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Q9QZS2

- RNF4_MOUSE

UniProt

Q9QZS2 - RNF4_MOUSE

Protein

E3 ubiquitin-protein ligase RNF4

Gene

Rnf4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation. Regulates the degradation of several proteins including PML and the transcriptional activator PEA3. Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation. Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1. Alternatively, it may also bind DNA/nucleosomes and have a more direct role in the regulation of transcription for instance enhancing basal transcription and steroid receptor-mediated transcriptional activation.1 Publication

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri136 – 18146RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB
    2. ligase activity Source: UniProtKB-KW
    3. nucleosome binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. SUMO polymer binding Source: UniProtKB
    6. transcription factor binding Source: MGI
    7. ubiquitin-protein transferase activity Source: UniProtKB
    8. zinc ion binding Source: InterPro

    GO - Biological processi

    1. positive regulation of transcription, DNA-templated Source: UniProtKB
    2. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    3. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    4. protein autoubiquitination Source: UniProtKB
    5. protein K11-linked ubiquitination Source: UniProtKB
    6. protein K48-linked ubiquitination Source: UniProtKB
    7. protein K63-linked ubiquitination Source: UniProtKB
    8. protein K6-linked ubiquitination Source: UniProtKB
    9. regulation of kinetochore assembly Source: UniProtKB
    10. regulation of spindle assembly Source: UniProtKB
    11. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Ligase

    Keywords - Biological processi

    Transcription, Transcription regulation, Ubl conjugation pathway

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase RNF4 (EC:6.3.2.-)
    Alternative name(s):
    RING finger protein 4
    Gene namesi
    Name:Rnf4
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:1201691. Rnf4.

    Subcellular locationi

    Cytoplasm. Nucleus. NucleusPML body By similarity. Nucleusnucleoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. microtubule cytoskeleton Source: Ensembl
    3. nucleus Source: UniProtKB
    4. PML body Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi134 – 1341V → E: Abolishes homodimerization. Strongly reduced E3 ubiquitin ligase activity. 1 Publication
    Mutagenesisi155 – 1551S → A: No effect. 1 Publication
    Mutagenesisi155 – 1551S → E: Abolishes homodimerization. Strongly reduced E3 ubiquitin ligase activity. 1 Publication
    Mutagenesisi161 – 1611V → A: Abolishes homodimerization. Strongly reduced E3 ubiquitin ligase activity. 1 Publication
    Mutagenesisi193 – 1931Y → A: Abolishes homodimerization. Loss of E3 ubiquitin ligase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 194194E3 ubiquitin-protein ligase RNF4PRO_0000056044Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei98 – 981Phosphoserine1 Publication
    Modified residuei99 – 991PhosphoserineBy similarity

    Post-translational modificationi

    Sumoylated; conjugated by one or two SUMO1 moieties.By similarity
    Autoubiquitinated.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiQ9QZS2.

    PTM databases

    PhosphoSiteiQ9QZS2.

    Miscellaneous databases

    PMAP-CutDBQ9QZS2.

    Expressioni

    Tissue specificityi

    In the embryo, expressed primarily in the developing nervous system with strong expression in the dorsal root ganglia and gonads. Ubiquitously expressed in the adult.

    Developmental stagei

    Expression is detected from embryonic day 7 and continues throughout development and into adulthood.

    Gene expression databases

    ArrayExpressiQ9QZS2.
    BgeeiQ9QZS2.
    CleanExiMM_RNF4.
    GenevestigatoriQ9QZS2.

    Interactioni

    Subunit structurei

    Homodimer (via RING-type zinc finger domain). Interacts with AR/the androgen receptor and TBP By similarity. Interacts with PATZ1 By similarity. Interacts with PML; SUMO1-dependent. Interacts with PML; SUMO2-dependent By similarity. Interacts with TRPS1; negatively regulates the TRPS1 transcriptional repressor activity. Interacts with GSC2. Interacts with TCF20. Interacts with PARP1. Interacts with PML By similarity.By similarity

    Protein-protein interaction databases

    BioGridi202920. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9QZS2.
    SMRiQ9QZS2. Positions 129-194.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 2020Required for ubiquitination activityAdd
    BLAST
    Regioni6 – 6560Mediates interaction with TRPS1Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi40 – 434SUMO interaction motif 1; mediates the binding to polysumoylated substrates
    Motifi50 – 534SUMO interaction motif 2; mediates the binding to polysumoylated substrates
    Motifi61 – 633SUMO interaction motif 3; mediates the binding to polysumoylated substrates
    Motifi71 – 744SUMO interaction motif 4; mediates the binding to polysumoylated substrates

    Domaini

    The RING-type zinc finger domain is required for the ubiquitination.By similarity

    Sequence similaritiesi

    Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri136 – 18146RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG327779.
    GeneTreeiENSGT00390000010318.
    HOVERGENiHBG018577.
    InParanoidiQ9QZS2.
    OMAiTHRQYHP.
    OrthoDBiEOG7SN8F1.
    PhylomeDBiQ9QZS2.
    TreeFamiTF328387.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view]
    PfamiPF13639. zf-RING_2. 1 hit.
    [Graphical view]
    SMARTiSM00184. RING. 1 hit.
    [Graphical view]
    PROSITEiPS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9QZS2-1 [UniParc]FASTAAdd to Basket

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    MSTRNPQRKR RGGTVNSRQT QKRTRETTST PEVSLETEPI ELVETVGDEI    50
    VDLTCESLEP VVVDLTHNDS VVIVEERRRP RRNGRRLRQD HADSCVVSSD 100
    DEELSRDKDV YVTTHTPRST KDDGATGPRP SGTVSCPICM DGYSEIVQNG 150
    RLIVSTECGH VFCSQCLRDS LKNANTCPTC RKKINHKRYH PIYI 194
    Length:194
    Mass (Da):21,911
    Last modified:May 1, 2000 - v1
    Checksum:i9A0A4277725C62E5
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF169300 mRNA. Translation: AAF00620.1.
    AK019171 mRNA. Translation: BAB31585.1.
    AK090162 mRNA. Translation: BAC41119.1.
    AK147057 mRNA. Translation: BAE27641.1.
    AK151116 mRNA. Translation: BAE30125.1.
    AK158987 mRNA. Translation: BAE34757.1.
    AK159778 mRNA. Translation: BAE35362.1.
    AK159949 mRNA. Translation: BAE35505.1.
    BC003282 mRNA. Translation: AAH03282.1.
    U95141 mRNA. Translation: AAC53539.1.
    CCDSiCCDS57336.1.
    RefSeqiNP_035408.1. NM_011278.4.
    XP_006503866.1. XM_006503803.1.
    XP_006503867.1. XM_006503804.1.
    XP_006503868.1. XM_006503805.1.
    UniGeneiMm.21281.

    Genome annotation databases

    EnsembliENSMUST00000030992; ENSMUSP00000030992; ENSMUSG00000029110.
    ENSMUST00000182047; ENSMUSP00000138411; ENSMUSG00000029110.
    ENSMUST00000182709; ENSMUSP00000138555; ENSMUSG00000029110.
    GeneIDi19822.
    KEGGimmu:19822.
    UCSCiuc008xcc.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF169300 mRNA. Translation: AAF00620.1 .
    AK019171 mRNA. Translation: BAB31585.1 .
    AK090162 mRNA. Translation: BAC41119.1 .
    AK147057 mRNA. Translation: BAE27641.1 .
    AK151116 mRNA. Translation: BAE30125.1 .
    AK158987 mRNA. Translation: BAE34757.1 .
    AK159778 mRNA. Translation: BAE35362.1 .
    AK159949 mRNA. Translation: BAE35505.1 .
    BC003282 mRNA. Translation: AAH03282.1 .
    U95141 mRNA. Translation: AAC53539.1 .
    CCDSi CCDS57336.1.
    RefSeqi NP_035408.1. NM_011278.4.
    XP_006503866.1. XM_006503803.1.
    XP_006503867.1. XM_006503804.1.
    XP_006503868.1. XM_006503805.1.
    UniGenei Mm.21281.

    3D structure databases

    ProteinModelPortali Q9QZS2.
    SMRi Q9QZS2. Positions 129-194.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202920. 2 interactions.

    PTM databases

    PhosphoSitei Q9QZS2.

    Proteomic databases

    PRIDEi Q9QZS2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030992 ; ENSMUSP00000030992 ; ENSMUSG00000029110 .
    ENSMUST00000182047 ; ENSMUSP00000138411 ; ENSMUSG00000029110 .
    ENSMUST00000182709 ; ENSMUSP00000138555 ; ENSMUSG00000029110 .
    GeneIDi 19822.
    KEGGi mmu:19822.
    UCSCi uc008xcc.1. mouse.

    Organism-specific databases

    CTDi 6047.
    MGIi MGI:1201691. Rnf4.

    Phylogenomic databases

    eggNOGi NOG327779.
    GeneTreei ENSGT00390000010318.
    HOVERGENi HBG018577.
    InParanoidi Q9QZS2.
    OMAi THRQYHP.
    OrthoDBi EOG7SN8F1.
    PhylomeDBi Q9QZS2.
    TreeFami TF328387.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    ChiTaRSi RNF4. mouse.
    NextBioi 297289.
    PMAP-CutDB Q9QZS2.
    PROi Q9QZS2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9QZS2.
    Bgeei Q9QZS2.
    CleanExi MM_RNF4.
    Genevestigatori Q9QZS2.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    Pfami PF13639. zf-RING_2. 1 hit.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    [Graphical view ]
    PROSITEi PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Rnf4, a RING protein expressed in the developing nervous and reproductive systems, interacts with Gscl, a gene within the DiGeorge critical region."
      Galili N., Nayak S., Epstein J.A., Buck C.A.
      Dev. Dyn. 218:102-111(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH GSC2.
      Strain: CD-1.
      Tissue: Embryo.
    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, Embryo, Kidney, Lymph node and Visual cortex.
    3. "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].
    4. "Identification and characterization of a novel RING-finger gene (RNF4) mapping at 4p16.3."
      Chiariotti L., Benvenuto G., Fedele M., Santoro M., Simeone A., Fusco A., Bruni C.B.
      Genomics 47:258-265(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-178.
      Tissue: Embryo.
    5. "Interaction between the transcription factor SPBP and the positive cofactor RNF4. An interplay between protein binding zinc fingers."
      Lyngsoe C., Bouteiller G., Damgaard C.K., Ryom D., Sanchez-Munoz S., Noerby P.L., Bonven B.J., Joergensen P.
      J. Biol. Chem. 275:26144-26149(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TCF20.
    6. "The RING finger protein RNF4, a co-regulator of transcription, interacts with the TRPS1 transcription factor."
      Kaiser F.J., Moeroey T., Chang G.T., Horsthemke B., Luedecke H.J.
      J. Biol. Chem. 278:38780-38785(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TRPS1.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    8. "PARP-1 transcriptional activity is regulated by sumoylation upon heat shock."
      Martin N., Schwamborn K., Schreiber V., Werner A., Guillier C., Zhang X.D., Bischof O., Seeler J.S., Dejean A.
      EMBO J. 28:3534-3548(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PARP1.
    9. "RING domain dimerization is essential for RNF4 function."
      Liew C.W., Sun H., Hunter T., Day C.L.
      Biochem. J. 431:23-29(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, AUTOUBIQUITINATION, MUTAGENESIS OF VAL-134; SER-155; VAL-161 AND TYR-193, SUBUNIT.

    Entry informationi

    Entry nameiRNF4_MOUSE
    AccessioniPrimary (citable) accession number: Q9QZS2
    Secondary accession number(s): O35941, Q541Z6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 117 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

    External Data

    Dasty 3