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Q9WVS6

- PRKN2_MOUSE

UniProt

Q9WVS6 - PRKN2_MOUSE

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Protein
E3 ubiquitin-protein ligase parkin
Gene
Park2, Prkn
Organism
Mus musculus (Mouse)
Status
Reviewed - 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, 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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei430 – 4301 By similarity

Regions

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

GO - Molecular functioni

  1. ligase activity Source: UniProtKB-KW
  2. protein binding Source: UniProtKB
  3. ubiquitin-protein transferase activity Source: MGI
  4. 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. neuron death Source: UniProtKB
  10. norepinephrine metabolic process Source: MGI
  11. protein K48-linked ubiquitination Source: UniProtKB
  12. protein metabolic process Source: MGI
  13. protein monoubiquitination Source: UniProtKB
  14. protein ubiquitination Source: UniProtKB
  15. regulation of autophagy Source: UniProtKB
  16. regulation of neurotransmitter secretion Source: MGI
  17. regulation of synaptic transmission Source: MGI
  18. regulation of transcription, DNA-templated Source: UniProtKB-KW
  19. startle response Source: MGI
  20. synaptic transmission, dopaminergic Source: MGI
  21. synaptic transmission, glutamatergic Source: MGI
  22. transcription, DNA-templated Source: UniProtKB-KW
  23. ubiquitin-dependent protein catabolic process Source: UniProtKB
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
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 Inferred. 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.2 Publications

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
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 parkin
PRO_0000058577Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei65 – 651Phosphoserine; by PINK1 By similarity

Post-translational modificationi

Auto-ubiquitinates in an E2-dependent manner leading to its own degradation By similarity. Also polyubiquitinated by RNF41 for proteasomal degradation By similarity.
S-nitrosylated.
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.
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.1 Publication

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

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.

Miscellaneous databases

EvolutionaryTraceiQ9WVS6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7676Ubiquitin-like
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni204 – 23835SYT11 binding 1
Add
BLAST
Regioni257 – 29337SYT11 binding 2
Add
BLAST
Regioni377 – 40933REP By similarity
Add
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.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei244 – 26118RSPVL…VICLD → SHLPLSSGASVWTRPHLH in isoform 3.
VSP_011713Add
BLAST
Alternative sequencei245 – 25410SPVLVFQCNH → FMRMSKHRTS in isoform 2.
VSP_011714
Alternative sequencei255 – 464210Missing in isoform 2.
VSP_011715Add
BLAST
Alternative sequencei262 – 464203Missing in isoform 3.
VSP_011716Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti137 – 1371P → PA1 Publication
Sequence conflicti137 – 1371P → PA in AAG13890. 1 Publication

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

« 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: September 3, 2014
This is version 116 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.

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