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Q9BYM8

- HOIL1_HUMAN

UniProt

Q9BYM8 - HOIL1_HUMAN

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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

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. ubiquitin binding Source: UniProtKB
  3. ubiquitin-protein transferase activity Source: UniProtKB
  4. zinc ion binding Source: InterPro

GO - Biological processi

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

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
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Polyglucosan body myopathy, early-onset, with or without immunodeficiency (PBMEI) [MIM:615895]: A disease characterized by polyglucosan storage myopathy associated with early-onset progressive muscle weakness and progressive dilated cardiomyopathy, which may necessitate cardiac transplant in severe cases. Some patients present with severe immunodeficiency, invasive bacterial infections and chronic autoinflammation.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti18 – 181A → P in PBMEI. 1 Publication
VAR_071385
Natural varianti387 – 3871N → S in PBMEI. 1 Publication
VAR_071386

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

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi615895. phenotype.
Orphaneti329173. Autoinflammatory syndrome with pyogenic bacterial infection and amylopectinosis.
397937. Polyglucosan body myopathy.
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

BgeeiQ9BYM8.
CleanExiHS_RBCK1.
ExpressionAtlasiQ9BYM8. baseline and differential.
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. 64 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.
GeneTreeiENSGT00530000063620.
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

        10         20         30         40         50
MDEKTKKAEE MALSLTRAVA GGDEQVAMKC AIWLAEQRVP LSVQLKPEVS
60 70 80 90 100
PTQDIRLWVS VEDAQMHTVT IWLTVRPDMT VASLKDMVFL DYGFPPVLQQ
110 120 130 140 150
WVIGQRLARD QETLHSHGVR QNGDSAYLYL LSARNTSLNP QELQRERQLR
160 170 180 190 200
MLEDLGFKDL TLQPRGPLEP GPPKPGVPQE PGRGQPDAVP EPPPVGWQCP
210 220 230 240 250
GCTFINKPTR PGCEMCCRAR PEAYQVPASY QPDEEERARL AGEEEALRQY
260 270 280 290 300
QQRKQQQQEG NYLQHVQLDQ RSLVLNTEPA ECPVCYSVLA PGEAVVLREC
310 320 330 340 350
LHTFCRECLQ GTIRNSQEAE VSCPFIDNTY SCSGKLLERE IKALLTPEDY
360 370 380 390 400
QRFLDLGISI AENRSAFSYH CKTPDCKGWC FFEDDVNEFT CPVCFHVNCL
410 420 430 440 450
LCKAIHEQMN CKEYQEDLAL RAQNDVAARQ TTEMLKVMLQ QGEAMRCPQC
460 470 480 490 500
QIVVQKKDGC DWIRCTVCHT EICWVTKGPR WGPGGPGDTS GGCRCRVNGI
510
PCHPSCQNCH
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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti18 – 181A → P in PBMEI. 1 Publication
VAR_071385
Natural varianti387 – 3871N → S in PBMEI. 1 Publication
VAR_071386

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. 64 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.
615895. phenotype.
neXtProti NX_Q9BYM8.
Orphaneti 329173. Autoinflammatory syndrome with pyogenic bacterial infection and amylopectinosis.
397937. Polyglucosan body myopathy.
PharmGKBi PA25723.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG249934.
GeneTreei ENSGT00530000063620.
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

Bgeei Q9BYM8.
CleanExi HS_RBCK1.
ExpressionAtlasi Q9BYM8. baseline and differential.
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

« Hide 'large scale' publications
  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: INVOLVEMENT IN PBMEI.
  16. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. Cited for: INVOLVEMENT IN PBMEI, VARIANTS PBMEI PRO-18 AND SER-387.
  18. "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.
  19. "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.
  20. "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 29, 2014
This is version 137 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. 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

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