| Tag | Content |
|---|
| CPLM ID | CPLM-018249 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | E3 ubiquitin-protein ligase RNF139 |
Protein Synonyms/Alias | RING finger protein 139; Translocation in renal carcinoma on chromosome 8 protein |
Gene Name | RNF139 |
Gene Synonyms/Alias | TRC8 |
Created Date | July 27, 2013 |
Organism | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 230 | LLMEDTWKRIRFPDI | ubiquitination | [1] |
|
Reference | [1] Systematic and quantitative assessment of the ubiquitin-modified proteome. Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP. Mol Cell. 2011 Oct 21;44(2):325-40. [ PMID: 21906983] |
Functional Description | E3-ubiquitin ligase; acts as a negative regulator of the cell proliferation through mechanisms involving G2/M arrest and cell death. Required for MHC class I ubiquitination in cells expressing the cytomegalovirus protein US2 before dislocation from the endoplasmic reticulum (ER). Affects SREBP processing by hindering the SREBP/SCAP complex translocation from the ER to the Golgi, thereby reducing SREBF2 target gene expression. Required for INSIG1 ubiquitination. May be required for EIF3 complex ubiquitination. May function as a signaling receptor. |
Sequence Annotation | ZN_FING 547 586 RING-type; atypical.
MOD_RES 663 663 Phosphothreonine. |
Keyword | Chromosomal rearrangement; Complete proteome; Endoplasmic reticulum; Ligase; Membrane; Metal-binding; Phosphoprotein; Receptor; Reference proteome; Transmembrane; Transmembrane helix; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 664 AA |
Protein Sequence | MAAVGPPQQQ VRMAHQQVWA ALEVALRVPC LYIIDAIFNS YPDSSQSRFC IVLQIFLRLF 60
GVFASSIVLI LSQRSLFKFY TYSSAFLLAA TSVLVNYYAS LHIDFYGAYN TSAFGIELLP 120
RKGPSLWMAL IVLQLTFGIG YVTLLQIHSI YSQLIILDLL VPVIGLITEL PLHIRETLLF 180
TSSLILTLNT VFVLAVKLKW FYYSTRYVYL LVRHMYRIYG LQLLMEDTWK RIRFPDILRV 240
FWLTRVTAQA TVLMYILRMA NETDSFFISW DDFWDLICNL IISGCDSTLT VLGMSAVISS 300
VAHYLGLGIL AFIGSTEEDD RRLGFVAPVL FFILALQTGL SGLRPEERLI RLSRNMCLLL 360
TAVLHFIHGM TDPVLMSLSA SHVSSFRRHF PVLFVSACLF ILPVLLSYVL WHHYALNTWL 420
FAVTAFCVEL CLKVIVSLTV YTLFMIDGYY NVLWEKLDDY VYYVRSTGSI IEFIFGVVMF 480
GNGAYTMMFE SGSKIRAFMM CLHAYFNIYL QAKNGWKTFM NRRTAVKKIN SLPEIKGSRL 540
QEINDVCAIC YHEFTTSARI TPCNHYFHAL CLRKWLYIQD TCPMCHQKVY IEDDIKDNSN 600
VSNNNGFIPP NETPEEAVRE AAAESDRELN EDDSTDCDDD VQRERNGVIQ HTGAAAEEFN 660
DDTD 664 |
Gene Ontology | GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. GO:0016021; C:integral to membrane; TAS:UniProtKB. GO:0004872; F:receptor activity; TAS:UniProtKB. GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB. GO:0017148; P:negative regulation of translation; IDA:UniProtKB. GO:0060628; P:regulation of ER to Golgi vesicle-mediated transport; IDA:UniProtKB. GO:0070613; P:regulation of protein processing; IDA:UniProtKB. GO:0031396; P:regulation of protein ubiquitination; IDA:UniProtKB. |
Interpro | |
Pfam | |
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PROSITE | |
PRINTS | |