| UniProt ID | TM87B_HUMAN | |
|---|---|---|
| UniProt AC | Q96K49 | |
| Protein Name | Transmembrane protein 87B {ECO:0000305} | |
| Gene Name | TMEM87B {ECO:0000312|HGNC:HGNC:25913} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 555 | |
| Subcellular Localization |
Golgi apparatus membrane Multi-pass membrane protein . |
|
| Protein Description | May be involved in retrograde transport from endosomes to the trans-Golgi network (TGN).. | |
| Protein Sequence | MVAACRSVAGLLPRRRRCFPARAPLLRVALCLLCWTPAAVRAVPELGLWLETVNDKSGPLIFRKTMFNSTDIKLSVKSFHCSGPVKFTIVWHLKYHTCHNEHSNLEELFQKHKLSVDEDFCHYLKNDNCWTTKNENLDCNSDSQVFPSLNNKELINIRNVSNQERSMDVVARTQKDGFHIFIVSIKTENTDASWNLNVSLSMIGPHGYISASDWPLMIFYMVMCIVYILYGILWLTWSACYWKDILRIQFWIAAVIFLGMLEKAVFYSEYQNISNTGLSTQGLLIFAELISAIKRTLARLLVIIVSLGYGIVKPRLGTVMHRVIGLGLLYLIFAAVEGVMRVIGGSNHLAVVLDDIILAVIDSIFVWFIFISLAQTMKTLRLRKNTVKFSLYRHFKNTLIFAVLASIVFMGWTTKTFRIAKCQSDWMERWVDDAFWSFLFSLILIVIMFLWRPSANNQRYAFMPLIDDSDDEIEEFMVTSENLTEGIKLRASKSVSNGTAKPATSENFDEDLKWVEENIPSSFTDVALPVLVDSDEEIMTRSEMAEKMFSSEKIM | |
| 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 |
|---|---|---|---|---|---|
| 7 | Phosphorylation | -MVAACRSVAGLLPR -CHHHHHHHHCCCCC | 19.06 | 24043423 | |
| 68 | N-linked_Glycosylation | IFRKTMFNSTDIKLS EEEEECCCCCCEEEE | 32.93 | UniProtKB CARBOHYD | |
| 111 | Ubiquitination | NLEELFQKHKLSVDE CHHHHHHHHCCCCCH | 35.06 | 29967540 | |
| 113 | Ubiquitination | EELFQKHKLSVDEDF HHHHHHHCCCCCHHH | 49.87 | 29967540 | |
| 197 | N-linked_Glycosylation | TDASWNLNVSLSMIG CCCCEEEEEEEEEEC | 20.37 | UniProtKB CARBOHYD | |
| 268 | Phosphorylation | LEKAVFYSEYQNISN HHHHHHHHHHCCCCC | 20.54 | - | |
| 272 | N-linked_Glycosylation | VFYSEYQNISNTGLS HHHHHHCCCCCCCCC | 38.46 | UniProtKB CARBOHYD | |
| 274 | Phosphorylation | YSEYQNISNTGLSTQ HHHHCCCCCCCCCHH | 35.57 | - | |
| 292 | Ubiquitination | IFAELISAIKRTLAR HHHHHHHHHHHHHHH | 12.34 | 27667366 | |
| 460 | Phosphorylation | PSANNQRYAFMPLID CCCCCCCEEEEEEEC | 8.40 | 20639409 | |
| 469 | Phosphorylation | FMPLIDDSDDEIEEF EEEEECCCCHHHHHH | 43.12 | 24043423 | |
| 479 | Phosphorylation | EIEEFMVTSENLTEG HHHHHEECCCCCCCC | 20.66 | 29691806 | |
| 480 | Phosphorylation | IEEFMVTSENLTEGI HHHHEECCCCCCCCE | 17.05 | 29691806 | |
| 484 | Phosphorylation | MVTSENLTEGIKLRA EECCCCCCCCEEEEE | 43.69 | 29691806 | |
| 492 | Ubiquitination | EGIKLRASKSVSNGT CCEEEEECCCCCCCC | 21.01 | 27667366 | |
| 492 | Phosphorylation | EGIKLRASKSVSNGT CCEEEEECCCCCCCC | 21.01 | 28102081 | |
| 493 | Ubiquitination | GIKLRASKSVSNGTA CEEEEECCCCCCCCC | 54.62 | 27667366 | |
| 494 | Phosphorylation | IKLRASKSVSNGTAK EEEEECCCCCCCCCC | 28.43 | 23927012 | |
| 496 | Phosphorylation | LRASKSVSNGTAKPA EEECCCCCCCCCCCC | 36.31 | 23401153 | |
| 499 | Phosphorylation | SKSVSNGTAKPATSE CCCCCCCCCCCCCCC | 35.44 | 23927012 | |
| 501 | Ubiquitination | SVSNGTAKPATSENF CCCCCCCCCCCCCCH | 34.72 | 33845483 | |
| 504 | Phosphorylation | NGTAKPATSENFDED CCCCCCCCCCCHHHH | 45.13 | 23403867 | |
| 505 | Phosphorylation | GTAKPATSENFDEDL CCCCCCCCCCHHHHH | 32.42 | 23403867 | |
| 521 | Phosphorylation | WVEENIPSSFTDVAL HHHHHCCCCCCCCEE | 34.00 | 20639409 | |
| 522 | Phosphorylation | VEENIPSSFTDVALP HHHHCCCCCCCCEEE | 27.15 | 20639409 | |
| 524 | Phosphorylation | ENIPSSFTDVALPVL HHCCCCCCCCEEEEE | 31.35 | 28176443 | |
| 534 | Phosphorylation | ALPVLVDSDEEIMTR EEEEEECCCHHHHCH | 39.17 | 28355574 | |
| 540 | Phosphorylation | DSDEEIMTRSEMAEK CCCHHHHCHHHHHHH | 36.38 | 28176443 | |
| 542 | Phosphorylation | DEEIMTRSEMAEKMF CHHHHCHHHHHHHHH | 23.66 | 22115753 | |
| 547 | Ubiquitination | TRSEMAEKMFSSEKI CHHHHHHHHHCCCCC | 35.39 | 33845483 | |
| 550 | Phosphorylation | EMAEKMFSSEKIM-- HHHHHHHCCCCCC-- | 33.80 | 24719451 | |
| 553 | Ubiquitination | EKMFSSEKIM----- HHHHCCCCCC----- | 46.12 | 33845483 |
| 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 TM87B_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TM87B_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 TM87B_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of TM87B_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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| Phosphorylation | |
| Reference | PubMed |
| "Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-469, AND MASSSPECTROMETRY. | |