LONP1 | ENSG00000196365 | NCBI 9361

Details for: LONP1

Gene ID: 9361

Symbol: LONP1

Ensembl ID: ENSG00000196365

Description: lon peptidase 1, mitochondrial

Associated with

Metabolism of proteins
(R-HSA-392499)
Mitochondrial protein degradation
(R-HSA-9837999)
Adp binding
(GO:0043531)
Atp-dependent peptidase activity
(GO:0004176)
Atp binding
(GO:0005524)
Atp hydrolysis activity
(GO:0016887)
Cellular response to oxidative stress
(GO:0034599)
Chaperone-mediated protein complex assembly
(GO:0051131)
Cytosol
(GO:0005829)
Dna polymerase binding
(GO:0070182)
G-quadruplex dna binding
(GO:0051880)
Identical protein binding
(GO:0042802)
Insulin receptor substrate binding
(GO:0043560)
Membrane
(GO:0016020)
Mitochondrial dna metabolic process
(GO:0032042)
Mitochondrial genome maintenance
(GO:0000002)
Mitochondrial matrix
(GO:0005759)
Mitochondrial nucleoid
(GO:0042645)
Mitochondrial promoter sequence-specific dna binding
(GO:0001018)
Mitochondrion
(GO:0005739)
Mitochondrion organization
(GO:0007005)
Negative regulation of insulin receptor signaling pathway
(GO:0046627)
Nucleoplasm
(GO:0005654)
Oxidation-dependent protein catabolic process
(GO:0070407)
Ph domain binding
(GO:0042731)
Protein binding
(GO:0005515)
Protein catabolic process
(GO:0030163)
Protein quality control for misfolded or incompletely synthesized proteins
(GO:0006515)
Proteolysis involved in protein catabolic process
(GO:0051603)
Regulation of peptidyl-tyrosine phosphorylation
(GO:0050730)
Response to aluminum ion
(GO:0010044)
Response to hormone
(GO:0009725)
Response to hypoxia
(GO:0001666)
Sequence-specific dna binding
(GO:0043565)
Serine-type endopeptidase activity
(GO:0004252)
Single-stranded dna binding
(GO:0003697)
Single-stranded rna binding
(GO:0003727)

Other Information

Proteins

LONHs

Genular Protein ID: 3385982149

Symbol: LONM_HUMAN

Name: LONHs

UniProtKB Accession Codes:

P36776 B3KPH8 D6W635 E5KMH8 F5GZ27 P36777 Q8N8K8 Q9UQ95

Database IDs:

Citations:

PubMed ID: 8248235

Title: A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease.

PubMed ID: 8248235

DOI: 10.1073/pnas.90.23.11247

PubMed ID: 20843780

Title: Identification of rare DNA variants in mitochondrial disorders with improved array-based sequencing.

PubMed ID: 20843780

DOI: 10.1093/nar/gkq750

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15057824

Title: The DNA sequence and biology of human chromosome 19.

PubMed ID: 15057824

DOI: 10.1038/nature02399

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 8119403

Title: Cloning and sequence analysis of cDNA for a human homolog of eubacterial ATP-dependent Lon proteases.

PubMed ID: 8119403

DOI: 10.1016/0014-5793(94)80166-5

PubMed ID: 7961901

Title: Synthesis, processing, and localization of human Lon protease.

PubMed ID: 7961901

DOI: 10.1016/s0021-9258(19)62045-4

PubMed ID: 9485316

Title: The human LON protease binds to mitochondrial promoters in a single-stranded, site-specific, strand-specific manner.

PubMed ID: 9485316

DOI: 10.1021/bi970928c

PubMed ID: 12198491

Title: Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism.

PubMed ID: 12198491

DOI: 10.1038/ncb836

PubMed ID: 14739292

Title: DNA and RNA binding by the mitochondrial lon protease is regulated by nucleotide and protein substrate.

PubMed ID: 14739292

DOI: 10.1074/jbc.m309642200

PubMed ID: 15870080

Title: Cleavage site selection within a folded substrate by the ATP-dependent lon protease.

PubMed ID: 15870080

DOI: 10.1074/jbc.m502796200

PubMed ID: 17420247

Title: Roles for the human ATP-dependent Lon protease in mitochondrial DNA maintenance.

PubMed ID: 17420247

DOI: 10.1074/jbc.m611540200

PubMed ID: 17579211

Title: Turnover of mitochondrial steroidogenic acute regulatory (StAR) protein by Lon protease: the unexpected effect of proteasome inhibitors.

PubMed ID: 17579211

DOI: 10.1210/me.2005-0458

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24520911

Title: Mutations to a glycine loop in the catalytic site of human Lon changes its protease, peptidase and ATPase activities.

PubMed ID: 24520911

DOI: 10.1111/febs.12740

PubMed ID: 25369343

Title: Three-dimensional reconstruction of the S885A mutant of human mitochondrial Lon protease.

PubMed ID: 25369343

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25574826

Title: CODAS syndrome is associated with mutations of LONP1, encoding mitochondrial AAA+ Lon protease.

PubMed ID: 25574826

DOI: 10.1016/j.ajhg.2014.12.003

PubMed ID: 25808063

Title: Mutations in LONP1, a mitochondrial matrix protease, cause CODAS syndrome.

PubMed ID: 25808063

DOI: 10.1002/ajmg.a.37029

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 28377575

Title: The role of Lon-mediated proteolysis in the dynamics of mitochondrial nucleic acid-protein complexes.

PubMed ID: 28377575

DOI: 10.1038/s41598-017-00632-8

PubMed ID: 37327776

Title: A mitochondrial iron-responsive pathway regulated by DELE1.

PubMed ID: 37327776

DOI: 10.1016/j.molcel.2023.05.031

PubMed ID: 20222013

Title: Structure of the catalytic domain of the human mitochondrial Lon protease: proposed relation of oligomer formation and activity.

PubMed ID: 20222013

DOI: 10.1002/pro.376

PubMed ID: 27632940

Title: The N-terminal domain plays a crucial role in the structure of a full-length human mitochondrial Lon protease.

PubMed ID: 27632940

DOI: 10.1038/srep33631

Sequence Information:

Length: 959
Mass: 106489
Checksum: B5E03D9C27C220FF
Sequence:

MAASTGYVRL WGAARCWVLR RPMLAAAGGR VPTAAGAWLL RGQRTCDASP PWALWGRGPA 
IGGQWRGFWE ASSRGGGAFS GGEDASEGGA EEGAGGAGGS AGAGEGPVIT ALTPMTIPDV 
FPHLPLIAIT RNPVFPRFIK IIEVKNKKLV ELLRRKVRLA QPYVGVFLKR DDSNESDVVE 
SLDEIYHTGT FAQIHEMQDL GDKLRMIVMG HRRVHISRQL EVEPEEPEAE NKHKPRRKSK 
RGKKEAEDEL SARHPAELAM EPTPELPAEV LMVEVENVVH EDFQVTEEVK ALTAEIVKTI 
RDIIALNPLY RESVLQMMQA GQRVVDNPIY LSDMGAALTG AESHELQDVL EETNIPKRLY 
KALSLLKKEF ELSKLQQRLG REVEEKIKQT HRKYLLQEQL KIIKKELGLE KDDKDAIEEK 
FRERLKELVV PKHVMDVVDE ELSKLGLLDN HSSEFNVTRN YLDWLTSIPW GKYSNENLDL 
ARAQAVLEED HYGMEDVKKR ILEFIAVSQL RGSTQGKILC FYGPPGVGKT SIARSIARAL 
NREYFRFSVG GMTDVAEIKG HRRTYVGAMP GKIIQCLKKT KTENPLILID EVDKIGRGYQ 
GDPSSALLEL LDPEQNANFL DHYLDVPVDL SKVLFICTAN VTDTIPEPLR DRMEMINVSG 
YVAQEKLAIA ERYLVPQARA LCGLDESKAK LSSDVLTLLI KQYCRESGVR NLQKQVEKVL 
RKSAYKIVSG EAESVEVTPE NLQDFVGKPV FTVERMYDVT PPGVVMGLAW TAMGGSTLFV 
ETSLRRPQDK DAKGDKDGSL EVTGQLGEVM KESARIAYTF ARAFLMQHAP ANDYLVTSHI 
HLHVPEGATP KDGPSAGCTI VTALLSLAMG RPVRQNLAMT GEVSLTGKIL PVGGIKEKTI 
AAKRAGVTCI VLPAENKKDF YDLAAFITEG LEVHFVEHYR EIFDIAFPDE QAEALAVER

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: LONP1

Associated with

Other Information

A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease. PubMed ID: 8248235

Identification of rare DNA variants in mitochondrial disorders with improved array-based sequencing. PubMed ID: 20843780

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

The DNA sequence and biology of human chromosome 19. PubMed ID: 15057824

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Cloning and sequence analysis of cDNA for a human homolog of eubacterial ATP-dependent Lon proteases. PubMed ID: 8119403

Synthesis, processing, and localization of human Lon protease. PubMed ID: 7961901

The human LON protease binds to mitochondrial promoters in a single-stranded, site-specific, strand-specific manner. PubMed ID: 9485316

Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism. PubMed ID: 12198491

DNA and RNA binding by the mitochondrial lon protease is regulated by nucleotide and protein substrate. PubMed ID: 14739292

Cleavage site selection within a folded substrate by the ATP-dependent lon protease. PubMed ID: 15870080

Roles for the human ATP-dependent Lon protease in mitochondrial DNA maintenance. PubMed ID: 17420247

Turnover of mitochondrial steroidogenic acute regulatory (StAR) protein by Lon protease: the unexpected effect of proteasome inhibitors. PubMed ID: 17579211

Initial characterization of the human central proteome. PubMed ID: 21269460

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

Mutations to a glycine loop in the catalytic site of human Lon changes its protease, peptidase and ATPase activities. PubMed ID: 24520911

Three-dimensional reconstruction of the S885A mutant of human mitochondrial Lon protease. PubMed ID: 25369343

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

CODAS syndrome is associated with mutations of LONP1, encoding mitochondrial AAA+ Lon protease. PubMed ID: 25574826

Mutations in LONP1, a mitochondrial matrix protease, cause CODAS syndrome. PubMed ID: 25808063

N-terminome analysis of the human mitochondrial proteome. PubMed ID: 25944712

The role of Lon-mediated proteolysis in the dynamics of mitochondrial nucleic acid-protein complexes. PubMed ID: 28377575

A mitochondrial iron-responsive pathway regulated by DELE1. PubMed ID: 37327776

Structure of the catalytic domain of the human mitochondrial Lon protease: proposed relation of oligomer formation and activity. PubMed ID: 20222013

The N-terminal domain plays a crucial role in the structure of a full-length human mitochondrial Lon protease. PubMed ID: 27632940