| UniProt ID | BT3A1_HUMAN | |
|---|---|---|
| UniProt AC | O00481 | |
| Protein Name | Butyrophilin subfamily 3 member A1 | |
| Gene Name | BTN3A1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 513 | |
| Subcellular Localization |
Cell membrane Single-pass type I membrane protein . |
|
| Protein Description | Plays a role in T-cell activation and in the adaptive immune response. Regulates the proliferation of activated T-cells. Regulates the release of cytokines and IFNG by activated T-cells. Mediates the response of T-cells toward infected and transformed cells that are characterized by high levels of phosphorylated metabolites, such as isopentenyl pyrophosphate.. | |
| Protein Sequence | MKMASFLAFLLLNFRVCLLLLQLLMPHSAQFSVLGPSGPILAMVGEDADLPCHLFPTMSAETMELKWVSSSLRQVVNVYADGKEVEDRQSAPYRGRTSILRDGITAGKAALRIHNVTASDSGKYLCYFQDGDFYEKALVELKVAALGSDLHVDVKGYKDGGIHLECRSTGWYPQPQIQWSNNKGENIPTVEAPVVADGVGLYAVAASVIMRGSSGEGVSCTIRSSLLGLEKTASISIADPFFRSAQRWIAALAGTLPVLLLLLGGAGYFLWQQQEEKKTQFRKKKREQELREMAWSTMKQEQSTRVKLLEELRWRSIQYASRGERHSAYNEWKKALFKPADVILDPKTANPILLVSEDQRSVQRAKEPQDLPDNPERFNWHYCVLGCESFISGRHYWEVEVGDRKEWHIGVCSKNVQRKGWVKMTPENGFWTMGLTDGNKYRTLTEPRTNLKLPKPPKKVGVFLDYETGDISFYNAVDGSHIHTFLDVSFSEALYPVFRILTLEPTALTICPA | |
| 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 |
|---|---|---|---|---|---|
| 70 | Phosphorylation | MELKWVSSSLRQVVN HHHHHHHHHHHHHHE | 24.63 | 25954137 | |
| 71 | Phosphorylation | ELKWVSSSLRQVVNV HHHHHHHHHHHHHEE | 21.77 | 25954137 | |
| 83 | Ubiquitination | VNVYADGKEVEDRQS HEEEECCCCCCCCCC | 60.16 | - | |
| 83 (in isoform 2) | Ubiquitination | - | 60.16 | 21906983 | |
| 83 (in isoform 1) | Ubiquitination | - | 60.16 | 21906983 | |
| 98 | Phosphorylation | APYRGRTSILRDGIT CCCCCCCCHHHCCCC | 20.47 | 24719451 | |
| 108 | Ubiquitination | RDGITAGKAALRIHN HCCCCCCCHHHEEEE | 28.20 | - | |
| 112 | Methylation | TAGKAALRIHNVTAS CCCCHHHEEEEEECC | 24.32 | - | |
| 115 | N-linked_Glycosylation | KAALRIHNVTASDSG CHHHEEEEEECCCCC | 30.39 | 22846996 | |
| 123 | Ubiquitination | VTASDSGKYLCYFQD EECCCCCCEEEEEEC | 38.71 | - | |
| 155 | Ubiquitination | SDLHVDVKGYKDGGI CCEEEEECEEECCCE | 52.65 | - | |
| 244 | O-linked_Glycosylation | IADPFFRSAQRWIAA ECCHHHHHHHHHHHH | 24.48 | 29351928 | |
| 255 | O-linked_Glycosylation | WIAALAGTLPVLLLL HHHHHHCHHHHHHHH | 23.45 | 29351928 | |
| 299 | Ubiquitination | EMAWSTMKQEQSTRV HHHHHHHHHHHHHHH | 51.26 | - | |
| 316 | Phosphorylation | LEELRWRSIQYASRG HHHHHHHHHHHHHCC | 13.69 | - | |
| 327 | Phosphorylation | ASRGERHSAYNEWKK HHCCCCCHHHHHHHH | 38.37 | 28857561 | |
| 334 | Ubiquitination | SAYNEWKKALFKPAD HHHHHHHHHHCCCCC | 51.93 | - | |
| 338 | Ubiquitination | EWKKALFKPADVILD HHHHHHCCCCCEEEC | 39.90 | - | |
| 347 | Ubiquitination | ADVILDPKTANPILL CCEEECCCCCCCEEE | 60.99 | - | |
| 392 | Phosphorylation | LGCESFISGRHYWEV EECCCEECCCCEEEE | 27.97 | 24719451 | |
| 441 | Phosphorylation | GLTDGNKYRTLTEPR CCCCCCCEECCCCCC | 16.90 | - |
| 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 BT3A1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of BT3A1_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 BT3A1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| TFF1_HUMAN | TFF1 | physical | 21982860 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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