E3 ubiquitin-protein ligase TRIM13

UniProt data

UniProt name: TRI13_HUMAN (O60858)

Gene name: TRIM13; Synonyms=LEU5, RFP2, RNF77

Organism: Homo sapiens (Human).

Function: E3 ubiquitin ligase involved in the retrotranslocation and turnover of membrane and secretory proteins from the ER through a set of processes named ER-associated degradation (ERAD). This process acts on misfolded proteins as well as in the regulated degradation of correctly folded proteins. Enhances ionizing radiation-induced p53/TP53 stability and apoptosis via ubiquitinating MDM2 and AKT1 and decreasing AKT1 kinase activity through MDM2 and AKT1 proteasomal degradation. Regulates ER stress-induced autophagy, and may act as a tumor suppressor. {ECO:0000269|PubMed:17314412, ECO:0000269|PubMed:21333377, ECO:0000269|PubMed:22178386}.

Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17314412, ECO:0000269|PubMed:21333377, ECO:0000269|PubMed:22178386}; Single-pass membrane protein {ECO:0000269|PubMed:17314412, ECO:0000269|PubMed:21333377, ECO:0000269|PubMed:22178386}. Note=Concentrates and colocalizes with p62/SQSTM1 and ZFYVE1 at the perinuclear endoplasmic reticulum.

Transmembrane domains:

  1. 317-337, 21 AA, Helical. {ECO:0000255}.

Sequence: 407 AA

10 20 30 40 50 60 MELLEEDLTC PICCSLFDDP RVLPCSHNFC KKCLEGILEG SVRNSLWRPA PFKCPTCRKE 70 80 90 100 110 120 TSATGINSLQ VNYSLKGIVE KYNKIKISPK MPVCKGHLGQ PLNIFCLTDM QLICGICATR 130 140 150 160 170 180 GEHTKHVFCS IEDAYAQERD AFESLFQSFE TWRRGDALSR LDTLETSKRK SLQLLTKDSD 190 200 210 220 230 240 KVKEFFEKLQ HTLDQKKNEI LSDFETMKLA VMQAYDPEIN KLNTILQEQR MAFNIAEAFK 250 260 270 280 290 300 DVSEPIVFLQ QMQEFREKIK VIKETPLPPS NLPASPLMKN FDTSQWEDIK LVDVDKLSLP 310 320 330 340 350 360 QDTGTFISKI PWSFYKLFLL ILLLGLVIVF GPTMFLEWSL FDDLATWKGC LSNFSSYLTK 370 380 390 400 TADFIEQSVF YWEQVTDGFF IFNERFKNFT LVVLNNVAEF VCKYKLL

CATM prediction

The sequence of TRI13_HUMAN returned 1 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
        320       330       3
 +    |    +    |    +    |		 (Å) (°) (Å) (°)  
Model 1 FYKLFLLILLLGLVIVFGATMFLEWSL 7.0 -55.1° 1.5 45.0 -5.9
Prolines* FYKLFLLILLLGLVIVFGPTMFLEWSL          

* 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:


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Download model 1 structure: PDB, PyMOL session

List of hydrogen bonds:

Donor Acceptor Distance
B, 331, GLY, HA1 A, 328, ILE, O 2.97Å
B, 332, ALA, HA A, 331, GLY, O 3.48Å
A, 331, GLY, HA1 B, 328, ILE, O 2.97Å
A, 332, ALA, HA B, 331, GLY, O 3.48Å