| Tag |
Content |
LipidDB ID |
LipidDB-9606-01355 |
Entry Name |
|
UniProt Accession |
|
Theoretical PI |
4.64 |
Molecular Weight |
17443.74 |
Genbank Protein ID |
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Genbank Nucleotide ID |
|
Protein Name |
RING finger protein 11 |
Protein Synonyms/Alias |
|
Gene Name |
RNF11 |
Gene Synonyms/Alias |
CGI-123; |
Created Date |
06-JUN-2002 |
| Lipid Modification Sites |
|---|
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
2 | Canonical | ******MGNCLKSPT | [1][2] | N-Myristoylation |
|
Organism |
Homo sapiens (Human) |
NCBI Taxa ID |
9606 |
Reference |
[1] Suzuki T, Moriya K, Nagatoshi K, Ota Y, Ezure T, Ando E, Tsunasawa S, UtsumiT. Strategy for comprehensive identification of human N-myristoylated proteinsusing an insect cell-free protein synthesis system. Proteomics. 2010May;10(9):1780-93. doi: 10.1002/pmic.200900783.[ PMID:20213681]
[2] Santonico E, Belleudi F, Panni S, Torrisi MR, Cesareni G, Castagnoli L.Multiple modification and protein interaction signals drive the Ring fingerprotein 11 (RNF11) E3 ligase to the endosomal compartment. Oncogene. 2010 Oct14;29(41):5604-18. doi: 10.1038/onc.2010.294. Epub 2010 Aug 2.[ PMID:20676133]
|
Functional Description |
Essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. Promotes the association of TNFAIP3 to RIPK1 after TNF stimulation. TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Recruits STAMBP to the E3 ubiquitin-ligase SMURF2 for ubiquitination, leading to its degradation by the 26S proteasome. |
Sequence Annotation |
Motif: 37 40 WW-binding.
Modified residue: 135 135 Phosphothreonine; by PKB/AKT1.
|
Protein Length |
154 AA. |
Protein Sequence
(Canonical) |
MGNCLKSPTS DDISLLHESQ SDRASFGEGT EPDQEPPPPY QEQVPVPVYH PTPSQTRLAT 60
QLTEEEQIRI AQRIGLIQHL PKGVYDPGRD GSEKKIRECV ICMMDFVYGD PIRFLPCMHI 120
YHLDCIDDWL MRSFTCPSCM EPVDAALLSS YETN 154
|
FASTA
(Canonical) |
>LipidDB-9606-01355|Q9Y3C5
MGNCLKSPTSDDISLLHESQSDRASFGEGTEPDQEPPPPYQEQVPVPVYHPTPSQTRLAT
QLTEEEQIRIAQRIGLIQHLPKGVYDPGRDGSEKKIRECVICMMDFVYGDPIRFLPCMHI
YHLDCIDDWLMRSFTCPSCMEPVDAALLSSYETN
|
Gene Ontology |
GO:0005768; C:endosome; IEA:UniProtKB-KW GO:0070062; C:extracellular vesicular exosome; IDA:UniProt GO:0005634; C:nucleus; IEA:UniProtKB-KW GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB GO:0003677; F:DNA binding; TAS:ProtInc GO:0004842; F:ubiquitin-protein transferase activity; IDA:FlyBase GO:0008270; F:zinc ion binding; TAS:ProtInc GO:0051865; P:protein autoubiquitination; IDA:FlyBase GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:UniProtKB |
Interpro |
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Pfam |
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SMART |
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PROSITE |
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PRINTS |
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