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Protein

E3 ubiquitin-protein ligase RNF6

Gene

Rnf6

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

E3 ubiquitin-protein ligase mediating 'Lys-48'-linked polyubiquitination of LIMK1 and its subsequent targeting to the proteasome for degradation. Negatively regulates axonal outgrowth through regulation of the LIMK1 turnover. Mediates 'Lys-6' and 'Lys-27'-linked polyubiquitination of AR/androgen receptor thereby modulating its transcriptional activity. May also bind DNA and function as a transcriptional regulator.2 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri614 – 65542RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • androgen receptor binding Source: UniProtKB
  • DNA binding Source: MGI
  • ligase activity Source: UniProtKB-KW
  • ubiquitin protein ligase activity Source: MGI
  • ubiquitin-protein transferase activity Source: MGI
  • zinc ion binding Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF6 (EC:6.3.2.-)
Alternative name(s):
RLIM-like protein
Gene namesi
Name:Rnf6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1921382. Rnf6.

Subcellular locationi

GO - Cellular componenti

  • axon Source: MGI
  • cytoplasm Source: MGI
  • intracellular membrane-bounded organelle Source: MGI
  • nuclear membrane Source: MGI
  • nucleus Source: UniProtKB
  • PML body Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 667667E3 ubiquitin-protein ligase RNF6PRO_0000395751Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei559 – 5591PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9DBU5.
MaxQBiQ9DBU5.
PaxDbiQ9DBU5.
PRIDEiQ9DBU5.

PTM databases

iPTMnetiQ9DBU5.
PhosphoSiteiQ9DBU5.

Expressioni

Tissue specificityi

Widely expressed with higher expression in the testis in both germ cells and Sertoli cells.1 Publication

Developmental stagei

Expressed in the floor plate and ventral portions of the developing neural tube of E12.5 to E13 mouse embryos. Found in developing neuronal projections (at protein level).1 Publication

Gene expression databases

BgeeiQ9DBU5.
ExpressionAtlasiQ9DBU5. baseline and differential.
GenevisibleiQ9DBU5. MM.

Interactioni

Subunit structurei

Interacts with AR (By similarity). Interacts with LIMK1.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi216515. 2 interactions.
IntActiQ9DBU5. 2 interactions.
MINTiMINT-8174122.
STRINGi10090.ENSMUSP00000067559.

Structurei

3D structure databases

ProteinModelPortaliQ9DBU5.
SMRiQ9DBU5. Positions 613-655.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni589 – 66779Required for polyubiquitinationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi174 – 410237Arg-richAdd
BLAST

Sequence similaritiesi

Belongs to the RNF12 family.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri614 – 65542RING-type; atypicalPROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG0800. Eukaryota.
ENOG41121N2. LUCA.
GeneTreeiENSGT00730000110459.
HOGENOMiHOG000273881.
HOVERGENiHBG009886.
InParanoidiQ9DBU5.
OMAiTIRIPLR.
OrthoDBiEOG7M6D6Z.
PhylomeDBiQ9DBU5.
TreeFamiTF325756.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9DBU5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPSRSRSGG SGEESSFQEN ERRWQQERLH REEAYYQFIN ELSDEDYRLM
60 70 80 90 100
RDHNLLGTPG EITSEELQQR LERAKEQLAS QPGSDSAASD GDSESLRAHS
110 120 130 140 150
DEDSLLRWLN TFRRTGNVTR SGQNGNQSWR AVSRTNPNSG EFGFSLEIHI
160 170 180 190 200
NPDNRGSEMH GEDSTDIPLS GVNREHRQQR PSSPVARRTR SQTSMSSSGP
210 220 230 240 250
RGRRGARRQG SVQGSFATLG RLRNGIGVAL GVPRVSAPRT NVINSHTNQS
260 270 280 290 300
DGSTLRQGGR QRFGAAHIWE NGARSNVTVR NTNQRLEPIR LRPAFSSRSR
310 320 330 340 350
SPIQRQNGTV HHNSQRQGRP VQQTGRNRSV RHRGVTRVFL EQGREHRGTD
360 370 380 390 400
YTPLSNSRLV SRITVEEGES SRSSAATQRH PAITLDLQVR RIRPGETRDR
410 420 430 440 450
DSIANRTRSR AGLAESTVES TSGGFHRTIS HLERSGVRTY VSTITVPLRR
460 470 480 490 500
ISENDVVEPS SVALRSILRQ IMTGFGELSS LMEVEPASEN QSNGQRLPEV
510 520 530 540 550
YLELSNGDAA DDSGQHGRAS SQASQAQDGA EMLAVREPAP PQARPSGSRS
560 570 580 590 600
RRQLGRADSV VEAGTLPILR LAHFFLLNEG DDDPIRGLTK EQIDNLSTRS
610 620 630 640 650
YEQDGVDSEL GKVCSVCISD YVAGNKLRQL PCLHEFHIHC IDRWLSENCT
660
CPVCRRPVLE FGATSSG
Length:667
Mass (Da):74,091
Last modified:June 1, 2001 - v1
Checksum:i66B26D8DC20D571A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti3 – 31P → L in AAK84435 (PubMed:11971979).Curated
Sequence conflicti3 – 31P → L in EDL05801 (Ref. 3) Curated
Sequence conflicti3 – 31P → L in EDL05802 (Ref. 3) Curated
Sequence conflicti346 – 3461H → R in AAK84435 (PubMed:11971979).Curated
Sequence conflicti346 – 3461H → R in EDL05801 (Ref. 3) Curated
Sequence conflicti346 – 3461H → R in EDL05802 (Ref. 3) Curated
Sequence conflicti346 – 3461H → R in AAI38546 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY039004 mRNA. Translation: AAK84435.1.
AK004745 mRNA. Translation: BAB23526.1.
AK150269 mRNA. Translation: BAE29425.1.
AK152106 mRNA. Translation: BAE30953.1.
CH466614 Genomic DNA. Translation: EDL05801.1.
CH466614 Genomic DNA. Translation: EDL05802.1.
BC138545 mRNA. Translation: AAI38546.1.
CCDSiCCDS19868.1.
RefSeqiNP_001243014.1. NM_001256085.1.
NP_001243016.1. NM_001256087.1.
NP_083050.1. NM_028774.3.
UniGeneiMm.26696.

Genome annotation databases

EnsembliENSMUST00000067837; ENSMUSP00000067559; ENSMUSG00000029634.
ENSMUST00000161859; ENSMUSP00000124293; ENSMUSG00000029634.
ENSMUST00000169407; ENSMUSP00000128774; ENSMUSG00000029634.
GeneIDi74132.
KEGGimmu:74132.
UCSCiuc009anb.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY039004 mRNA. Translation: AAK84435.1.
AK004745 mRNA. Translation: BAB23526.1.
AK150269 mRNA. Translation: BAE29425.1.
AK152106 mRNA. Translation: BAE30953.1.
CH466614 Genomic DNA. Translation: EDL05801.1.
CH466614 Genomic DNA. Translation: EDL05802.1.
BC138545 mRNA. Translation: AAI38546.1.
CCDSiCCDS19868.1.
RefSeqiNP_001243014.1. NM_001256085.1.
NP_001243016.1. NM_001256087.1.
NP_083050.1. NM_028774.3.
UniGeneiMm.26696.

3D structure databases

ProteinModelPortaliQ9DBU5.
SMRiQ9DBU5. Positions 613-655.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi216515. 2 interactions.
IntActiQ9DBU5. 2 interactions.
MINTiMINT-8174122.
STRINGi10090.ENSMUSP00000067559.

PTM databases

iPTMnetiQ9DBU5.
PhosphoSiteiQ9DBU5.

Proteomic databases

EPDiQ9DBU5.
MaxQBiQ9DBU5.
PaxDbiQ9DBU5.
PRIDEiQ9DBU5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000067837; ENSMUSP00000067559; ENSMUSG00000029634.
ENSMUST00000161859; ENSMUSP00000124293; ENSMUSG00000029634.
ENSMUST00000169407; ENSMUSP00000128774; ENSMUSG00000029634.
GeneIDi74132.
KEGGimmu:74132.
UCSCiuc009anb.2. mouse.

Organism-specific databases

CTDi6049.
MGIiMGI:1921382. Rnf6.

Phylogenomic databases

eggNOGiKOG0800. Eukaryota.
ENOG41121N2. LUCA.
GeneTreeiENSGT00730000110459.
HOGENOMiHOG000273881.
HOVERGENiHBG009886.
InParanoidiQ9DBU5.
OMAiTIRIPLR.
OrthoDBiEOG7M6D6Z.
PhylomeDBiQ9DBU5.
TreeFamiTF325756.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

PROiQ9DBU5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DBU5.
ExpressionAtlasiQ9DBU5. baseline and differential.
GenevisibleiQ9DBU5. MM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
[Graphical view]
PROSITEiPS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Gene control in germinal differentiation: RNF6, a transcription regulatory protein in the mouse sertoli cell."
    Lopez P., Vidal F., Martin L., Lopez-Fernandez L.A., Rual J.F., Rosen B.S., Cuzin F., Rassoulzadegan M.
    Mol. Cell. Biol. 22:3488-3496(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: C57BL/6 X DBA/2.
    Tissue: Testis.
  2. "The transcriptional landscape of the mammalian genome."
    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.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Bone marrow and Lung.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  5. Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INTERACTION WITH LIMK1.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Heart, Kidney, Lung and Spleen.

Entry informationi

Entry nameiRNF6_MOUSE
AccessioniPrimary (citable) accession number: Q9DBU5
Secondary accession number(s): B2RRR0, Q8K565
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.