1.F.1.2.3 E3 ubiquitin-protein ligase, Tripartite motif 11, TRIM11, of 468 aas and possibly 1 C-terminal TMS. It disaggregates and degrades misfolded tau. In Alzheimer's disease and other taupathies, tau protein misfolds and forms oligomers, which clump together to form filamentious aggregates. TRIM11 breaks up these aggregates and facilitates the proteasomal degradation of misfolded tau (Noble and Hanger 2023). TRIM11 is down regulated in Alzheimer's disease, and up-regulation helps to reverse the symptoms of Alzheimer's diseease. Upon overexpression, TRIM11 reduces HIV-1 and murine leukemia virus infectivity by suppressing viral gene expression (Uchil et al. 2008).
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Accession Number: | Q6ZMU5 |
Protein Name: | Tripartite motif-containing protein 72 |
Length: | 477 |
Molecular Weight: | 52731.00 |
Species: | Homo sapiens (Human) [9606] |
Location1 / Topology2 / Orientation3: |
Cell membrane1 |
Substrate |
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1: MSAAPGLLHQ ELSCPLCLQL FDAPVTAECG HSFCRACLGR VAGEPAADGT VLCPCCQAPT
61: RPQALSTNLQ LARLVEGLAQ VPQGHCEEHL DPLSIYCEQD RALVCGVCAS LGSHRGHRLL
121: PAAEAHARLK TQLPQQKLQL QEACMRKEKS VAVLEHQLVE VEETVRQFRG AVGEQLGKMR
181: VFLAALEGSL DREAERVRGE AGVALRRELG SLNSYLEQLR QMEKVLEEVA DKPQTEFLMK
241: YCLVTSRLQK ILAESPPPAR LDIQLPIISD DFKFQVWRKM FRALMPALEE LTFDPSSAHP
301: SLVVSSSGRR VECSEQKAPP AGEDPRQFDK AVAVVAHQQL SEGEHYWEVD VGDKPRWALG
361: VIAAEAPRRG RLHAVPSQGL WLLGLREGKI LEAHVEAKEP RALRSPERRP TRIGLYLSFG
421: DGVLSFYDAS DADALVPLFA FHERLPRPVY PFFDVCWHDK GKNAQPLLLV GPEGAEA