PTEN induced kinase 1

mammalian protein found in Homo sapiens

Protein protein Q21112306

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PTEN induced kinase 1

Summary

PTEN induced kinase 1 is a protein^[1].

Key Facts

PTEN induced kinase 1's instance of is recorded as protein^[2].
PTEN induced kinase 1's UniProt protein ID is recorded as Q9BXM7^[3].
PTEN induced kinase 1's RefSeq protein ID is recorded as NP_115785^[4].
PTEN induced kinase 1's molecular function is recorded as C3HC4-type RING finger domain binding^[5].
PTEN induced kinase 1's molecular function is recorded as kinase activity^[6].
PTEN induced kinase 1's molecular function is recorded as ATP binding^[7].
PTEN induced kinase 1's molecular function is recorded as protein kinase activity^[8].
PTEN induced kinase 1's molecular function is recorded as metal ion binding^[9].
PTEN induced kinase 1's molecular function is recorded as protein serine/threonine kinase activity^[10].
PTEN induced kinase 1's molecular function is recorded as calcium-dependent protein kinase activity^[11].
PTEN induced kinase 1's molecular function is recorded as peptidase activator activity^[12].
PTEN induced kinase 1's molecular function is recorded as magnesium ion binding^[13].
PTEN induced kinase 1's molecular function is recorded as transferase activity^[14].
PTEN induced kinase 1's molecular function is recorded as protease binding^[15].
PTEN induced kinase 1's molecular function is recorded as protein binding^[16].
PTEN induced kinase 1's molecular function is recorded as nucleotide binding^[17].
PTEN induced kinase 1's molecular function is recorded as protein kinase B binding^[18].
PTEN induced kinase 1's molecular function is recorded as ubiquitin protein ligase binding^[19].
PTEN induced kinase 1's cell component is recorded as cytoplasm^[20].
PTEN induced kinase 1's cell component is recorded as cytosol^[21].
PTEN induced kinase 1's cell component is recorded as membrane^[22].
PTEN induced kinase 1's cell component is recorded as mitochondrial intermembrane space^[23].
PTEN induced kinase 1's cell component is recorded as mitochondrion^[24].
PTEN induced kinase 1's cell component is recorded as perinuclear region of cytoplasm^[25].
PTEN induced kinase 1's cell component is recorded as cytoskeleton^[26].

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Quick Facts

Instance of protein

Properties

Biological process negative regulation of neuron apoptotic process, positive regulation of mitophagy in response to mitochondrial depolarization, positive regulation of free ubiquitin chain polymerization, regulation of protein ubiquitination, cellular response to toxic substance, positive regulation of catecholamine secretion, regulation of synaptic vesicle transport, positive regulation of translation, protein phosphorylation, positive regulation of dopamine secretion, macroautophagy, regulation of protein-containing complex assembly, cellular response to hypoxia, negative regulation of autophagosome assembly, positive regulation of protein kinase B signaling, positive regulation of protein dephosphorylation, ubiquitin-dependent protein catabolic process, peptidyl-serine autophosphorylation, regulation of neuron apoptotic process, response to oxidative stress, negative regulation of gene expression, positive regulation of peptidyl-serine phosphorylation, negative regulation of mitochondrial fission, positive regulation of mitochondrial electron transport, NADH to ubiquinone, positive regulation of macroautophagy, regulation of autophagy of mitochondrion, positive regulation of ubiquitin-protein transferase activity, negative regulation of hydrogen peroxide-induced neuron intrinsic apoptotic signaling pathway, protein ubiquitination, negative regulation of oxidative stress-induced cell death, negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide, positive regulation of synaptic transmission, dopaminergic, negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway, regulation of oxidative phosphorylation, regulation of mitochondrion organization, regulation of hydrogen peroxide metabolic process, negative regulation of oxidative stress-induced neuron death, protein stabilization, mitochondrion organization, positive regulation of DNA-binding transcription factor activity, negative regulation of autophagy of mitochondrion, regulation of reactive oxygen species metabolic process, positive regulation of ATP biosynthetic process, maintenance of protein location in mitochondrion, regulation of protein targeting to mitochondrion, positive regulation of release of cytochrome c from mitochondria, respiratory electron transport chain, positive regulation of protein ubiquitination, regulation of proteasomal protein catabolic process, activation of protein kinase B activity, intracellular signal transduction, negative regulation of macroautophagy, positive regulation of protein targeting to mitochondrion, positive regulation of cristae formation, positive regulation of peptidase activity, TORC2 signaling, regulation of mitochondrial membrane potential, autophagy, negative regulation of JNK cascade, establishment of protein localization to mitochondrion, autophagy of mitochondrion, peptidyl-serine phosphorylation, positive regulation of I-kappaB kinase/NF-kappaB signaling, cellular response to oxidative stress, negative regulation of reactive oxygen species metabolic process, negative regulation of apoptotic process, positive regulation of protein phosphorylation, positive regulation of histone deacetylase activity, mitochondrion to lysosome transport, regulation of cellular response to oxidative stress, response to ischemia, positive regulation of mitochondrial fission, positive regulation of autophagy of mitochondrion in response to mitochondrial depolarization, cellular response to hydrogen sulfide, phosphorylation, negative regulation of neuron death, positive regulation of NMDA glutamate receptor activity, negative regulation of intrinsic apoptotic signaling pathway

Cell component cytoplasm, cytosol, membrane, mitochondrial intermembrane space, mitochondrion, perinuclear region of cytoplasm, cytoskeleton, nucleus, Lewy body, integral component of mitochondrial outer membrane, mitochondrial outer membrane, chromatin, TORC2 complex, integral component of membrane, ubiquitin ligase complex, mitochondrial outer membrane translocase complex, astrocyte projection, axon, cell body, mitochondrial inner membrane, growth cone

Encoded by PINK1

Found in taxon Homo sapiens

Imported from wholeness_audit_2026-05-02

Molecular function C3HC4-type RING finger domain binding, kinase activity, ATP binding, protein kinase activity, metal ion binding, protein serine/threonine kinase activity, calcium-dependent protein kinase activity, peptidase activator activity, magnesium ion binding, transferase activity, protease binding, protein binding, nucleotide binding, protein kinase B binding, ubiquitin protein ligase binding

External References (3)

Ensembl protein id ENSP00000364204

Refseq protein id NP_115785

Uniprot protein id Q9BXM7

References

Programmatic citations — every numbered marker resolves to a verifiable graph row below.

Direct Wikidata claims

[2] ↑ PTEN induced kinase 1 — instance of (P31): protein. Q905695. Retrieved 2019-11-13. wikidata.org.
[3] ↑ PTEN induced kinase 1 — UniProt protein ID (P352): Q9BXM7. Q905695. Retrieved 2019-11-13. wikidata.org.
[4] ↑ PTEN induced kinase 1 — RefSeq protein ID (P637): NP_115785. Q20641742. Retrieved 2020-05-30. wikidata.org.
[5] ↑ PTEN induced kinase 1 — molecular function (P680): C3HC4-type RING finger domain binding. Phosphorylation of parkin by Parkinson disease-linked kinase PINK1 activates parkin E3 ligase function and NF-kappaB signaling. Retrieved 2018-02-27. ebi.ac.uk. Provenance: wikidata.org.
[6] ↑ PTEN induced kinase 1 — molecular function (P680): kinase activity. Synaptic vesicle trafficking and Parkinson's disease. Retrieved 2018-02-27. ebi.ac.uk. Provenance: wikidata.org.
[7] ↑ PTEN induced kinase 1 — molecular function (P680): ATP binding. GOA. Retrieved 2018-02-27. ebi.ac.uk. Provenance: wikidata.org.
[8] ↑ PTEN induced kinase 1 — molecular function (P680): protein kinase activity. PINK1 kinase catalytic activity is regulated by phosphorylation on serines 228 and 402. Retrieved 2018-02-27. ebi.ac.uk. Provenance: wikidata.org.
[9] ↑ PTEN induced kinase 1 — molecular function (P680): metal ion binding. GOA. Retrieved 2018-02-27. ebi.ac.uk. Provenance: wikidata.org.
[10] ↑ PTEN induced kinase 1 — molecular function (P680): protein serine/threonine kinase activity. Oxidative Stress-Induced Signaling Pathways Implicated in the Pathogenesis of Parkinson’s Disease. Retrieved 2018-02-27. ebi.ac.uk. Provenance: wikidata.org.
[11] ↑ PTEN induced kinase 1 — molecular function (P680): calcium-dependent protein kinase activity. Phosphorylation of parkin by Parkinson disease-linked kinase PINK1 activates parkin E3 ligase function and NF-kappaB signaling. Retrieved 2018-02-27. ebi.ac.uk. Provenance: wikidata.org.
[12] ↑ PTEN induced kinase 1 — molecular function (P680): peptidase activator activity. Oxidative Stress-Induced Signaling Pathways Implicated in the Pathogenesis of Parkinson’s Disease. Retrieved 2018-02-27. ebi.ac.uk. Provenance: wikidata.org.
[13] ↑ PTEN induced kinase 1 — molecular function (P680): magnesium ion binding. GOA. Retrieved 2018-02-27. ebi.ac.uk. Provenance: wikidata.org.
[14] ↑ PTEN induced kinase 1 — molecular function (P680): transferase activity. GOA. Retrieved 2018-02-27. ebi.ac.uk. Provenance: wikidata.org.
[15] ↑ PTEN induced kinase 1 — molecular function (P680): protease binding. Oxidative Stress-Induced Signaling Pathways Implicated in the Pathogenesis of Parkinson’s Disease. Retrieved 2018-02-27. ebi.ac.uk. Provenance: wikidata.org.
[16] ↑ PTEN induced kinase 1 — molecular function (P680): protein binding. Parkin, PINK1, and DJ-1 form a ubiquitin E3 ligase complex promoting unfolded protein degradation. Retrieved 2018-02-27. ebi.ac.uk. Provenance: wikidata.org.
[17] ↑ PTEN induced kinase 1 — molecular function (P680): nucleotide binding. GOA. Retrieved 2018-02-27. ebi.ac.uk. Provenance: wikidata.org.
[18] ↑ PTEN induced kinase 1 — molecular function (P680): protein kinase B binding. A new cytosolic pathway from a Parkinson disease-associated kinase, BRPK/PINK1: activation of AKT via mTORC2. Retrieved 2018-02-27. ebi.ac.uk. Provenance: wikidata.org.
[19] ↑ PTEN induced kinase 1 — molecular function (P680): ubiquitin protein ligase binding. The PINK1/Parkin-mediated mitophagy is compromised by PD-associated mutations. Retrieved 2018-02-27. ebi.ac.uk. Provenance: wikidata.org.
[20] ↑ PTEN induced kinase 1 — cell component (P681): cytoplasm. GOA. Retrieved 2018-02-27. ebi.ac.uk. Provenance: wikidata.org.
[21] ↑ PTEN induced kinase 1 — cell component (P681): cytosol. GOA. Retrieved 2018-02-27. ebi.ac.uk. Provenance: wikidata.org.
[22] ↑ PTEN induced kinase 1 — cell component (P681): membrane. GOA. Retrieved 2018-02-27. ebi.ac.uk. Provenance: wikidata.org.
[23] ↑ PTEN induced kinase 1 — cell component (P681): mitochondrial intermembrane space. GOA. Retrieved 2018-02-27. ebi.ac.uk. Provenance: wikidata.org.
[24] ↑ PTEN induced kinase 1 — cell component (P681): mitochondrion. Mitochondrial impairment increases FL-PINK1 levels by calcium-dependent gene expression. Retrieved 2018-02-27. ebi.ac.uk. Provenance: wikidata.org.
[25] ↑ PTEN induced kinase 1 — cell component (P681): perinuclear region of cytoplasm. PINK1 protein in normal human brain and Parkinson's disease. Retrieved 2018-02-27. ebi.ac.uk. Provenance: wikidata.org.
[26] ↑ PTEN induced kinase 1 — cell component (P681): cytoskeleton. PARK13 regulates PINK1 and subcellular relocation patterns under oxidative stress in neurons. Retrieved 2018-02-27. ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

[1] ↑ PTEN induced kinase 1 is an instance of protein (Q8054) [P31, primary]. Wikidata. wikidata.org.

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BibTeX

@misc{4ortxyz_pten-induced-kinase-1_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{PTEN induced kinase 1}}, year = {2026}, url = {https://4ort.xyz/entity/pten-induced-kinase-1}, note = {Accessed: 2026-05-03}}

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