| UniProt ID | UBXN1_HUMAN | |
|---|---|---|
| UniProt AC | Q04323 | |
| Protein Name | UBX domain-containing protein 1 | |
| Gene Name | UBXN1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 297 | |
| Subcellular Localization | Cytoplasm . | |
| Protein Description | Ubiquitin-binding protein that plays a role in the modulation of innate immune response. Blocks both the RIG-I-like receptors (RLR) and NF-kappa-B pathways. Following viral infection, UBXN1 is induced and recruited to the RLR component MAVS. In turn, interferes with MAVS oligomerization, and disrupts the MAVS/TRAF3/TRAF6 signalosome. This function probably serves as a brake to prevent excessive RLR signaling. [PubMed: 23545497 Interferes with the TNFalpha-triggered NF-kappa-B pathway by interacting with cellular inhibitors of apoptosis proteins (cIAPs) and thereby inhibiting their recruitment to TNFR1] | |
| Protein Sequence | MAELTALESLIEMGFPRGRAEKALALTGNQGIEAAMDWLMEHEDDPDVDEPLETPLGHILGREPTSSEQGGLEGSGSAAGEGKPALSEEERQEQTKRMLELVAQKQREREEREEREALERERQRRRQGQELSAARQRLQEDEMRRAAEERRREKAEELAARQRVREKIERDKAERAKKYGGSVGSQPPPVAPEPGPVPSSPSQEPPTKREYDQCRIQVRLPDGTSLTQTFRAREQLAAVRLYVELHRGEELGGGQDPVQLLSGFPRRAFSEADMERPLQELGLVPSAVLIVAKKCPS | |
| 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 |
|---|---|---|---|---|---|
| 2 | Acetylation | ------MAELTALES ------CHHHHHHHH | 22.10 | 19413330 | |
| 75 | Phosphorylation | EQGGLEGSGSAAGEG CCCCCCCCCCCCCCC | 21.87 | 25159151 | |
| 83 | Ubiquitination | GSAAGEGKPALSEEE CCCCCCCCCCCCHHH | 23.86 | 22053931 | |
| 83 (in isoform 1) | Ubiquitination | - | 23.86 | 21890473 | |
| 83 | Acetylation | GSAAGEGKPALSEEE CCCCCCCCCCCCHHH | 23.86 | 26822725 | |
| 83 | Sumoylation | GSAAGEGKPALSEEE CCCCCCCCCCCCHHH | 23.86 | - | |
| 83 (in isoform 2) | Ubiquitination | - | 23.86 | 21890473 | |
| 87 | Phosphorylation | GEGKPALSEEERQEQ CCCCCCCCHHHHHHH | 45.10 | 21815630 | |
| 96 (in isoform 2) | Ubiquitination | - | 35.19 | 21890473 | |
| 96 (in isoform 1) | Ubiquitination | - | 35.19 | 21890473 | |
| 96 | Acetylation | EERQEQTKRMLELVA HHHHHHHHHHHHHHH | 35.19 | 26051181 | |
| 96 | Ubiquitination | EERQEQTKRMLELVA HHHHHHHHHHHHHHH | 35.19 | 21906983 | |
| 98 | Sulfoxidation | RQEQTKRMLELVAQK HHHHHHHHHHHHHHH | 3.48 | 21406390 | |
| 105 (in isoform 1) | Ubiquitination | - | 41.40 | 21890473 | |
| 105 | Ubiquitination | MLELVAQKQREREER HHHHHHHHHHHHHHH | 41.40 | 22053931 | |
| 105 (in isoform 2) | Ubiquitination | - | 41.40 | 21890473 | |
| 105 | Acetylation | MLELVAQKQREREER HHHHHHHHHHHHHHH | 41.40 | 25953088 | |
| 132 | Phosphorylation | RRQGQELSAARQRLQ HHHHHHHHHHHHHHH | 21.09 | 27470641 | |
| 132 (in isoform 2) | Phosphorylation | - | 21.09 | 24719451 | |
| 154 (in isoform 1) | Ubiquitination | - | 60.32 | 21890473 | |
| 154 | Acetylation | AEERRREKAEELAAR HHHHHHHHHHHHHHH | 60.32 | 25953088 | |
| 154 (in isoform 2) | Ubiquitination | - | 60.32 | 21890473 | |
| 154 | Ubiquitination | AEERRREKAEELAAR HHHHHHHHHHHHHHH | 60.32 | 22053931 | |
| 167 | Ubiquitination | ARQRVREKIERDKAE HHHHHHHHHHHHHHH | 39.02 | - | |
| 178 (in isoform 2) | Ubiquitination | - | 48.41 | 21890473 | |
| 178 | Ubiquitination | DKAERAKKYGGSVGS HHHHHHHHHCCCCCC | 48.41 | 21890473 | |
| 178 (in isoform 1) | Ubiquitination | - | 48.41 | 21890473 | |
| 179 | Phosphorylation | KAERAKKYGGSVGSQ HHHHHHHHCCCCCCC | 26.47 | 23927012 | |
| 182 | Phosphorylation | RAKKYGGSVGSQPPP HHHHHCCCCCCCCCC | 20.95 | 23927012 | |
| 185 | Phosphorylation | KYGGSVGSQPPPVAP HHCCCCCCCCCCCCC | 37.04 | 23927012 | |
| 199 (in isoform 2) | Phosphorylation | - | 55.93 | 24719451 | |
| 199 | Phosphorylation | PEPGPVPSSPSQEPP CCCCCCCCCCCCCCC | 55.93 | 22167270 | |
| 200 (in isoform 2) | Phosphorylation | - | 23.62 | 27251275 | |
| 200 | Phosphorylation | EPGPVPSSPSQEPPT CCCCCCCCCCCCCCC | 23.62 | 22167270 | |
| 202 | Phosphorylation | GPVPSSPSQEPPTKR CCCCCCCCCCCCCCC | 49.47 | 22167270 | |
| 207 | Phosphorylation | SPSQEPPTKREYDQC CCCCCCCCCCCCCCE | 54.15 | 22167270 | |
| 208 | Acetylation | PSQEPPTKREYDQCR CCCCCCCCCCCCCEE | 49.35 | 26051181 | |
| 208 | Ubiquitination | PSQEPPTKREYDQCR CCCCCCCCCCCCCEE | 49.35 | 2190698 | |
| 208 (in isoform 1) | Ubiquitination | - | 49.35 | 21890473 | |
| 208 (in isoform 2) | Ubiquitination | - | 49.35 | 21890473 | |
| 211 | Phosphorylation | EPPTKREYDQCRIQV CCCCCCCCCCEEEEE | 18.49 | 26074081 | |
| 224 | Phosphorylation | QVRLPDGTSLTQTFR EEECCCCCCHHHHHH | 28.13 | 30576142 | |
| 225 | Phosphorylation | VRLPDGTSLTQTFRA EECCCCCCHHHHHHH | 34.64 | 30576142 | |
| 227 | Phosphorylation | LPDGTSLTQTFRARE CCCCCCHHHHHHHHH | 25.90 | 28857561 | |
| 229 | Phosphorylation | DGTSLTQTFRAREQL CCCCHHHHHHHHHHH | 15.17 | 25850435 | |
| 242 (in isoform 2) | Phosphorylation | - | 4.94 | 27642862 | |
| 242 | Phosphorylation | QLAAVRLYVELHRGE HHHHHHHHHHCCCCC | 4.94 | 29978859 | |
| 262 | Phosphorylation | QDPVQLLSGFPRRAF CCHHHHHHCCCCCCC | 47.16 | - | |
| 270 | Phosphorylation | GFPRRAFSEADMERP CCCCCCCCHHHCCCH | 30.78 | 26434776 | |
| 286 | Phosphorylation | QELGLVPSAVLIVAK HHCCCCCCEEEEEEE | 24.43 | 27690223 | |
| 293 | Ubiquitination | SAVLIVAKKCPS--- CEEEEEEECCCC--- | 43.97 | - | |
| 293 (in isoform 1) | Ubiquitination | - | 43.97 | 21890473 | |
| 294 | Ubiquitination | AVLIVAKKCPS---- EEEEEEECCCC---- | 41.46 | - | |
| 297 | Phosphorylation | IVAKKCPS------- EEEECCCC------- | 63.42 | 26074081 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 200 | S | Phosphorylation | Kinase | MAPK12 | P53778 | Uniprot |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of UBXN1_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 UBXN1_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-270, AND MASSSPECTROMETRY. | |
| "A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, AND MASSSPECTROMETRY. | |
| "Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-179; SER-199; SER-200AND THR-207, AND MASS SPECTROMETRY. | |
| "A novel UBA and UBX domain protein that binds polyubiquitin and VCPand is a substrate for SAPKs."; McNeill H., Knebel A., Arthur J.S., Cuenda A., Cohen P.; Biochem. J. 384:391-400(2004). Cited for: PROTEIN SEQUENCE OF 220-231 AND 276-285, PHOSPHORYLATION AT SER-200,AND INTERACTION WITH VCP. | |
