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Identification
HMDB Protein ID HMDBP09315
Secondary Accession Numbers
  • 15149
Name E3 ubiquitin-protein ligase TRIM11
Synonyms
  1. Protein BIA1
  2. RING finger protein 92
  3. Tripartite motif-containing protein 11
Gene Name TRIM11
Protein Type Enzyme
Biological Properties
General Function Involved in zinc ion binding
Specific Function E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX. Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis. May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences. May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation pathway. Mediates MED15 ubiquitination leading to proteasomal degradation. May contribute to the innate restriction of retroviruses. Upon overexpression, reduces HIV-1 and murine leukemia virus infectivity, by suppressing viral gene expression. Antiviral activity depends on a functional E3 ubiquitin-protein ligase domain. May regulate TRIM5 turnover via the proteasome pathway, thus counteracting the TRIM5-mediated cross-species restriction of retroviral infection at early stages of the retroviral life cycle
Pathways Not Available
Reactions Not Available
GO Classification
Component
cell part
intracellular
Function
ion binding
cation binding
metal ion binding
binding
transition metal ion binding
zinc ion binding
protein binding
Cellular Location
  1. Nucleus
  2. Cytoplasm
Gene Properties
Chromosome Location Chromosome:1
Locus 1q42.13
SNPs TRIM11
Gene Sequence
>1407 bp
ATGGCCGCCCCCGACCTGTCCACCAACCTCCAGGAGGAGGCCACCTGCGCCATCTGCCTC
GACTACTTCACGGATCCGGTGATGACCGACTGCGGCCACAACTTCTGCCGCGAGTGCATC
CGGCGCTGCTGGGGCCAGCCCGAGGGCCCGTACGCGTGCCCCGAGTGCCGCGAGCTGTCC
CCGCAGAGGAACCTGCGGCCCAACCGCCCGCTTGCTAAGATGGCCGAGATGGCGCGGCGC
CTGCACCCGCCGTCGCCGGTCCCGCAGGGCGTGTGCCCCGCGCACCGCGAGCCACTGGCC
GCCTTCTGTGGCGACGAGCTGCGCCTCCTGTGTGCGGCCTGCGAGCGCTCTGGGGAGCAC
TGGGCGCACCGCGTGCGGCCGCTGCAGGACGCGGCCGAAGACCTCAAGGCGAAGCTGGAG
AAGTCACTGGAGCATCTCCGGAAGCAGATGCAGGATGCGTTGCTGTTCCAAGCCCAGGCG
GATGAGACCTGCGTCTTGTGGCAGAAGATGGTGGAGAGCCAGCGGCAGAACGTGCTGGGT
GAGTTCGAGCGTCTTCGCCGTTTGCTGGCAGAGGAGGAGCAGCAGCTGCTGCAGAGGCTG
GAGGAGGAGGAGCTGGAGGTGCTGCCCCGGCTGCGGGAGGGCGCAGCCCACCTAGGCCAG
CAGAGCGCCCACCTAGCTGAGCTCATCGCCGAGCTCGAGGGCCGCTGCCAGCTGCCTGCT
CTGGGGCTGCTGCAGGACATCAAGGACGCCCTGCGCAGGGTCCAGGATGTGAAGCTGCAG
CCCCCAGAAGTTGTGCCTATGGAGCTGAGGACCGTGTGCAGGGTCCCGGGACTGGTAGAG
ACACTGCGGAGGTTTCGAGGGGACGTGACCTTGGACCCGGACACCGCCAACCCTGAGCTG
ATCCTGTCTGAAGACAGGCGGAGCGTGCAGCGGGGGGACCTACGGCAGGCCCTGCCGGAC
AGCCCAGAGCGCTTTGACCCCGGCCCCTGCGTGCTGGGCCAGGAGCGCTTCACCTCAGGC
CGCCACTACTGGGAGGTGGAGGTTGGGGACCGCACCAGCTGGGCCCTGGGGGTGTGCAGG
GAGAACGTGAACAGGAAGGAGAAGGGCGAGCTGTCCGCGGGCAACGGCTTCTGGATCCTG
GTCTTCCTGGGGAGCTATTACAATTCCTCGGAACGGGCCTTGGCTCCACTCCGGGACCCA
CCCAGGCGCGTGGGGATCTTTCTGGACTACGAGGCTGGACATCTCTCTTTCTACAGTGCC
ACCGATGGGTCACTGCTATTCATCTTTCCCGAGATCCCCTTCTCGGGGACGCTGCGGCCC
CTCTTCTCACCCCTGTCCAGCAGCCCGACCCCGATGACTATCTGCCGGCCGAAAGGTGGG
TCCGGGGACACCCTGGCTCCCCAGTGA
Protein Properties
Number of Residues 468
Molecular Weight 52773.6
Theoretical pI 5.42
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>E3 ubiquitin-protein ligase TRIM11
MAAPDLSTNLQEEATCAICLDYFTDPVMTDCGHNFCRECIRRCWGQPEGPYACPECRELS
PQRNLRPNRPLAKMAEMARRLHPPSPVPQGVCPAHREPLAAFCGDELRLLCAACERSGEH
WAHRVRPLQDAAEDLKAKLEKSLEHLRKQMQDALLFQAQADETCVLWQKMVESQRQNVLG
EFERLRRLLAEEEQQLLQRLEEEELEVLPRLREGAAHLGQQSAHLAELIAELEGRCQLPA
LGLLQDIKDALRRVQDVKLQPPEVVPMELRTVCRVPGLVETLRRFRGDVTLDPDTANPEL
ILSEDRRSVQRGDLRQALPDSPERFDPGPCVLGQERFTSGRHYWEVEVGDRTSWALGVCR
ENVNRKEKGELSAGNGFWILVFLGSYYNSSERALAPLRDPPRRVGIFLDYEAGHLSFYSA
TDGSLLFIFPEIPFSGTLRPLFSPLSSSPTPMTICRPKGGSGDTLAPQ
GenBank ID Protein 21630277
UniProtKB/Swiss-Prot ID Q96F44
UniProtKB/Swiss-Prot Entry Name TRI11_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_145214.2
GeneCard ID TRIM11
GenAtlas ID TRIM11
HGNC ID HGNC:16281
References
General References
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  3. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed:16710414 ]
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  5. Ishikawa H, Tachikawa H, Miura Y, Takahashi N: TRIM11 binds to and destabilizes a key component of the activator-mediated cofactor complex (ARC105) through the ubiquitin-proteasome system. FEBS Lett. 2006 Sep 4;580(20):4784-92. Epub 2006 Aug 4. [PubMed:16904669 ]
  6. Uchil PD, Quinlan BD, Chan WT, Luna JM, Mothes W: TRIM E3 ligases interfere with early and late stages of the retroviral life cycle. PLoS Pathog. 2008 Feb 8;4(2):e16. doi: 10.1371/journal.ppat.0040016. [PubMed:18248090 ]