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Protein

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

Gene

Rbck1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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).By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri188 – 220RanBP2-typePROSITE-ProRule annotationAdd BLAST33
Zinc fingeri280 – 325RING-type 1PROSITE-ProRule annotationAdd BLAST46
Zinc fingeri360 – 409IBR-typeAdd BLAST50
Zinc fingeri435 – 461RING-type 2PROSITE-ProRule annotationAdd BLAST27

GO - Molecular functioni

GO - Biological processi

  • negative regulation of necroptotic process Source: MGI
  • negative regulation of NF-kappaB transcription factor activity Source: MGI
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of extrinsic apoptotic signaling pathway Source: MGI
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • positive regulation of NF-kappaB import into nucleus Source: UniProtKB
  • positive regulation of NF-kappaB transcription factor activity Source: MGI
  • proteasome-mediated ubiquitin-dependent protein catabolic process Source: MGI
  • protein linear polyubiquitination Source: UniProtKB
  • protein polyubiquitination Source: MGI
  • T cell receptor signaling pathway Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-5357905. Regulation of TNFR1 signaling.
R-MMU-5357956. TNFR1-induced NFkappaB signaling pathway.
R-MMU-983168. 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
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1344372. Rbck1.

Subcellular locationi

GO - Cellular componenti

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)DescriptionActionsGraphical viewLength
ChainiPRO_00000562961 – 508RanBP-type and C3HC4-type zinc finger-containing protein 1Add BLAST508

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei50PhosphoserineBy similarity1
Modified residuei328PhosphotyrosineCombined sources1

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

EPDiQ9WUB0.
MaxQBiQ9WUB0.
PaxDbiQ9WUB0.
PeptideAtlasiQ9WUB0.
PRIDEiQ9WUB0.

PTM databases

iPTMnetiQ9WUB0.
PhosphoSitePlusiQ9WUB0.

Expressioni

Gene expression databases

BgeeiENSMUSG00000027466.
ExpressionAtlasiQ9WUB0. baseline and differential.
GenevisibleiQ9WUB0. MM.

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).By similarity

Binary interactionsi

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

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204899. 8 interactors.
DIPiDIP-59198N.
IntActiQ9WUB0. 4 interactors.
STRINGi10090.ENSMUSP00000028964.

Structurei

Secondary structure

1508
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi194 – 196Combined sources3
Turni198 – 200Combined sources3
Turni212 – 214Combined sources3
Helixi232 – 245Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3B08X-ray1.70B/E/H/K192-250[»]
3B0AX-ray1.90B/E192-250[»]
ProteinModelPortaliQ9WUB0.
SMRiQ9WUB0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini55 – 119Ubiquitin-likePROSITE-ProRule annotationAdd BLAST65

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 268Interaction with TAB2By similarityAdd BLAST268
Regioni1 – 218Interaction with IRF3By similarityAdd BLAST218
Regioni69 – 131Interaction with RNF31By similarityAdd BLAST63

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili231 – 259Sequence analysisAdd BLAST29

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

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)DescriptionActionsGraphical viewLength
Zinc fingeri188 – 220RanBP2-typePROSITE-ProRule annotationAdd BLAST33
Zinc fingeri280 – 325RING-type 1PROSITE-ProRule annotationAdd BLAST46
Zinc fingeri360 – 409IBR-typeAdd BLAST50
Zinc fingeri435 – 461RING-type 2PROSITE-ProRule annotationAdd BLAST27

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1815. Eukaryota.
ENOG410XP9Y. LUCA.
GeneTreeiENSGT00530000063620.
HOVERGENiHBG061515.
InParanoidiQ9WUB0.
KOiK10630.
OMAiLGWCVYE.
OrthoDBiEOG091G04QK.
PhylomeDBiQ9WUB0.
TreeFamiTF323486.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
IPR027370. Znf-RING_LisH.
IPR001876. Znf_RanBP2.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF13445. zf-RING_UBOX. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF90209. SSF90209. 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

        10         20         30         40         50
MDEKTKKAEE MALSLARAVA GGDEQAAIKY ATWLAEQRVP LRVQVKPEVS
60 70 80 90 100
PTQDIRLCVS VEDAYMHTVT IWLTVRPDMT VASLKDMVFL DYGFPPSLQQ
110 120 130 140 150
WVVGQRLARD QETLHSHGIR RNGDGAYLYL LSARNTSLNP QELQRQRQLR
160 170 180 190 200
MLEDLGFKDL TLQSRGPLEP VLPKPRTNQE PGQPDAAPES PPVGWQCPGC
210 220 230 240 250
TFINKPTRPG CEMCCRARPE TYQIPASYQP DEEERARLAG EEEALRQYQQ
260 270 280 290 300
RKQQQQEGNY LQHVQLEQRS LVLNTEPTEC PVCYSVLAPG EAVVLRECLH
310 320 330 340 350
TFCRECLQGT IRNSQEAEVA CPFIDSTYSC PGKLLEREIR ALLSPEDYQR
360 370 380 390 400
FLDLGVSIAE NRSTLSYHCK TPDCRGWCFF EDDVNEFTCP VCTRVNCLLC
410 420 430 440 450
KAIHEHMNCR EYQDDLALRA QNDVAARQTT EMLKVMLQQG EAMHCPQCRI
460 470 480 490 500
VVQKKDGCDW IRCTVCHTEI CWVTKGPRWG PGGPGDTSGG CRCRVNGIPC

HPSCQNCH
Length:508
Mass (Da):57,534
Last modified:January 15, 2008 - v2
Checksum:iCBD3B40CD4E55180
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti322P → S in BAE38556 (PubMed:16141072).Curated1
Sequence conflicti406H → R in BAC40440 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
Mm.472312.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.
Mm.472312.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3B08X-ray1.70B/E/H/K192-250[»]
3B0AX-ray1.90B/E192-250[»]
ProteinModelPortaliQ9WUB0.
SMRiQ9WUB0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204899. 8 interactors.
DIPiDIP-59198N.
IntActiQ9WUB0. 4 interactors.
STRINGi10090.ENSMUSP00000028964.

PTM databases

iPTMnetiQ9WUB0.
PhosphoSitePlusiQ9WUB0.

Proteomic databases

EPDiQ9WUB0.
MaxQBiQ9WUB0.
PaxDbiQ9WUB0.
PeptideAtlasiQ9WUB0.
PRIDEiQ9WUB0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi10616.
MGIiMGI:1344372. Rbck1.

Phylogenomic databases

eggNOGiKOG1815. Eukaryota.
ENOG410XP9Y. LUCA.
GeneTreeiENSGT00530000063620.
HOVERGENiHBG061515.
InParanoidiQ9WUB0.
KOiK10630.
OMAiLGWCVYE.
OrthoDBiEOG091G04QK.
PhylomeDBiQ9WUB0.
TreeFamiTF323486.

Enzyme and pathway databases

ReactomeiR-MMU-5357905. Regulation of TNFR1 signaling.
R-MMU-5357956. TNFR1-induced NFkappaB signaling pathway.
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiRbck1. mouse.
PROiQ9WUB0.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000027466.
ExpressionAtlasiQ9WUB0. baseline and differential.
GenevisibleiQ9WUB0. MM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
IPR027370. Znf-RING_LisH.
IPR001876. Znf_RanBP2.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamiPF13445. zf-RING_UBOX. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00547. ZnF_RBZ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF90209. SSF90209. 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]
ProtoNetiSearch...

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: November 2, 2016
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

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.