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E3 ubiquitin-protein ligase parkin (EC 2.3.2.-) (Parkin RBR E3 ubiquitin-protein ligase)

 PRKN_RAT                Reviewed;         465 AA.
Q9JK66; Q8K5C3; Q8K5C4; Q8K5C5; Q8K5C6; Q8VHY6; Q9JLL1; Q9JM64;
11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
22-NOV-2017, entry version 134.
RecName: Full=E3 ubiquitin-protein ligase parkin {ECO:0000305};
EC=2.3.2.- {ECO:0000269|PubMed:23661642};
AltName: Full=Parkin RBR E3 ubiquitin-protein ligase {ECO:0000250|UniProtKB:O60260};
Name=Prkn {ECO:0000250|UniProtKB:O60260};
Synonyms=Park2 {ECO:0000312|RGD:61797};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6).
STRAIN=Sprague-Dawley;
PubMed=10686358; DOI=10.1016/S0169-328X(99)00286-7;
D'Agata V., Zhao W., Cavallaro S.;
"Cloning and distribution of the rat parkin mRNA.";
Brain Res. Mol. Brain Res. 75:345-349(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Hypothalamus;
PubMed=10737637; DOI=10.1046/j.1471-4159.2000.0741773.x;
Gu W.-J., Abbas N., Lagunes M.Z., Parent A., Pradier L., Bohme G.A.,
Agid Y., Hirsch E.C., Raisman-Vozari R., Brice A.;
"Cloning of rat parkin cDNA and distribution of parkin in rat brain.";
J. Neurochem. 74:1773-1776(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=Sprague-Dawley;
Hattori N., Wang M., Mizuno Y.;
"The expression of parkin mRNA in developing, adult and ageing rat
CNS.";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
STRAIN=Sprague-Dawley; TISSUE=Brain;
Soda M., Imai Y., Takahashi R.;
"Molecular cloning of rat Parkin gene.";
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[5]
INTERACTION WITH SUMO1.
PubMed=16955485; DOI=10.1002/jnr.21041;
Um J.W., Chung K.C.;
"Functional modulation of parkin through physical interaction with
SUMO-1.";
J. Neurosci. Res. 84:1543-1554(2006).
[6]
X-RAY CRYSTALLOGRAPHY (6.5 ANGSTROMS), X-RAY CRYSTALLOGRAPHY (2.8
ANGSTROMS) OF 141-465, RING-TYPE ZINC-FINGERS, CATALYTIC ACTIVITY,
ACTIVE SITE, AUTOUBIQUITINATION, ENZYME REGULATION, AND MUTAGENESIS OF
TRP-403.
PubMed=23661642; DOI=10.1126/science.1237908;
Trempe J.F., Sauve V., Grenier K., Seirafi M., Tang M.Y., Menade M.,
Al-Abdul-Wahid S., Krett J., Wong K., Kozlov G., Nagar B., Fon E.A.,
Gehring K.;
"Structure of parkin reveals mechanisms for ubiquitin ligase
activation.";
Science 340:1451-1455(2013).
-!- FUNCTION: 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. {ECO:0000250|UniProtKB:O60260}.
-!- CATALYTIC ACTIVITY: 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. {ECO:0000269|PubMed:23661642}.
-!- ENZYME REGULATION: 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 PRKN
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 PRKN 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.
{ECO:0000250|UniProtKB:O60260, ECO:0000269|PubMed:23661642}.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: 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 PRKN, 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 PRKN and GPR37, thus facilitating PRKN-
mediated GPR37 ubiquitination. HSP70 transiently associates with
unfolded GPR37 and inhibits the E3 activity of PRKN, whereas,
STUB1 enhances the E3 activity of PRKN through promotion of
dissociation of HSP70 from PRKN-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 PRKN transport into the mitochondria. Interacts
with MFN2 (phosphorylated), promotes PRKN 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 PRKN. Forms a complex with PINK1 and PARK7 (By
similarity). {ECO:0000250}.
-!- INTERACTION:
D4A054:Ranbp2; NbExp=2; IntAct=EBI-973793, EBI-973937;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Endoplasmic reticulum
{ECO:0000250}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:O60260}.
Cell projection, dendrite {ECO:0000250}. Cell junction, synapse,
postsynaptic cell membrane, postsynaptic density {ECO:0000250}.
Mitochondrion {ECO:0000250|UniProtKB:O60260}. Cell junction,
synapse {ECO:0000250}. 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). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=Q9JK66-1; Sequence=Displayed;
Name=2;
IsoId=Q9JK66-2; Sequence=VSP_011722, VSP_011723;
Name=3;
IsoId=Q9JK66-3; Sequence=VSP_011717;
Name=4;
IsoId=Q9JK66-4; Sequence=VSP_011718;
Name=5;
IsoId=Q9JK66-5; Sequence=VSP_011719;
Name=6;
IsoId=Q9JK66-6; Sequence=VSP_011717, VSP_011720, VSP_011721;
-!- TISSUE SPECIFICITY: 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.
{ECO:0000269|PubMed:10737637}.
-!- DOMAIN: The ubiquitin-like domain binds the PSMD4 subunit of 26S
proteasomes. {ECO:0000250}.
-!- DOMAIN: The RING-type 1 zinc finger domain is required to repress
p53/TP53 transcription. {ECO:0000250}.
-!- PTM: Auto-ubiquitinates in an E2-dependent manner leading to its
own degradation. {ECO:0000269|PubMed:23661642}.
-!- PTM: S-nitrosylated. {ECO:0000250}.
-!- PTM: Phosphorylation at Ser-65 by PINK1 contributes to activate
PRKN activity. It is however not sufficient and requires binding
to phosphorylated ubiquitin as well (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the RBR family. Parkin subfamily.
{ECO:0000305}.
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EMBL; AF343574; AAL73348.1; -; mRNA.
EMBL; AF381277; AAM21452.1; -; mRNA.
EMBL; AF381278; AAM21453.1; -; mRNA.
EMBL; AF381279; AAM21454.1; -; mRNA.
EMBL; AF381280; AAM21455.1; -; mRNA.
EMBL; AF381281; AAM21456.1; -; mRNA.
EMBL; AF168004; AAF34874.1; -; mRNA.
EMBL; AF210434; AAG37013.1; -; mRNA.
EMBL; AF257234; AAF68666.1; -; mRNA.
EMBL; AB039878; BAA92431.1; -; mRNA.
RefSeq; NP_064478.1; NM_020093.1.
UniGene; Rn.207194; -.
PDB; 2KNB; NMR; -; A=1-76.
PDB; 4K7D; X-ray; 2.80 A; A/B/C=141-465.
PDB; 4K95; X-ray; 6.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-465.
PDB; 4ZYN; X-ray; 2.54 A; A/B=1-465.
PDBsum; 2KNB; -.
PDBsum; 4K7D; -.
PDBsum; 4K95; -.
PDBsum; 4ZYN; -.
ProteinModelPortal; Q9JK66; -.
SMR; Q9JK66; -.
BioGrid; 248590; 13.
DIP; DIP-37656N; -.
IntAct; Q9JK66; 1.
MINT; MINT-220162; -.
STRING; 10116.ENSRNOP00000040511; -.
iPTMnet; Q9JK66; -.
PhosphoSitePlus; Q9JK66; -.
PaxDb; Q9JK66; -.
PRIDE; Q9JK66; -.
GeneID; 56816; -.
KEGG; rno:56816; -.
CTD; 5071; -.
RGD; 61797; Prkn.
eggNOG; KOG0006; Eukaryota.
eggNOG; ENOG410YG4B; LUCA.
HOVERGEN; HBG053682; -.
InParanoid; Q9JK66; -.
KO; K04556; -.
PhylomeDB; Q9JK66; -.
UniPathway; UPA00143; -.
EvolutionaryTrace; Q9JK66; -.
PRO; PR:Q9JK66; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016235; C:aggresome; ISS:ParkinsonsUK-UCL.
GO; GO:0030424; C:axon; IDA:RGD.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL.
GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
GO; GO:0000139; C:Golgi membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0005622; C:intracellular; IDA:RGD.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0043005; C:neuron projection; IDA:ParkinsonsUK-UCL.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0005634; C:nucleus; ISO:RGD.
GO; GO:1990452; C:Parkin-FBXW7-Cul1 ubiquitin ligase complex; ISS:ParkinsonsUK-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:ParkinsonsUK-UCL.
GO; GO:0014069; C:postsynaptic density; IDA:RGD.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
GO; GO:0043234; C:protein complex; ISO:RGD.
GO; GO:0045202; C:synapse; IDA:ParkinsonsUK-UCL.
GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
GO; GO:0030672; C:synaptic vesicle membrane; IDA:RGD.
GO; GO:0043195; C:terminal bouton; IDA:ParkinsonsUK-UCL.
GO; GO:0000151; C:ubiquitin ligase complex; ISS:ParkinsonsUK-UCL.
GO; GO:0003779; F:actin binding; ISO:RGD.
GO; GO:0008013; F:beta-catenin binding; ISO:RGD.
GO; GO:0051087; F:chaperone binding; ISO:RGD.
GO; GO:0097602; F:cullin family protein binding; ISS:ParkinsonsUK-UCL.
GO; GO:0019899; F:enzyme binding; ISO:RGD.
GO; GO:1990444; F:F-box domain binding; ISS:ParkinsonsUK-UCL.
GO; GO:0001664; F:G-protein coupled receptor binding; ISS:ParkinsonsUK-UCL.
GO; GO:0031072; F:heat shock protein binding; ISO:RGD.
GO; GO:0042826; F:histone deacetylase binding; ISO:RGD.
GO; GO:0030544; F:Hsp70 protein binding; ISO:RGD.
GO; GO:0042802; F:identical protein binding; ISS:ParkinsonsUK-UCL.
GO; GO:0019900; F:kinase binding; ISO:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0030165; F:PDZ domain binding; ISS:ParkinsonsUK-UCL.
GO; GO:0043274; F:phospholipase binding; ISO:RGD.
GO; GO:0032403; F:protein complex binding; IDA:RGD.
GO; GO:0019901; F:protein kinase binding; ISS:ParkinsonsUK-UCL.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; ISS:ParkinsonsUK-UCL.
GO; GO:0015631; F:tubulin binding; ISO:RGD.
GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
GO; GO:0031624; F:ubiquitin conjugating enzyme binding; ISS:ParkinsonsUK-UCL.
GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
GO; GO:1990381; F:ubiquitin-specific protease binding; ISO:RGD.
GO; GO:0008344; P:adult locomotory behavior; ISS:ParkinsonsUK-UCL.
GO; GO:0070842; P:aggresome assembly; ISS:ParkinsonsUK-UCL.
GO; GO:0000422; P:autophagy of mitochondrion; IDA:ParkinsonsUK-UCL.
GO; GO:0007420; P:brain development; IEP:RGD.
GO; GO:0044257; P:cellular protein catabolic process; ISO:RGD.
GO; GO:0006464; P:cellular protein modification process; TAS:RGD.
GO; GO:1905232; P:cellular response to L-glutamate; IDA:RGD.
GO; GO:1904845; P:cellular response to L-glutamine; IEP:RGD.
GO; GO:0071287; P:cellular response to manganese ion; IEP:RGD.
GO; GO:0097237; P:cellular response to toxic substance; ISS:ParkinsonsUK-UCL.
GO; GO:0042417; P:dopamine metabolic process; ISO:RGD.
GO; GO:0051583; P:dopamine uptake involved in synaptic transmission; ISO:RGD.
GO; GO:0010994; P:free ubiquitin chain polymerization; ISO:RGD.
GO; GO:0007612; P:learning; ISO:RGD.
GO; GO:0007626; P:locomotory behavior; ISO:RGD.
GO; GO:0000266; P:mitochondrial fission; ISS:ParkinsonsUK-UCL.
GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; IMP:RGD.
GO; GO:0051646; P:mitochondrion localization; IDA:ParkinsonsUK-UCL.
GO; GO:0007005; P:mitochondrion organization; ISS:ParkinsonsUK-UCL.
GO; GO:0099074; P:mitochondrion to lysosome transport; ISO:RGD.
GO; GO:0000423; P:mitophagy; ISO:RGD.
GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:RGD.
GO; GO:0044828; P:negative regulation by host of viral genome replication; ISO:RGD.
GO; GO:0032232; P:negative regulation of actin filament bundle assembly; ISO:RGD.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISO:RGD.
GO; GO:0060548; P:negative regulation of cell death; ISO:RGD.
GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; ISS:ParkinsonsUK-UCL.
GO; GO:1903382; P:negative regulation of endoplasmic reticulum stress-induced neuron intrinsic apoptotic signaling pathway; ISO:RGD.
GO; GO:0090394; P:negative regulation of excitatory postsynaptic potential; IMP:RGD.
GO; GO:1903542; P:negative regulation of exosomal secretion; ISO:RGD.
GO; GO:0010629; P:negative regulation of gene expression; ISO:RGD.
GO; GO:0033132; P:negative regulation of glucokinase activity; ISS:ParkinsonsUK-UCL.
GO; GO:0046676; P:negative regulation of insulin secretion; ISS:ParkinsonsUK-UCL.
GO; GO:1905366; P:negative regulation of intralumenal vesicle formation; ISO:RGD.
GO; GO:1902254; P:negative regulation of intrinsic apoptotic signaling pathway by p53 class mediator; ISO:RGD.
GO; GO:0046329; P:negative regulation of JNK cascade; ISS:ParkinsonsUK-UCL.
GO; GO:0090258; P:negative regulation of mitochondrial fission; IMP:RGD.
GO; GO:0010637; P:negative regulation of mitochondrial fusion; ISS:ParkinsonsUK-UCL.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IMP:RGD.
GO; GO:1901215; P:negative regulation of neuron death; IGI:MGI.
GO; GO:1903204; P:negative regulation of oxidative stress-induced neuron death; IGI:ParkinsonsUK-UCL.
GO; GO:1903377; P:negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; ISS:ParkinsonsUK-UCL.
GO; GO:1902283; P:negative regulation of primary amine oxidase activity; ISO:RGD.
GO; GO:0001933; P:negative regulation of protein phosphorylation; ISS:ParkinsonsUK-UCL.
GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; IMP:RGD.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; ISS:ParkinsonsUK-UCL.
GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISS:ParkinsonsUK-UCL.
GO; GO:1904049; P:negative regulation of spontaneous neurotransmitter secretion; ISO:RGD.
GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IMP:RGD.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISO:RGD.
GO; GO:0070050; P:neuron cellular homeostasis; ISS:ParkinsonsUK-UCL.
GO; GO:0042415; P:norepinephrine metabolic process; ISO:RGD.
GO; GO:0061734; P:parkin-mediated stimulation of mitophagy in response to mitochondrial depolarization; ISO:RGD.
GO; GO:2001171; P:positive regulation of ATP biosynthetic process; IMP:RGD.
GO; GO:1903599; P:positive regulation of autophagy of mitochondrion; ISO:RGD.
GO; GO:1903861; P:positive regulation of dendrite extension; ISO:RGD.
GO; GO:0043388; P:positive regulation of DNA binding; ISS:ParkinsonsUK-UCL.
GO; GO:0010628; P:positive regulation of gene expression; ISO:RGD.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:ParkinsonsUK-UCL.
GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; IMP:RGD.
GO; GO:0090141; P:positive regulation of mitochondrial fission; ISS:ParkinsonsUK-UCL.
GO; GO:0010636; P:positive regulation of mitochondrial fusion; ISS:ParkinsonsUK-UCL.
GO; GO:0010918; P:positive regulation of mitochondrial membrane potential; IMP:RGD.
GO; GO:0098779; P:positive regulation of mitophagy in response to mitochondrial depolarization; ISO:RGD.
GO; GO:0051582; P:positive regulation of neurotransmitter uptake; ISO:RGD.
GO; GO:1903378; P:positive regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; ISO:RGD.
GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; ISO:RGD.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:RGD.
GO; GO:0032092; P:positive regulation of protein binding; ISO:RGD.
GO; GO:1902530; P:positive regulation of protein linear polyubiquitination; ISO:RGD.
GO; GO:1905477; P:positive regulation of protein localization to membrane; ISO:RGD.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:ParkinsonsUK-UCL.
GO; GO:1903265; P:positive regulation of tumor necrosis factor-mediated signaling pathway; ISS:ParkinsonsUK-UCL.
GO; GO:0010498; P:proteasomal protein catabolic process; ISO:RGD.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:ParkinsonsUK-UCL.
GO; GO:0051865; P:protein autoubiquitination; ISS:ParkinsonsUK-UCL.
GO; GO:0031648; P:protein destabilization; ISO:RGD.
GO; GO:0070979; P:protein K11-linked ubiquitination; ISS:UniProtKB.
GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
GO; GO:0085020; P:protein K6-linked ubiquitination; ISS:UniProtKB.
GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:ParkinsonsUK-UCL.
GO; GO:0070585; P:protein localization to mitochondrion; IDA:ParkinsonsUK-UCL.
GO; GO:0019538; P:protein metabolic process; ISO:RGD.
GO; GO:0006513; P:protein monoubiquitination; ISS:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; ISS:ParkinsonsUK-UCL.
GO; GO:0050821; P:protein stabilization; ISO:RGD.
GO; GO:0016567; P:protein ubiquitination; IDA:ParkinsonsUK-UCL.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; ISS:ParkinsonsUK-UCL.
GO; GO:0010506; P:regulation of autophagy; ISS:UniProtKB.
GO; GO:1900407; P:regulation of cellular response to oxidative stress; ISS:ParkinsonsUK-UCL.
GO; GO:0042053; P:regulation of dopamine metabolic process; ISO:RGD.
GO; GO:0010468; P:regulation of gene expression; IMP:RGD.
GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISO:RGD.
GO; GO:0010821; P:regulation of mitochondrion organization; ISS:ParkinsonsUK-UCL.
GO; GO:0046928; P:regulation of neurotransmitter secretion; ISO:RGD.
GO; GO:0031647; P:regulation of protein stability; ISO:RGD.
GO; GO:0031396; P:regulation of protein ubiquitination; ISO:RGD.
GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; ISO:RGD.
GO; GO:0051412; P:response to corticosterone; IEP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0034976; P:response to endoplasmic reticulum stress; IEP:RGD.
GO; GO:0014850; P:response to muscle activity; IEP:RGD.
GO; GO:0006979; P:response to oxidative stress; ISS:ParkinsonsUK-UCL.
GO; GO:0006986; P:response to unfolded protein; IDA:RGD.
GO; GO:0001964; P:startle response; ISO:RGD.
GO; GO:0001963; P:synaptic transmission, dopaminergic; ISO:RGD.
GO; GO:0035249; P:synaptic transmission, glutamatergic; ISO:RGD.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:RGD.
GO; GO:0055069; P:zinc ion homeostasis; ISS:ParkinsonsUK-UCL.
InterPro; IPR031127; E3_UB_ligase_RBR.
InterPro; IPR002867; IBR_dom.
InterPro; IPR003977; Parkin.
InterPro; IPR029071; Ubiquitin-like_domsf.
InterPro; IPR000626; Ubiquitin_dom.
PANTHER; PTHR11685; PTHR11685; 1.
Pfam; PF01485; IBR; 2.
Pfam; PF00240; ubiquitin; 1.
PIRSF; PIRSF037880; Parkin; 1.
PRINTS; PR01475; PARKIN.
SMART; SM00647; IBR; 2.
SMART; SM00213; UBQ; 1.
SUPFAM; SSF54236; SSF54236; 1.
PROSITE; PS50053; UBIQUITIN_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Autophagy; Cell junction;
Cell membrane; Cell projection; Complete proteome; Cytoplasm;
Endoplasmic reticulum; Membrane; Metal-binding; Mitochondrion;
Nucleus; Phosphoprotein; Postsynaptic cell membrane;
Reference proteome; Repeat; Synapse; Transcription;
Transcription regulation; Transferase; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 465 E3 ubiquitin-protein ligase parkin.
/FTId=PRO_0000058578.
DOMAIN 1 76 Ubiquitin-like. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
ZN_FING 141 225 RING-type 0; atypical.
ZN_FING 238 293 RING-type 1; atypical.
ZN_FING 313 377 IBR-type.
ZN_FING 418 449 RING-type 2.
REGION 204 238 SYT11 binding 1.
{ECO:0000250|UniProtKB:O60260}.
REGION 257 293 SYT11 binding 2.
{ECO:0000250|UniProtKB:O60260}.
REGION 378 410 REP.
ACT_SITE 431 431 {ECO:0000269|PubMed:23661642}.
MOD_RES 65 65 Phosphoserine; by PINK1.
{ECO:0000250|UniProtKB:O60260}.
MOD_RES 80 80 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9WVS6}.
VAR_SEQ 1 191 Missing (in isoform 3 and isoform 6).
{ECO:0000303|PubMed:10686358}.
/FTId=VSP_011717.
VAR_SEQ 57 57 Q -> QHPQDGFCHKSHLAVHNLSQQDVTQ (in
isoform 4).
{ECO:0000303|PubMed:10686358}.
/FTId=VSP_011718.
VAR_SEQ 179 206 Missing (in isoform 5).
{ECO:0000303|PubMed:10686358}.
/FTId=VSP_011719.
VAR_SEQ 390 394 AYRVD -> EDVCT (in isoform 6).
{ECO:0000303|PubMed:10686358}.
/FTId=VSP_011720.
VAR_SEQ 395 465 Missing (in isoform 6).
{ECO:0000303|PubMed:10686358}.
/FTId=VSP_011721.
VAR_SEQ 429 446 GGCMHMKCPQPQCKLEWC -> ERMHVQYTMCIPGAHGGY
(in isoform 2).
{ECO:0000303|PubMed:10686358}.
/FTId=VSP_011722.
VAR_SEQ 447 465 Missing (in isoform 2).
{ECO:0000303|PubMed:10686358}.
/FTId=VSP_011723.
MUTAGEN 403 403 W->A: Increased autoubiquitination.
{ECO:0000269|PubMed:23661642}.
CONFLICT 24 24 F -> C (in Ref. 1; AAF34874).
{ECO:0000305}.
CONFLICT 138 138 E -> A (in Ref. 3; BAA92431).
{ECO:0000305}.
CONFLICT 348 348 K -> R (in Ref. 3; BAA92431).
{ECO:0000305}.
STRAND 2 11 {ECO:0000244|PDB:4ZYN}.
STRAND 13 16 {ECO:0000244|PDB:4ZYN}.
HELIX 23 34 {ECO:0000244|PDB:4ZYN}.
HELIX 38 40 {ECO:0000244|PDB:4ZYN}.
STRAND 41 45 {ECO:0000244|PDB:4ZYN}.
STRAND 48 50 {ECO:0000244|PDB:4ZYN}.
HELIX 56 59 {ECO:0000244|PDB:4ZYN}.
STRAND 65 71 {ECO:0000244|PDB:4ZYN}.
STRAND 147 150 {ECO:0000244|PDB:4ZYN}.
TURN 151 154 {ECO:0000244|PDB:4ZYN}.
STRAND 156 166 {ECO:0000244|PDB:4ZYN}.
TURN 167 170 {ECO:0000244|PDB:4ZYN}.
STRAND 174 178 {ECO:0000244|PDB:4K7D}.
HELIX 183 187 {ECO:0000244|PDB:4ZYN}.
STRAND 193 196 {ECO:0000244|PDB:4K7D}.
STRAND 205 215 {ECO:0000244|PDB:4ZYN}.
STRAND 223 225 {ECO:0000244|PDB:4ZYN}.
TURN 239 241 {ECO:0000244|PDB:4ZYN}.
STRAND 246 250 {ECO:0000244|PDB:4ZYN}.
STRAND 253 255 {ECO:0000244|PDB:4K7D}.
STRAND 257 260 {ECO:0000244|PDB:4ZYN}.
HELIX 261 274 {ECO:0000244|PDB:4ZYN}.
STRAND 278 280 {ECO:0000244|PDB:4ZYN}.
TURN 281 283 {ECO:0000244|PDB:4ZYN}.
STRAND 284 286 {ECO:0000244|PDB:4ZYN}.
HELIX 301 307 {ECO:0000244|PDB:4ZYN}.
HELIX 309 316 {ECO:0000244|PDB:4ZYN}.
HELIX 318 326 {ECO:0000244|PDB:4ZYN}.
TURN 335 337 {ECO:0000244|PDB:4K7D}.
STRAND 348 350 {ECO:0000244|PDB:4ZYN}.
HELIX 355 357 {ECO:0000244|PDB:4K7D}.
STRAND 363 365 {ECO:0000244|PDB:4K7D}.
STRAND 366 368 {ECO:0000244|PDB:4ZYN}.
HELIX 395 400 {ECO:0000244|PDB:4ZYN}.
STRAND 401 403 {ECO:0000244|PDB:4K7D}.
STRAND 415 417 {ECO:0000244|PDB:4ZYN}.
TURN 419 421 {ECO:0000244|PDB:4ZYN}.
STRAND 424 426 {ECO:0000244|PDB:4ZYN}.
STRAND 429 431 {ECO:0000244|PDB:4K7D}.
STRAND 433 435 {ECO:0000244|PDB:4K7D}.
TURN 439 441 {ECO:0000244|PDB:4ZYN}.
STRAND 444 446 {ECO:0000244|PDB:4K7D}.
TURN 447 449 {ECO:0000244|PDB:4ZYN}.
HELIX 455 461 {ECO:0000244|PDB:4ZYN}.
SEQUENCE 465 AA; 51709 MW; E13CF170AD6D042B CRC64;
MIVFVRFNSS YGFPVEVDSD TSIFQLKEVV AKRQGVPADQ LRVIFAGKEL QNHLTVQNCD
LEQQSIVHIV QRPQRKSHET NASGGDKPQS TPEGSIWEPR SLTRVDLSSH ILPADSVGLA
VILDTDSKSD SEAARGPEAK PTYHSFFVYC KGPCHKVQPG KLRVQCGTCR QATLTLAQGP
SCWDDVLIPN RMSGECQSPD CPGTRAEFFF KCGAHPTSDK DTSVALNLIT NNSRSIPCIA
CTDVRNPVLV FQCNHRHVIC LDCFHLYCVT RLNDRQFVHD AQLGYSLPCV AGCPNSLIKE
LHHFRILGEE QYNRYQQYGA EECVLQMGGV LCPRPGCGAG LLPEQGQKKV TCEGGNGLGC
GFVFCRDCKE AYHEGECDSM FEASGATSQA YRVDQRAAEQ ARWEEASKET IKKTTKPCPR
CNVPIEKNGG CMHMKCPQPQ CKLEWCWNCG CEWNRACMGD HWFDV


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