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Protein

E3 ubiquitin-protein ligase RNF144B

Gene

Rnf144b

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates such as LCMT2, thereby promoting their degradation. Induces apoptosis via a p53/TP53-dependent but caspase-independent mechanism. However, its overexpression also produces a decrease of the ubiquitin-dependent stability of BAX, a pro-apoptotic protein, ultimately leading to protection of cell death; But, it is not an anti-apoptotic protein per se (By similarity).By similarity

Catalytic activityi

S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.By similarity

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei204By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri30 – 80RING-type 1; atypicalAdd BLAST51
Zinc fingeri101 – 166IBR-typeAdd BLAST66
Zinc fingeri191 – 220RING-type 2; degenerateAdd BLAST30

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Apoptosis, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase RNF144B (EC:2.3.2.-By similarity)
Alternative name(s):
IBR domain-containing protein 2
RING finger protein 144B
Gene namesi
Name:Rnf144b
Synonyms:Ibrdc2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:2384986. Rnf144b.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei256 – 276HelicalSequence analysisAdd BLAST21

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000559121 – 301E3 ubiquitin-protein ligase RNF144BAdd BLAST301

Post-translational modificationi

Auto-ubiquitinated.By similarity

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiQ8BKD6.
PRIDEiQ8BKD6.

PTM databases

PhosphoSitePlusiQ8BKD6.

Expressioni

Gene expression databases

BgeeiENSMUSG00000038068.
CleanExiMM_RNF144B.
GenevisibleiQ8BKD6. MM.

Interactioni

Subunit structurei

Interacts with UBE2L3, UBE2L6 and LCMT2 as well as with BAX.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000071017.

Structurei

3D structure databases

ProteinModelPortaliQ8BKD6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING domain, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved cysteine residue in the second RING domain.By similarity

Sequence similaritiesi

Belongs to the RBR family. RNF144 subfamily.Curated
Contains 1 IBR-type zinc finger.Curated
Contains 2 RING-type zinc fingers.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri30 – 80RING-type 1; atypicalAdd BLAST51
Zinc fingeri101 – 166IBR-typeAdd BLAST66
Zinc fingeri191 – 220RING-type 2; degenerateAdd BLAST30

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

eggNOGiKOG1815. Eukaryota.
ENOG410XP9Y. LUCA.
GeneTreeiENSGT00840000129738.
HOGENOMiHOG000007696.
HOVERGENiHBG052072.
InParanoidiQ8BKD6.
KOiK11975.
OMAiCRIYIER.
OrthoDBiEOG091G0FQQ.
PhylomeDBiQ8BKD6.
TreeFamiTF324777.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR031127. E3_UB_ligase_RBR.
IPR002867. IBR_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR11685. PTHR11685. 1 hit.
PfamiPF01485. IBR. 2 hits.
[Graphical view]
SMARTiSM00647. IBR. 2 hits.
SM00184. RING. 2 hits.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BKD6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDSVDGLQCL TMTAENPPSG DLIPAPLVTC KLCLCEQSLD KMTMLQECQC
60 70 80 90 100
IFCTPCLKQY MVLSIREGCG SPITCPDMVC LNHGTLQETE IACLVPLDEF
110 120 130 140 150
QLYQRLKFER EVHMDPLRTW CPVADCQTVC HISAGDPGQP VLVECPSCHL
160 170 180 190 200
KFCSCCKDAW HEESSCRDSQ SAMPEHGALF GTDADAPIKQ CPVCRIYIER
210 220 230 240 250
NEGCAQMMCK NCKHTFCWYC LQNLDNDIFL RHYDKGPCRN KLGHSRASVM
260 270 280 290 300
WNRTQVVGIL VGLGVIALVT SPLLLLASPC IICCVCKSCR GKKKKHDPST

T
Length:301
Mass (Da):33,495
Last modified:January 4, 2005 - v2
Checksum:iB31B474C83E7C575
GO

Sequence cautioni

The sequence AAH25007 differs from that shown. Reason: Frameshift at position 147.Curated
The sequence AAH25007 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti174P → T in BAC35416 (PubMed:16141072).Curated1
Sequence conflicti211N → K in BAC35416 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK040939 mRNA. Translation: BAC30754.1.
AK052846 mRNA. Translation: BAC35173.1.
AK053529 mRNA. Translation: BAC35416.1.
BC025007 mRNA. Translation: AAH25007.1. Sequence problems.
CCDSiCCDS26491.1.
RefSeqiNP_001164114.1. NM_001170643.1.
NP_666154.3. NM_146042.4.
UniGeneiMm.287609.

Genome annotation databases

EnsembliENSMUST00000068891; ENSMUSP00000071017; ENSMUSG00000038068.
ENSMUST00000110111; ENSMUSP00000105738; ENSMUSG00000038068.
GeneIDi218215.
KEGGimmu:218215.
UCSCiuc007qhx.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK040939 mRNA. Translation: BAC30754.1.
AK052846 mRNA. Translation: BAC35173.1.
AK053529 mRNA. Translation: BAC35416.1.
BC025007 mRNA. Translation: AAH25007.1. Sequence problems.
CCDSiCCDS26491.1.
RefSeqiNP_001164114.1. NM_001170643.1.
NP_666154.3. NM_146042.4.
UniGeneiMm.287609.

3D structure databases

ProteinModelPortaliQ8BKD6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000071017.

PTM databases

PhosphoSitePlusiQ8BKD6.

Proteomic databases

PaxDbiQ8BKD6.
PRIDEiQ8BKD6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000068891; ENSMUSP00000071017; ENSMUSG00000038068.
ENSMUST00000110111; ENSMUSP00000105738; ENSMUSG00000038068.
GeneIDi218215.
KEGGimmu:218215.
UCSCiuc007qhx.2. mouse.

Organism-specific databases

CTDi255488.
MGIiMGI:2384986. Rnf144b.

Phylogenomic databases

eggNOGiKOG1815. Eukaryota.
ENOG410XP9Y. LUCA.
GeneTreeiENSGT00840000129738.
HOGENOMiHOG000007696.
HOVERGENiHBG052072.
InParanoidiQ8BKD6.
KOiK11975.
OMAiCRIYIER.
OrthoDBiEOG091G0FQQ.
PhylomeDBiQ8BKD6.
TreeFamiTF324777.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiRnf144b. mouse.
PROiQ8BKD6.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000038068.
CleanExiMM_RNF144B.
GenevisibleiQ8BKD6. MM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR031127. E3_UB_ligase_RBR.
IPR002867. IBR_dom.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR11685. PTHR11685. 1 hit.
PfamiPF01485. IBR. 2 hits.
[Graphical view]
SMARTiSM00647. IBR. 2 hits.
SM00184. RING. 2 hits.
[Graphical view]
PROSITEiPS00518. ZF_RING_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiR144B_MOUSE
AccessioniPrimary (citable) accession number: Q8BKD6
Secondary accession number(s): Q8BG97, Q8R195
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: January 4, 2005
Last modified: November 30, 2016
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Lacks the His residue in the RING-type domain 2 that is one of the conserved features of the family.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.