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Q9D304

- RN128_MOUSE

UniProt

Q9D304 - RN128_MOUSE

Protein

E3 ubiquitin-protein ligase RNF128

Gene

Rnf128

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase that catalyzes 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains formation. Functions as an inhibitor of cytokine gene transcription. Inhibits IL2 and IL4 transcription, thereby playing an important role in the induction of the anergic phenotype, a long-term stable state of T-lymphocyte unresponsiveness to antigenic stimulation associated with the blockade of interleukin production. Ubiquitinates ARPC5 with 'Lys-48' linkages and COR1A with 'Lys-63' linkages leading to their degradation, down-regulation of these cytosleletal components results in impaired lamellipodium formation and reduced accumulation of F-actin at the immunological synapse. Functions in the patterning of the dorsal ectoderm; sensitizes ectoderm to respond to neural-inducing signals By similarity.By similarity

    Pathwayi

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri277 – 31842RING-type; atypicalPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ligase activity Source: UniProtKB-KW
    2. ubiquitin-protein transferase activity Source: MGI
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. negative regulation of cytokine biosynthetic process Source: MGI

    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 RNF128 (EC:6.3.2.-)
    Alternative name(s):
    Gene related to anergy in lymphocytes protein
    Goliath-related E3 ubiquitin-protein ligase 1
    RING finger protein 128
    Gene namesi
    Name:Rnf128
    Synonyms:Grail, Greul1
    ORF Names:MNCb-3816
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome X

    Organism-specific databases

    MGIiMGI:1914139. Rnf128.

    Subcellular locationi

    Endomembrane system By similarity; Single-pass membrane protein By similarity. Cytoplasmcytoskeleton By similarity. Cytoplasmperinuclear region By similarity
    Note: Localized in an asymmetric perinuclear punctate manner. Localizes to the internal pool of the transferrin recycling endosomal pathway. Partially colocalized with the endoplasmic reticulum resident HSPA5, with Golgi resident STX5, and with the late endosomal GTPase RAB7A By similarity.By similarity

    GO - Cellular componenti

    1. cytoskeleton Source: UniProtKB-SubCell
    2. endoplasmic reticulum Source: MGI
    3. Golgi apparatus Source: MGI
    4. integral component of membrane Source: UniProtKB-KW
    5. late endosome Source: MGI
    6. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi277 – 2771C → G: Loss of ubiquitination activity. 2 Publications
    Mutagenesisi280 – 2801C → G: Loss of ubiquitination activity. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3838Sequence AnalysisAdd
    BLAST
    Chaini39 – 428390E3 ubiquitin-protein ligase RNF128PRO_0000261413Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi48 – 481N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi59 – 591N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi101 – 1011N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Auto-ubiquitinated. Controls the development of T-cell clonal anergy by ubiquitination By similarity.By similarity

    Keywords - PTMi

    Glycoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiQ9D304.

    PTM databases

    PhosphoSiteiQ9D304.

    Expressioni

    Tissue specificityi

    Expressed in brain, kidney, heart, liver, ovary, testis and thymus. Expression increased as early as 4 hours by 5- to 7-fold in anergized cultures as compared to resting or activated cells.1 Publication

    Developmental stagei

    At E6.0, expressed in both the extraembryonic endoderm and extraembryonic ectoderm. After the beginning of gastrulation, expression remains extraembryonic, and is mostly confined to the visceral endoderm. At E8.5, expression appears within the mesodermally derived allantois, and is highly expressed in the epithelial layer of the yolk sac. At E9.5, expressed in the hindgut and adjoining yolk sac. At stage E10, appears to be widely expressed throughout the embryo with higher expression within the branchial arches and within intersomitic endothelial cells.1 Publication

    Inductioni

    Induced under anergic conditions. Up-regulated during T-cell anergy induction following signaling through the T-cell antigen receptor By similarity.By similarity

    Gene expression databases

    ArrayExpressiQ9D304.
    BgeeiQ9D304.
    CleanExiMM_RNF128.
    GenevestigatoriQ9D304.

    Interactioni

    Protein-protein interaction databases

    BioGridi211790. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9D304.
    SMRiQ9D304. Positions 38-204, 277-320.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei208 – 22821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini75 – 183109PAAdd
    BLAST

    Domaini

    Binding to E2 ubiquitin-conjugating enzyme requires an intact RING finger domain.By similarity

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri277 – 31842RING-type; atypicalPROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG271676.
    GeneTreeiENSGT00730000110457.
    HOGENOMiHOG000231432.
    HOVERGENiHBG057659.
    InParanoidiQ9D304.
    KOiK10629.
    PhylomeDBiQ9D304.
    TreeFamiTF317486.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR003137. Protease-assoc_domain.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    PfamiPF02225. PA. 1 hit.
    PF13639. 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.

    Q9D304-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGPPPGIGVY CRGGCGAARL LAWCFLLALS PHAPGSRGAE AVWTAYLNVS    50
    WRVPHTGVNR TVWELSEEGV YGQDSPLEPV SGVLVPPDGP GALNACNPHT 100
    NFTVPTVWGS TVQVSWLALI QRGGGCTFAD KIHLASERGA SGAVIFNFPG 150
    TRNEVIPMSH PGAGDIVAIM IGNLKGTKIL QSIQRGIQVT MVIEVGKKHG 200
    PWVNHYSIFF VSVSFFIITA ATVGYFIFYS ARRLRNARAQ SRKQRQLKAD 250
    AKKAIGKLQL RTLKQGDKEI GPDGDSCAVC IELYKPNDLV RILTCNHIFH 300
    KTCVDPWLLE HRTCPMCKCD ILKALGIEVD VEDGSVSLQV PVSNEASNTA 350
    SPHEEDSRSE TASSGYASVQ GADEPPLEEH AQSANENLQL VNHEANSVAV 400
    DVVPHVDNPT FEEDETPDQE AAVREIKS 428
    Length:428
    Mass (Da):46,276
    Last modified:June 1, 2001 - v1
    Checksum:i480DCF46C75E238F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti125 – 1251G → S in BAB23613. (PubMed:16141072)Curated
    Sequence conflicti131 – 1311K → N in BAB23613. (PubMed:16141072)Curated
    Sequence conflicti132 – 1321I → V in BAA95033. 1 PublicationCurated
    Sequence conflicti352 – 3521P → H in BAE27025. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY112656 mRNA. Translation: AAM51876.1.
    AF426411 mRNA. Translation: AAL34514.1.
    AB041548 mRNA. Translation: BAA95033.1.
    AK004847 mRNA. Translation: BAB23613.1.
    AK008312 mRNA. Translation: BAB25595.3.
    AK018582 mRNA. Translation: BAB31291.1.
    AK146266 mRNA. Translation: BAE27025.1.
    AK167031 mRNA. Translation: BAE39203.1.
    BC010477 mRNA. Translation: AAH10477.1.
    CCDSiCCDS30435.1.
    RefSeqiNP_001241690.1. NM_001254761.1.
    NP_075759.3. NM_023270.5.
    UniGeneiMm.27764.

    Genome annotation databases

    EnsembliENSMUST00000113026; ENSMUSP00000108649; ENSMUSG00000031438.
    GeneIDi66889.
    KEGGimmu:66889.
    UCSCiuc009uki.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY112656 mRNA. Translation: AAM51876.1 .
    AF426411 mRNA. Translation: AAL34514.1 .
    AB041548 mRNA. Translation: BAA95033.1 .
    AK004847 mRNA. Translation: BAB23613.1 .
    AK008312 mRNA. Translation: BAB25595.3 .
    AK018582 mRNA. Translation: BAB31291.1 .
    AK146266 mRNA. Translation: BAE27025.1 .
    AK167031 mRNA. Translation: BAE39203.1 .
    BC010477 mRNA. Translation: AAH10477.1 .
    CCDSi CCDS30435.1.
    RefSeqi NP_001241690.1. NM_001254761.1.
    NP_075759.3. NM_023270.5.
    UniGenei Mm.27764.

    3D structure databases

    ProteinModelPortali Q9D304.
    SMRi Q9D304. Positions 38-204, 277-320.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 211790. 2 interactions.

    PTM databases

    PhosphoSitei Q9D304.

    Proteomic databases

    PRIDEi Q9D304.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000113026 ; ENSMUSP00000108649 ; ENSMUSG00000031438 .
    GeneIDi 66889.
    KEGGi mmu:66889.
    UCSCi uc009uki.2. mouse.

    Organism-specific databases

    CTDi 79589.
    MGIi MGI:1914139. Rnf128.

    Phylogenomic databases

    eggNOGi NOG271676.
    GeneTreei ENSGT00730000110457.
    HOGENOMi HOG000231432.
    HOVERGENi HBG057659.
    InParanoidi Q9D304.
    KOi K10629.
    PhylomeDBi Q9D304.
    TreeFami TF317486.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    NextBioi 322937.
    PROi Q9D304.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9D304.
    Bgeei Q9D304.
    CleanExi MM_RNF128.
    Genevestigatori Q9D304.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR003137. Protease-assoc_domain.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    Pfami PF02225. PA. 1 hit.
    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. "The E3 ubiquitin ligase GREUL1 anteriorizes ectoderm during Xenopus development."
      Borchers A.G.M., Hufton A.L., Eldridge A.G., Jackson P.K., Harland R.M., Baker J.C.
      Dev. Biol. 251:395-408(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF CYS-277 AND CYS-280.
      Strain: CD-1.
    2. "GRAIL: an E3 ubiquitin ligase that inhibits cytokine gene transcription is expressed in anergic CD4+ T cells."
      Anandasabapathy N., Ford G.S., Bloom D., Holness C., Paragas V., Seroogy C., Skrenta H., Hollenhorst M., Fathman C.G., Soares L.
      Immunity 18:535-547(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN UBIQUITINATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS.
    3. "Isolation of full-length cDNA clones from mouse brain cDNA library made by oligo-capping method."
      Osada N., Kusuda J., Tanuma R., Ito A., Hirata M., Sugano S., Hashimoto K.
      Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6.
      Tissue: Brain.
    4. "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: Cecum, Liver and Small intestine.
    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].
      Strain: 129.
      Tissue: Mammary tumor.

    Entry informationi

    Entry nameiRN128_MOUSE
    AccessioniPrimary (citable) accession number: Q9D304
    Secondary accession number(s): Q3UJY0
    , Q9CVG1, Q9DBN3, Q9JJF8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2006
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 107 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