Entry sw:RN139_MOUSE

ID   RN139_MOUSE             Reviewed;         668 AA.
AC   Q7TMV1; Q8BZU9;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   02-NOV-2016, entry version 119.
DE   RecName: Full=E3 ubiquitin-protein ligase RNF139;
DE            EC=6.3.2.-;
DE   AltName: Full=RING finger protein 139;
DE   AltName: Full=Translocation in renal carcinoma on chromosome 8 protein;
GN   Name=Rnf139 {ECO:0000312|MGI:MGI:1923091};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1] {ECO:0000312|EMBL:BAC28327.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC28327.1};
RC   TISSUE=Colon {ECO:0000312|EMBL:BAC28327.1};
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2] {ECO:0000312|EMBL:AAH52901.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6NCr {ECO:0000312|EMBL:AAH52901.1};
RC   TISSUE=Hematopoietic stem cell;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-667, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-667, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, and Liver;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: E3-ubiquitin ligase; acts as a negative regulator of the
CC       cell proliferation through mechanisms involving G2/M arrest and
CC       cell death. Required for MHC class I ubiquitination in cells
CC       expressing the cytomegalovirus protein US2 before dislocation from
CC       the endoplasmic reticulum (ER). Affects SREBP processing by
CC       hindering the SREBP/SCAP complex translocation from the ER to the
CC       Golgi, thereby reducing SREBF2 target gene expression. Required
CC       for INSIG1 ubiquitination. May be required for EIF3 complex
CC       ubiquitination. May function as a signaling receptor (By
CC       similarity). {ECO:0000250}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with VHL. Interacts with MHC class I and HM13.
CC       Component of SCAP/SREBP complex composed of SREBF2, SCAP and
CC       RNF139; the complex hampers the interaction between SCAP and
CC       SEC24B, thereby reducing SREBF2 proteolytic processing. Interacts
CC       with SREBF2 (via C-terminal domain). Interacts with SCAP; the
CC       interaction inhibits the interaction of SCAP with SEC24B and
CC       hampering the ER to Golgi transport of the SCAP/SREBP complex.
CC       Interacts with SEC24B. Interacts with INSIG1 and INSIG2. Interacts
CC       with EIF3F and EIF3H; the interaction leads to protein translation
CC       inhibitions in a ubiquitination-dependent manner. Interacts with
CC       XBP1 isoform 1; the interaction induces ubiquitination and
CC       degradation of XBP1 isoform 1 (By similarity).
CC       {ECO:0000250|UniProtKB:Q8WU17}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass
CC       membrane protein.
CC   -!- DOMAIN: The RING-type zinc finger domain may be essential for
CC       ubiquitin ligase activity. {ECO:0000250|UniProtKB:O75485}.
CC   -!- PTM: Autoubiquitinated. Ubiquitination is induced by sterol and
CC       leads to ist degradation via the ubiquitin-proteasome pathway (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC       {ECO:0000255|PROSITE-ProRule:PRU00175}.
DR   EMBL; AK033506; BAC28327.1; -; mRNA.
DR   EMBL; BC052901; AAH52901.1; -; mRNA.
DR   CCDS; CCDS27494.1; -.
DR   RefSeq; NP_780435.1; NM_175226.4.
DR   UniGene; Mm.4537; -.
DR   UniGene; Mm.460627; -.
DR   ProteinModelPortal; Q7TMV1; -.
DR   SMR; Q7TMV1; -.
DR   STRING; 10090.ENSMUSP00000046467; -.
DR   iPTMnet; Q7TMV1; -.
DR   PhosphoSitePlus; Q7TMV1; -.
DR   PaxDb; Q7TMV1; -.
DR   PeptideAtlas; Q7TMV1; -.
DR   PRIDE; Q7TMV1; -.
DR   GeneID; 75841; -.
DR   KEGG; mmu:75841; -.
DR   UCSC; uc007vtq.2; mouse.
DR   CTD; 11236; -.
DR   MGI; MGI:1923091; Rnf139.
DR   eggNOG; KOG0802; Eukaryota.
DR   eggNOG; COG5243; LUCA.
DR   HOGENOM; HOG000267029; -.
DR   HOVERGEN; HBG053146; -.
DR   InParanoid; Q7TMV1; -.
DR   KO; K15703; -.
DR   PhylomeDB; Q7TMV1; -.
DR   TreeFam; TF318635; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q7TMV1; -.
DR   Proteomes; UP000000589; Unplaced.
DR   Bgee; ENSMUSG00000037075; -.
DR   CleanEx; MM_RNF139; -.
DR   GO; GO:0036513; C:Derlin-1 retrotranslocation complex; ISO:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0002020; F:protease binding; ISO:MGI.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0019787; F:ubiquitin-like protein transferase activity; ISO:MGI.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0036503; P:ERAD pathway; ISO:MGI.
DR   GO; GO:0008285; P:negative regulation of cell proliferation; ISO:MGI.
DR   GO; GO:0017148; P:negative regulation of translation; ISO:MGI.
DR   GO; GO:2000060; P:positive regulation of protein ubiquitination involved in ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0031648; P:protein destabilization; ISS:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; ISO:MGI.
DR   GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0060628; P:regulation of ER to Golgi vesicle-mediated transport; ISO:MGI.
DR   GO; GO:0070613; P:regulation of protein processing; ISO:MGI.
DR   GO; GO:0031396; P:regulation of protein ubiquitination; ISS:UniProtKB.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR025754; TRC8_N_dom.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR011016; Znf_RING-CH.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF13705; TRC8_N; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00744; RINGv; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Complete proteome; Endoplasmic reticulum; Ligase;
KW   Membrane; Metal-binding; Phosphoprotein; Receptor; Reference proteome;
KW   Transmembrane; Transmembrane helix; Ubl conjugation;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   INIT_MET      1      1       Removed. {ECO:0000250|UniProtKB:Q8WU17}.
FT   CHAIN         2    668       E3 ubiquitin-protein ligase RNF139.
FT                                /FTId=PRO_0000056099.
FT   TRANSMEM     51     71       Helical. {ECO:0000255}.
FT   TRANSMEM     85    105       Helical. {ECO:0000255}.
FT   TRANSMEM    125    145       Helical. {ECO:0000255}.
FT   TRANSMEM    154    174       Helical. {ECO:0000255}.
FT   TRANSMEM    178    198       Helical. {ECO:0000255}.
FT   TRANSMEM    293    313       Helical. {ECO:0000255}.
FT   TRANSMEM    323    343       Helical. {ECO:0000255}.
FT   TRANSMEM    356    376       Helical. {ECO:0000255}.
FT   TRANSMEM    390    410       Helical. {ECO:0000255}.
FT   TRANSMEM    420    440       Helical. {ECO:0000255}.
FT   TRANSMEM    470    490       Helical. {ECO:0000255}.
FT   ZN_FING     547    586       RING-type; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00175}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000250|UniProtKB:Q8WU17}.
FT   MOD_RES     636    636       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q8WU17}.
FT   MOD_RES     637    637       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q8WU17}.
FT   MOD_RES     667    667       Phosphothreonine.
FT                                {ECO:0000244|PubMed:17242355,
FT                                ECO:0000244|PubMed:21183079}.
FT   CONFLICT    248    248       T -> A (in Ref. 1; BAC28327).
FT                                {ECO:0000305}.
CC   --------------------------------------------------------------------------
CC   The following FT lines are automated annotations from the MyHits database.
CC   --------------------------------------------------------------------------
FT   MYHIT       547    585       ismart:RING [T]
FT   MYHIT       546    585       ipfam:zf-RING_2 [T]
FT   MYHIT       546    586       ismart:RINGv [T]
FT   MYHIT        20    516       ipfam:TRC8_N [T]
FT   MYHIT       547    586       iprf:ZF_RING_2 [T]
SQ   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
//