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Q9WVS6

- PRKN2_MOUSE

UniProt

Q9WVS6 - PRKN2_MOUSE

Protein

E3 ubiquitin-protein ligase parkin

Gene

Park2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    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, a 22 kDa O-linked glycosylated isoform of SNCAIP, SEPT5, TOMM20, USP30, ZNF746 and AIMP2. Mediates monoubiquitination as well as '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 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 the ubiquitination of mitochondrial proteins such as TOMM20, RHOT1/MIRO1 and USP30. 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.3 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 By similarity.By similarity

    Pathwayi

    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

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

    GO - Biological processi

    1. adult locomotory behavior Source: MGI
    2. cell death Source: UniProtKB
    3. cellular protein catabolic process Source: ParkinsonsUK-UCL
    4. dopamine metabolic process Source: MGI
    5. dopamine uptake involved in synaptic transmission Source: MGI
    6. learning Source: MGI
    7. locomotory behavior Source: MGI
    8. mitochondrion degradation Source: UniProtKB
    9. negative regulation of neuron death Source: ParkinsonsUK-UCL
    10. neuron death Source: UniProtKB
    11. norepinephrine metabolic process Source: MGI
    12. protein K48-linked ubiquitination Source: UniProtKB
    13. protein metabolic process Source: MGI
    14. protein monoubiquitination Source: UniProtKB
    15. protein ubiquitination Source: UniProtKB
    16. regulation of autophagy Source: UniProtKB
    17. regulation of neurotransmitter secretion Source: MGI
    18. regulation of synaptic transmission Source: MGI
    19. regulation of transcription, DNA-templated Source: UniProtKB-KW
    20. startle response Source: MGI
    21. synaptic transmission, dopaminergic Source: MGI
    22. synaptic transmission, glutamatergic Source: MGI
    23. transcription, DNA-templated Source: UniProtKB-KW
    24. ubiquitin-dependent protein catabolic process Source: UniProtKB

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:1355296. Park2.

    Subcellular locationi

    Nucleus By similarity. Endoplasmic reticulum By similarity. Cytoplasmcytosol 2 Publications. 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. Relocates to dysfunctional mitochondria that have lost the mitochondial membrane potential; recruitment to mitochondria is PINK1-dependent By similarity.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: UniProtKB
    4. dendrite Source: UniProtKB-SubCell
    5. endoplasmic reticulum Source: UniProtKB-SubCell
    6. mitochondrion Source: UniProtKB
    7. neuron projection Source: MGI
    8. nucleus Source: MGI
    9. postsynaptic density Source: UniProtKB-SubCell
    10. postsynaptic membrane Source: UniProtKB-KW
    11. protein complex Source: MGI

    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.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.
    GenevestigatoriQ9WVS6.

    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 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. 17 interactions.
    IntActiQ9WVS6. 8 interactions.
    MINTiMINT-2736580.
    STRINGi10090.ENSMUSP00000063644.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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
    Regioni204 – 23835SYT11 binding 1Add
    BLAST
    Regioni257 – 29337SYT11 binding 2Add
    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.
    HOGENOMiHOG000013184.
    HOVERGENiHBG053682.
    InParanoidiQ2KHJ9.
    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. Align

    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

    MIVFVRFNSS YGFPVEVDSD TSILQLKEVV AKRQGVPADQ LRVIFAGKEL    50
    PNHLTVQNCD LEQQSIVHIV QRPRRRSHET NASGGDEPQS TSEGSIWESR 100
    SLTRVDLSSH TLPVDSVGLA VILDTDSKRD SEAARGPVKP TYNSFFIYCK 150
    GPCHKVQPGK LRVQCGTCKQ ATLTLAQGPS CWDDVLIPNR MSGECQSPDC 200
    PGTRAEFFFK CGAHPTSDKD TSVALNLITS NRRSIPCIAC TDVRSPVLVF 250
    QCNHRHVICL DCFHLYCVTR LNDRQFVHDA QLGYSLPCVA GCPNSLIKEL 300
    HHFRILGEEQ YTRYQQYGAE ECVLQMGGVL CPRPGCGAGL LPEQGQRKVT 350
    CEGGNGLGCG FVFCRDCKEA YHEGDCDSLL EPSGATSQAY RVDKRAAEQA 400
    RWEEASKETI KKTTKPCPRC NVPIEKNGGC MHMKCPQPQC KLEWCWNCGC 450
    EWNRACMGDH WFDV 464
    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:
    EMBL
    GenBank
    DDBJ
    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

    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:
    EMBL
    GenBank
    DDBJ
    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 .
    RefSeqi NP_057903.1. NM_016694.3. [Q9WVS6-1 ]
    XP_006523403.1. XM_006523340.1.
    UniGenei Mm.311110.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1MG8 NMR - A 1-76 [» ]
    2ZEQ X-ray 1.65 A 1-76 [» ]
    3B1L X-ray 1.85 X 1-76 [» ]
    ProteinModelPortali Q9WVS6.
    SMRi Q9WVS6. Positions 1-76, 140-464.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 206136. 17 interactions.
    IntActi Q9WVS6. 8 interactions.
    MINTi MINT-2736580.
    STRINGi 10090.ENSMUSP00000063644.

    PTM databases

    PhosphoSitei Q9WVS6.

    Proteomic databases

    PRIDEi Q9WVS6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 50873.
    KEGGi mmu:50873.
    UCSCi uc008akj.1. mouse. [Q9WVS6-3 ]
    uc008akk.1. mouse. [Q9WVS6-1 ]

    Organism-specific databases

    CTDi 5071.
    MGIi MGI:1355296. Park2.

    Phylogenomic databases

    eggNOGi NOG278133.
    HOGENOMi HOG000013184.
    HOVERGENi HBG053682.
    InParanoidi Q2KHJ9.
    KOi K04556.
    PhylomeDBi Q9WVS6.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    EvolutionaryTracei Q9WVS6.
    NextBioi 307835.
    PROi Q9WVS6.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_PARK2.
    Genevestigatori Q9WVS6.

    Family and domain databases

    InterProi IPR003977. Parkin.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    IPR002867. Znf_C6HC.
    [Graphical view ]
    Pfami PF01485. IBR. 2 hits.
    PF00240. ubiquitin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037880. Parkin. 1 hit.
    PRINTSi PR01475. PARKIN.
    SMARTi SM00647. IBR. 2 hits.
    SM00213. UBQ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54236. SSF54236. 1 hit.
    PROSITEi PS50053. UBIQUITIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 117 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