Q9BYM8 (HOIL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	RBCK1
Synonyms:	C20orf18, RNF54, UBCE7IP3, XAP3, XAP4

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	510 AA.
Sequence status	Complete.
Protein existence	Evidence 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 polyubiquitin chains in a head-to-tail manner 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. Binds polyubiquitin of different linkage types. Ref.2 Ref.7 Ref.8 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16
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.8 Ref.10
Induction	By viral transfection. Ref.10
Domain	The RanBP2-type zinc fingers mediate the specific interaction with ubiquitin. Ref.16
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. Ref.6 Ref.9 Ref.11
Sequence similarities	Contains 1 B box-type zinc finger. Contains 2 IBR-type zinc fingers. Contains 1 RanBP2-type zinc finger. Contains 1 RING-type zinc finger. 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 process	Host-virus interaction Ubl conjugation pathway
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Ligase
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	T cell receptor signaling pathway Inferred from direct assay Ref.12. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of NF-kappaB transcription factor activity Inferred from direct assay Ref.8. Source: UniProtKB positive regulation of I-kappaB kinase/NF-kappaB cascade Inferred from direct assay Ref.13Ref.14. Source: UniProtKB positive regulation of NF-kappaB transcription factor activity Inferred from direct assay Ref.13. Source: UniProtKB proteasomal ubiquitin-dependent protein catabolic process Inferred from mutant phenotype Ref.8. Source: UniProtKB protein linear polyubiquitination Inferred from direct assay Ref.14Ref.15Ref.16. Source: UniProtKB
Cellular component	LUBAC complex Inferred from direct assay Ref.7Ref.14Ref.15Ref.16. Source: UniProtKB
Molecular function	protein binding Inferred from physical interaction Ref.8Ref.10. Source: UniProtKB ubiquitin binding Inferred from direct assay Ref.16. Source: UniProtKB ubiquitin-protein ligase activity Inferred from direct assay Ref.2Ref.7. Source: UniProtKB zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 510

510

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

PRO_0000056295

Regions

Domain

55 – 119

65

Ubiquitin-like

Zinc finger

193 – 222

30

RanBP2-type

Zinc finger

282 – 327

46

RING-type

Zinc finger

362 – 411

50

IBR-type 1

Zinc finger

376 – 411

36

B box-type

Zinc finger

440 – 476

37

IBR-type 2

Region

1 – 270

270

Interaction with TAB2

Region

1 – 220

220

Interaction with IRF3

Region

69 – 131

63

Interaction with RNF31

Coiled coil

233 – 261

29

Potential

Amino acid modifications

Modified residue

330

1

Phosphotyrosine Ref.6 Ref.9 Ref.11

Natural variations

Alternative sequence

1 – 55

55

MDEKT…PTQDI → MGTATPDGREDQE in isoform 2 and isoform 3.

VSP_005766

Alternative sequence

253 – 272

20

RKQQQ…LDQRS → GVPAGHHPQQPGGGGLLPLH in isoform 3.

VSP_005767

Alternative sequence

273 – 510

238

Missing in isoform 3.

VSP_005768

Experimental info

Mutagenesis

282

1

C → 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

Mutagenesis

285

1

C → 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 conflict

236

1

E → D in BAC75409. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

510

Helix Strand Turn

Details...

Beta strand

184 – 187

4

Turn

190 – 192

3

Beta strand

204 – 206

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (HOIL-1L) [UniParc]. Last modified January 15, 2008. Version 2. Checksum: C6EF957B1F152FF2	FASTA	510	57,572
	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
	Isoform 2 [UniParc]. Checksum: 5B4420D28508EE16	FASTA	468	52,936
	10 20 30 40 50 60 MGTATPDGRE DQERLWVSVE DAQMHTVTIW LTVRPDMTVA SLKDMVFLDY GFPPVLQQWV 70 80 90 100 110 120 IGQRLARDQE TLHSHGVRQN GDSAYLYLLS ARNTSLNPQE LQRERQLRML EDLGFKDLTL 130 140 150 160 170 180 QPRGPLEPGP PKPGVPQEPG RGQPDAVPEP PPVGWQCPGC TFINKPTRPG CEMCCRARPE 190 200 210 220 230 240 AYQVPASYQP DEEERARLAG EEEALRQYQQ RKQQQQEGNY LQHVQLDQRS LVLNTEPAEC 250 260 270 280 290 300 PVCYSVLAPG EAVVLRECLH TFCRECLQGT IRNSQEAEVS CPFIDNTYSC SGKLLEREIK 310 320 330 340 350 360 ALLTPEDYQR FLDLGISIAE NRSAFSYHCK TPDCKGWCFF EDDVNEFTCP VCFHVNCLLC 370 380 390 400 410 420 KAIHEQMNCK EYQEDLALRA QNDVAARQTT EMLKVMLQQG EAMRCPQCQI VVQKKDGCDW 430 440 450 460 IRCTVCHTEI CWVTKGPRWG PGGPGDTSGG CRCRVNGIPC HPSCQNCH
	Isoform 3 [UniParc]. Checksum: 8EDB1C28B96BF8D4	FASTA	230	25,654
	10 20 30 40 50 60 MGTATPDGRE DQERLWVSVE DAQMHTVTIW LTVRPDMTVA SLKDMVFLDY GFPPVLQQWV 70 80 90 100 110 120 IGQRLARDQE TLHSHGVRQN GDSAYLYLLS ARNTSLNPQE LQRERQLRML EDLGFKDLTL 130 140 150 160 170 180 QPRGPLEPGP PKPGVPQEPG RGQPDAVPEP PPVGWQCPGC TFINKPTRPG CEMCCRARPE 190 200 210 220 230 AYQVPASYQP DEEERARLAG EEEALRQYQQ GVPAGHHPQQ PGGGGLLPLH

References

	« Hide 'large scale' referencesShow '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: 9195957] [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: 12629548] [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: 11780052] [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: 15489334] [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: 14759258] [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: 15951569] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-330, MASS SPECTROMETRY. 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: 17006537] [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: 17449468] [Abstract] Cited for: FUNCTION, INTERACTION WITH TAB2; TAB3; MAP3K7; TRAF6 AND RIPK1.
[9]	"Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks." Wolf-Yadlin A., Hautaniemi S., Lauffenburger D.A., White F.M. Proc. Natl. Acad. Sci. U.S.A. 104:5860-5865(2007) [PubMed: 17389395] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-330, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[10]	"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: 18711448] [Abstract] Cited for: FUNCTION, INDUCTION, INTERACTION WITH IRF3.
[11]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-330, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[12]	"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: 20005846] [Abstract] Cited for: MASS SPECTROMETRY, POLYUBIQUITIN-BINDING, FUNCTION OF THE LUBAC COMPLEX, ASSOCIATION WITH TNF-RSC.
[13]	"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: 19136968] [Abstract] Cited for: FUNCTION OF THE LUBAC COMPLEX.
[14]	"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: 21455173] [Abstract] Cited for: IDENTIFICATION IN THE LUBAC COMPLEX, FUNCTION.
[15]	"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: 21455180] [Abstract] Cited for: IDENTIFICATION IN THE LUBAC COMPLEX, FUNCTION.
[16]	"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: 21455181] [Abstract] Cited for: IDENTIFICATION IN THE LUBAC COMPLEX, FUNCTION, DOMAIN RANBP2-TYPE, UBIQUITIN-BINDING.
[17]	"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 184-222.
+	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.

IPI

IPI00010748.
IPI00220104.
IPI00783058.

RefSeq

NP_006453.1. NM_006462.4.
NP_112506.2. NM_031229.2.

UniGene

Hs.247280.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CRC	NMR	-	A	194-232	[»]

ProteinModelPortal

Q9BYM8.

SMR

Q9BYM8. Positions 54-130, 194-232, 277-412, 441-495.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9BYM8. 10 interactions.

MINT

MINT-6768751.

STRING

Q9BYM8.

PTM databases

PhosphoSite

Q9BYM8.

Polymorphism databases

DMDM

166214993.

Proteomic databases

PRIDE

Q9BYM8.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000356286; ENSP00000348632; ENSG00000125826.

GeneID

10616.

KEGG

hsa:10616.

UCSC

uc002wdp.2. human.
uc002wdq.2. human.

Organism-specific databases

CTD

10616.

GeneCards

GC20P000388.

H-InvDB

HIX0015553.

HGNC

HGNC:15864. RBCK1.

HPA

HPA024185.

MIM

610924. gene.

neXtProt

NX_Q9BYM8.

PharmGKB

PA25723.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG09358.

GeneTree

ENSGT00530000063620.

HOGENOM

HBG446806.

HOVERGEN

HBG061515.

InParanoid

Q9BYM8.

OMA

TQDIRLW.

PhylomeDB

Q9BYM8.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q9BYM8.

Bgee

Q9BYM8.

CleanEx

HS_RBCK1.

Genevestigator

Q9BYM8.

GermOnline

ENSG00000125826. Homo sapiens.

Family and domain databases

InterPro

IPR019955. Ubiquitin_supergroup.
IPR002867. Znf_C6HC.
IPR001876. Znf_RanBP2.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]

Gene3D

G3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 1 hit.

KO

K10630.

Pfam

PF01485. IBR. 2 hits.
[Graphical view]

SMART

SM00184. RING. 1 hit.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view]

PROSITE

PS50053. UBIQUITIN_2. 1 hit.
PS50119. ZF_BBOX. False negative.
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]

ProtoNet

Search...

Other

NextBio

40334.

SOURCE

Search...

Entry information

Entry name

HOIL1_HUMAN

Accession

Primary (citable) accession number: Q9BYM8
Secondary accession number(s): O95623 , Q86SL2, Q96BS3, Q9BYM9

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	January 15, 2008
Last modified:	December 14, 2011
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.