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E3 ubiquitin-protein ligase RNF139 (EC 2.3.2.27) (RING finger protein 139) (RING-type E3 ubiquitin transferase RNF139) (Translocation in renal carcinoma on chromosome 8 protein)

 RN139_HUMAN             Reviewed;         664 AA.
Q8WU17; B3KMD5; O75485; Q7LDL3;
06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
20-JUN-2018, entry version 152.
RecName: Full=E3 ubiquitin-protein ligase RNF139;
EC=2.3.2.27;
AltName: Full=RING finger protein 139;
AltName: Full=RING-type E3 ubiquitin transferase RNF139 {ECO:0000305};
AltName: Full=Translocation in renal carcinoma on chromosome 8 protein;
Name=RNF139 {ECO:0000312|HGNC:HGNC:17023};
Synonyms=TRC8 {ECO:0000312|EMBL:AAC39930.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAC39930.1}
NUCLEOTIDE SEQUENCE [MRNA], NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-60,
TISSUE SPECIFICITY, AND CHROMOSOMAL TRANSLOCATION WITH FHIT.
PubMed=9689122; DOI=10.1073/pnas.95.16.9572;
Gemmill R.M., West J.D., Boldog F., Tanaka N., Robinson L.J.,
Smith D.I., Li F., Drabkin H.A.;
"The hereditary renal cell carcinoma 3;8 translocation fuses FHIT to a
patched-related gene, TRC8.";
Proc. Natl. Acad. Sci. U.S.A. 95:9572-9577(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000312|EMBL:AAH21571.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung {ECO:0000312|EMBL:AAH21571.1}, and
Pancreas {ECO:0000312|EMBL:AAH64636.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5] {ECO:0000305}
FUNCTION.
PubMed=10500182; DOI=10.1073/pnas.96.20.11364;
Lorick K.L., Jensen J.P., Fang S., Ong A.M., Hatakeyama S.,
Weissman A.M.;
"RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent
ubiquitination.";
Proc. Natl. Acad. Sci. U.S.A. 96:11364-11369(1999).
[6] {ECO:0000305}
FUNCTION, INTERACTION WITH VHL, AND SUBCELLULAR LOCATION.
PubMed=12032852; DOI=10.1038/sj.onc.1205437;
Gemmill R.M., Bemis L.T., Lee J.P., Sozen M.A., Baron A., Zeng C.,
Erickson P.F., Hooper J.E., Drabkin H.A.;
"The TRC8 hereditary kidney cancer gene suppresses growth and
functions with VHL in a common pathway.";
Oncogene 21:3507-3516(2002).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-663, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[8]
FUNCTION, AND MUTAGENESIS OF 547-CYS--CYS-550; 547-CYS--HIS-586;
557-SER--ARG-559; 572-LEU--LYS-574 AND 582-CYS--CYS-585.
PubMed=17016439; DOI=10.1038/sj.onc.1210017;
Brauweiler A., Lorick K.L., Lee J.P., Tsai Y.C., Chan D.,
Weissman A.M., Drabkin H.A., Gemmill R.M.;
"RING-dependent tumor suppression and G2/M arrest induced by the TRC8
hereditary kidney cancer gene.";
Oncogene 26:2263-2271(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-663, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-663, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
FUNCTION, INTERACTION WITH SREBF2; SCAP AND SEC24B, UBIQUITINATION,
AND MUTAGENESIS OF 547-CYS--CYS-550 AND 547-CYS--HIS-586.
PubMed=19706601; DOI=10.1074/jbc.M109.041376;
Irisawa M., Inoue J., Ozawa N., Mori K., Sato R.;
"The sterol-sensing endoplasmic reticulum (ER) membrane protein TRC8
hampers ER to Golgi transport of sterol regulatory element-binding
protein-2 (SREBP-2)/SREBP cleavage-activated protein and reduces
SREBP-2 cleavage.";
J. Biol. Chem. 284:28995-29004(2009).
[13]
FUNCTION, INTERACTION WITH MHC CLASS I AND HM13, AND MUTAGENESIS OF
547-CYS--CYS-550 AND 547-CYS--HIS-586.
PubMed=19720873; DOI=10.1083/jcb.200906110;
Stagg H.R., Thomas M., van den Boomen D., Wiertz E.J., Drabkin H.A.,
Gemmill R.M., Lehner P.J.;
"The TRC8 E3 ligase ubiquitinates MHC class I molecules before
dislocation from the ER.";
J. Cell Biol. 186:685-692(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-663, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[15]
FUNCTION, INTERACTION WITH INSIG1; INSIG2; EIF3F AND EIF3H, INDUCTION,
AND MUTAGENESIS OF 547-CYS--CYS-550 AND 547-CYS--HIS-586.
PubMed=20068067; DOI=10.1158/1541-7786.MCR-08-0491;
Lee J.P., Brauweiler A., Rudolph M., Hooper J.E., Drabkin H.A.,
Gemmill R.M.;
"The TRC8 ubiquitin ligase is sterol regulated and interacts with
lipid and protein biosynthetic pathways.";
Mol. Cancer Res. 8:93-106(2010).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-663, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-663, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-663, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
INTERACTION WITH HM13 AND XBP1.
PubMed=25239945; DOI=10.15252/embj.201488208;
Chen C.Y., Malchus N.S., Hehn B., Stelzer W., Avci D., Langosch D.,
Lemberg M.K.;
"Signal peptide peptidase functions in ERAD to cleave the unfolded
protein response regulator XBP1u.";
EMBO J. 33:2492-2506(2014).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634 AND THR-635, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:10500182, ECO:0000269|PubMed:12032852,
ECO:0000269|PubMed:17016439, ECO:0000269|PubMed:19706601,
ECO:0000269|PubMed:19720873, ECO:0000269|PubMed:20068067}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Interacts with MHC class I and HM13 (PubMed:19720873,
PubMed:25239945). Interacts with VHL. Component of SCAP/SREBP
complex composed of SREBF2, SCAP and RNF139; the complex hampers
the interaction between SCAP and SEC24B, thereby reducing SREBF2
proteolytic processing. Interacts with SREBF2 (via C-terminal
domain). Interacts with SCAP; the interaction inhibits the
interaction of SCAP with SEC24B and hampering the ER to Golgi
transport of the SCAP/SREBP complex. Interacts with SEC24B.
Interacts with INSIG1 and INSIG2. Interacts with EIF3F and EIF3H;
the interaction leads to protein translation inhibitions in a
ubiquitination-dependent manner (PubMed:12032852, PubMed:19706601,
PubMed:20068067). Interacts with XBP1 isoform 1; the interaction
induces ubiquitination and degradation of XBP1 isoform 1
(PubMed:25239945). {ECO:0000269|PubMed:12032852,
ECO:0000269|PubMed:19706601, ECO:0000269|PubMed:19720873,
ECO:0000269|PubMed:20068067, ECO:0000269|PubMed:25239945}.
-!- INTERACTION:
Q8TCT9:HM13; NbExp=2; IntAct=EBI-1551681, EBI-347472;
P40337:VHL; NbExp=2; IntAct=EBI-1551681, EBI-301246;
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:12032852}; Multi-pass membrane protein
{ECO:0000269|PubMed:12032852}.
-!- TISSUE SPECIFICITY: Highly expressed in testis, placenta and
adrenal gland. Moderate expression in heart, brain, liver,
skeletal muscle and pancreas, and low expression in lung and
kidney. {ECO:0000269|PubMed:9689122}.
-!- INDUCTION: Down-regulated by sterols (at protein level).
{ECO:0000269|PubMed:20068067}.
-!- DOMAIN: The RING-type zinc finger domain mediates ubiquitin ligase
activity.
-!- PTM: Autoubiquitinated. Ubiquitination is induced by sterol and
leads to ist degradation via the ubiquitin-proteasome pathway.
{ECO:0000269|PubMed:19706601}.
-!- DISEASE: Renal cell carcinoma (RCC) [MIM:144700]: Renal cell
carcinoma is a heterogeneous group of sporadic or hereditary
carcinoma derived from cells of the proximal renal tubular
epithelium. It is subclassified into clear cell renal carcinoma
(non-papillary carcinoma), papillary renal cell carcinoma,
chromophobe renal cell carcinoma, collecting duct carcinoma with
medullary carcinoma of the kidney, and unclassified renal cell
carcinoma. Clear cell renal cell carcinoma is the most common
subtype. Note=The disease may be caused by mutations affecting the
gene represented in this entry. A chromosomal aberration involving
RNF139 has been found in a lymphoblastoid cell line established
from a family with renal cell carcinoma and thyroid carcinoma.
Translocation (3;8)(q14.2;q24.1) with FHIT. RNF139 is found to be
fused to FHIT and disrupted within the sterol-sensing domain. In
contrast, the FHIT coding region is maintained and expressed.
Sporadic cases of renal carcinoma, where an acquired mutation in
RNF139 results in the duplication of 12 nucleotides in the 5'-UTR,
has also been identified.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TRC8ID500.html";
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EMBL; AF064800; AAC39931.1; -; Genomic_DNA.
EMBL; AF064801; AAC39930.1; -; mRNA.
EMBL; AK001602; BAG50947.1; -; mRNA.
EMBL; CH471060; EAW92064.1; -; Genomic_DNA.
EMBL; BC021571; AAH21571.1; -; mRNA.
EMBL; BC064636; AAH64636.1; -; mRNA.
CCDS; CCDS6350.1; -.
RefSeq; NP_009149.2; NM_007218.3.
UniGene; Hs.744151; -.
ProteinModelPortal; Q8WU17; -.
SMR; Q8WU17; -.
BioGrid; 116401; 18.
IntAct; Q8WU17; 8.
MINT; Q8WU17; -.
STRING; 9606.ENSP00000304051; -.
iPTMnet; Q8WU17; -.
PhosphoSitePlus; Q8WU17; -.
BioMuta; RNF139; -.
DMDM; 74760542; -.
EPD; Q8WU17; -.
MaxQB; Q8WU17; -.
PaxDb; Q8WU17; -.
PeptideAtlas; Q8WU17; -.
PRIDE; Q8WU17; -.
ProteomicsDB; 74623; -.
Ensembl; ENST00000303545; ENSP00000304051; ENSG00000170881.
GeneID; 11236; -.
KEGG; hsa:11236; -.
UCSC; uc003yrc.4; human.
CTD; 11236; -.
DisGeNET; 11236; -.
EuPathDB; HostDB:ENSG00000170881.4; -.
GeneCards; RNF139; -.
HGNC; HGNC:17023; RNF139.
HPA; HPA001202; -.
MalaCards; RNF139; -.
MIM; 144700; phenotype.
MIM; 603046; gene.
neXtProt; NX_Q8WU17; -.
OpenTargets; ENSG00000170881; -.
Orphanet; 151; Familial renal cell carcinoma.
PharmGKB; PA134945850; -.
eggNOG; KOG0802; Eukaryota.
eggNOG; COG5243; LUCA.
GeneTree; ENSGT00530000062938; -.
HOGENOM; HOG000267029; -.
HOVERGEN; HBG053146; -.
InParanoid; Q8WU17; -.
KO; K15703; -.
OMA; RIRFPDI; -.
OrthoDB; EOG091G020N; -.
PhylomeDB; Q8WU17; -.
TreeFam; TF318635; -.
Reactome; R-HSA-901032; ER Quality Control Compartment (ERQC).
UniPathway; UPA00143; -.
GeneWiki; RNF139; -.
GenomeRNAi; 11236; -.
PRO; PR:Q8WU17; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000170881; -.
CleanEx; HS_RNF139; -.
ExpressionAtlas; Q8WU17; baseline and differential.
Genevisible; Q8WU17; HS.
GO; GO:0036513; C:Derlin-1 retrotranslocation complex; IDA:ParkinsonsUK-UCL.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IEA:GOC.
GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
GO; GO:0016874; F:ligase activity; TAS:UniProtKB.
GO; GO:0002020; F:protease binding; IPI:UniProtKB.
GO; GO:0038023; F:signaling receptor activity; TAS:UniProtKB.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0019787; F:ubiquitin-like protein transferase activity; IDA:UniProtKB.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:1904380; P:endoplasmic reticulum mannose trimming; TAS:Reactome.
GO; GO:0036503; P:ERAD pathway; IMP:ParkinsonsUK-UCL.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0017148; P:negative regulation of translation; IDA:UniProtKB.
GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
GO; GO:0031648; P:protein destabilization; IMP:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
GO; GO:0060628; P:regulation of ER to Golgi vesicle-mediated transport; IDA:UniProtKB.
GO; GO:0070613; P:regulation of protein processing; IDA:UniProtKB.
GO; GO:0031396; P:regulation of protein ubiquitination; IDA:UniProtKB.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR025754; TRC8_N_dom.
InterPro; IPR001841; Znf_RING.
InterPro; IPR011016; Znf_RING-CH.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
Pfam; PF13705; TRC8_N; 1.
Pfam; PF13639; zf-RING_2; 1.
SMART; SM00184; RING; 1.
SMART; SM00744; RINGv; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Acetylation; Chromosomal rearrangement; Complete proteome;
Endoplasmic reticulum; Membrane; Metal-binding; Phosphoprotein;
Receptor; Reference proteome; Transferase; Transmembrane;
Transmembrane helix; Ubl conjugation; Ubl conjugation pathway; Zinc;
Zinc-finger.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 664 E3 ubiquitin-protein ligase RNF139.
/FTId=PRO_0000056098.
TRANSMEM 51 71 Helical. {ECO:0000255}.
TRANSMEM 85 105 Helical. {ECO:0000255}.
TRANSMEM 125 145 Helical. {ECO:0000255}.
TRANSMEM 154 174 Helical. {ECO:0000255}.
TRANSMEM 178 198 Helical. {ECO:0000255}.
TRANSMEM 293 313 Helical. {ECO:0000255}.
TRANSMEM 323 343 Helical. {ECO:0000255}.
TRANSMEM 356 376 Helical. {ECO:0000255}.
TRANSMEM 390 410 Helical. {ECO:0000255}.
TRANSMEM 420 440 Helical. {ECO:0000255}.
TRANSMEM 469 489 Helical. {ECO:0000255}.
TRANSMEM 495 512 Helical. {ECO:0000255}.
ZN_FING 547 586 RING-type; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00175}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 634 634 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 635 635 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 663 663 Phosphothreonine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MUTAGEN 547 586 Missing: Increases proliferation. Rescues
MHC class I to the cell surface. Fails to
down-regulate SREBF1 and SREBF2.
{ECO:0000269|PubMed:17016439,
ECO:0000269|PubMed:19706601,
ECO:0000269|PubMed:19720873,
ECO:0000269|PubMed:20068067}.
MUTAGEN 547 550 CAIC->SAIS: Abolishes ubiquitination
activity. Increases proliferation. Does
not phosphorylates CHEK2 on T-68. Does
not phosphorylates ATM on S-1981. Rescues
MHC class I to the cell surface.
Suppresses SREBF2 processing in the
presence or absence of sterols. Fails to
down-regulate SREBF1 and SREBF2.
Decreases INSIG1 ubiquitination.
{ECO:0000269|PubMed:17016439,
ECO:0000269|PubMed:19706601,
ECO:0000269|PubMed:19720873,
ECO:0000269|PubMed:20068067}.
MUTAGEN 557 559 SAR->AAA: Retaines about 30% of
ubiquitination activity.
{ECO:0000269|PubMed:17016439}.
MUTAGEN 572 574 LRK->AAA: Abolishes ubiquitination
activity. Increases proliferation.
{ECO:0000269|PubMed:17016439}.
MUTAGEN 582 585 CPMC->APMA: Abolishes ubiquitination
activity. Increases proliferation.
{ECO:0000269|PubMed:17016439}.
CONFLICT 18 18 V -> I (in Ref. 1; AAC39930/AAC39931).
{ECO:0000305}.
SEQUENCE 664 AA; 75994 MW; 9885F5915F019EF5 CRC64;
MAAVGPPQQQ VRMAHQQVWA ALEVALRVPC LYIIDAIFNS YPDSSQSRFC IVLQIFLRLF
GVFASSIVLI LSQRSLFKFY TYSSAFLLAA TSVLVNYYAS LHIDFYGAYN TSAFGIELLP
RKGPSLWMAL IVLQLTFGIG YVTLLQIHSI YSQLIILDLL VPVIGLITEL PLHIRETLLF
TSSLILTLNT VFVLAVKLKW FYYSTRYVYL LVRHMYRIYG LQLLMEDTWK RIRFPDILRV
FWLTRVTAQA TVLMYILRMA NETDSFFISW DDFWDLICNL IISGCDSTLT VLGMSAVISS
VAHYLGLGIL AFIGSTEEDD RRLGFVAPVL FFILALQTGL SGLRPEERLI RLSRNMCLLL
TAVLHFIHGM TDPVLMSLSA SHVSSFRRHF PVLFVSACLF ILPVLLSYVL WHHYALNTWL
FAVTAFCVEL CLKVIVSLTV YTLFMIDGYY NVLWEKLDDY VYYVRSTGSI IEFIFGVVMF
GNGAYTMMFE SGSKIRAFMM CLHAYFNIYL QAKNGWKTFM NRRTAVKKIN SLPEIKGSRL
QEINDVCAIC YHEFTTSARI TPCNHYFHAL CLRKWLYIQD TCPMCHQKVY IEDDIKDNSN
VSNNNGFIPP NETPEEAVRE AAAESDRELN EDDSTDCDDD VQRERNGVIQ HTGAAAEEFN
DDTD


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