RNF6_MOUSE
ID RNF6_MOUSE Reviewed; 667 AA.
AC Q9DBU5; B2RRR0; Q8K565;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=E3 ubiquitin-protein ligase RNF6;
DE EC=2.3.2.27;
DE AltName: Full=RING-type E3 ubiquitin transferase RNF6 {ECO:0000305};
DE AltName: Full=RLIM-like protein;
GN Name=Rnf6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6 X DBA/2; TISSUE=Testis;
RX PubMed=11971979; DOI=10.1128/mcb.22.10.3488-3496.2002;
RA Lopez P., Vidal F., Martin L., Lopez-Fernandez L.A., Rual J.F., Rosen B.S.,
RA Cuzin F., Rassoulzadegan M.;
RT "Gene control in germinal differentiation: RNF6, a transcription regulatory
RT protein in the mouse sertoli cell.";
RL Mol. Cell. Biol. 22:3488-3496(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Lung;
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., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., 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., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INTERACTION WITH
RP LIMK1.
RX PubMed=16204183; DOI=10.1101/gad.1340605;
RA Tursun B., Schlueter A., Peters M.A., Viehweger B., Ostendorff H.P.,
RA Soosairajah J., Drung A., Bossenz M., Johnsen S.A., Schweizer M.,
RA Bernard O., Bach I.;
RT "The ubiquitin ligase Rnf6 regulates local LIM kinase 1 levels in axonal
RT growth cones.";
RL Genes Dev. 19:2307-2319(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart, Kidney, Lung, and Spleen;
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 expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: E3 ubiquitin-protein ligase mediating 'Lys-48'-linked
CC polyubiquitination of LIMK1 and its subsequent targeting to the
CC proteasome for degradation. Negatively regulates axonal outgrowth
CC through regulation of the LIMK1 turnover. Mediates 'Lys-6' and 'Lys-
CC 27'-linked polyubiquitination of AR/androgen receptor thereby
CC modulating its transcriptional activity. May also bind DNA and function
CC as a transcriptional regulator. {ECO:0000269|PubMed:11971979,
CC ECO:0000269|PubMed:16204183}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Interacts with AR (By similarity). Interacts with LIMK1.
CC {ECO:0000250, ECO:0000269|PubMed:16204183}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cell projection, axon.
CC Nucleus, PML body. Note=Localizes to the PML nuclear bodies in Sertoli
CC cells.
CC -!- TISSUE SPECIFICITY: Widely expressed with higher expression in the
CC testis in both germ cells and Sertoli cells.
CC {ECO:0000269|PubMed:11971979}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the floor plate and ventral portions
CC of the developing neural tube of 12.5 dpc to 13 dpc mouse embryos.
CC Found in developing neuronal projections (at protein level).
CC {ECO:0000269|PubMed:16204183}.
CC -!- SIMILARITY: Belongs to the RNF12 family. {ECO:0000305}.
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DR EMBL; AY039004; AAK84435.1; -; mRNA.
DR EMBL; AK004745; BAB23526.1; -; mRNA.
DR EMBL; AK150269; BAE29425.1; -; mRNA.
DR EMBL; AK152106; BAE30953.1; -; mRNA.
DR EMBL; CH466614; EDL05801.1; -; Genomic_DNA.
DR EMBL; CH466614; EDL05802.1; -; Genomic_DNA.
DR EMBL; BC138545; AAI38546.1; -; mRNA.
DR CCDS; CCDS19868.1; -.
DR RefSeq; NP_001243014.1; NM_001256085.1.
DR RefSeq; NP_001243016.1; NM_001256087.1.
DR RefSeq; NP_083050.1; NM_028774.3.
DR AlphaFoldDB; Q9DBU5; -.
DR SMR; Q9DBU5; -.
DR BioGRID; 216515; 2.
DR IntAct; Q9DBU5; 2.
DR MINT; Q9DBU5; -.
DR STRING; 10090.ENSMUSP00000124293; -.
DR iPTMnet; Q9DBU5; -.
DR PhosphoSitePlus; Q9DBU5; -.
DR EPD; Q9DBU5; -.
DR jPOST; Q9DBU5; -.
DR MaxQB; Q9DBU5; -.
DR PaxDb; Q9DBU5; -.
DR PRIDE; Q9DBU5; -.
DR ProteomicsDB; 301628; -.
DR Antibodypedia; 35204; 254 antibodies from 30 providers.
DR DNASU; 74132; -.
DR Ensembl; ENSMUST00000067837; ENSMUSP00000067559; ENSMUSG00000029634.
DR Ensembl; ENSMUST00000161859; ENSMUSP00000124293; ENSMUSG00000029634.
DR Ensembl; ENSMUST00000169407; ENSMUSP00000128774; ENSMUSG00000029634.
DR GeneID; 74132; -.
DR KEGG; mmu:74132; -.
DR UCSC; uc009anb.2; mouse.
DR CTD; 6049; -.
DR MGI; MGI:1921382; Rnf6.
DR VEuPathDB; HostDB:ENSMUSG00000029634; -.
DR eggNOG; KOG0800; Eukaryota.
DR GeneTree; ENSGT00940000158530; -.
DR HOGENOM; CLU_025933_0_0_1; -.
DR InParanoid; Q9DBU5; -.
DR OMA; HLPEMHS; -.
DR OrthoDB; 1487241at2759; -.
DR PhylomeDB; Q9DBU5; -.
DR TreeFam; TF325756; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 74132; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Rnf6; mouse.
DR PRO; PR:Q9DBU5; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9DBU5; protein.
DR Bgee; ENSMUSG00000029634; Expressed in lacrimal gland and 254 other tissues.
DR ExpressionAtlas; Q9DBU5; baseline and differential.
DR Genevisible; Q9DBU5; MM.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050681; F:nuclear androgen receptor binding; ISS:UniProtKB.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:MGI.
DR GO; GO:0048675; P:axon extension; IMP:MGI.
DR GO; GO:0030517; P:negative regulation of axon extension; IMP:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0044314; P:protein K27-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; IMP:UniProtKB.
DR GO; GO:0085020; P:protein K6-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0060765; P:regulation of androgen receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IDA:MGI.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Cell projection; Cytoplasm; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..667
FT /note="E3 ubiquitin-protein ligase RNF6"
FT /id="PRO_0000395751"
FT ZN_FING 614..655
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..667
FT /note="Required for polyubiquitination"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 559
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT 3
FT /note="P -> L (in Ref. 1; AAK84435 and 3; EDL05801/
FT EDL05802)"
FT /evidence="ECO:0000305"
FT CONFLICT 346
FT /note="H -> R (in Ref. 1; AAK84435, 3; EDL05801/EDL05802
FT and 4; AAI38546)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 667 AA; 74091 MW; 66B26D8DC20D571A CRC64;
MDPSRSRSGG SGEESSFQEN ERRWQQERLH REEAYYQFIN ELSDEDYRLM RDHNLLGTPG
EITSEELQQR LERAKEQLAS QPGSDSAASD GDSESLRAHS DEDSLLRWLN TFRRTGNVTR
SGQNGNQSWR AVSRTNPNSG EFGFSLEIHI NPDNRGSEMH GEDSTDIPLS GVNREHRQQR
PSSPVARRTR SQTSMSSSGP RGRRGARRQG SVQGSFATLG RLRNGIGVAL GVPRVSAPRT
NVINSHTNQS DGSTLRQGGR QRFGAAHIWE NGARSNVTVR NTNQRLEPIR LRPAFSSRSR
SPIQRQNGTV HHNSQRQGRP VQQTGRNRSV RHRGVTRVFL EQGREHRGTD YTPLSNSRLV
SRITVEEGES SRSSAATQRH PAITLDLQVR RIRPGETRDR DSIANRTRSR AGLAESTVES
TSGGFHRTIS HLERSGVRTY VSTITVPLRR ISENDVVEPS SVALRSILRQ IMTGFGELSS
LMEVEPASEN QSNGQRLPEV YLELSNGDAA DDSGQHGRAS SQASQAQDGA EMLAVREPAP
PQARPSGSRS RRQLGRADSV VEAGTLPILR LAHFFLLNEG DDDPIRGLTK EQIDNLSTRS
YEQDGVDSEL GKVCSVCISD YVAGNKLRQL PCLHEFHIHC IDRWLSENCT CPVCRRPVLE
FGATSSG
