| Tag | Content |
|---|
| CPLM ID | CPLM-016055 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | E3 ubiquitin-protein ligase TRIM56 |
Protein Synonyms/Alias | Tripartite motif-containing protein 56 |
Gene Name | Trim56 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 87 | NGLLDLVKARAPGDV | ubiquitination | [1] | | 270 | LKSLLAQKQEVLGQL | ubiquitination | [1] | | 374 | RLIFEEPKQSPKDSG | ubiquitination | [1] | | 405 | DDRTKIGKQGGAQPL | 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 mediates 'Lys-63'- linked polyubiquitination of TMEM173/STING, thereby playing a key role in innate immunity. TMEM173/STING 'Lys-63'-linked ubiquitination activates the production of type I interferon IFN- beta following detection of pathogen- and host-derived double- stranded DNA. |
Sequence Annotation | ZN_FING 21 60 RING-type.
ZN_FING 98 149 B box-type 1.
ZN_FING 164 205 B box-type 2.
MOD_RES 314 314 Phosphoserine.
MOD_RES 448 448 Phosphoserine.
MOD_RES 450 450 Phosphoserine.
MOD_RES 454 454 Phosphoserine. |
Keyword | Antiviral defense; Coiled coil; Complete proteome; Cytoplasm; Immunity; Innate immunity; Ligase; Metal-binding; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation pathway; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 734 AA |
Protein Sequence | MNSKVSSPTL LEALSSDFLA CKICLEQLHT PKTLPCLHTY CQDCLAQLDI GGQVRCPECR 60
EIVPVPAEGV AAFKTNFFVN GLLDLVKARA PGDVHSGKPT CALCPLVGGK SSGGPATARC 120
LDCADDLCQA CADGHRCSRQ THKHRVVDLV GYRAGWYDEE ARERQASQCP QHPGEALCFL 180
CQPCSQLLCK DCRLGPHIDH PCLPLAEAVR SRKPGLEELL AGVDSNLVEL EATRVAEKEA 240
LALLREQAAS VGTQVEEAAE RILKSLLAQK QEVLGQLRAL VEAAEEATRE RLTKIERQEQ 300
VAKAAAAFAR RVLSLGLEAE ILSLEGAITQ RLRQLQDAPW TSGPTRCVLP QLELHPGLED 360
KNCHLLRLIF EEPKQSPKDS GKGGAGTQGG DEAQGQGDDR TKIGKQGGAQ PLTPKEGKDQ 420
NPQEDDGVFI ERGNRPNKKK KCKGRGKSVS REPSPILRPN LEGSGLLPRP VFSWSFPTRM 480
PGDKRSPRIT GLCPYGPQEI LVADEQNRVL KRFSLNGDYK GTVQVPEGCS PCSVAALQNA 540
VAFSANAKLY LVSPDGEIQW RRSLSLTQSS HAVAAMPCGD RVAVSVAGHV EVYKKDGSLA 600
TRFIPGGKAS RGQRALVFLT TSPQGNFVGS DWQQNSVVFC DGLGQVIWEY KGPGLHGCQP 660
GSVSVDKKGY IFLTLREVNK VVILDPKGSL LGDFLTAYHG LEKPRVTTMV DGKYLVVSLS 720
NGTIHVFRVR FPDS 734 |
Gene Ontology | GO:0005737; C:cytoplasm; 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; IMP:UniProtKB. GO:0032608; P:interferon-beta production; IMP:UniProtKB. GO:0070534; P:protein K63-linked ubiquitination; IDA:UniProtKB. GO:0034340; P:response to type I interferon; IDA:UniProtKB. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |