UniProt data
UniProt name: UBP19_HUMAN (O94966)
Gene name: USP19; Synonyms=KIAA0891, ZMYND9
Organism: Homo sapiens (Human).
Function: Deubiquitinating enzyme that regulates the degradation of various proteins. Deubiquitinates and prevents proteasomal degradation of RNF123 which in turn stimulates CDKN1B ubiquitin- dependent degradation thereby playing a role in cell proliferation. Involved in decreased protein synthesis in atrophying skeletal muscle. Modulates transcription of major myofibrillar proteins. Also involved in turnover of endoplasmic- reticulum-associated degradation (ERAD) substrates. Regulates the stability of BIRC2/c-IAP1 and BIRC3/c-IAP2 by preventing their ubiquitination. Required for cells to mount an appropriate response to hypoxia and rescues HIF1A from degradation in a non- catalytic manner. Plays an important role in 17 beta-estradiol (E2)-inhibited myogenesis. Decreases the levels of ubiquitinated proteins during skeletal muscle formation and acts to repress myogenesis. Exhibits a preference towards 'Lys-63'-linked Ubiquitin chains. {ECO:0000269|PubMed:19465887, ECO:0000269|PubMed:21849505, ECO:0000269|PubMed:22128162, ECO:0000269|PubMed:22689415}.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19465887}; Single-pass membrane protein {ECO:0000269|PubMed:19465887}.
Transmembrane domains:
- 1292-1312, 21 AA, Helical. {ECO:0000255}.
Sequence: 1318 AA
CATM prediction
The sequence of UBP19_HUMAN returned 2 potential models
The positions at the dimer's interface are highlighted in yellow. The position at the crossing point is highlighted in orange.
| # | Sequence and interface | d | θ | Z' | ω' | Score |
|---|---|---|---|---|---|---|
| 1290 1300 1310 | + | + | + |
(Å) | (°) | (Å) | (°) | ||
| Model 1 | LRYFVLGTVAALVALVLNVFYALVSQS | 6.9 | -40.0° | 4.5 | 44.0 | -25.2 |
| Model 2 | LRYFVLGTVAALVALVLNVFYALVSQS | 7.0 | -42.0° | 1.9 | 33.4 | -4.6 |
| Prolines* | LRYFVLGTVAALVALVLNVFYPLVSQS |
* Note: this sequence contains Pro residues. CATM substituted them with Ala during the modeling. The positions are marked.
Click on the model number to visualize its details below.
MODEL 1 DETAILS
Precited structure:
Download model 1 structure: PDB, PyMOL session
List of hydrogen bonds:
| Donor | Acceptor | Distance |
|---|---|---|
| B, 1295, GLY, HA1 | A, 1292, PHE, O | 3.10Å |
| A, 1295, GLY, HA1 | B, 1292, PHE, O | 3.10Å |


