| Tag | Content |
|---|
| CPLM ID | CPLM-020897 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | E3 ubiquitin-protein ligase RNF125 |
Protein Synonyms/Alias | RING finger protein 125 |
Gene Name | Rnf125 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 66 | SCIATSIKNNNKWTC | ubiquitination | [1] | | 92 | VPATDIAKRMKSEYQ | ubiquitination | [1] | | 126 | TCEKYIDKYGPLLEL | ubiquitination | [1] |
|
Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | E3 ubiquitin-protein ligase that acts as a positive regulator of T-cell activation. E3 ligase proteins mediate ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). |
Sequence Annotation | ZN_FING 37 77 RING-type.
LIPID 2 2 N-myristoyl glycine (Potential). |
Keyword | Adaptive immunity; Alternative splicing; Complete proteome; Immunity; Ligase; Lipoprotein; Metal-binding; Myristate; Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 233 AA |
Protein Sequence | MGSLLSSDSS KSAPASATPR TLERSGDSEL PITSFDCSVC LEVLHQPVRT RCGHVFCRSC 60
IATSIKNNNK WTCPYCRAYL PSEGVPATDI AKRMKSEYQN CAECGTLVCL SDMRAHIRTC 120
EKYIDKYGPL LELGDTTARC VCPFCQRELD EDCLLDHCII HHRSERRPVF CPLCHSRPDE 180
SPSTFNGSLI RHLQVSHTLF YDDFIDFDII EEAIIRRVLD RSLLEYVNQS NTT 233 |
Gene Ontology | |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |