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Q9WUB0

- HOIL1_MOUSE

UniProt

Q9WUB0 - HOIL1_MOUSE

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Protein

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

Gene
Rbck1, Rbck, Ubce7ip3, Uip28
Organism
Mus musculus (Mouse)
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 By similarity.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri188 – 22033RanBP2-typeAdd
BLAST
Zinc fingeri280 – 32546RING-type 1Add
BLAST
Zinc fingeri360 – 40950IBR-typeAdd
BLAST
Zinc fingeri435 – 46127RING-type 2Add
BLAST

GO - Molecular functioni

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

GO - Biological processi

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

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_199115. 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):
Heme-oxidized IRP2 ubiquitin ligase 1 homolog
Short name:
HOIL-1
UbcM4-interacting protein 28
Ubiquitin-conjugating enzyme 7-interacting protein 3
Gene namesi
Name:Rbck1
Synonyms:Rbck, Ubce7ip3, Uip28
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1344372. Rbck1.

Subcellular locationi

GO - Cellular componenti

  1. LUBAC complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Impaired TNF-alpha-mediated NF-kappa-B activation and enhanced JNK-mediated apoptosis.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 508508RanBP-type and C3HC4-type zinc finger-containing protein 1PRO_0000056296Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Modified residuei328 – 3281Phosphotyrosine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9WUB0.
PRIDEiQ9WUB0.

PTM databases

PhosphoSiteiQ9WUB0.

Expressioni

Gene expression databases

BgeeiQ9WUB0.
GenevestigatoriQ9WUB0.

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. 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 similarity.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
Eya1P977672EBI-6141072,EBI-1368503

Protein-protein interaction databases

BioGridi204899. 8 interactions.
DIPiDIP-59198N.
IntActiQ9WUB0. 2 interactions.

Structurei

Secondary structure

1
508
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi194 – 1963
Turni198 – 2003
Turni212 – 2143
Helixi232 – 24514

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3B08X-ray1.70B/E/H/K192-250[»]
3B0AX-ray1.90B/E192-250[»]
ProteinModelPortaliQ9WUB0.
SMRiQ9WUB0. Positions 51-139, 192-249, 276-324.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 11965Ubiquitin-likeAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 268268Interaction with TAB2 By similarityAdd
BLAST
Regioni1 – 218218Interaction with IRF3 By similarityAdd
BLAST
Regioni69 – 13163Interaction with RNF31 By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili231 – 25929 Reviewed predictionAdd
BLAST

Domaini

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

Sequence similaritiesi

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri188 – 22033RanBP2-typeAdd
BLAST
Zinc fingeri280 – 32546RING-type 1Add
BLAST
Zinc fingeri360 – 40950IBR-typeAdd
BLAST
Zinc fingeri435 – 46127RING-type 2Add
BLAST

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG249934.
GeneTreeiENSGT00530000063620.
HOVERGENiHBG061515.
InParanoidiQ9WUB0.
KOiK10630.
OMAiQDIRLWV.
OrthoDBiEOG7PGDQN.
PhylomeDBiQ9WUB0.
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]

Sequencei

Sequence statusi: Complete.

Q9WUB0-1 [UniParc]FASTAAdd to Basket

« Hide

MDEKTKKAEE MALSLARAVA GGDEQAAIKY ATWLAEQRVP LRVQVKPEVS    50
PTQDIRLCVS VEDAYMHTVT IWLTVRPDMT VASLKDMVFL DYGFPPSLQQ 100
WVVGQRLARD QETLHSHGIR RNGDGAYLYL LSARNTSLNP QELQRQRQLR 150
MLEDLGFKDL TLQSRGPLEP VLPKPRTNQE PGQPDAAPES PPVGWQCPGC 200
TFINKPTRPG CEMCCRARPE TYQIPASYQP DEEERARLAG EEEALRQYQQ 250
RKQQQQEGNY LQHVQLEQRS LVLNTEPTEC PVCYSVLAPG EAVVLRECLH 300
TFCRECLQGT IRNSQEAEVA CPFIDSTYSC PGKLLEREIR ALLSPEDYQR 350
FLDLGVSIAE NRSTLSYHCK TPDCRGWCFF EDDVNEFTCP VCTRVNCLLC 400
KAIHEHMNCR EYQDDLALRA QNDVAARQTT EMLKVMLQQG EAMHCPQCRI 450
VVQKKDGCDW IRCTVCHTEI CWVTKGPRWG PGGPGDTSGG CRCRVNGIPC 500
HPSCQNCH 508
Length:508
Mass (Da):57,534
Last modified:January 15, 2008 - v2
Checksum:iCBD3B40CD4E55180
GO

Sequence cautioni

The sequence AAD24572.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAH34555.1 differs from that shown. Reason: Erroneous initiation.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti322 – 3221P → S in BAE38556. 1 Publication
Sequence conflicti406 – 4061H → R in BAC40440. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK088591 mRNA. Translation: BAC40440.1.
AK166075 mRNA. Translation: BAE38556.1.
AL831735, AL928568 Genomic DNA. Translation: CAM24727.1.
AL928568, AL831735 Genomic DNA. Translation: CAM23203.1.
BC034555 mRNA. Translation: AAH34555.1. Different initiation.
AF124663 mRNA. Translation: AAD24572.1. Different initiation.
CCDSiCCDS38273.1.
RefSeqiNP_001077390.1. NM_001083921.1.
NP_062679.2. NM_019705.3.
UniGeneiMm.182145.

Genome annotation databases

EnsembliENSMUST00000028964; ENSMUSP00000028964; ENSMUSG00000027466.
ENSMUST00000109847; ENSMUSP00000105473; ENSMUSG00000027466.
GeneIDi24105.
KEGGimmu:24105.
UCSCiuc008nfd.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK088591 mRNA. Translation: BAC40440.1 .
AK166075 mRNA. Translation: BAE38556.1 .
AL831735 , AL928568 Genomic DNA. Translation: CAM24727.1 .
AL928568 , AL831735 Genomic DNA. Translation: CAM23203.1 .
BC034555 mRNA. Translation: AAH34555.1 . Different initiation.
AF124663 mRNA. Translation: AAD24572.1 . Different initiation.
CCDSi CCDS38273.1.
RefSeqi NP_001077390.1. NM_001083921.1.
NP_062679.2. NM_019705.3.
UniGenei Mm.182145.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3B08 X-ray 1.70 B/E/H/K 192-250 [» ]
3B0A X-ray 1.90 B/E 192-250 [» ]
ProteinModelPortali Q9WUB0.
SMRi Q9WUB0. Positions 51-139, 192-249, 276-324.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204899. 8 interactions.
DIPi DIP-59198N.
IntActi Q9WUB0. 2 interactions.

PTM databases

PhosphoSitei Q9WUB0.

Proteomic databases

PaxDbi Q9WUB0.
PRIDEi Q9WUB0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000028964 ; ENSMUSP00000028964 ; ENSMUSG00000027466 .
ENSMUST00000109847 ; ENSMUSP00000105473 ; ENSMUSG00000027466 .
GeneIDi 24105.
KEGGi mmu:24105.
UCSCi uc008nfd.1. mouse.

Organism-specific databases

CTDi 10616.
MGIi MGI:1344372. Rbck1.

Phylogenomic databases

eggNOGi NOG249934.
GeneTreei ENSGT00530000063620.
HOVERGENi HBG061515.
InParanoidi Q9WUB0.
KOi K10630.
OMAi QDIRLWV.
OrthoDBi EOG7PGDQN.
PhylomeDBi Q9WUB0.
TreeFami TF323486.

Enzyme and pathway databases

Reactomei REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSi RBCK1. mouse.
NextBioi 304117.
PROi Q9WUB0.
SOURCEi Search...

Gene expression databases

Bgeei Q9WUB0.
Genevestigatori Q9WUB0.

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 transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NOD.
    Tissue: Lung and Thymus.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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].
    Strain: FVB/N.
    Tissue: Salivary gland.
  4. "A family of structurally related RING finger proteins interacts specifically with the ubiquitin-conjugating enzyme UbcM4."
    Martinez-Noel G., Niedenthal R., Tamura T., Harbers K.
    FEBS Lett. 454:257-261(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-508.
    Strain: BALB/c.
    Tissue: Liver.
  5. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-328, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  6. Cited for: DISRUPTION PHENOTYPE.
  7. "Sipl1 and Rbck1 are novel Eya1-binding proteins with a role in craniofacial development."
    Landgraf K., Bollig F., Trowe M.O., Besenbeck B., Ebert C., Kruspe D., Kispert A., Hanel F., Englert C.
    Mol. Cell. Biol. 30:5764-5775(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EYA1.
  8. "Specific recognition of linear ubiquitin chains by the Npl4 zinc finger (NZF) domain of the HOIL-1L subunit of the linear ubiquitin chain assembly complex."
    Sato Y., Fujita H., Yoshikawa A., Yamashita M., Yamagata A., Kaiser S.E., Iwai K., Fukai S.
    Proc. Natl. Acad. Sci. U.S.A. 108:20520-20525(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 192-250 IN COMPLEX WITH LINEAR DIUBIQUITIN.

Entry informationi

Entry nameiHOIL1_MOUSE
AccessioniPrimary (citable) accession number: Q9WUB0
Secondary accession number(s): A2ANR4, Q3TM86, Q8C2I0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: January 15, 2008
Last modified: September 3, 2014
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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