UniProt ID | TRI14_HUMAN | |
---|---|---|
UniProt AC | Q14142 | |
Protein Name | Tripartite motif-containing protein 14 | |
Gene Name | TRIM14 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 442 | |
Subcellular Localization | Mitochondrion outer membrane . | |
Protein Description | Plays a role in the innate immune defense against viruses. Facilitates the type I IFN response by interacting with MAVS at the outer mitochondria membrane and thereby recruiting NF-kappa-B essential modulator IKBKG/NEMO to the MAVS signalosome, leading to the activation of both the IFN regulatory factor 3/IRF3 and NF-kappa-B pathways. [PubMed: 24379373 Positively regulates the CGAS-induced type I interferon signaling pathway by stabilizing CGAS and inhibiting its autophagic degradation] | |
Protein Sequence | MAGAATGSRTPGRSELVEGCGWRCPEHGDRVAELFCRRCRRCVCALCPVLGAHRGHPVGLALEAAVHVQKLSQECLKQLAIKKQQHIDNITQIEDATEKLKANAESSKTWLKGKFTELRLLLDEEEALAKKFIDKNTQLTLQVYREQADSCREQLDIMNDLSNRVWSISQEPDPVQRLQAYTATEQEMQQQMSLGELCHPVPLSFEPVKSFFKGLVEAVESTLQTPLDIRLKESINCQLSDPSSTKPGTLLKTSPSPERSLLLKYARTPTLDPDTMHARLRLSADRLTVRCGLLGSLGPVPVLRFDALWQVLARDCFATGRHYWEVDVQEAGAGWWVGAAYASLRRRGASAAARLGCNRQSWCLKRYDLEYWAFHDGQRSRLRPRDDLDRLGVFLDYEAGVLAFYDVTGGMSHLHTFRATFQEPLYPALRLWEGAISIPRLP | |
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 |
---|---|---|---|---|---|
6 | Phosphorylation | --MAGAATGSRTPGR --CCCCCCCCCCCCC | 34.85 | 27251275 | |
8 | Phosphorylation | MAGAATGSRTPGRSE CCCCCCCCCCCCCHH | 28.73 | 24719451 | |
10 | Phosphorylation | GAATGSRTPGRSELV CCCCCCCCCCCHHHC | 31.62 | 21712546 | |
14 | Phosphorylation | GSRTPGRSELVEGCG CCCCCCCHHHCCCCC | 40.99 | 21712546 | |
70 | Ubiquitination | EAAVHVQKLSQECLK HHHHHHHHHCHHHHH | 49.36 | - | |
72 | Phosphorylation | AVHVQKLSQECLKQL HHHHHHHCHHHHHHH | 30.85 | 26074081 | |
77 | Ubiquitination | KLSQECLKQLAIKKQ HHCHHHHHHHHHHHH | 55.73 | - | |
83 | Ubiquitination | LKQLAIKKQQHIDNI HHHHHHHHHHHHHCC | 49.42 | - | |
99 | Ubiquitination | QIEDATEKLKANAES HHHHHHHHHHHHHHH | 51.43 | - | |
108 | Ubiquitination | KANAESSKTWLKGKF HHHHHHCCHHHHCCH | 53.66 | - | |
114 | Ubiquitination | SKTWLKGKFTELRLL CCHHHHCCHHHHHHH | 47.74 | - | |
130 | Ubiquitination | DEEEALAKKFIDKNT CHHHHHHHHHCCCCC | 49.41 | - | |
131 | Ubiquitination | EEEALAKKFIDKNTQ HHHHHHHHHCCCCCC | 41.78 | - | |
135 | Ubiquitination | LAKKFIDKNTQLTLQ HHHHHCCCCCCEEEH | 58.01 | - | |
139 (in isoform 4) | Phosphorylation | - | 4.93 | 24114839 | |
232 | Ubiquitination | TPLDIRLKESINCQL CCCCCEEHHHHCCCC | 39.30 | - | |
246 | Ubiquitination | LSDPSSTKPGTLLKT CCCCCCCCCCCEEEC | 43.32 | - | |
252 | Ubiquitination | TKPGTLLKTSPSPER CCCCCEEECCCCHHH | 50.50 | - | |
264 | Ubiquitination | PERSLLLKYARTPTL HHHHHHHHHCCCCCC | 36.51 | - | |
365 | Ubiquitination | NRQSWCLKRYDLEYW CCCCHHCCCCCCEEE | 45.86 | - | |
371 | Phosphorylation | LKRYDLEYWAFHDGQ CCCCCCEEEEEECCC | 14.88 | 20049867 | |
437 | Phosphorylation | RLWEGAISIPRLP-- HHHCCCCCCCCCC-- | 26.46 | 24719451 |
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 TRI14_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TRI14_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 TRI14_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
MAVS_HUMAN | MAVS | physical | 24379373 | |
NEMO_HUMAN | IKBKG | physical | 24379373 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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