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Q9BYM8

- HOIL1_HUMAN

UniProt

Q9BYM8 - HOIL1_HUMAN

Protein

RanBP-type and C3HC4-type zinc finger-containing protein 1

Gene

RBCK1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 2 (15 Jan 2008)
      Previous versions | rss
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    Functioni

    E3 ubiquitin-protein ligase, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, such as UBE2L3/UBCM4, and then transfers it to substrates. Functions as an E3 ligase for oxidized IREB2 and both heme and oxygen are necessary for IREB2 ubiquitination. Promotes ubiquitination of TAB2 and IRF3 and their degradation by the proteasome. Component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation. LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways. Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation. LUBAC is proposed to be recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex. Together with FAM105B/otulin, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis. Binds polyubiquitin of different linkage types.9 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri193 – 22230RanBP2-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri282 – 32746RING-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri362 – 41150IBR-typeAdd
    BLAST
    Zinc fingeri437 – 46327RING-type 2PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

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

    GO - Biological processi

    1. negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
    2. positive regulation of apoptotic process Source: Ensembl
    3. positive regulation of extrinsic apoptotic signaling pathway Source: Ensembl
    4. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    5. positive regulation of NF-kappaB import into nucleus Source: Ensembl
    6. positive regulation of NF-kappaB transcription factor activity Source: UniProtKB
    7. proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
    8. protein linear polyubiquitination Source: UniProtKB
    9. protein polyubiquitination Source: UniProtKB
    10. T cell receptor signaling pathway Source: UniProtKB
    11. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Host-virus interaction, Ubl conjugation pathway

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RanBP-type and C3HC4-type zinc finger-containing protein 1 (EC:6.3.2.-)
    Alternative name(s):
    HBV-associated factor 4
    Heme-oxidized IRP2 ubiquitin ligase 1
    Short name:
    HOIL-1
    Hepatitis B virus X-associated protein 4
    RING finger protein 54
    Ubiquitin-conjugating enzyme 7-interacting protein 3
    Gene namesi
    Name:RBCK1
    Synonyms:C20orf18, RNF54, UBCE7IP3, XAP3, XAP4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:15864. RBCK1.

    Subcellular locationi

    GO - Cellular componenti

    1. LUBAC complex Source: UniProtKB

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi282 – 2821C → S: Binds to IREB2 in iron-treated cells. Reversed iron-induced down-regulation of IREB2. No ubiquitination of heme-loaded IREB2; when associated with S-285. 1 Publication
    Mutagenesisi285 – 2851C → S: Binds to IREB2 in iron-treated cells. Reversed iron-induced down-regulation of IREB2. No ubiquitination of heme-loaded IREB2; when associated with S-282. 1 Publication

    Organism-specific databases

    Orphaneti329173. Autoinflammatory syndrome with pyogenic bacterial infection and amylopectinosis.
    PharmGKBiPA25723.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 510510RanBP-type and C3HC4-type zinc finger-containing protein 1PRO_0000056295Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei330 – 3301Phosphotyrosine1 Publication

    Post-translational modificationi

    Auto-ubiquitinated. Auto-ubiquitination leads to degradation by the proteasome By similarity.By similarity
    Phosphorylated. In vitro, phosphorylation inhibits auto-ubiquitination activity By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9BYM8.
    PaxDbiQ9BYM8.
    PRIDEiQ9BYM8.

    PTM databases

    PhosphoSiteiQ9BYM8.

    Expressioni

    Inductioni

    By viral transfection.1 Publication

    Gene expression databases

    ArrayExpressiQ9BYM8.
    BgeeiQ9BYM8.
    CleanExiHS_RBCK1.
    GenevestigatoriQ9BYM8.

    Organism-specific databases

    HPAiHPA024185.

    Interactioni

    Subunit structurei

    Forms homodimers in vitro By similarity. Component of the LUBAC complex (linear ubiquitin chain assembly complex) which consists of SHARPIN, RBCK1 and RNF31. LUBAC has a MW of approximative 600 kDa suggesting a heteromultimeric assembly of its subunits. Interacts with beta-I-type (PRKCB1) and zeta-type protein kinase C (PRKCZ) and with UBE2L3. Interacts with PRKCH. Interacts with the HBV pX/HBx protein, which is required to activate transcription of the viral genome. Isoform 1 and isoform 2 interact with IREB2 only in iron-rich conditions. Associates with the TNF-R1 signaling complex (TNF-RSC) in a stimulation-dependent manner. Interacts with EYA1, TAB2, TAB3, MAP3K7 TRAF6 and RIPK1. Interacts with IRF3.By similarity9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Hoxa1P090223EBI-2340624,EBI-3957603From a different organism.
    IKBKGQ9Y6K94EBI-2340624,EBI-81279
    RNF31Q96EP020EBI-2340624,EBI-948111
    Socs6Q9JLY05EBI-2340624,EBI-8500205From a different organism.
    Traf1Q4VA122EBI-2340624,EBI-6116765From a different organism.

    Protein-protein interaction databases

    BioGridi115862. 60 interactions.
    DIPiDIP-47737N.
    IntActiQ9BYM8. 26 interactions.
    MINTiMINT-6768751.
    STRINGi9606.ENSP00000348632.

    Structurei

    Secondary structure

    1
    510
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi55 – 6612
    Beta strandi69 – 757
    Helixi81 – 9212
    Helixi96 – 983
    Beta strandi99 – 1035
    Beta strandi106 – 1083
    Helixi115 – 1173
    Beta strandi125 – 1306
    Beta strandi194 – 1974
    Turni200 – 2023
    Beta strandi214 – 2163

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CRCNMR-A194-232[»]
    2LGYNMR-A51-139[»]
    4DBGX-ray2.71A37-137[»]
    ProteinModelPortaliQ9BYM8.
    SMRiQ9BYM8. Positions 51-139, 194-232, 263-485.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BYM8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini55 – 11965Ubiquitin-likePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 270270Interaction with TAB2Add
    BLAST
    Regioni1 – 220220Interaction with IRF3Add
    BLAST
    Regioni69 – 13163Interaction with RNF31Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili233 – 26129Sequence AnalysisAdd
    BLAST

    Domaini

    The RanBP2-type zinc finger, also called Npl4 zinc finger (NZF), mediates binding to 'Met-1'-linked polyubiquitins.By similarity
    The UBL domain mediates association with RNF31 via interaction with its UBA domain.1 Publication

    Sequence similaritiesi

    Contains 1 IBR-type zinc finger.Curated
    Contains 1 RanBP2-type zinc finger.PROSITE-ProRule annotation
    Contains 2 RING-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri193 – 22230RanBP2-typePROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri282 – 32746RING-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri362 – 41150IBR-typeAdd
    BLAST
    Zinc fingeri437 – 46327RING-type 2PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG249934.
    HOVERGENiHBG061515.
    InParanoidiQ9BYM8.
    KOiK10630.
    OMAiQDIRLWV.
    PhylomeDBiQ9BYM8.
    TreeFamiTF323486.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    IPR002867. Znf_C6HC.
    IPR001876. Znf_RanBP2.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view]
    PfamiPF01485. IBR. 2 hits.
    PF13639. zf-RING_2. 1 hit.
    [Graphical view]
    SMARTiSM00184. RING. 1 hit.
    SM00547. ZnF_RBZ. 1 hit.
    [Graphical view]
    SUPFAMiSSF54236. SSF54236. 1 hit.
    PROSITEiPS50053. UBIQUITIN_2. 1 hit.
    PS01358. ZF_RANBP2_1. 1 hit.
    PS50199. ZF_RANBP2_2. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: Experimental confirmation may be lacking for some isoforms.

    Isoform 1 (identifier: Q9BYM8-1) [UniParc]FASTAAdd to Basket

    Also known as: HOIL-1L

    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

    MDEKTKKAEE MALSLTRAVA GGDEQVAMKC AIWLAEQRVP LSVQLKPEVS    50
    PTQDIRLWVS VEDAQMHTVT IWLTVRPDMT VASLKDMVFL DYGFPPVLQQ 100
    WVIGQRLARD QETLHSHGVR QNGDSAYLYL LSARNTSLNP QELQRERQLR 150
    MLEDLGFKDL TLQPRGPLEP GPPKPGVPQE PGRGQPDAVP EPPPVGWQCP 200
    GCTFINKPTR PGCEMCCRAR PEAYQVPASY QPDEEERARL AGEEEALRQY 250
    QQRKQQQQEG NYLQHVQLDQ RSLVLNTEPA ECPVCYSVLA PGEAVVLREC 300
    LHTFCRECLQ GTIRNSQEAE VSCPFIDNTY SCSGKLLERE IKALLTPEDY 350
    QRFLDLGISI AENRSAFSYH CKTPDCKGWC FFEDDVNEFT CPVCFHVNCL 400
    LCKAIHEQMN CKEYQEDLAL RAQNDVAARQ TTEMLKVMLQ QGEAMRCPQC 450
    QIVVQKKDGC DWIRCTVCHT EICWVTKGPR WGPGGPGDTS GGCRCRVNGI 500
    PCHPSCQNCH 510
    Length:510
    Mass (Da):57,572
    Last modified:January 15, 2008 - v2
    Checksum:iC6EF957B1F152FF2
    GO
    Isoform 2 (identifier: Q9BYM8-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-55: MDEKTKKAEEMALSLTRAVAGGDEQVAMKCAIWLAEQRVPLSVQLKPEVSPTQDI → MGTATPDGREDQE

    Show »
    Length:468
    Mass (Da):52,936
    Checksum:i5B4420D28508EE16
    GO
    Isoform 3 (identifier: Q9BYM8-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-55: MDEKTKKAEEMALSLTRAVAGGDEQVAMKCAIWLAEQRVPLSVQLKPEVSPTQDI → MGTATPDGREDQE
         253-272: RKQQQQEGNYLQHVQLDQRS → GVPAGHHPQQPGGGGLLPLH
         273-510: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:230
    Mass (Da):25,654
    Checksum:i8EDB1C28B96BF8D4
    GO

    Sequence cautioni

    The sequence AAH15219.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti236 – 2361E → D in BAC75409. (PubMed:12629548)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5555MDEKT…PTQDI → MGTATPDGREDQE in isoform 2 and isoform 3. 3 PublicationsVSP_005766Add
    BLAST
    Alternative sequencei253 – 27220RKQQQ…LDQRS → GVPAGHHPQQPGGGGLLPLH in isoform 3. 1 PublicationVSP_005767Add
    BLAST
    Alternative sequencei273 – 510238Missing in isoform 3. 1 PublicationVSP_005768Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U67322 mRNA. Translation: AAD00162.1.
    AB107766 mRNA. Translation: BAC75409.1.
    AL121747 Genomic DNA. Translation: CAC17516.1.
    AL121747 Genomic DNA. Translation: CAC28312.2.
    BC000983 mRNA. No translation available.
    BC015219 mRNA. Translation: AAH15219.2. Different initiation.
    CCDSiCCDS12998.1. [Q9BYM8-3]
    CCDS13000.2. [Q9BYM8-1]
    RefSeqiNP_006453.1. NM_006462.4. [Q9BYM8-3]
    NP_112506.2. NM_031229.2. [Q9BYM8-1]
    UniGeneiHs.247280.

    Genome annotation databases

    EnsembliENST00000353660; ENSP00000254960; ENSG00000125826. [Q9BYM8-3]
    ENST00000356286; ENSP00000348632; ENSG00000125826. [Q9BYM8-1]
    GeneIDi10616.
    KEGGihsa:10616.
    UCSCiuc002wdp.4. human. [Q9BYM8-1]
    uc002wdq.4. human. [Q9BYM8-3]

    Polymorphism databases

    DMDMi166214993.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U67322 mRNA. Translation: AAD00162.1 .
    AB107766 mRNA. Translation: BAC75409.1 .
    AL121747 Genomic DNA. Translation: CAC17516.1 .
    AL121747 Genomic DNA. Translation: CAC28312.2 .
    BC000983 mRNA. No translation available.
    BC015219 mRNA. Translation: AAH15219.2 . Different initiation.
    CCDSi CCDS12998.1. [Q9BYM8-3 ]
    CCDS13000.2. [Q9BYM8-1 ]
    RefSeqi NP_006453.1. NM_006462.4. [Q9BYM8-3 ]
    NP_112506.2. NM_031229.2. [Q9BYM8-1 ]
    UniGenei Hs.247280.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CRC NMR - A 194-232 [» ]
    2LGY NMR - A 51-139 [» ]
    4DBG X-ray 2.71 A 37-137 [» ]
    ProteinModelPortali Q9BYM8.
    SMRi Q9BYM8. Positions 51-139, 194-232, 263-485.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115862. 60 interactions.
    DIPi DIP-47737N.
    IntActi Q9BYM8. 26 interactions.
    MINTi MINT-6768751.
    STRINGi 9606.ENSP00000348632.

    PTM databases

    PhosphoSitei Q9BYM8.

    Polymorphism databases

    DMDMi 166214993.

    Proteomic databases

    MaxQBi Q9BYM8.
    PaxDbi Q9BYM8.
    PRIDEi Q9BYM8.

    Protocols and materials databases

    DNASUi 10616.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000353660 ; ENSP00000254960 ; ENSG00000125826 . [Q9BYM8-3 ]
    ENST00000356286 ; ENSP00000348632 ; ENSG00000125826 . [Q9BYM8-1 ]
    GeneIDi 10616.
    KEGGi hsa:10616.
    UCSCi uc002wdp.4. human. [Q9BYM8-1 ]
    uc002wdq.4. human. [Q9BYM8-3 ]

    Organism-specific databases

    CTDi 10616.
    GeneCardsi GC20P000388.
    HGNCi HGNC:15864. RBCK1.
    HPAi HPA024185.
    MIMi 610924. gene.
    neXtProti NX_Q9BYM8.
    Orphaneti 329173. Autoinflammatory syndrome with pyogenic bacterial infection and amylopectinosis.
    PharmGKBi PA25723.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG249934.
    HOVERGENi HBG061515.
    InParanoidi Q9BYM8.
    KOi K10630.
    OMAi QDIRLWV.
    PhylomeDBi Q9BYM8.
    TreeFami TF323486.

    Enzyme and pathway databases

    Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    ChiTaRSi RBCK1. human.
    EvolutionaryTracei Q9BYM8.
    GeneWikii RBCK1.
    GenomeRNAii 10616.
    NextBioi 40334.
    PROi Q9BYM8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BYM8.
    Bgeei Q9BYM8.
    CleanExi HS_RBCK1.
    Genevestigatori Q9BYM8.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    IPR002867. Znf_C6HC.
    IPR001876. Znf_RanBP2.
    IPR001841. Znf_RING.
    IPR013083. Znf_RING/FYVE/PHD.
    IPR017907. Znf_RING_CS.
    [Graphical view ]
    Pfami PF01485. IBR. 2 hits.
    PF13639. zf-RING_2. 1 hit.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    SM00547. ZnF_RBZ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54236. SSF54236. 1 hit.
    PROSITEi PS50053. UBIQUITIN_2. 1 hit.
    PS01358. ZF_RANBP2_1. 1 hit.
    PS50199. ZF_RANBP2_2. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The hepatitis B virus X-associated protein, XAP3, is a protein kinase C-binding protein."
      Cong Y.-S., Yao Y.-L., Yang W.-M., Kuzhandaivelu N., Seto E.
      J. Biol. Chem. 272:16482-16489(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH PRKCH AND PX OF HBV.
    2. "Identification of the ubiquitin-protein ligase that recognizes oxidized IRP2."
      Yamanaka K., Ishikawa H., Megumi Y., Tokunaga F., Kanie M., Rouault T.A., Morishima I., Minato N., Ishimori K., Iwai K.
      Nat. Cell Biol. 5:336-340(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH IREB2, MUTAGENESIS OF CYS-282 AND CYS-285.
      Tissue: Kidney adenocarcinoma.
    3. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [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] (ISOFORMS 1 AND 3).
      Tissue: Lung and Placenta.
    5. Cited for: SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
    6. "Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules."
      Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M.
      Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-330, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mammary epithelium.
    7. "A ubiquitin ligase complex assembles linear polyubiquitin chains."
      Kirisako T., Kamei K., Murata S., Kato M., Fukumoto H., Kanie M., Sano S., Tokunaga F., Tanaka K., Iwai K.
      EMBO J. 25:4877-4887(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE LUBAC COMPLEX, FUNCTION OF THE LUBAC COMPLEX.
    8. "RBCK1 negatively regulates tumor necrosis factor- and interleukin-1-triggered NF-kappaB activation by targeting TAB2/3 for degradation."
      Tian Y., Zhang Y., Zhong B., Wang Y.Y., Diao F.C., Wang R.P., Zhang M., Chen D.Y., Zhai Z.H., Shu H.B.
      J. Biol. Chem. 282:16776-16782(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TAB2; TAB3; MAP3K7; TRAF6 AND RIPK1.
    9. "Negative feedback regulation of cellular antiviral signaling by RBCK1-mediated degradation of IRF3."
      Zhang M., Tian Y., Wang R.P., Gao D., Zhang Y., Diao F.C., Chen D.Y., Zhai Z.H., Shu H.B.
      Cell Res. 18:1096-1104(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION, INTERACTION WITH IRF3.
    10. "Recruitment of the linear ubiquitin chain assembly complex stabilizes the TNF-R1 signaling complex and is required for TNF-mediated gene induction."
      Haas T.L., Emmerich C.H., Gerlach B., Schmukle A.C., Cordier S.M., Rieser E., Feltham R., Vince J., Warnken U., Wenger T., Koschny R., Komander D., Silke J., Walczak H.
      Mol. Cell 36:831-844(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: POLYUBIQUITIN-BINDING, FUNCTION OF THE LUBAC COMPLEX, ASSOCIATION WITH TNF-RSC, IDENTIFICATION BY MASS SPECTROMETRY.
    11. Cited for: FUNCTION OF THE LUBAC COMPLEX.
    12. Cited for: IDENTIFICATION IN THE LUBAC COMPLEX, FUNCTION.
    13. "SHARPIN is a component of the NF-kappaB-activating linear ubiquitin chain assembly complex."
      Tokunaga F., Nakagawa T., Nakahara M., Saeki Y., Taniguchi M., Sakata S., Tanaka K., Nakano H., Iwai K.
      Nature 471:633-636(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE LUBAC COMPLEX, FUNCTION.
    14. Cited for: IDENTIFICATION IN THE LUBAC COMPLEX, FUNCTION, DOMAIN RANBP2-TYPE, UBIQUITIN-BINDING.
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Solution structure of the ZF-RANBP domain of the protein HBV associated factor."
      RIKEN structural genomics initiative (RSGI)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 194-232.
    17. "A non-canonical UBA-UBL interaction forms the linear-ubiquitin-chain assembly complex."
      Yagi H., Ishimoto K., Hiromoto T., Fujita H., Mizushima T., Uekusa Y., Yagi-Utsumi M., Kurimoto E., Noda M., Uchiyama S., Tokunaga F., Iwai K., Kato K.
      EMBO Rep. 13:462-468(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.71 ANGSTROMS) OF 37-137, INTERACTION WITH RNF31.
    18. "Solution structure of the E3 ligase HOIL-1 Ubl domain."
      Beasley S.A., Safadi S.S., Barber K.R., Shaw G.S.
      Protein Sci. 21:1085-1092(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 51-139.

    Entry informationi

    Entry nameiHOIL1_HUMAN
    AccessioniPrimary (citable) accession number: Q9BYM8
    Secondary accession number(s): O95623
    , Q86SL2, Q96BS3, Q9BYM9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2001
    Last sequence update: January 15, 2008
    Last modified: October 1, 2014
    This is version 136 of the entry and version 2 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 20
      Human chromosome 20: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3