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Q8TEB7

- RN128_HUMAN

UniProt

Q8TEB7 - RN128_HUMAN

Protein

E3 ubiquitin-protein ligase RNF128

Gene

RNF128

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 1 (01 Jun 2002)
      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.2 Publications

    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: Ensembl
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. negative regulation of cytokine biosynthetic process Source: Ensembl

    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
    Short name:
    GRAIL
    RING finger protein 128
    Gene namesi
    Name:RNF128
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:21153. RNF128.

    Subcellular locationi

    Endomembrane system By similarity; Single-pass membrane protein By similarity. Cytoplasmcytoskeleton 2 Publications. 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: Ensembl
    3. Golgi apparatus Source: Ensembl
    4. integral component of membrane Source: UniProtKB-KW
    5. late endosome Source: Ensembl
    6. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134868457.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3838Sequence AnalysisAdd
    BLAST
    Chaini39 – 428390E3 ubiquitin-protein ligase RNF128PRO_0000261412Add
    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...)1 Publication

    Post-translational modificationi

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

    Keywords - PTMi

    Glycoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ8TEB7.
    PaxDbiQ8TEB7.
    PRIDEiQ8TEB7.

    PTM databases

    PhosphoSiteiQ8TEB7.

    Expressioni

    Inductioni

    Induced under anergic conditions. Up-regulated during T-cell anergy induction following signaling through the T-cell antigen receptor.1 Publication

    Gene expression databases

    ArrayExpressiQ8TEB7.
    BgeeiQ8TEB7.
    CleanExiHS_RNF128.
    GenevestigatoriQ8TEB7.

    Organism-specific databases

    HPAiHPA019675.

    Interactioni

    Protein-protein interaction databases

    BioGridi122731. 12 interactions.
    IntActiQ8TEB7. 2 interactions.
    STRINGi9606.ENSP00000255499.

    Structurei

    Secondary structure

    1
    428
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi42 – 5211
    Beta strandi61 – 7111
    Beta strandi80 – 856
    Beta strandi116 – 1227
    Helixi128 – 13710
    Beta strandi141 – 1466
    Beta strandi165 – 1717
    Helixi173 – 18412
    Beta strandi189 – 19911

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ICUX-ray2.10A38-204[»]
    ProteinModelPortaliQ8TEB7.
    SMRiQ8TEB7. Positions 38-204, 277-320.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8TEB7.

    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.

    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.
    HOGENOMiHOG000231432.
    HOVERGENiHBG057659.
    InParanoidiQ8TEB7.
    KOiK10629.
    OMAiTVPGDWG.
    PhylomeDBiQ8TEB7.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8TEB7-1) [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

    MGPPPGAGVS CRGGCGFSRL LAWCFLLALS PQAPGSRGAE AVWTAYLNVS    50
    WRVPHTGVNR TVWELSEEGV YGQDSPLEPV AGVLVPPDGP GALNACNPHT 100
    NFTVPTVWGS TVQVSWLALI QRGGGCTFAD KIHLAYERGA SGAVIFNFPG 150
    TRNEVIPMSH PGAVDIVAIM IGNLKGTKIL QSIQRGIQVT MVIEVGKKHG 200
    PWVNHYSIFF VSVSFFIITA ATVGYFIFYS ARRLRNARAQ SRKQRQLKAD 250
    AKKAIGRLQL RTLKQGDKEI GPDGDSCAVC IELYKPNDLV RILTCNHIFH 300
    KTCVDPWLLE HRTCPMCKCD ILKALGIEVD VEDGSVSLQV PVSNEISNSA 350
    SSHEEDNRSE TASSGYASVQ GTDEPPLEEH VQSTNESLQL VNHEANSVAV 400
    DVIPHVDNPT FEEDETPNQE TAVREIKS 428
    Length:428
    Mass (Da):46,521
    Last modified:June 1, 2002 - v1
    Checksum:i32F9CDB32BF208FA
    GO
    Isoform 2 (identifier: Q8TEB7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-161: MGPPPGAGVS...RNEVIPMSHP → MNQENRSSFF...GNQTIQMANF

    Note: No experimental confirmation available.

    Show »
    Length:402
    Mass (Da):44,617
    Checksum:iCCE3A965DB2F4F2E
    GO

    Sequence cautioni

    The sequence BAB15682.1 differs from that shown. Reason: Frameshift at position 291.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti4 – 41P → L in AAK77554. (PubMed:12705856)Curated
    Sequence conflicti214 – 2141S → P in AAK77554. (PubMed:12705856)Curated
    Sequence conflicti223 – 2231V → G in AAK77554. (PubMed:12705856)Curated
    Sequence conflicti255 – 2551I → L in BAB15682. (PubMed:14702039)Curated
    Sequence conflicti257 – 2571R → G in AAH56677. (PubMed:15489334)Curated
    Sequence conflicti261 – 2611R → L in BAB15682. (PubMed:14702039)Curated
    Sequence conflicti336 – 3361V → A in BAB15682. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 161161MGPPP…PMSHP → MNQENRSSFFWLLVIFTFLL KITASFSMSAYVTVTYYNET SNYTAIETCECGVYGLASPV ANAMGVVGIPKNNNYQACDH NTEFSNTKKPWIALIERGNC TFSEKIQTAGRRNADAVVIY NAPETGNQTIQMANF in isoform 2. 1 PublicationVSP_021685Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF394689 mRNA. Translation: AAK77554.1.
    AK027169 mRNA. Translation: BAB15682.1. Frameshift.
    AK074264 mRNA. Translation: BAB85033.1.
    AK126553 mRNA. Translation: BAC86589.1.
    AL391315 Genomic DNA. Translation: CAI39545.1.
    AL391315, AL606833 Genomic DNA. Translation: CAI39546.1.
    AL606833, AL391315 Genomic DNA. Translation: CAI41228.1.
    BC030951 mRNA. Translation: AAH30951.1.
    BC056677 mRNA. Translation: AAH56677.1.
    BC063404 mRNA. Translation: AAH63404.1.
    CCDSiCCDS14520.1. [Q8TEB7-2]
    CCDS14521.1. [Q8TEB7-1]
    RefSeqiNP_078815.3. NM_024539.3. [Q8TEB7-2]
    NP_919445.1. NM_194463.1. [Q8TEB7-1]
    UniGeneiHs.496542.

    Genome annotation databases

    EnsembliENST00000255499; ENSP00000255499; ENSG00000133135. [Q8TEB7-1]
    ENST00000324342; ENSP00000316127; ENSG00000133135. [Q8TEB7-2]
    GeneIDi79589.
    KEGGihsa:79589.
    UCSCiuc004emk.3. human. [Q8TEB7-2]
    uc004eml.3. human. [Q8TEB7-1]

    Polymorphism databases

    DMDMi74751443.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF394689 mRNA. Translation: AAK77554.1 .
    AK027169 mRNA. Translation: BAB15682.1 . Frameshift.
    AK074264 mRNA. Translation: BAB85033.1 .
    AK126553 mRNA. Translation: BAC86589.1 .
    AL391315 Genomic DNA. Translation: CAI39545.1 .
    AL391315 , AL606833 Genomic DNA. Translation: CAI39546.1 .
    AL606833 , AL391315 Genomic DNA. Translation: CAI41228.1 .
    BC030951 mRNA. Translation: AAH30951.1 .
    BC056677 mRNA. Translation: AAH56677.1 .
    BC063404 mRNA. Translation: AAH63404.1 .
    CCDSi CCDS14520.1. [Q8TEB7-2 ]
    CCDS14521.1. [Q8TEB7-1 ]
    RefSeqi NP_078815.3. NM_024539.3. [Q8TEB7-2 ]
    NP_919445.1. NM_194463.1. [Q8TEB7-1 ]
    UniGenei Hs.496542.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3ICU X-ray 2.10 A 38-204 [» ]
    ProteinModelPortali Q8TEB7.
    SMRi Q8TEB7. Positions 38-204, 277-320.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 122731. 12 interactions.
    IntActi Q8TEB7. 2 interactions.
    STRINGi 9606.ENSP00000255499.

    PTM databases

    PhosphoSitei Q8TEB7.

    Polymorphism databases

    DMDMi 74751443.

    Proteomic databases

    MaxQBi Q8TEB7.
    PaxDbi Q8TEB7.
    PRIDEi Q8TEB7.

    Protocols and materials databases

    DNASUi 79589.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000255499 ; ENSP00000255499 ; ENSG00000133135 . [Q8TEB7-1 ]
    ENST00000324342 ; ENSP00000316127 ; ENSG00000133135 . [Q8TEB7-2 ]
    GeneIDi 79589.
    KEGGi hsa:79589.
    UCSCi uc004emk.3. human. [Q8TEB7-2 ]
    uc004eml.3. human. [Q8TEB7-1 ]

    Organism-specific databases

    CTDi 79589.
    GeneCardsi GC0XP105937.
    HGNCi HGNC:21153. RNF128.
    HPAi HPA019675.
    MIMi 300439. gene.
    neXtProti NX_Q8TEB7.
    PharmGKBi PA134868457.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG271676.
    HOGENOMi HOG000231432.
    HOVERGENi HBG057659.
    InParanoidi Q8TEB7.
    KOi K10629.
    OMAi TVPGDWG.
    PhylomeDBi Q8TEB7.
    TreeFami TF317486.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    EvolutionaryTracei Q8TEB7.
    GeneWikii RNF128.
    GenomeRNAii 79589.
    NextBioi 35460171.
    PROi Q8TEB7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8TEB7.
    Bgeei Q8TEB7.
    CleanExi HS_RNF128.
    Genevestigatori Q8TEB7.

    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. "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] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INDUCTION, MUTAGENESIS.
    2. "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: Hepatoma, Lung and Mammary gland.
    3. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 1).
      Tissue: Brain.
    5. "GRAIL (gene related to anergy in lymphocytes) regulates cytoskeletal reorganization through ubiquitination and degradation of Arp2/3 subunit 5 and coronin 1A."
      Ichikawa D., Mizuno M., Yamamura T., Miyake S.
      J. Biol. Chem. 286:43465-43474(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    6. "PA domain of the E3 ligase GRAIL."
      Structural genomics consortium (SGC)
      Submitted (OCT-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 38-204, GLYCOSYLATION AT ASN-101.

    Entry informationi

    Entry nameiRN128_HUMAN
    AccessioniPrimary (citable) accession number: Q8TEB7
    Secondary accession number(s): A0PJI4
    , Q6PH80, Q6ZTJ8, Q96RF3, Q9H5E4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2006
    Last sequence update: June 1, 2002
    Last modified: October 1, 2014
    This is version 111 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 X
      Human chromosome X: 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