Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9BYM8 (HOIL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:RBCK1
Synonyms:C20orf18, RNF54, UBCE7IP3, XAP3, XAP4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length510 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14

Subunit structure

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. Ref.1 Ref.2 Ref.7 Ref.8 Ref.9 Ref.12 Ref.13 Ref.14 Ref.17

Induction

By viral transfection. Ref.9

Domain

The RanBP2-type zinc finger, also called Npl4 zinc finger (NZF), mediates binding to 'Met-1'-linked polyubiquitins By similarity. Ref.14

The UBL domain mediates association with RNF31 via interaction with its UBA domain. Ref.14

Post-translational modification

Auto-ubiquitinated. Auto-ubiquitination leads to degradation by the proteasome By similarity.

Phosphorylated. In vitro, phosphorylation inhibits auto-ubiquitination activity By similarity.

Sequence similarities

Contains 1 IBR-type zinc finger.

Contains 1 RanBP2-type zinc finger.

Contains 2 RING-type zinc fingers.

Contains 1 ubiquitin-like domain.

Sequence caution

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

Ontologies

Keywords
   Biological processHost-virus interaction
Ubl conjugation pathway
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Repeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionLigase
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processT cell receptor signaling pathway

Inferred from direct assay Ref.10. Source: UniProtKB

negative regulation of NF-kappaB transcription factor activity

Inferred from direct assay Ref.8. Source: UniProtKB

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from direct assay Ref.11Ref.12. Source: UniProtKB

positive regulation of NF-kappaB import into nucleus

Inferred from electronic annotation. Source: Ensembl

positive regulation of NF-kappaB transcription factor activity

Inferred from direct assay Ref.11. Source: UniProtKB

positive regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of extrinsic apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

proteasome-mediated ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype Ref.8. Source: UniProtKB

protein linear polyubiquitination

Inferred from direct assay Ref.12Ref.13Ref.14. Source: UniProtKB

protein polyubiquitination

Inferred from direct assay Ref.2Ref.7. Source: UniProtKB

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentLUBAC complex

Inferred from direct assay Ref.7Ref.12Ref.13Ref.14. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction Ref.8Ref.9PubMed 16083853PubMed 16083853. Source: UniProtKB

ubiquitin binding

Inferred from direct assay Ref.14. Source: UniProtKB

ubiquitin-protein transferase activity

Inferred from direct assay Ref.2Ref.7. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Note: Experimental confirmation may be lacking for some isoforms.
Isoform 1 (identifier: Q9BYM8-1)

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.
Isoform 2 (identifier: Q9BYM8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-55: MDEKTKKAEEMALSLTRAVAGGDEQVAMKCAIWLAEQRVPLSVQLKPEVSPTQDI → MGTATPDGREDQE
Isoform 3 (identifier: Q9BYM8-4)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 510510RanBP-type and C3HC4-type zinc finger-containing protein 1
PRO_0000056295

Regions

Domain55 – 11965Ubiquitin-like
Zinc finger193 – 22230RanBP2-type
Zinc finger282 – 32746RING-type 1
Zinc finger362 – 41150IBR-type
Zinc finger437 – 46327RING-type 2
Region1 – 270270Interaction with TAB2
Region1 – 220220Interaction with IRF3
Region69 – 13163Interaction with RNF31
Coiled coil233 – 26129 Potential

Amino acid modifications

Modified residue11N-acetylmethionine Ref.15
Modified residue3301Phosphotyrosine Ref.6

Natural variations

Alternative sequence1 – 5555MDEKT…PTQDI → MGTATPDGREDQE in isoform 2 and isoform 3.
VSP_005766
Alternative sequence253 – 27220RKQQQ…LDQRS → GVPAGHHPQQPGGGGLLPLH in isoform 3.
VSP_005767
Alternative sequence273 – 510238Missing in isoform 3.
VSP_005768

Experimental info

Mutagenesis2821C → 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. Ref.2
Mutagenesis2851C → 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. Ref.2
Sequence conflict2361E → D in BAC75409. Ref.2

Secondary structure

...................... 510
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (HOIL-1L) [UniParc].

Last modified January 15, 2008. Version 2.
Checksum: C6EF957B1F152FF2

FASTA51057,572
        10         20         30         40         50         60 
MDEKTKKAEE MALSLTRAVA GGDEQVAMKC AIWLAEQRVP LSVQLKPEVS PTQDIRLWVS 

        70         80         90        100        110        120 
VEDAQMHTVT IWLTVRPDMT VASLKDMVFL DYGFPPVLQQ WVIGQRLARD QETLHSHGVR 

       130        140        150        160        170        180 
QNGDSAYLYL LSARNTSLNP QELQRERQLR MLEDLGFKDL TLQPRGPLEP GPPKPGVPQE 

       190        200        210        220        230        240 
PGRGQPDAVP EPPPVGWQCP GCTFINKPTR PGCEMCCRAR PEAYQVPASY QPDEEERARL 

       250        260        270        280        290        300 
AGEEEALRQY QQRKQQQQEG NYLQHVQLDQ RSLVLNTEPA ECPVCYSVLA PGEAVVLREC 

       310        320        330        340        350        360 
LHTFCRECLQ GTIRNSQEAE VSCPFIDNTY SCSGKLLERE IKALLTPEDY QRFLDLGISI 

       370        380        390        400        410        420 
AENRSAFSYH CKTPDCKGWC FFEDDVNEFT CPVCFHVNCL LCKAIHEQMN CKEYQEDLAL 

       430        440        450        460        470        480 
RAQNDVAARQ TTEMLKVMLQ QGEAMRCPQC QIVVQKKDGC DWIRCTVCHT EICWVTKGPR 

       490        500        510 
WGPGGPGDTS GGCRCRVNGI PCHPSCQNCH 

« Hide

Isoform 2 [UniParc].

Checksum: 5B4420D28508EE16
Show »

FASTA46852,936
Isoform 3 [UniParc].

Checksum: 8EDB1C28B96BF8D4
Show »

FASTA23025,654

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"An unappreciated role for RNA surveillance."
Hillman R.T., Green R.E., Brenner S.E.
Genome Biol. 5:R8.1-R8.16(2004) [PubMed] [Europe PMC] [Abstract]
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]"Involvement of linear polyubiquitylation of NEMO in NF-kappaB activation."
Tokunaga F., Sakata S., Saeki Y., Satomi Y., Kirisako T., Kamei K., Nakagawa T., Kato M., Murata S., Yamaoka S., Yamamoto M., Akira S., Takao T., Tanaka K., Iwai K.
Nat. Cell Biol. 11:123-132(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE LUBAC COMPLEX.
[12]"Linear ubiquitination prevents inflammation and regulates immune signalling."
Gerlach B., Cordier S.M., Schmukle A.C., Emmerich C.H., Rieser E., Haas T.L., Webb A.I., Rickard J.A., Anderton H., Wong W.W., Nachbur U., Gangoda L., Warnken U., Purcell A.W., Silke J., Walczak H.
Nature 471:591-596(2011) [PubMed] [Europe PMC] [Abstract]
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]"SHARPIN forms a linear ubiquitin ligase complex regulating NF-kappaB activity and apoptosis."
Ikeda F., Deribe Y.L., Skanland S.S., Stieglitz B., Grabbe C., Franz-Wachtel M., van Wijk S.J., Goswami P., Nagy V., Terzic J., Tokunaga F., Androulidaki A., Nakagawa T., Pasparakis M., Iwai K., Sundberg J.P., Schaefer L., Rittinger K., Macek B., Dikic I.
Nature 471:637-641(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE LUBAC COMPLEX, FUNCTION, DOMAIN RANBP2-TYPE, UBIQUITIN-BINDING.
[15]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS12998.1. [Q9BYM8-3]
CCDS13000.2. [Q9BYM8-1]
RefSeqNP_006453.1. NM_006462.4. [Q9BYM8-3]
NP_112506.2. NM_031229.2. [Q9BYM8-1]
UniGeneHs.247280.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CRCNMR-A194-232[»]
2LGYNMR-A51-139[»]
4DBGX-ray2.71A37-137[»]
ProteinModelPortalQ9BYM8.
SMRQ9BYM8. Positions 51-139, 194-232, 263-485.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115862. 60 interactions.
DIPDIP-47737N.
IntActQ9BYM8. 26 interactions.
MINTMINT-6768751.
STRING9606.ENSP00000348632.

PTM databases

PhosphoSiteQ9BYM8.

Polymorphism databases

DMDM166214993.

Proteomic databases

MaxQBQ9BYM8.
PaxDbQ9BYM8.
PRIDEQ9BYM8.

Protocols and materials databases

DNASU10616.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000353660; ENSP00000254960; ENSG00000125826. [Q9BYM8-3]
ENST00000356286; ENSP00000348632; ENSG00000125826. [Q9BYM8-1]
GeneID10616.
KEGGhsa:10616.
UCSCuc002wdp.4. human. [Q9BYM8-1]
uc002wdq.4. human. [Q9BYM8-3]

Organism-specific databases

CTD10616.
GeneCardsGC20P000388.
HGNCHGNC:15864. RBCK1.
HPAHPA024185.
MIM610924. gene.
neXtProtNX_Q9BYM8.
Orphanet329173. Autoinflammatory syndrome with pyogenic bacterial infection and amylopectinosis.
PharmGKBPA25723.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG249934.
HOVERGENHBG061515.
InParanoidQ9BYM8.
KOK10630.
OMAQDIRLWV.
PhylomeDBQ9BYM8.
TreeFamTF323486.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressQ9BYM8.
BgeeQ9BYM8.
CleanExHS_RBCK1.
GenevestigatorQ9BYM8.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR000626. 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]
PfamPF01485. IBR. 2 hits.
PF13639. zf-RING_2. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view]
SUPFAMSSF54236. SSF54236. 1 hit.
PROSITEPS50053. 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]
ProtoNetSearch...

Other

ChiTaRSRBCK1. human.
EvolutionaryTraceQ9BYM8.
GeneWikiRBCK1.
GenomeRNAi10616.
NextBio40334.
PROQ9BYM8.
SOURCESearch...

Entry information

Entry nameHOIL1_HUMAN
AccessionPrimary (citable) accession number: Q9BYM8
Secondary accession number(s): O95623 expand/collapse secondary AC list , Q86SL2, Q96BS3, Q9BYM9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: January 15, 2008
Last modified: July 9, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM