| Tag | Content |
|---|
| CPLM ID | CPLM-020010 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | E3 ubiquitin-protein ligase TRIM11 |
Protein Synonyms/Alias | Tripartite motif-containing protein 11 |
Gene Name | Trim11 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 260 | EREASIAKDIKDALC | acetylation | [1] |
|
Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | 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. |
Sequence Annotation | DOMAIN 267 460 B30.2/SPRY.
ZN_FING 16 57 RING-type.
ZN_FING 87 127 B box-type. |
Keyword | Alternative splicing; Antiviral defense; Coiled coil; Complete proteome; Cytoplasm; Ligase; Metal-binding; Nucleus; Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 467 AA |
Protein Sequence | MAAPDLSTNL QEEATCAICL DYFTDPVMTD CGHNFCRECI RRCWGQPEGP YACPECRELS 60
AQRNLRPNRP LAKMAEMARR LHPPSPVPQG VCAAHREPLT TFCGDDLSLL CPICERSEHW 120
THRVRPLQEA ADDLKGRLEK SLEHLRKQME DAMLFQAQAE ETCALWQKMV ESQRQNVLGE 180
FERLRRLLAE EEQQLLQKLE EEELEVLPRL REGAARLGQQ STQLAALISE LESRCQLPAL 240
GLLQLCIECC ALEREASIAK DIKDALCRVQ DVKLQPPAVV PMELRTVCRV PGLVETLRRF 300
RGDITLDPDT ANPELVLSED RRSVQRGEQR QALPDNPERF DPGPCVLGQE RITSGRHYWE 360
VEVGDQTSWA LGVCKETANR KEKGELSAGN GFWILVFLGS FYNSNEPAFS PLRDPPKRVG 420
IFLDYEAGHL SFYSATDGSL LFIFPETLFS GTLRPLFSPL SSSPTPMTIC RLIGVSGDTL 480
GPQ 483 |
Gene Ontology | GO:0005737; C:cytoplasm; IDA:UniProtKB. GO:0005634; C:nucleus; IDA:UniProtKB. GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. GO:0050768; P:negative regulation of neurogenesis; IMP:UniProtKB. GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB. |
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Pfam | |
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PRINTS | |