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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_MOUSE             Reviewed;         668 AA.
Q7TMV1; Q8BZU9;
06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
01-OCT-2003, sequence version 1.
25-APR-2018, entry version 125.
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|MGI:MGI:1923091};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000312|EMBL:BAC28327.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC28327.1};
TISSUE=Colon {ECO:0000312|EMBL:BAC28327.1};
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2] {ECO:0000312|EMBL:AAH52901.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6NCr {ECO:0000312|EMBL:AAH52901.1};
TISSUE=Hematopoietic stem cell;
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).
[3]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-667, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-667, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, and Liver;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- 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:0000250|UniProtKB:Q8WU17}.
-!- 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 VHL. Interacts with MHC class I and HM13.
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. Interacts with
XBP1 isoform 1; the interaction induces ubiquitination and
degradation of XBP1 isoform 1. {ECO:0000250|UniProtKB:Q8WU17}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
membrane protein.
-!- DOMAIN: The RING-type zinc finger domain may be essential for
ubiquitin ligase activity. {ECO:0000250|UniProtKB:O75485}.
-!- PTM: Autoubiquitinated. Ubiquitination is induced by sterol and
leads to ist degradation via the ubiquitin-proteasome pathway.
{ECO:0000250|UniProtKB:Q8WU17}.
-----------------------------------------------------------------------
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EMBL; AK033506; BAC28327.1; -; mRNA.
EMBL; BC052901; AAH52901.1; -; mRNA.
CCDS; CCDS27494.1; -.
RefSeq; NP_780435.1; NM_175226.4.
UniGene; Mm.4537; -.
UniGene; Mm.460627; -.
ProteinModelPortal; Q7TMV1; -.
SMR; Q7TMV1; -.
STRING; 10090.ENSMUSP00000046467; -.
iPTMnet; Q7TMV1; -.
PhosphoSitePlus; Q7TMV1; -.
MaxQB; Q7TMV1; -.
PaxDb; Q7TMV1; -.
PeptideAtlas; Q7TMV1; -.
PRIDE; Q7TMV1; -.
GeneID; 75841; -.
KEGG; mmu:75841; -.
UCSC; uc007vtq.2; mouse.
CTD; 11236; -.
MGI; MGI:1923091; Rnf139.
eggNOG; KOG0802; Eukaryota.
eggNOG; COG5243; LUCA.
HOGENOM; HOG000267029; -.
HOVERGEN; HBG053146; -.
InParanoid; Q7TMV1; -.
KO; K15703; -.
PhylomeDB; Q7TMV1; -.
TreeFam; TF318635; -.
UniPathway; UPA00143; -.
PRO; PR:Q7TMV1; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_RNF139; -.
GO; GO:0036513; C:Derlin-1 retrotranslocation complex; ISO:MGI.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0002020; F:protease binding; ISO:MGI.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0019787; F:ubiquitin-like protein transferase activity; ISO:MGI.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0036503; P:ERAD pathway; ISO:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; ISO:MGI.
GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
GO; GO:0031648; P:protein destabilization; ISS:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
GO; GO:0060628; P:regulation of ER to Golgi vesicle-mediated transport; ISO:MGI.
GO; GO:0070613; P:regulation of protein processing; ISO:MGI.
GO; GO:0031396; P:regulation of protein ubiquitination; ISS: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; 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:0000250|UniProtKB:Q8WU17}.
CHAIN 2 668 E3 ubiquitin-protein ligase RNF139.
/FTId=PRO_0000056099.
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 470 490 Helical. {ECO:0000255}.
ZN_FING 547 586 RING-type; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00175}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q8WU17}.
MOD_RES 636 636 Phosphoserine.
{ECO:0000250|UniProtKB:Q8WU17}.
MOD_RES 637 637 Phosphothreonine.
{ECO:0000250|UniProtKB:Q8WU17}.
MOD_RES 667 667 Phosphothreonine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
CONFLICT 248 248 T -> A (in Ref. 1; BAC28327).
{ECO:0000305}.
SEQUENCE 668 AA; 76185 MW; 6DA76DFC64C6374D CRC64;
MAAVGPPQQQ VRMAQQQVWA ALEVALRVPC LYIIDAIFNS YYDSSQSRFC IGLQIFLRLL
GIVVSSIVLI LSQRSLFKFY MYSSAFLLAA TSVLVNYYAA LHIDFYGAYN TSAFGIELLP
RKGPSLWMAL IVLQLTFGIG YVTLLQIQSI YSQLMILNIL VPIIGLITEL PLHIRETVVL
MSSLILIFNT VLVLAVKLKW FYYSTRYVYL LVRHMYRIYG LQLLMEDTWK RIRFPDILRV
FWLTRITTQA TVLMYILRMA NETESFFISW DDFWDVICNL IISGCDSTLT VLGMSAVISS
IAHYLGLGIL AFIGSTEEDD RRLGFVAPVL FFILALQTGL SGLRPEERLI RLSRNMCLLL
TAVLHFIHGM TDPVLMSLSA SHVSSFHRHF PVLFVSACLF ILPVLLSYVL WHHYALNTWL
FAVTAFCVEL CLKVIVSLTV YTLFMIDGYY NVLWEKLDDY VYFVRSTGNI IEFIFGVVMF
GNGAYTMMFE SGSKIRACMM CLHAYFNIYL QVKNGWKTFM NRRTAVKKIN SLPEIKGSHL
QEIDDVCAIC YHEFTTSARI TPCNHYFHAL CLRKWLYIQD TCPMCHQKVY IEDEIKDNSN
ASNNNGFIAP NENPNPEEAL REDAAGSDRE LNEDDSTDCD DDAQRERNGG IQHTGAAAAA
AEFNDDTD


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