3 ubiquitin ligase | K5 | P90489 | PMID:22199232 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CD86_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 CD86_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| MARH1_HUMAN | MARCH1 | physical | 21896490 | |
| PARP1_HUMAN | PARP1 | physical | 21988832 | |
| CTLA4_HUMAN | CTLA4 | physical | 25241761 | |
| CD80_HUMAN | CD80 | physical | 25241761 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| D03203 | Abatacept (genetical recombination) (JAN); Abatacept (USAN/INN); Orencia (TN) | |||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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