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P78317

- RNF4_HUMAN

UniProt

P78317 - RNF4_HUMAN

Protein

E3 ubiquitin-protein ligase RNF4

Gene

RNF4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      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.6 Publications

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri132 – 17746RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. androgen receptor binding Source: UniProtKB
    2. DNA binding Source: UniProtKB
    3. ligase activity Source: UniProtKB-KW
    4. nucleosome binding Source: UniProtKB
    5. protein binding Source: UniProtKB
    6. sequence-specific DNA binding transcription factor activity Source: ProtInc
    7. SUMO polymer binding Source: UniProtKB
    8. transcription coactivator activity Source: UniProtKB
    9. ubiquitin-protein transferase activity Source: UniProtKB
    10. zinc ion binding Source: ProtInc

    GO - Biological processi

    1. androgen receptor signaling pathway Source: UniProtKB
    2. positive regulation of transcription, DNA-templated Source: UniProtKB
    3. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    4. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    5. protein autoubiquitination Source: UniProtKB
    6. protein K11-linked ubiquitination Source: UniProtKB
    7. protein K48-linked ubiquitination Source: UniProtKB
    8. protein K63-linked ubiquitination Source: UniProtKB
    9. protein K6-linked ubiquitination Source: UniProtKB
    10. regulation of kinetochore assembly Source: UniProtKB
    11. regulation of spindle assembly Source: UniProtKB
    12. response to arsenic-containing substance Source: UniProtKB
    13. 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_75842. 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
    Small nuclear ring finger protein
    Short name:
    Protein SNURF
    Gene namesi
    Name:RNF4
    Synonyms:SNURF
    ORF Names:RES4-26
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:10067. RNF4.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. nucleus Source: UniProtKB
    3. PML body Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34439.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 190190E3 ubiquitin-protein ligase RNF4PRO_0000056043Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei94 – 941Phosphoserine2 Publications
    Modified residuei95 – 951Phosphoserine2 Publications

    Post-translational modificationi

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

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP78317.
    PaxDbiP78317.
    PRIDEiP78317.

    PTM databases

    PhosphoSiteiP78317.

    Expressioni

    Tissue specificityi

    Widely expressed at low levels in many tissues; highly expressed in testis.1 Publication

    Gene expression databases

    ArrayExpressiP78317.
    BgeeiP78317.
    CleanExiHS_RNF4.
    GenevestigatoriP78317.

    Organism-specific databases

    HPAiHPA049356.

    Interactioni

    Subunit structurei

    Homodimer (via RING-type zinc finger domain). Interacts with GSC2 By similarity. Interacts with AR/the androgen receptor and TBP By similarity. Interacts with TCF20 By similarity. Interacts with PATZ1. Interacts with TRPS1; negatively regulates TRPS1 transcriptional repressor activity. Interacts with PML; SUMO1-dependent. Interacts with PML; SUMO2-dependent. Interacts with PARP1. Interacts with PML (isoform PML-1, isoform PML-2, isoform PML-3, isoform PML-4, isoform PML-5 and isoform PML-6).By similarity6 Publications

    Protein-protein interaction databases

    BioGridi111974. 44 interactions.
    IntActiP78317. 19 interactions.
    MINTiMINT-271054.
    STRINGi9606.ENSP00000315212.

    Structurei

    Secondary structure

    1
    190
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni133 – 1353
    Helixi139 – 1446
    Beta strandi149 – 1524
    Beta strandi153 – 1553
    Beta strandi157 – 1593
    Helixi160 – 16910
    Turni174 – 1763
    Turni181 – 1833
    Beta strandi185 – 1873

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EA6NMR-A122-183[»]
    2XEUX-ray1.50A130-190[»]
    4PPEX-ray2.00A/B120-190[»]
    ProteinModelPortaliP78317.
    SMRiP78317. Positions 124-190.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP78317.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 1616Required for ubiquitination activityBy similarityAdd
    BLAST
    Regioni4 – 6158Mediates interaction with TRPS1By similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi36 – 394SUMO interaction motif 1; mediates the binding to polysumoylated substrates
    Motifi46 – 494SUMO interaction motif 2; mediates the binding to polysumoylated substrates
    Motifi57 – 593SUMO interaction motif 3; mediates the binding to polysumoylated substrates
    Motifi67 – 704SUMO interaction motif 4; mediates the binding to polysumoylated substrates

    Domaini

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

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri132 – 17746RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG327779.
    HOGENOMiHOG000059548.
    HOVERGENiHBG018577.
    InParanoidiP78317.
    OMAiTHRQYHP.
    PhylomeDBiP78317.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P78317-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSTRKRRGGA INSRQAQKRT REATSTPEIS LEAEPIELVE TAGDEIVDLT    50
    CESLEPVVVD LTHNDSVVIV DERRRPRRNA RRLPQDHADS CVVSSDDEEL 100
    SRDRDVYVTT HTPRNARDEG ATGLRPSGTV SCPICMDGYS EIVQNGRLIV 150
    STECGHVFCS QCLRDSLKNA NTCPTCRKKI NHKRYHPIYI 190
    Length:190
    Mass (Da):21,319
    Last modified:May 1, 1997 - v1
    Checksum:iE5E3AE4A9B28CF9D
    GO
    Isoform 2 (identifier: P78317-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         72-113: ERRRPRRNAR...RDVYVTTHTP → GPQVLSVVPS...SSVASASVIP
         114-190: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:113
    Mass (Da):12,126
    Checksum:iC65BF8B284670597
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei72 – 11342ERRRP…TTHTP → GPQVLSVVPSAWTDTQRSCR MDVSSFPQNAAMSSVASASV IP in isoform 2. 1 PublicationVSP_045789Add
    BLAST
    Alternative sequencei114 – 19077Missing in isoform 2. 1 PublicationVSP_045790Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB000468 mRNA. Translation: BAA19122.1.
    U95140 mRNA. Translation: AAC52022.1.
    AK128038 mRNA. Translation: BAG54620.1.
    AK309509 mRNA. No translation available.
    AK312534 mRNA. Translation: BAG35433.1.
    AL110117 Genomic DNA. No translation available.
    AL645924 Genomic DNA. No translation available.
    BX322586 Genomic DNA. No translation available.
    CR450722 Genomic DNA. No translation available.
    CR545473 Genomic DNA. No translation available.
    BC031935 mRNA. Translation: AAH31935.1.
    CCDSiCCDS47001.1. [P78317-1]
    CCDS54713.1. [P78317-2]
    RefSeqiNP_001171938.1. NM_001185009.2. [P78317-1]
    NP_001171939.1. NM_001185010.2. [P78317-2]
    NP_002929.1. NM_002938.4. [P78317-1]
    UniGeneiHs.66394.

    Genome annotation databases

    GeneIDi6047.
    KEGGihsa:6047.
    UCSCiuc003gfb.3. human. [P78317-1]

    Polymorphism databases

    DMDMi18202358.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB000468 mRNA. Translation: BAA19122.1 .
    U95140 mRNA. Translation: AAC52022.1 .
    AK128038 mRNA. Translation: BAG54620.1 .
    AK309509 mRNA. No translation available.
    AK312534 mRNA. Translation: BAG35433.1 .
    AL110117 Genomic DNA. No translation available.
    AL645924 Genomic DNA. No translation available.
    BX322586 Genomic DNA. No translation available.
    CR450722 Genomic DNA. No translation available.
    CR545473 Genomic DNA. No translation available.
    BC031935 mRNA. Translation: AAH31935.1 .
    CCDSi CCDS47001.1. [P78317-1 ]
    CCDS54713.1. [P78317-2 ]
    RefSeqi NP_001171938.1. NM_001185009.2. [P78317-1 ]
    NP_001171939.1. NM_001185010.2. [P78317-2 ]
    NP_002929.1. NM_002938.4. [P78317-1 ]
    UniGenei Hs.66394.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EA6 NMR - A 122-183 [» ]
    2XEU X-ray 1.50 A 130-190 [» ]
    4PPE X-ray 2.00 A/B 120-190 [» ]
    ProteinModelPortali P78317.
    SMRi P78317. Positions 124-190.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111974. 44 interactions.
    IntActi P78317. 19 interactions.
    MINTi MINT-271054.
    STRINGi 9606.ENSP00000315212.

    PTM databases

    PhosphoSitei P78317.

    Polymorphism databases

    DMDMi 18202358.

    Proteomic databases

    MaxQBi P78317.
    PaxDbi P78317.
    PRIDEi P78317.

    Protocols and materials databases

    DNASUi 6047.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 6047.
    KEGGi hsa:6047.
    UCSCi uc003gfb.3. human. [P78317-1 ]

    Organism-specific databases

    CTDi 6047.
    GeneCardsi GC04P002463.
    HGNCi HGNC:10067. RNF4.
    HPAi HPA049356.
    MIMi 602850. gene.
    neXtProti NX_P78317.
    PharmGKBi PA34439.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG327779.
    HOGENOMi HOG000059548.
    HOVERGENi HBG018577.
    InParanoidi P78317.
    OMAi THRQYHP.
    PhylomeDBi P78317.
    TreeFami TF328387.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .
    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    ChiTaRSi RNF4. human.
    EvolutionaryTracei P78317.
    GeneWikii RNF4.
    GenomeRNAii 6047.
    NextBioi 23561.
    PROi P78317.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P78317.
    Bgeei P78317.
    CleanExi HS_RNF4.
    Genevestigatori P78317.

    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. "The primary structure and genomic organization of five novel transcripts located close to the Huntington's disease gene on human chromosome 4p16.3."
      Hadano S., Ishida Y., Ikeda J.-E.
      DNA Res. 5:177-186(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Brain.
    2. "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] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Brain.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Hair follicle dermal papilla, Testis and Tongue.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1).
      Tissue: Testis.
    6. "A novel member of the BTB/POZ family, PATZ, associates with the RNF4 RING finger protein and acts as a transcriptional repressor."
      Fedele M., Benvenuto G., Pero R., Majello B., Battista S., Lembo F., Vollono E., Day P.M., Santoro M., Lania L., Bruni C.B., Fusco A., Chiatiotti L.
      J. Biol. Chem. 275:7894-7901(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PATZ1.
    7. "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: FUNCTION, INTERACTION WITH TRPS1, SUBCELLULAR LOCATION.
    8. "SUMO-1 promotes association of SNURF (RNF4) with PML nuclear bodies."
      Haekli M., Karvonen U., Jaenne O.A., Palvimo J.J.
      Exp. Cell Res. 304:224-233(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PML, SUBCELLULAR LOCATION.
    9. "RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation."
      Tatham M.H., Geoffroy M.C., Shen L., Plechanovova A., Hattersley N., Jaffray E.G., Palvimo J.J., Hay R.T.
      Nat. Cell Biol. 10:538-546(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94 AND SER-95, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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.
    12. "Extracellular signal-regulated kinase mitogen-activated protein kinase signaling initiates a dynamic interplay between sumoylation and ubiquitination to regulate the activity of the transcriptional activator PEA3."
      Guo B., Sharrocks A.D.
      Mol. Cell. Biol. 29:3204-3218(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94 AND SER-95, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "The SUMO protease SENP6 is essential for inner kinetochore assembly."
      Mukhopadhyay D., Arnaoutov A., Dasso M.
      J. Cell Biol. 188:681-692(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. "Arsenic-induced SUMO-dependent recruitment of RNF4 into PML nuclear bodies."
      Geoffroy M.C., Jaffray E.G., Walker K.J., Hay R.T.
      Mol. Biol. Cell 21:4227-4239(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SUMOYLATED PML, SUBCELLULAR LOCATION.
    16. "RNF4 and VHL regulate the proteasomal degradation of SUMO-conjugated Hypoxia-Inducible Factor-2alpha."
      van Hagen M., Overmeer R.M., Abolvardi S.S., Vertegaal A.C.
      Nucleic Acids Res. 38:1922-1931(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. "Requirement of PML SUMO interacting motif for RNF4- or arsenic trioxide-induced degradation of nuclear PML isoforms."
      Maroui M.A., Kheddache-Atmane S., El Asmi F., Dianoux L., Aubry M., Chelbi-Alix M.K.
      PLoS ONE 7:E44949-E44949(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PML.
    18. "Solution structure of the RING domain of the human RING finger protein 4."
      RIKEN structural genomics initiative (RSGI)
      Submitted (JUL-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 122-183.

    Entry informationi

    Entry nameiRNF4_HUMAN
    AccessioniPrimary (citable) accession number: P78317
    Secondary accession number(s): B2R6D6, D6RF58, Q49AR8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 135 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3