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Q9Y3C5

- RNF11_HUMAN

UniProt

Q9Y3C5 - RNF11_HUMAN

Protein

RING finger protein 11

Gene

RNF11

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Essential component of a ubiquitin-editing protein complex, comprising also TNFAIP3, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. Promotes the association of TNFAIP3 to RIPK1 after TNF stimulation. TNFAIP3 deubiquitinates 'Lys-63' polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Recruits STAMBP to the E3 ubiquitin-ligase SMURF2 for ubiquitination, leading to its degradation by the 26S proteasome.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri99 – 14042RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: ProtInc
    2. protein binding Source: IntAct
    3. ubiquitin-protein transferase activity Source: FlyBase
    4. zinc ion binding Source: ProtInc

    GO - Biological processi

    1. protein autoubiquitination Source: FlyBase
    2. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: UniProtKB

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RING finger protein 11
    Gene namesi
    Name:RNF11
    ORF Names:CGI-123
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:10056. RNF11.

    Subcellular locationi

    Early endosome. Recycling endosome. Cytoplasm. Nucleus
    Note: Predominantly cytoplasmic, when unphosphorylated, and nuclear, when phosphorylated by PKB/AKT1.1 Publication

    GO - Cellular componenti

    1. early endosome Source: UniProtKB-SubCell
    2. extracellular vesicular exosome Source: UniProt
    3. nucleus Source: UniProtKB-SubCell
    4. recycling endosome Source: UniProtKB-SubCell
    5. ubiquitin ligase complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Endosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi2 – 21G → A: Loss of myristoylation. Change in subcellular location: Becomes diffused throughout the cytosol. Strong reduction of ubiquitination. Reduced efficiency of ITCH-binding. 1 Publication
    Mutagenesisi4 – 41C → S: Change in subcellular location: Becomes partially cytosolic and retained in association with the Golgi apparatus. Partial reduction of ubiquitination. 1 Publication
    Mutagenesisi12 – 121D → A: Loss of GGA1-binding. 1 Publication
    Mutagenesisi15 – 151L → A: Loss of GGA1-binding. 1 Publication
    Mutagenesisi16 – 161L → A: Loss of GGA1-binding. 1 Publication
    Mutagenesisi40 – 401Y → A: Loss of ITCH-, SMURF2- and WWP1-binding. Partial loss of ubiquitination by ITCH. No effect on STAMBP-binding; when associated with S-99 and S-102. Persistent TNF-mediated NFKBIA phosphorylation. Loss of stimulus-dependent complex formation with TAX1BP1, TNFAIP3 and RIPK1. 5 Publications
    Mutagenesisi99 – 991C → S: No effect on STAMBP- and SMURF2-binding; when associated with S-102. Persistent TNF-mediated NFKBIA phosphorylation. No effect on STAMBP-binding; when associated with A-40 and S-102. No effect on ubiquitination by ITCH; when associated with S-102. Loss of stimulus-dependent complex formation with TAX1BP1, TNFAIP3 and RIPK1. 4 Publications
    Mutagenesisi102 – 1021C → S: No effect on STAMBP- and SMURF2-binding; when associated with S-99. No effect on ubiquitination by ITCH; when associated with S-102. No effect on STAMBP-binding; when associated with A-40 and S-99. 3 Publications
    Mutagenesisi103 – 1031M → A or G: Loss of UBE2N-binding. No gain of UBE2L3-binding. 1 Publication
    Mutagenesisi103 – 1031M → L: No effect on UBE2N-binding. No gain of UBE2L3-binding; when associated with L-127 and L-128. 1 Publication
    Mutagenesisi103 – 1031M → V: No effect on UBE2N-binding. Gain of UBE2L3-binding. 1 Publication
    Mutagenesisi127 – 1271D → L: No effect on UBE2N-binding. No gain of UBE2L3-binding; when associated with L-128. 1 Publication
    Mutagenesisi128 – 1281D → L: No effect on UBE2N-binding. No gain of UBE2L3-binding. 1 Publication
    Mutagenesisi135 – 1351T → E: Loss of phosphorylation and of 14-3-3-binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA34420.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 154153RING finger protein 11PRO_0000056050Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine2 Publications
    Lipidationi4 – 41S-palmitoyl cysteine1 Publication
    Modified residuei135 – 1351Phosphothreonine; by PKB/AKT11 Publication

    Post-translational modificationi

    Ubiquitinated in the presence of ITCH, or SMURF2, and UBE2D1, as well as WWP1.2 Publications
    Phosphorylation by PKB/AKT1 may accelerate degradation by the proteasome.1 Publication
    Acylation at both Gly-2 and Cys-4 is required for proper localization to the endosomes.1 Publication

    Keywords - PTMi

    Lipoprotein, Myristate, Palmitate, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9Y3C5.
    PaxDbiQ9Y3C5.
    PRIDEiQ9Y3C5.

    PTM databases

    PhosphoSiteiQ9Y3C5.

    Expressioni

    Tissue specificityi

    Expressed at low levels in the lung, liver, kidney, pancreas, spleen, prostate, thymus, ovary, small intestine, colon, and peripheral blood lymphocytes, and, at intermediate levels, in the testis, heart, brain and placenta. Highest expression in the skeletal muscle. In the brain, expressed at different levels in several regions: high levels in the amygdala, moderate in the hippocampus and thalamus, low in the caudate and extremely low levels in the corpus callosum (at protein level). Restricted to neurons, enriched in somatodendritic compartments and excluded from white matter (at protein level). In substantia nigra, present in cell bodies and processes of dopaminergic and nondopaminergic cells (at protein level). In Parkinson disease, sequestered in Lewy bodies and neurites. Overexpressed in breast cancer cells, but not detected in the surrounding stroma and weakly, if at all, in normal breast epithelial cells (at protein level). Also expressed in several tumor cell lines.3 Publications

    Gene expression databases

    BgeeiQ9Y3C5.
    CleanExiHS_RNF11.
    GenevestigatoriQ9Y3C5.

    Organism-specific databases

    HPAiHPA045781.
    HPA050359.

    Interactioni

    Subunit structurei

    Interacts (when phosphorylated) with 14-3-3. Interacts with the E3 ubiquitin-ligases NEDD4, ITCH, SMURF2 and WWP1 By similarity. Also interacts with the E2 ubiquitin-conjugating enzymes UBE2D1 and UBE2N, but neither with CDC34, nor with UBE2L3. Interacts with ZNF350, EPS15 and STAMBP. After TNF stimulation, interacts with TAX1BP1, TNFAIP3 and RIPK1; these interaction are transient and they are lost after 1 hour of stimulation with TNF By similarity. Interacts with GGA1.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GGA1Q9UJY53EBI-396669,EBI-447141
    ITCHQ96J022EBI-396669,EBI-1564678
    NEDD4P469342EBI-396669,EBI-726944
    SMURF2Q9HAU45EBI-396669,EBI-396727
    STAMBPO956302EBI-396669,EBI-396676
    TAX1BP1Q86VP12EBI-396669,EBI-529518
    TNFAIP3P215802EBI-396669,EBI-527670
    UBBP0CG472EBI-396669,EBI-413034
    UBE2D1P516684EBI-396669,EBI-743540
    UBE2D2P628375EBI-396669,EBI-347677
    UBE2D3P610773EBI-396669,EBI-348268
    UBE2D4Q9Y2X84EBI-396669,EBI-745527
    UBE2E1P519652EBI-396669,EBI-348546
    UBE2NP610884EBI-396669,EBI-1052908

    Protein-protein interaction databases

    BioGridi117941. 91 interactions.
    IntActiQ9Y3C5. 60 interactions.
    MINTiMINT-1180165.
    STRINGi9606.ENSP00000242719.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y3C5.
    SMRiQ9Y3C5. Positions 98-139.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi37 – 404WW-binding

    Domaini

    The WW-binding motif mediates interaction with NEDD4.By similarity

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri99 – 14042RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG265447.
    HOGENOMiHOG000007448.
    HOVERGENiHBG058444.
    InParanoidiQ9Y3C5.
    KOiK11980.
    OMAiQEQIHVP.
    OrthoDBiEOG7H4DVW.
    PhylomeDBiQ9Y3C5.
    TreeFamiTF318022.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9Y3C5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGNCLKSPTS DDISLLHESQ SDRASFGEGT EPDQEPPPPY QEQVPVPVYH    50
    PTPSQTRLAT QLTEEEQIRI AQRIGLIQHL PKGVYDPGRD GSEKKIRECV 100
    ICMMDFVYGD PIRFLPCMHI YHLDCIDDWL MRSFTCPSCM EPVDAALLSS 150
    YETN 154
    Length:154
    Mass (Da):17,444
    Last modified:November 1, 1999 - v1
    Checksum:iC368E38148FC1D0D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti124 – 1241D → G in BAF85736. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti11 – 111D → E.
    Corresponds to variant rs12077069 [ dbSNP | Ensembl ].
    VAR_058272

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB024703 mRNA. Translation: BAA84683.1.
    AF151881 mRNA. Translation: AAD34118.1.
    AK293047 mRNA. Translation: BAF85736.1.
    AK313140 mRNA. Translation: BAG35959.1.
    AL162430 Genomic DNA. Translation: CAI13140.1.
    CH471059 Genomic DNA. Translation: EAX06831.1.
    BC020964 mRNA. Translation: AAH20964.1.
    BC047654 mRNA. Translation: AAH47654.1.
    CCDSiCCDS556.1.
    RefSeqiNP_055187.1. NM_014372.4.
    UniGeneiHs.309641.

    Genome annotation databases

    EnsembliENST00000242719; ENSP00000242719; ENSG00000123091.
    GeneIDi26994.
    KEGGihsa:26994.
    UCSCiuc001csi.4. human.

    Polymorphism databases

    DMDMi21362884.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB024703 mRNA. Translation: BAA84683.1 .
    AF151881 mRNA. Translation: AAD34118.1 .
    AK293047 mRNA. Translation: BAF85736.1 .
    AK313140 mRNA. Translation: BAG35959.1 .
    AL162430 Genomic DNA. Translation: CAI13140.1 .
    CH471059 Genomic DNA. Translation: EAX06831.1 .
    BC020964 mRNA. Translation: AAH20964.1 .
    BC047654 mRNA. Translation: AAH47654.1 .
    CCDSi CCDS556.1.
    RefSeqi NP_055187.1. NM_014372.4.
    UniGenei Hs.309641.

    3D structure databases

    ProteinModelPortali Q9Y3C5.
    SMRi Q9Y3C5. Positions 98-139.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117941. 91 interactions.
    IntActi Q9Y3C5. 60 interactions.
    MINTi MINT-1180165.
    STRINGi 9606.ENSP00000242719.

    PTM databases

    PhosphoSitei Q9Y3C5.

    Polymorphism databases

    DMDMi 21362884.

    Proteomic databases

    MaxQBi Q9Y3C5.
    PaxDbi Q9Y3C5.
    PRIDEi Q9Y3C5.

    Protocols and materials databases

    DNASUi 26994.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000242719 ; ENSP00000242719 ; ENSG00000123091 .
    GeneIDi 26994.
    KEGGi hsa:26994.
    UCSCi uc001csi.4. human.

    Organism-specific databases

    CTDi 26994.
    GeneCardsi GC01P051701.
    HGNCi HGNC:10056. RNF11.
    HPAi HPA045781.
    HPA050359.
    MIMi 612598. gene.
    neXtProti NX_Q9Y3C5.
    PharmGKBi PA34420.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG265447.
    HOGENOMi HOG000007448.
    HOVERGENi HBG058444.
    InParanoidi Q9Y3C5.
    KOi K11980.
    OMAi QEQIHVP.
    OrthoDBi EOG7H4DVW.
    PhylomeDBi Q9Y3C5.
    TreeFami TF318022.

    Miscellaneous databases

    ChiTaRSi RNF11. human.
    GeneWikii RNF11.
    GenomeRNAii 26994.
    NextBioi 49462.
    PROi Q9Y3C5.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9Y3C5.
    CleanExi HS_RNF11.
    Genevestigatori Q9Y3C5.

    Family and domain databases

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

    Publicationsi

    1. "Cloning and expression profile of mouse and human genes, Rnf11/RNF11, encoding a novel RING-H2 finger protein."
      Seki N., Hattori A., Hayashi A., Kozuma S., Sasaki M., Suzuki Y., Sugano S., Muramatsu M., Saito T.
      Biochim. Biophys. Acta 1489:421-427(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
      Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
      Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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].
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 and Skin.
    7. "Molecular characterization of ring finger protein 11."
      Connor M.K., Azmi P.B., Subramaniam V., Li H., Seth A.K.
      Mol. Cancer Res. 3:453-461(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 70-113 AND 132-154, PHOSPHORYLATION AT THR-135, SUBCELLULAR LOCATION, INTERACTION WITH 14-3-3, MUTAGENESIS OF THR-135.
    8. "The RING-H2 protein RNF11 is differentially expressed in breast tumours and interacts with HECT-type E3 ligases."
      Kitching R., Wong M.J., Koehler D., Burger A.M., Landberg G., Gish G., Seth A.K.
      Biochim. Biophys. Acta 1639:104-112(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ITCH, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF TYR-40.
    9. "The RING-H2 protein RNF11 is overexpressed in breast cancer and is a target of Smurf2 E3 ligase."
      Subramaniam V., Li H., Wong M.J., Kitching R., Attisano L., Wrana J., Zubovits J., Burger A.M., Seth A.K.
      Br. J. Cancer 89:1538-1544(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH SMURF2 AND UBE2D1, UBIQUITINATION, MUTAGENESIS OF TYR-40; CYS-99 AND CYS-102.
    10. "An RNF11: Smurf2 complex mediates ubiquitination of the AMSH protein."
      Li H., Seth A.K.
      Oncogene 23:1801-1808(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ZNF350; EPS15 AND STAMBP, MUTAGENESIS OF TYR-40; CYS-99 AND CYS-102.
    11. "PARK10 candidate RNF11 is expressed by vulnerable neurons and localizes to Lewy bodies in Parkinson disease brain."
      Anderson L.R., Betarbet R., Gearing M., Gulcher J., Hicks A.A., Stefansson K., Lah J.J., Levey A.I.
      J. Neuropathol. Exp. Neurol. 66:955-964(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    12. "The WW domain containing E3 ubiquitin protein ligase 1 upregulates ErbB2 and EGFR through RING finger protein 11."
      Chen C., Zhou Z., Liu R., Li Y., Azmi P.B., Seth A.K.
      Oncogene 27:6845-6855(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WWP1, MUTAGENESIS OF TYR-40.
    13. "The ubiquitin-editing enzyme A20 requires RNF11 to downregulate NF-kappaB signalling."
      Shembade N., Parvatiyar K., Harhaj N.S., Harhaj E.W.
      EMBO J. 28:513-522(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TAX1BP1; TNFAIP3 AND RIPK1, MUTAGENESIS OF TYR-40 AND CYS-99.
    14. "Analysis of electrostatic contributions to the selectivity of interactions between RING-finger domains and ubiquitin-conjugating enzymes."
      Scheper J., Oliva B., Villa-Freixa J., Thomson T.M.
      Proteins 74:92-103(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UBE2N, MUTAGENESIS OF MET-103; ASP-127 AND ASP-128.
    15. "Multiple modification and protein interaction signals drive the Ring finger protein 11 (RNF11) E3 ligase to the endosomal compartment."
      Santonico E., Belleudi F., Panni S., Torrisi M.R., Cesareni G., Castagnoli L.
      Oncogene 29:5604-5618(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GGA1, MYRISTOYLATION AT GLY-2, PALMITOYLATION AT CYS-4, UBIQUITINATION BY ITCH, MUTAGENESIS OF GLY-2; CYS-4; ASP-12; LEU-15; LEU-16; CYS-99 AND CYS-102.
    16. "Strategy for comprehensive identification of human N-myristoylated proteins using an insect cell-free protein synthesis system."
      Suzuki T., Moriya K., Nagatoshi K., Ota Y., Ezure T., Ando E., Tsunasawa S., Utsumi T.
      Proteomics 10:1780-1793(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: MYRISTOYLATION AT GLY-2.

    Entry informationi

    Entry nameiRNF11_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y3C5
    Secondary accession number(s): A8KAI2, Q5T7R8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 6, 2002
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 119 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3