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Protein

E3 ubiquitin-protein ligase parkin

Gene

Park2

Organism
Rattus norvegicus (Rat)
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 similarity

Enzyme regulationi

In the autoinhibited state the side chain of Phe-463 inserts into a hydrophobic groove in RING-0, occluding the ubiquitin acceptor site Cys-431, 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-431 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 similarity1 Publication

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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei431 – 43111 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri141 – 22585RING-type 0; atypicalAdd
BLAST
Zinc fingeri238 – 29356RING-type 1; atypicalAdd
BLAST
Zinc fingeri313 – 37765IBR-typeAdd
BLAST
Zinc fingeri418 – 44932RING-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

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase parkin (EC:6.3.2.-)
Gene namesi
Name:Park2
Synonyms:Prkn
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi61797. Park2.

Subcellular locationi

  • Nucleus By similarity
  • Endoplasmic reticulum By similarity
  • Cytoplasmcytosol By similarity
  • Cell projectiondendrite By similarity
  • Cell junctionsynapsepostsynaptic cell membranepostsynaptic density By similarity
  • Mitochondrion By similarity
  • Cell junctionsynapse By similarity

  • Note: Mainly localizes in the cytosol. Expressed in the endoplasmic reticulum, dendrites, some presynaptic terminals and in postsynaptic densities (By similarity). Relocates to dysfunctional mitochondria that have lost the mitochondrial membrane potential; recruitment to mitochondria is PINK1-dependent (By similarity).By similarity

GO - Cellular componenti

  • aggresome Source: ParkinsonsUK-UCL
  • cell junction Source: UniProtKB-KW
  • cytoplasm Source: UniProtKB
  • cytoplasmic vesicle Source: RGD
  • cytosol Source: UniProtKB
  • dendrite Source: UniProtKB-SubCell
  • endoplasmic reticulum Source: RGD
  • endoplasmic reticulum membrane Source: ParkinsonsUK-UCL
  • Golgi membrane Source: ParkinsonsUK-UCL
  • intracellular Source: RGD
  • membrane raft Source: RGD
  • mitochondrion Source: UniProtKB
  • neuron projection Source: RGD
  • nucleus Source: UniProtKB-SubCell
  • Parkin-FBXW7-Cul1 ubiquitin ligase complex Source: ParkinsonsUK-UCL
  • postsynaptic density Source: RGD
  • postsynaptic membrane Source: UniProtKB-KW
  • synapse Source: ParkinsonsUK-UCL
  • synaptic vesicle Source: RGD
  • synaptic vesicle membrane Source: RGD
  • ubiquitin ligase complex Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi403 – 4031W → A: Increased autoubiquitination. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 465465E3 ubiquitin-protein ligase parkinPRO_0000058578Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei65 – 651Phosphoserine; by PINK1By similarity
Modified residuei80 – 801PhosphothreonineBy similarity

Post-translational modificationi

Auto-ubiquitinates in an E2-dependent manner leading to its own degradation.1 Publication
S-nitrosylated.By similarity
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).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ9JK66.
PRIDEiQ9JK66.

PTM databases

iPTMnetiQ9JK66.
PhosphoSiteiQ9JK66.

Expressioni

Tissue specificityi

Largely confined to neuronal elements, including fibers and neuropil. Highly expressed at the forebrain level, in pyramidal cells of layer V, in various cortical regions and cerebellum. Expressed in the nucleus of diagonal band of Broca, nucleus basalis, bed nucleus of the stria terminalis, and olfactory tubercle. Moderate expression is seen in most neurons of the subthalamic nucleus, heart, skeletal muscle and testis. Moderate expression was found in frontal cortex, parietal cortex, cerebellum, heart, skeletal muscle and testis.1 Publication

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 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 LRRK2. 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 FBXO7; this promotes translocation to dysfunctional depolarized mitochondria (By similarity). 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
Ranbp2D4A0542EBI-973793,EBI-973937

GO - Molecular functioni

Protein-protein interaction databases

BioGridi248590. 12 interactions.
DIPiDIP-37656N.
IntActiQ9JK66. 1 interaction.
MINTiMINT-220162.
STRINGi10116.ENSRNOP00000040511.

Structurei

Secondary structure

1
465
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 1110Combined sources
Beta strandi13 – 164Combined sources
Helixi23 – 3412Combined sources
Helixi38 – 403Combined sources
Beta strandi41 – 455Combined sources
Beta strandi48 – 503Combined sources
Helixi56 – 594Combined sources
Beta strandi65 – 717Combined sources
Beta strandi147 – 1504Combined sources
Turni151 – 1544Combined sources
Beta strandi156 – 16611Combined sources
Turni167 – 1704Combined sources
Beta strandi174 – 1785Combined sources
Helixi183 – 1875Combined sources
Beta strandi193 – 1964Combined sources
Beta strandi205 – 21511Combined sources
Beta strandi223 – 2253Combined sources
Turni239 – 2413Combined sources
Beta strandi246 – 2505Combined sources
Beta strandi253 – 2553Combined sources
Beta strandi257 – 2604Combined sources
Helixi261 – 27414Combined sources
Beta strandi278 – 2803Combined sources
Turni281 – 2833Combined sources
Beta strandi284 – 2863Combined sources
Helixi301 – 3077Combined sources
Helixi309 – 3168Combined sources
Helixi318 – 3269Combined sources
Turni335 – 3373Combined sources
Beta strandi348 – 3503Combined sources
Helixi355 – 3573Combined sources
Beta strandi363 – 3653Combined sources
Beta strandi366 – 3683Combined sources
Helixi395 – 4006Combined sources
Beta strandi401 – 4033Combined sources
Beta strandi415 – 4173Combined sources
Turni419 – 4213Combined sources
Beta strandi424 – 4263Combined sources
Beta strandi429 – 4313Combined sources
Beta strandi433 – 4353Combined sources
Turni439 – 4413Combined sources
Beta strandi444 – 4463Combined sources
Turni447 – 4493Combined sources
Helixi455 – 4617Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KNBNMR-A1-76[»]
4K7DX-ray2.80A/B/C141-465[»]
4K95X-ray6.50A/B/C/D/E/F/G/H/I/J/K/L1-465[»]
4ZYNX-ray2.54A/B1-465[»]
ProteinModelPortaliQ9JK66.
SMRiQ9JK66. Positions 307-384.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9JK66.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni204 – 23835SYT11 binding 1By similarityAdd
BLAST
Regioni257 – 29337SYT11 binding 2By similarityAdd
BLAST
Regioni378 – 41033REPAdd
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 fingeri141 – 22585RING-type 0; atypicalAdd
BLAST
Zinc fingeri238 – 29356RING-type 1; atypicalAdd
BLAST
Zinc fingeri313 – 37765IBR-typeAdd
BLAST
Zinc fingeri418 – 44932RING-type 2Add
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0006. Eukaryota.
ENOG410YG4B. LUCA.
HOVERGENiHBG053682.
InParanoidiQ9JK66.
KOiK04556.
PhylomeDBiQ9JK66.

Family and domain databases

InterProiIPR031127. E3_UB_ligase_RBR.
IPR002867. IBR_dom.
IPR003977. Parkin.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PANTHERiPTHR11685. PTHR11685. 1 hit.
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 (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9JK66-1) [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 TSIFQLKEVV AKRQGVPADQ LRVIFAGKEL
60 70 80 90 100
QNHLTVQNCD LEQQSIVHIV QRPQRKSHET NASGGDKPQS TPEGSIWEPR
110 120 130 140 150
SLTRVDLSSH ILPADSVGLA VILDTDSKSD SEAARGPEAK PTYHSFFVYC
160 170 180 190 200
KGPCHKVQPG KLRVQCGTCR QATLTLAQGP SCWDDVLIPN RMSGECQSPD
210 220 230 240 250
CPGTRAEFFF KCGAHPTSDK DTSVALNLIT NNSRSIPCIA CTDVRNPVLV
260 270 280 290 300
FQCNHRHVIC LDCFHLYCVT RLNDRQFVHD AQLGYSLPCV AGCPNSLIKE
310 320 330 340 350
LHHFRILGEE QYNRYQQYGA EECVLQMGGV LCPRPGCGAG LLPEQGQKKV
360 370 380 390 400
TCEGGNGLGC GFVFCRDCKE AYHEGECDSM FEASGATSQA YRVDQRAAEQ
410 420 430 440 450
ARWEEASKET IKKTTKPCPR CNVPIEKNGG CMHMKCPQPQ CKLEWCWNCG
460
CEWNRACMGD HWFDV
Length:465
Mass (Da):51,709
Last modified:October 1, 2000 - v1
Checksum:iE13CF170AD6D042B
GO
Isoform 2 (identifier: Q9JK66-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     429-446: GGCMHMKCPQPQCKLEWC → ERMHVQYTMCIPGAHGGY
     447-465: Missing.

Show »
Length:446
Mass (Da):49,368
Checksum:iF06FAF788531DF5C
GO
Isoform 3 (identifier: Q9JK66-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-191: Missing.

Show »
Length:274
Mass (Da):30,642
Checksum:iB29BB58E86EB5DFE
GO
Isoform 4 (identifier: Q9JK66-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     57-57: Q → QHPQDGFCHKSHLAVHNLSQQDVTQ

Show »
Length:489
Mass (Da):54,418
Checksum:i49F53B8F358E2AB5
GO
Isoform 5 (identifier: Q9JK66-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     179-206: Missing.

Show »
Length:437
Mass (Da):48,734
Checksum:i3227286E41EBE5E3
GO
Isoform 6 (identifier: Q9JK66-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-191: Missing.
     390-394: AYRVD → EDVCT
     395-465: Missing.

Show »
Length:203
Mass (Da):22,288
Checksum:i3CFF551C49EB0783
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241F → C in AAF34874 (PubMed:10686358).Curated
Sequence conflicti138 – 1381E → A in BAA92431 (Ref. 3) Curated
Sequence conflicti348 – 3481K → R in BAA92431 (Ref. 3) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 191191Missing in isoform 3 and isoform 6. 1 PublicationVSP_011717Add
BLAST
Alternative sequencei57 – 571Q → QHPQDGFCHKSHLAVHNLSQ QDVTQ in isoform 4. 1 PublicationVSP_011718
Alternative sequencei179 – 20628Missing in isoform 5. 1 PublicationVSP_011719Add
BLAST
Alternative sequencei390 – 3945AYRVD → EDVCT in isoform 6. 1 PublicationVSP_011720
Alternative sequencei395 – 46571Missing in isoform 6. 1 PublicationVSP_011721Add
BLAST
Alternative sequencei429 – 44618GGCMH…KLEWC → ERMHVQYTMCIPGAHGGY in isoform 2. 1 PublicationVSP_011722Add
BLAST
Alternative sequencei447 – 46519Missing in isoform 2. 1 PublicationVSP_011723Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF343574 mRNA. Translation: AAL73348.1.
AF381277 mRNA. Translation: AAM21452.1.
AF381278 mRNA. Translation: AAM21453.1.
AF381279 mRNA. Translation: AAM21454.1.
AF381280 mRNA. Translation: AAM21455.1.
AF381281 mRNA. Translation: AAM21456.1.
AF168004 mRNA. Translation: AAF34874.1.
AF210434 mRNA. Translation: AAG37013.1.
AF257234 mRNA. Translation: AAF68666.1.
AB039878 mRNA. Translation: BAA92431.1.
RefSeqiNP_064478.1. NM_020093.1.
UniGeneiRn.207194.

Genome annotation databases

GeneIDi56816.
KEGGirno:56816.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF343574 mRNA. Translation: AAL73348.1.
AF381277 mRNA. Translation: AAM21452.1.
AF381278 mRNA. Translation: AAM21453.1.
AF381279 mRNA. Translation: AAM21454.1.
AF381280 mRNA. Translation: AAM21455.1.
AF381281 mRNA. Translation: AAM21456.1.
AF168004 mRNA. Translation: AAF34874.1.
AF210434 mRNA. Translation: AAG37013.1.
AF257234 mRNA. Translation: AAF68666.1.
AB039878 mRNA. Translation: BAA92431.1.
RefSeqiNP_064478.1. NM_020093.1.
UniGeneiRn.207194.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KNBNMR-A1-76[»]
4K7DX-ray2.80A/B/C141-465[»]
4K95X-ray6.50A/B/C/D/E/F/G/H/I/J/K/L1-465[»]
4ZYNX-ray2.54A/B1-465[»]
ProteinModelPortaliQ9JK66.
SMRiQ9JK66. Positions 307-384.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248590. 12 interactions.
DIPiDIP-37656N.
IntActiQ9JK66. 1 interaction.
MINTiMINT-220162.
STRINGi10116.ENSRNOP00000040511.

PTM databases

iPTMnetiQ9JK66.
PhosphoSiteiQ9JK66.

Proteomic databases

PaxDbiQ9JK66.
PRIDEiQ9JK66.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi56816.
KEGGirno:56816.

Organism-specific databases

CTDi5071.
RGDi61797. Park2.

Phylogenomic databases

eggNOGiKOG0006. Eukaryota.
ENOG410YG4B. LUCA.
HOVERGENiHBG053682.
InParanoidiQ9JK66.
KOiK04556.
PhylomeDBiQ9JK66.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

EvolutionaryTraceiQ9JK66.
PROiQ9JK66.

Family and domain databases

InterProiIPR031127. E3_UB_ligase_RBR.
IPR002867. IBR_dom.
IPR003977. Parkin.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PANTHERiPTHR11685. PTHR11685. 1 hit.
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...

Entry informationi

Entry nameiPRKN2_RAT
AccessioniPrimary (citable) accession number: Q9JK66
Secondary accession number(s): Q8K5C3
, Q8K5C4, Q8K5C5, Q8K5C6, Q8VHY6, Q9JLL1, Q9JM64
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 1, 2000
Last modified: September 7, 2016
This is version 124 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.