Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

E3 ubiquitin-protein ligase parkin

Gene

Park2

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

Functioni

Functions within a multiprotein E3 ubiquitin ligase complex, catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins, such as BCL2, SYT11, CCNE1, GPR37, RHOT1/MIRO1, MFN1, MFN2, STUB1, SNCAIP, SEPT5, TOMM20, USP30, ZNF746 and AIMP2. Mediates monoubiquitination as well as 'Lys-6', 'Lys-11', 'Lys-48'-linked and 'Lys-63'-linked polyubiquitination of substrates depending on the context. Participates in the removal and/or detoxification of abnormally folded or damaged protein by mediating 'Lys-63'-linked polyubiquitination of misfolded proteins such as PARK7: 'Lys-63'-linked polyubiquitinated misfolded proteins are then recognized by HDAC6, leading to their recruitment to aggresomes, followed by degradation. Mediates 'Lys-63'-linked polyubiquitination of a 22 kDa O-linked glycosylated isoform of SNCAIP, possibly playing a role in Lewy-body formation. Mediates monoubiquitination of BCL2, thereby acting as a positive regulator of autophagy. Promotes the autophagic degradation of dysfunctional depolarized mitochondria (mitophagy) by promoting the ubiquitination of mitochondrial proteins such as TOMM20, RHOT1/MIRO1 and USP30. Preferentially assembles 'Lys-6'-, 'Lys-11'- and 'Lys-63'-linked polyubiquitin chains following mitochondrial damage, leading to mitophagy. Mediates 'Lys-48'-linked polyubiquitination of ZNF746, followed by degradation of ZNF746 by the proteasome; possibly playing a role in the regulation of neuron death. Limits the production of reactive oxygen species (ROS). Regulates cyclin-E during neuronal apoptosis. In collaboration with CHPF isoform 2, may enhance cell viability and protect cells from oxidative stress. Independently of its ubiquitin ligase activity, protects from apoptosis by the transcriptional repression of p53/TP53. May protect neurons against alpha synuclein toxicity, proteasomal dysfunction, GPR37 accumulation, and kainate-induced excitotoxicity. May play a role in controlling neurotransmitter trafficking at the presynaptic terminal and in calcium-dependent exocytosis. May represent a tumor suppressor gene.By similarity3 Publications

Enzyme regulationi

In the autoinhibited state the side chain of Phe-462 inserts into a hydrophobic groove in RING-0, occluding the ubiquitin acceptor site Cys-430, whereas the REP repressor element binds RING-1 and blocks its E2-binding site. Activation of PARK2 requires 2 steps: (1) phosphorylation at Ser-65 by PINK1 and (2) binding to phosphorylated ubiquitin, leading to unlock repression of the catalytic Cys-430 by the RING-0 region via an allosteric mechanism and converting PARK2 to its fully-active form. According to another report, phosphorylation at Ser-65 by PINK1 is not essential for activation and only binding to phosphorylated ubiquitin is essential to unlock repression.By similarity

Pathway: 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei430 – 4301By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri140 – 22485RING-type 0; atypicalAdd
BLAST
Zinc fingeri237 – 29256RING-type 1; atypicalAdd
BLAST
Zinc fingeri312 – 37665IBR-typeAdd
BLAST
Zinc fingeri417 – 44832RING-type 2Add
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Autophagy, Transcription, Transcription regulation, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_343568. Antigen processing: Ubiquitination & Proteasome degradation.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase parkin (EC:6.3.2.-)
Gene namesi
Name:Park2
Synonyms:Prkn
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1355296. Park2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Endoplasmic reticulum, Membrane, Mitochondrion, Nucleus, Postsynaptic cell membrane, Synapse

Pathology & Biotechi

Disruption phenotypei

In brain, increased protein levels of p53/TP53 and CHPF.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 464464E3 ubiquitin-protein ligase parkinPRO_0000058577Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei65 – 651Phosphoserine; by PINK1By similarity

Post-translational modificationi

Auto-ubiquitinates in an E2-dependent manner leading to its own degradation. Also polyubiquitinated by RNF41 for proteasomal degradation.By similarity
S-nitrosylated.1 Publication
Phosphorylation at Ser-65 by PINK1 contributes to activate PARK2 activity. It is however not sufficient and requires binding to phosphorylated ubiquitin as well.By similarity

Keywords - PTMi

Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

PRIDEiQ9WVS6.

PTM databases

PhosphoSiteiQ9WVS6.

Expressioni

Tissue specificityi

Expressed in all subdivisions of the brain. Highly expressed in brainstem, cranial nerve, pontine, cerebellar nuclei, indusium griseum, nuclei reticularis, strata oriens and laccunosum moleculare of the hippocampal CA2 region. Low levels were found in the telencephalon and diencephalon. Expressed in heart, liver, skeletal muscle, kidney and testis.3 Publications

Developmental stagei

In late 10 dpc weakly expressed in postmitotic neurons in the mantle layer of the developing nervous system. Expression increased at 11-12 dpc. At 15-16 dpc, as more specialized neurons and nonneural cells are formed, expression is more tissue specific. Expression was highest in the neurites, moderate levels were observed in the migrating postmitotic neurons in the intermediate and neopallial layers. In the diencephalon and other CNS regions, while the weakest level of expression was observed in the cell bodies. In nonneural tissues, high levels of expression were found in the muscle walls of the intestine, the blood vessels and the dermis.1 Publication

Gene expression databases

CleanExiMM_PARK2.
ExpressionAtlasiQ9WVS6. baseline and differential.
GenevisibleiQ9WVS6. MM.

Interactioni

Subunit structurei

Forms an E3 ubiquitin ligase complex with UBE2L3 or UBE2L6. Mediates 'Lys-63'-linked polyubiquitination by associating with UBE2V1. Part of a SCF-like complex, consisting of PARK2, CUL1 and FBXW7. Interacts with FBXO7; this promotes translocation to dysfunctional depolarized mitochondria (By similarity). Interacts with SNCAIP. Binds to the C2A and C2B domains of SYT11. Interacts and regulates the turnover of SEPT5. Part of a complex, including STUB1, HSP70 and GPR37. The amount of STUB1 in the complex increases during ER stress. STUB1 promotes the dissociation of HSP70 from PARK2 and GPR37, thus facilitating PARK2-mediated GPR37 ubiquitination. HSP70 transiently associates with unfolded GPR37 and inhibits the E3 activity of PARK2, whereas, STUB1 enhances the E3 activity of PARK2 through promotion of dissociation of HSP70 from PARK2-GPR37 complexes. Interacts with PSMD4 and PACRG. Interacts with LRKK2. Interacts with RANBP2. Interacts with SUMO1 but not SUMO2, which promotes nuclear localization and autoubiquitination. Interacts (via first RING-type domain) with AIMP2 (via N-terminus). Interacts with PSMA7 and RNF41. Interacts with PINK1. Interacts with CHPF, the interaction may facilitate PARK2 transport into the mitochondria. Interacts with MFN2 (phosphorylated), promotes PARK2 localization in dysfunctional depolarized mitochondria. Interacts with heat shock protein 70 family members, including HSPA1L, HSPA1A and HSPA8; interaction HSPA1L promotes translocation to damaged mitochondria (By similarity). Interacts with BAG4 and, to a lesser extent, BAG5; interaction with BAG4 inhibits translocation to damaged mitochondria. Interacts (when phosphorylated at Ser-65) with ubiquitin (phosphorylated); binding to phosphorylated ubiquitin is required to activate PARK2. Forms a complex with PINK1 and PARK7 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ChpfQ6IQX7-23EBI-973635,EBI-9029659
Ranbp2Q9ERU92EBI-973635,EBI-643756
YwhahP685108EBI-973635,EBI-444641
Znf746Q3U1332EBI-973635,EBI-3862590

Protein-protein interaction databases

BioGridi206136. 22 interactions.
IntActiQ9WVS6. 11 interactions.
MINTiMINT-2736580.
STRINGi10090.ENSMUSP00000063644.

Structurei

Secondary structure

464
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1 – 1111Combined sources
Beta strandi13 – 175Combined sources
Helixi23 – 3412Combined sources
Helixi38 – 403Combined sources
Beta strandi41 – 455Combined sources
Beta strandi48 – 503Combined sources
Helixi56 – 583Combined sources
Beta strandi66 – 738Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MG8NMR-A1-76[»]
2ZEQX-ray1.65A1-76[»]
3B1LX-ray1.85X1-76[»]
ProteinModelPortaliQ9WVS6.
SMRiQ9WVS6. Positions 1-76, 140-464.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WVS6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7676Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni203 – 23735SYT11 binding 1By similarityAdd
BLAST
Regioni256 – 29237SYT11 binding 2By similarityAdd
BLAST
Regioni377 – 40933REPBy similarityAdd
BLAST

Domaini

The ubiquitin-like domain binds the PSMD4 subunit of 26S proteasomes.By similarity
The RING-type 1 zinc finger domain is required to repress p53/TP53 transcription.By similarity

Sequence similaritiesi

Belongs to the RBR family. Parkin subfamily.Curated
Contains 1 IBR-type zinc finger.Curated
Contains 3 RING-type zinc fingers.Curated
Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri140 – 22485RING-type 0; atypicalAdd
BLAST
Zinc fingeri237 – 29256RING-type 1; atypicalAdd
BLAST
Zinc fingeri312 – 37665IBR-typeAdd
BLAST
Zinc fingeri417 – 44832RING-type 2Add
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiNOG278133.
GeneTreeiENSGT00390000011034.
HOGENOMiHOG000013184.
HOVERGENiHBG053682.
InParanoidiQ9WVS6.
KOiK04556.
PhylomeDBiQ9WVS6.

Family and domain databases

InterProiIPR003977. Parkin.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR002867. Znf_C6HC.
[Graphical view]
PfamiPF01485. IBR. 2 hits.
PF00240. ubiquitin. 1 hit.
[Graphical view]
PIRSFiPIRSF037880. Parkin. 1 hit.
PRINTSiPR01475. PARKIN.
SMARTiSM00647. IBR. 2 hits.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9WVS6-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MIVFVRFNSS YGFPVEVDSD TSILQLKEVV AKRQGVPADQ LRVIFAGKEL
60 70 80 90 100
PNHLTVQNCD LEQQSIVHIV QRPRRRSHET NASGGDEPQS TSEGSIWESR
110 120 130 140 150
SLTRVDLSSH TLPVDSVGLA VILDTDSKRD SEAARGPVKP TYNSFFIYCK
160 170 180 190 200
GPCHKVQPGK LRVQCGTCKQ ATLTLAQGPS CWDDVLIPNR MSGECQSPDC
210 220 230 240 250
PGTRAEFFFK CGAHPTSDKD TSVALNLITS NRRSIPCIAC TDVRSPVLVF
260 270 280 290 300
QCNHRHVICL DCFHLYCVTR LNDRQFVHDA QLGYSLPCVA GCPNSLIKEL
310 320 330 340 350
HHFRILGEEQ YTRYQQYGAE ECVLQMGGVL CPRPGCGAGL LPEQGQRKVT
360 370 380 390 400
CEGGNGLGCG FVFCRDCKEA YHEGDCDSLL EPSGATSQAY RVDKRAAEQA
410 420 430 440 450
RWEEASKETI KKTTKPCPRC NVPIEKNGGC MHMKCPQPQC KLEWCWNCGC
460
EWNRACMGDH WFDV
Length:464
Mass (Da):51,618
Last modified:November 1, 1999 - v1
Checksum:i5574A285A9A1B080
GO
Isoform 2 (identifier: Q9WVS6-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     245-254: SPVLVFQCNH → FMRMSKHRTS
     255-464: Missing.

Show »
Length:254
Mass (Da):28,084
Checksum:i3D35E959C9C5ED03
GO
Isoform 3 (identifier: Q9WVS6-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     244-261: RSPVLVFQCNHRHVICLD → SHLPLSSGASVWTRPHLH
     262-464: Missing.

Show »
Length:261
Mass (Da):28,629
Checksum:i6DA482E28FE80671
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti137 – 1371P → PA (PubMed:10818204).Curated
Sequence conflicti137 – 1371P → PA in AAG13890 (PubMed:11122330).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei244 – 26118RSPVL…VICLD → SHLPLSSGASVWTRPHLH in isoform 3. 1 PublicationVSP_011713Add
BLAST
Alternative sequencei245 – 25410SPVLVFQCNH → FMRMSKHRTS in isoform 2. 1 PublicationVSP_011714
Alternative sequencei255 – 464210Missing in isoform 2. 1 PublicationVSP_011715Add
BLAST
Alternative sequencei262 – 464203Missing in isoform 3. 1 PublicationVSP_011716Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB019558 mRNA. Translation: BAA82404.1.
AF250293 mRNA. Translation: AAG13890.1.
AF250294 mRNA. Translation: AAG13891.1.
AF250295 mRNA. Translation: AAG13892.1.
BC113204 mRNA. Translation: AAI13205.1.
RefSeqiNP_057903.1. NM_016694.3. [Q9WVS6-1]
XP_006523403.1. XM_006523340.1.
UniGeneiMm.311110.

Genome annotation databases

EnsembliENSMUST00000191124; ENSMUSP00000140587; ENSMUSG00000023826. [Q9WVS6-1]
GeneIDi50873.
KEGGimmu:50873.
UCSCiuc008akj.1. mouse. [Q9WVS6-3]
uc008akk.1. mouse. [Q9WVS6-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB019558 mRNA. Translation: BAA82404.1.
AF250293 mRNA. Translation: AAG13890.1.
AF250294 mRNA. Translation: AAG13891.1.
AF250295 mRNA. Translation: AAG13892.1.
BC113204 mRNA. Translation: AAI13205.1.
RefSeqiNP_057903.1. NM_016694.3. [Q9WVS6-1]
XP_006523403.1. XM_006523340.1.
UniGeneiMm.311110.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MG8NMR-A1-76[»]
2ZEQX-ray1.65A1-76[»]
3B1LX-ray1.85X1-76[»]
ProteinModelPortaliQ9WVS6.
SMRiQ9WVS6. Positions 1-76, 140-464.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi206136. 22 interactions.
IntActiQ9WVS6. 11 interactions.
MINTiMINT-2736580.
STRINGi10090.ENSMUSP00000063644.

PTM databases

PhosphoSiteiQ9WVS6.

Proteomic databases

PRIDEiQ9WVS6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000191124; ENSMUSP00000140587; ENSMUSG00000023826. [Q9WVS6-1]
GeneIDi50873.
KEGGimmu:50873.
UCSCiuc008akj.1. mouse. [Q9WVS6-3]
uc008akk.1. mouse. [Q9WVS6-1]

Organism-specific databases

CTDi5071.
MGIiMGI:1355296. Park2.

Phylogenomic databases

eggNOGiNOG278133.
GeneTreeiENSGT00390000011034.
HOGENOMiHOG000013184.
HOVERGENiHBG053682.
InParanoidiQ9WVS6.
KOiK04556.
PhylomeDBiQ9WVS6.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiREACT_343568. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

EvolutionaryTraceiQ9WVS6.
NextBioi307835.
PROiQ9WVS6.
SOURCEiSearch...

Gene expression databases

CleanExiMM_PARK2.
ExpressionAtlasiQ9WVS6. baseline and differential.
GenevisibleiQ9WVS6. MM.

Family and domain databases

InterProiIPR003977. Parkin.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR002867. Znf_C6HC.
[Graphical view]
PfamiPF01485. IBR. 2 hits.
PF00240. ubiquitin. 1 hit.
[Graphical view]
PIRSFiPIRSF037880. Parkin. 1 hit.
PRINTSiPR01475. PARKIN.
SMARTiSM00647. IBR. 2 hits.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning, gene expression, and identification of a splicing variant of the mouse parkin gene."
    Kitada T., Asakawa S., Minoshima S., Mizuno Y., Shimizu N.
    Mamm. Genome 11:417-421(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Tissue: Skeletal muscle.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Strain: BALB/c.
    Tissue: Kidney.
  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] (ISOFORM 1).
  4. "Differential expression and tissue distribution of parkin isoforms during mouse development."
    Huynh D.P., Dy M., Nguyen D., Kiehl T.-R., Pulst S.M.
    Brain Res. Dev. Brain Res. 130:173-181(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  5. "S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function."
    Chung K.K.K., Thomas B., Li X., Pletnikova O., Troncoso J.C., Marsh L., Dawson V.L., Dawson T.M.
    Science 304:1328-1331(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UBIQUITINATION, S-NITROSYLATION.
  6. "Transcriptional repression of p53 by parkin and impairment by mutations associated with autosomal recessive juvenile Parkinson's disease."
    da Costa C.A., Sunyach C., Giaime E., West A., Corti O., Brice A., Safe S., Abou-Sleiman P.M., Wood N.W., Takahashi H., Goldberg M.S., Shen J., Checler F.
    Nat. Cell Biol. 11:1370-1375(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN APOPTOSIS, DISRUPTION PHENOTYPE.
  7. "Parkin interacts with Klokin1 for mitochondrial import and maintenance of membrane potential."
    Kuroda Y., Sako W., Goto S., Sawada T., Uchida D., Izumi Y., Takahashi T., Kagawa N., Matsumoto M., Matsumoto M., Takahashi R., Kaji R., Mitsui T.
    Hum. Mol. Genet. 21:991-1003(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CHPF, DISRUPTION PHENOTYPE.
  8. "NMR structure of ubiquitin-like domain in PARKIN: gene product of familial Parkinson's disease."
    Tashiro M., Okubo S., Shimotakahara S., Hatanaka H., Yasuda H., Kainosho M., Yokoyama S., Shindo H.
    J. Biomol. NMR 25:153-156(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-76.

Entry informationi

Entry nameiPRKN2_MOUSE
AccessioniPrimary (citable) accession number: Q9WVS6
Secondary accession number(s): Q2KHJ9, Q9ES22, Q9ES23
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: November 1, 1999
Last modified: June 24, 2015
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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).By similarity

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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.