| UniProt ID | UBL4A_HUMAN | |
|---|---|---|
| UniProt AC | P11441 | |
| Protein Name | Ubiquitin-like protein 4A {ECO:0000305} | |
| Gene Name | UBL4A {ECO:0000312|HGNC:HGNC:12505} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 157 | |
| Subcellular Localization | Cytoplasm, cytosol . Nucleus . | |
| Protein Description | As part of a cytosolic protein quality control complex, the BAG6/BAT3 complex, maintains misfolded and hydrophobic patches-containing proteins in a soluble state and participates to their proper delivery to the endoplasmic reticulum or alternatively can promote their sorting to the proteasome where they undergo degradation. [PubMed: 20676083] | |
| Protein Sequence | MQLTVKALQGRECSLQVPEDELVSTLKQLVSEKLNVPVRQQRLLFKGKALADGKRLSDYSIGPNSKLNLVVKPLEKVLLEEGEAQRLADSPPPQVWQLISKVLARHFSAADASRVLEQLQRDYERSLSRLTLDDIERLASRFLHPEVTETMEKGFSK | |
| 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 |
|---|---|---|---|---|---|
| 25 | Phosphorylation | PEDELVSTLKQLVSE CHHHHHHHHHHHHHH | 30.41 | 23403867 | |
| 27 | Ubiquitination | DELVSTLKQLVSEKL HHHHHHHHHHHHHHC | 41.49 | 32015554 | |
| 33 | Ubiquitination | LKQLVSEKLNVPVRQ HHHHHHHHCCCCHHH | 37.54 | - | |
| 48 | Acetylation | QRLLFKGKALADGKR HHHHHCCCCCCCCCC | 40.60 | 19666589 | |
| 48 | Ubiquitination | QRLLFKGKALADGKR HHHHHCCCCCCCCCC | 40.60 | PubMed | |
| 54 | Acetylation | GKALADGKRLSDYSI CCCCCCCCCCCCCCC | 51.19 | 19666589 | |
| 54 | Ubiquitination | GKALADGKRLSDYSI CCCCCCCCCCCCCCC | 51.19 | 24816145 | |
| 57 | Phosphorylation | LADGKRLSDYSIGPN CCCCCCCCCCCCCCC | 38.24 | 28555341 | |
| 59 | Phosphorylation | DGKRLSDYSIGPNSK CCCCCCCCCCCCCCC | 9.98 | 26074081 | |
| 60 | Phosphorylation | GKRLSDYSIGPNSKL CCCCCCCCCCCCCCC | 26.51 | 26074081 | |
| 65 | Phosphorylation | DYSIGPNSKLNLVVK CCCCCCCCCCCEEEE | 41.47 | 26074081 | |
| 66 | Acetylation | YSIGPNSKLNLVVKP CCCCCCCCCCEEEEC | 48.29 | 25953088 | |
| 66 | Ubiquitination | YSIGPNSKLNLVVKP CCCCCCCCCCEEEEC | 48.29 | 23000965 | |
| 72 | Acetylation | SKLNLVVKPLEKVLL CCCCEEEECHHHHHH | 36.08 | 25953088 | |
| 72 | Malonylation | SKLNLVVKPLEKVLL CCCCEEEECHHHHHH | 36.08 | 32601280 | |
| 72 | Ubiquitination | SKLNLVVKPLEKVLL CCCCEEEECHHHHHH | 36.08 | 23000965 | |
| 76 | Ubiquitination | LVVKPLEKVLLEEGE EEEECHHHHHHHCHH | 45.96 | 22053931 | |
| 90 | Phosphorylation | EAQRLADSPPPQVWQ HHHHHCCCCCHHHHH | 33.43 | 30278072 | |
| 100 | Phosphorylation | PQVWQLISKVLARHF HHHHHHHHHHHHHHC | 25.88 | 24719451 | |
| 101 | Ubiquitination | QVWQLISKVLARHFS HHHHHHHHHHHHHCC | 33.98 | 23000965 | |
| 108 | Phosphorylation | KVLARHFSAADASRV HHHHHHCCHHHHHHH | 19.20 | - | |
| 126 | Phosphorylation | LQRDYERSLSRLTLD HHHHHHHHHHCCCHH | 20.82 | 20068231 | |
| 128 | Phosphorylation | RDYERSLSRLTLDDI HHHHHHHHCCCHHHH | 26.87 | 23532336 | |
| 151 | Sulfoxidation | HPEVTETMEKGFSK- CHHHHHHHHHCCCC- | 4.00 | 21406390 | |
| 153 | Ubiquitination | EVTETMEKGFSK--- HHHHHHHHCCCC--- | 55.20 | 21890473 | |
| 157 | Ubiquitination | TMEKGFSK------- HHHHCCCC------- | 63.20 | 24816145 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of UBL4A_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 UBL4A_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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| Acetylation | |
| Reference | PubMed |
| "Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-48 AND LYS-54, AND MASSSPECTROMETRY. | |
| 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-90, 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-90, AND MASSSPECTROMETRY. | |
| "Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126, AND MASSSPECTROMETRY. | |