| UniProt ID | TXN4A_HUMAN | |
|---|---|---|
| UniProt AC | P83876 | |
| Protein Name | Thioredoxin-like protein 4A | |
| Gene Name | TXNL4A | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 142 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Essential role in pre-mRNA splicing as component of the U5 snRNP and U4/U6-U5 tri-snRNP complexes that are involved in spliceosome assembly.. | |
| Protein Sequence | MSYMLPHLHNGWQVDQAILSEEDRVVVIRFGHDWDPTCMKMDEVLYSIAEKVKNFAVIYLVDITEVPDFNKMYELYDPCTVMFFFRNKHIMIDLGTGNNNKINWAMEDKQEMVDIIETVYRGARKGRGLVVSPKDYSTKYRY | |
| 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 |
|---|---|---|---|---|---|
| 46 | Phosphorylation | MKMDEVLYSIAEKVK HCHHHHHHHHHHHHC | 11.82 | - | |
| 47 | Phosphorylation | KMDEVLYSIAEKVKN CHHHHHHHHHHHHCC | 15.91 | - | |
| 51 | Ubiquitination | VLYSIAEKVKNFAVI HHHHHHHHHCCEEEE | 49.87 | 21890473 | |
| 51 | Acetylation | VLYSIAEKVKNFAVI HHHHHHHHHCCEEEE | 49.87 | 25953088 | |
| 73 | Phosphorylation | VPDFNKMYELYDPCT CCCHHHHHHHCCCCE | 12.37 | 22817900 | |
| 76 | Phosphorylation | FNKMYELYDPCTVMF HHHHHHHCCCCEEEE | 13.10 | - | |
| 132 | Phosphorylation | KGRGLVVSPKDYSTK CCCCEEECCCCCCCC | 20.82 | 23401153 | |
| 132 | O-linked_Glycosylation | KGRGLVVSPKDYSTK CCCCEEECCCCCCCC | 20.82 | 29351928 | |
| 134 | Ubiquitination | RGLVVSPKDYSTKYR CCEEECCCCCCCCCC | 62.89 | 21890473 | |
| 136 | Phosphorylation | LVVSPKDYSTKYRY- EEECCCCCCCCCCC- | 25.11 | 26270265 | |
| 137 | Phosphorylation | VVSPKDYSTKYRY-- EECCCCCCCCCCC-- | 28.67 | 23312004 | |
| 138 | Phosphorylation | VSPKDYSTKYRY--- ECCCCCCCCCCC--- | 26.35 | 26270265 | |
| 139 | Ubiquitination | SPKDYSTKYRY---- CCCCCCCCCCC---- | 23.07 | 21890473 | |
| 139 | Acetylation | SPKDYSTKYRY---- CCCCCCCCCCC---- | 23.07 | 25953088 |
| 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 TXN4A_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of TXN4A_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 TXN4A_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| REBL1_HUMAN | RHEBL1 | physical | 16189514 | |
| HNRPF_HUMAN | HNRNPF | physical | 11054566 | |
| PQBP1_HUMAN | PQBP1 | physical | 11054566 | |
| PRP6_HUMAN | PRPF6 | physical | 16723661 | |
| WDFY1_HUMAN | WDFY1 | physical | 22939629 | |
| LZTS2_HUMAN | LZTS2 | physical | 25416956 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 608572 | Burn-McKeown syndrome (BMKS) | |||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| 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-132, 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-132, AND MASSSPECTROMETRY. | |