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P36776

- LONM_HUMAN

UniProt

P36776 - LONM_HUMAN

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Protein

Lon protease homolog, mitochondrial

Gene

LONP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial promoters and RNA in a single-stranded, site-specific, and strand-specific manner. May regulate mitochondrial DNA replication and/or gene expression using site-specific, single-stranded DNA binding to target the degradation of regulatory proteins binding to adjacent sites in mitochondrial promoters. Endogenous substrates include mitochondrial steroidogenic acute regulatory (StAR) protein.4 PublicationsUniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei855 – 8551UniRule annotation
Active sitei898 – 8981UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi523 – 5308ATPUniRule annotation

GO - Molecular functioni

  1. ADP binding Source: UniProtKB
  2. ATP binding Source: UniProtKB
  3. ATP-dependent peptidase activity Source: UniProtKB
  4. DNA polymerase binding Source: UniProtKB
  5. G-quadruplex DNA binding Source: UniProtKB
  6. mitochondrial heavy strand promoter anti-sense binding Source: UniProtKB
  7. mitochondrial light strand promoter anti-sense binding Source: UniProtKB
  8. sequence-specific DNA binding Source: UniProtKB
  9. serine-type endopeptidase activity Source: UniProtKB-HAMAP
  10. single-stranded DNA binding Source: Ensembl
  11. single-stranded RNA binding Source: UniProtKB

GO - Biological processi

  1. aging Source: Ensembl
  2. cellular response to oxidative stress Source: UniProtKB
  3. chaperone-mediated protein complex assembly Source: UniProtKB-HAMAP
  4. misfolded or incompletely synthesized protein catabolic process Source: UniProtKB-HAMAP
  5. mitochondrial DNA metabolic process Source: UniProtKB
  6. mitochondrial genome maintenance Source: UniProtKB
  7. mitochondrion organization Source: UniProtKB
  8. oxidation-dependent protein catabolic process Source: UniProtKB
  9. protein homooligomerization Source: UniProtKB
  10. proteolysis involved in cellular protein catabolic process Source: UniProtKB
  11. regulation of mitochondrial DNA replication Source: UniProtKB-HAMAP
  12. response to aluminum ion Source: Ensembl
  13. response to hormone Source: Ensembl
  14. response to hypoxia Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.4.21.53. 2681.

Protein family/group databases

MEROPSiS16.002.

Names & Taxonomyi

Protein namesi
Recommended name:
Lon protease homolog, mitochondrialUniRule annotation (EC:3.4.21.-UniRule annotation)
Alternative name(s):
LONHs
Lon protease-like proteinUniRule annotation
Short name:
LONPUniRule annotation
Mitochondrial ATP-dependent protease LonUniRule annotation
Serine protease 15UniRule annotation
Gene namesi
Name:LONP1UniRule annotation
Synonyms:PRSS15
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:9479. LONP1.

Subcellular locationi

Mitochondrion matrix 1 PublicationUniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. membrane Source: UniProtKB
  3. mitochondrial matrix Source: UniProtKB
  4. mitochondrial nucleoid Source: BHF-UCL
  5. mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi855 – 8551S → A: Lacks both ATPase and protease activity, but retains DNA binding activity. 1 Publication

Organism-specific databases

PharmGKBiPA162394145.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6767MitochondrionUniRule annotationAdd
BLAST
Chaini68 – 959892Lon protease homolog, mitochondrialPRO_0000026734Add
BLAST

Proteomic databases

MaxQBiP36776.
PaxDbiP36776.
PRIDEiP36776.

PTM databases

PhosphoSiteiP36776.

Expressioni

Tissue specificityi

Duodenum, heart, lung and liver, but not thymus.

Gene expression databases

BgeeiP36776.
CleanExiHS_LONP1.
ExpressionAtlasiP36776. baseline and differential.
GenevestigatoriP36776.

Organism-specific databases

HPAiHPA002034.
HPA002192.

Interactioni

Subunit structurei

Homohexamer or homoheptamer. Organized in a ring with a central cavity. DNA and RNA binding is stimulated by substrate and inhibited by ATP binding. Interacts with PEO1 and mitochondrial DNA polymerase subunit POLG.2 PublicationsUniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
CSN2P026666EBI-357448,EBI-5260183From a different organism.

Protein-protein interaction databases

BioGridi114762. 33 interactions.
IntActiP36776. 21 interactions.
MINTiMINT-3014242.
STRINGi9606.ENSP00000353826.

Structurei

Secondary structure

1
959
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi764 – 78623Combined sources
Beta strandi799 – 8046Combined sources
Helixi808 – 82821Combined sources
Helixi834 – 8374Combined sources
Beta strandi839 – 8435Combined sources
Turni850 – 8523Combined sources
Helixi853 – 8564Combined sources
Helixi857 – 86913Combined sources
Beta strandi877 – 8793Combined sources
Beta strandi887 – 8904Combined sources
Helixi895 – 90410Combined sources
Beta strandi909 – 9135Combined sources
Helixi914 – 9163Combined sources
Helixi917 – 9215Combined sources
Helixi925 – 9284Combined sources
Beta strandi932 – 9387Combined sources
Helixi939 – 9468Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2X36X-ray2.00A/B/C/D/E/F753-959[»]
ProteinModelPortaliP36776.
SMRiP36776. Positions 288-408, 419-953.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP36776.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini124 – 368245LonUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S16 family.UniRule annotation
Contains 1 Lon domain.UniRule annotation

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0466.
GeneTreeiENSGT00530000063553.
HOGENOMiHOG000261409.
HOVERGENiHBG000798.
InParanoidiP36776.
KOiK08675.
OMAiQTLPWRA.
OrthoDBiEOG7HQN7C.
PhylomeDBiP36776.
TreeFamiTF105001.

Family and domain databases

Gene3Di3.30.230.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_03120. lonm_euk.
InterProiIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR004815. Lon_bac/euk-typ.
IPR027065. Lon_Prtase.
IPR027503. Lonm_euk.
IPR027417. P-loop_NTPase.
IPR008269. Pept_S16_C.
IPR003111. Pept_S16_N.
IPR008268. Peptidase_S16_AS.
IPR015947. PUA-like_domain.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view]
PANTHERiPTHR10046. PTHR10046. 1 hit.
PfamiPF00004. AAA. 1 hit.
PF02190. LON. 1 hit.
PF05362. Lon_C. 1 hit.
[Graphical view]
PIRSFiPIRSF001174. Lon_proteas. 1 hit.
SMARTiSM00382. AAA. 1 hit.
SM00464. LON. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsiTIGR00763. lon. 1 hit.
PROSITEiPS01046. LON_SER. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P36776-1) [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

        10         20         30         40         50
MAASTGYVRL WGAARCWVLR RPMLAAAGGR VPTAAGAWLL RGQRTCDASP
60 70 80 90 100
PWALWGRGPA IGGQWRGFWE ASSRGGGAFS GGEDASEGGA EEGAGGAGGS
110 120 130 140 150
AGAGEGPVIT ALTPMTIPDV FPHLPLIAIT RNPVFPRFIK IIEVKNKKLV
160 170 180 190 200
ELLRRKVRLA QPYVGVFLKR DDSNESDVVE SLDEIYHTGT FAQIHEMQDL
210 220 230 240 250
GDKLRMIVMG HRRVHISRQL EVEPEEPEAE NKHKPRRKSK RGKKEAEDEL
260 270 280 290 300
SARHPAELAM EPTPELPAEV LMVEVENVVH EDFQVTEEVK ALTAEIVKTI
310 320 330 340 350
RDIIALNPLY RESVLQMMQA GQRVVDNPIY LSDMGAALTG AESHELQDVL
360 370 380 390 400
EETNIPKRLY KALSLLKKEF ELSKLQQRLG REVEEKIKQT HRKYLLQEQL
410 420 430 440 450
KIIKKELGLE KDDKDAIEEK FRERLKELVV PKHVMDVVDE ELSKLGLLDN
460 470 480 490 500
HSSEFNVTRN YLDWLTSIPW GKYSNENLDL ARAQAVLEED HYGMEDVKKR
510 520 530 540 550
ILEFIAVSQL RGSTQGKILC FYGPPGVGKT SIARSIARAL NREYFRFSVG
560 570 580 590 600
GMTDVAEIKG HRRTYVGAMP GKIIQCLKKT KTENPLILID EVDKIGRGYQ
610 620 630 640 650
GDPSSALLEL LDPEQNANFL DHYLDVPVDL SKVLFICTAN VTDTIPEPLR
660 670 680 690 700
DRMEMINVSG YVAQEKLAIA ERYLVPQARA LCGLDESKAK LSSDVLTLLI
710 720 730 740 750
KQYCRESGVR NLQKQVEKVL RKSAYKIVSG EAESVEVTPE NLQDFVGKPV
760 770 780 790 800
FTVERMYDVT PPGVVMGLAW TAMGGSTLFV ETSLRRPQDK DAKGDKDGSL
810 820 830 840 850
EVTGQLGEVM KESARIAYTF ARAFLMQHAP ANDYLVTSHI HLHVPEGATP
860 870 880 890 900
KDGPSAGCTI VTALLSLAMG RPVRQNLAMT GEVSLTGKIL PVGGIKEKTI
910 920 930 940 950
AAKRAGVTCI VLPAENKKDF YDLAAFITEG LEVHFVEHYR EIFDIAFPDE

QAEALAVER
Length:959
Mass (Da):106,489
Last modified:December 1, 2000 - v2
Checksum:iB5E03D9C27C220FF
GO
Isoform 2 (identifier: P36776-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     42-105: Missing.

Note: No experimental confirmation available.

Show »
Length:895
Mass (Da):100,397
Checksum:iEF213C4E36C69AE1
GO
Isoform 3 (identifier: P36776-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-196: Missing.

Note: No experimental confirmation available.

Show »
Length:763
Mass (Da):85,642
Checksum:i3FEBB8DEEA651D7A
GO

Sequence cautioni

The sequence CAA52291.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 5555MAAST…PWALW → MAGLWRRALATCDCGERRGA GCCGGRCWPRRGAGSHCSRS VVAPRPADLRRLSSLGTV in AAA61616. (PubMed:8248235)CuratedAdd
BLAST
Sequence conflicti65 – 662WR → CG in AAA61616. (PubMed:8248235)Curated
Sequence conflicti257 – 2582EL → DV in AAA61616. (PubMed:8248235)Curated
Sequence conflicti423 – 4231E → G in BAG51690. (PubMed:14702039)Curated
Sequence conflicti456 – 4561N → D in AAA61616. (PubMed:8248235)Curated
Sequence conflicti501 – 5011I → V in BAG51690. (PubMed:14702039)Curated
Sequence conflicti556 – 5561A → T in AAA61616. (PubMed:8248235)Curated
Sequence conflicti842 – 8421L → P in AAA61616. (PubMed:8248235)Curated
Sequence conflicti859 – 8591T → A in AAA61616. (PubMed:8248235)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti87 – 871E → D.
Corresponds to variant rs34413649 [ dbSNP | Ensembl ].
VAR_051564
Natural varianti241 – 2411R → Q.
Corresponds to variant rs11085147 [ dbSNP | Ensembl ].
VAR_051565
Natural varianti829 – 8291A → T.
Corresponds to variant rs35804229 [ dbSNP | Ensembl ].
VAR_067708
Natural varianti911 – 9111V → I.2 Publications
Corresponds to variant rs1062373 [ dbSNP | Ensembl ].
VAR_067709

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 196196Missing in isoform 3. 1 PublicationVSP_055310Add
BLAST
Alternative sequencei42 – 10564Missing in isoform 2. 1 PublicationVSP_054617Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U02389 mRNA. Translation: AAA61616.1.
HQ204946 Genomic DNA. Translation: ADP90374.1.
HQ204947 Genomic DNA. Translation: ADP90375.1.
HQ204948 Genomic DNA. Translation: ADP90376.1.
HQ204949 Genomic DNA. Translation: ADP90377.1.
HQ204950 Genomic DNA. Translation: ADP90378.1.
HQ204951 Genomic DNA. Translation: ADP90379.1.
HQ204952 Genomic DNA. Translation: ADP90380.1.
HQ204953 Genomic DNA. Translation: ADP90381.1.
HQ204954 Genomic DNA. Translation: ADP90382.1.
HQ204955 Genomic DNA. Translation: ADP90383.1.
HQ204956 Genomic DNA. Translation: ADP90384.1.
HQ204957 Genomic DNA. Translation: ADP90385.1.
HQ204958 Genomic DNA. Translation: ADP90386.1.
HQ204959 Genomic DNA. Translation: ADP90387.1.
HQ204960 Genomic DNA. Translation: ADP90388.1.
HQ204961 Genomic DNA. Translation: ADP90389.1.
HQ204962 Genomic DNA. Translation: ADP90390.1.
HQ204963 Genomic DNA. Translation: ADP90391.1.
HQ204964 Genomic DNA. Translation: ADP90392.1.
HQ204965 Genomic DNA. Translation: ADP90393.1.
HQ204966 Genomic DNA. Translation: ADP90394.1.
HQ204968 Genomic DNA. Translation: ADP90396.1.
HQ204969 Genomic DNA. Translation: ADP90397.1.
HQ204970 Genomic DNA. Translation: ADP90398.1.
HQ204971 Genomic DNA. Translation: ADP90399.1.
HQ204972 Genomic DNA. Translation: ADP90400.1.
HQ204973 Genomic DNA. Translation: ADP90401.1.
HQ204974 Genomic DNA. Translation: ADP90402.1.
HQ204975 Genomic DNA. Translation: ADP90403.1.
HQ204976 Genomic DNA. Translation: ADP90404.1.
HQ204977 Genomic DNA. Translation: ADP90405.1.
HQ204978 Genomic DNA. Translation: ADP90406.1.
HQ204979 Genomic DNA. Translation: ADP90407.1.
HQ204980 Genomic DNA. Translation: ADP90408.1.
HQ204981 Genomic DNA. Translation: ADP90409.1.
HQ204982 Genomic DNA. Translation: ADP90410.1.
HQ204983 Genomic DNA. Translation: ADP90411.1.
HQ204984 Genomic DNA. Translation: ADP90412.1.
HQ204985 Genomic DNA. Translation: ADP90413.1.
AF059309
, AF059296, AF059297, AF059298, AF059299, AF059300, AF059301, AF059302, AF059303, AF059304, AF059305, AF059306, AF059307, AF059308 Genomic DNA. Translation: AAD24414.1.
AK056366 mRNA. Translation: BAG51690.1.
AK096626 mRNA. Translation: BAC04829.1.
AC011499 Genomic DNA. No translation available.
CH471139 Genomic DNA. Translation: EAW69151.1.
CH471139 Genomic DNA. Translation: EAW69154.1.
BC000235 mRNA. Translation: AAH00235.1.
X74215 mRNA. Translation: CAA52291.1. Different initiation.
X76040 mRNA. Translation: CAA53625.1.
CCDSiCCDS12148.1. [P36776-1]
CCDS62507.1. [P36776-3]
CCDS62508.1. [P36776-2]
PIRiS42366.
S57342.
RefSeqiNP_001263408.1. NM_001276479.1. [P36776-2]
NP_001263409.1. NM_001276480.1. [P36776-3]
NP_004784.2. NM_004793.3. [P36776-1]
UniGeneiHs.350265.

Genome annotation databases

EnsembliENST00000360614; ENSP00000353826; ENSG00000196365. [P36776-1]
ENST00000540670; ENSP00000441523; ENSG00000196365. [P36776-3]
ENST00000593119; ENSP00000468541; ENSG00000196365. [P36776-2]
GeneIDi9361.
KEGGihsa:9361.
UCSCiuc002mcx.4. human. [P36776-1]
uc002mcy.3. human.

Polymorphism databases

DMDMi12644239.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U02389 mRNA. Translation: AAA61616.1 .
HQ204946 Genomic DNA. Translation: ADP90374.1 .
HQ204947 Genomic DNA. Translation: ADP90375.1 .
HQ204948 Genomic DNA. Translation: ADP90376.1 .
HQ204949 Genomic DNA. Translation: ADP90377.1 .
HQ204950 Genomic DNA. Translation: ADP90378.1 .
HQ204951 Genomic DNA. Translation: ADP90379.1 .
HQ204952 Genomic DNA. Translation: ADP90380.1 .
HQ204953 Genomic DNA. Translation: ADP90381.1 .
HQ204954 Genomic DNA. Translation: ADP90382.1 .
HQ204955 Genomic DNA. Translation: ADP90383.1 .
HQ204956 Genomic DNA. Translation: ADP90384.1 .
HQ204957 Genomic DNA. Translation: ADP90385.1 .
HQ204958 Genomic DNA. Translation: ADP90386.1 .
HQ204959 Genomic DNA. Translation: ADP90387.1 .
HQ204960 Genomic DNA. Translation: ADP90388.1 .
HQ204961 Genomic DNA. Translation: ADP90389.1 .
HQ204962 Genomic DNA. Translation: ADP90390.1 .
HQ204963 Genomic DNA. Translation: ADP90391.1 .
HQ204964 Genomic DNA. Translation: ADP90392.1 .
HQ204965 Genomic DNA. Translation: ADP90393.1 .
HQ204966 Genomic DNA. Translation: ADP90394.1 .
HQ204968 Genomic DNA. Translation: ADP90396.1 .
HQ204969 Genomic DNA. Translation: ADP90397.1 .
HQ204970 Genomic DNA. Translation: ADP90398.1 .
HQ204971 Genomic DNA. Translation: ADP90399.1 .
HQ204972 Genomic DNA. Translation: ADP90400.1 .
HQ204973 Genomic DNA. Translation: ADP90401.1 .
HQ204974 Genomic DNA. Translation: ADP90402.1 .
HQ204975 Genomic DNA. Translation: ADP90403.1 .
HQ204976 Genomic DNA. Translation: ADP90404.1 .
HQ204977 Genomic DNA. Translation: ADP90405.1 .
HQ204978 Genomic DNA. Translation: ADP90406.1 .
HQ204979 Genomic DNA. Translation: ADP90407.1 .
HQ204980 Genomic DNA. Translation: ADP90408.1 .
HQ204981 Genomic DNA. Translation: ADP90409.1 .
HQ204982 Genomic DNA. Translation: ADP90410.1 .
HQ204983 Genomic DNA. Translation: ADP90411.1 .
HQ204984 Genomic DNA. Translation: ADP90412.1 .
HQ204985 Genomic DNA. Translation: ADP90413.1 .
AF059309
, AF059296 , AF059297 , AF059298 , AF059299 , AF059300 , AF059301 , AF059302 , AF059303 , AF059304 , AF059305 , AF059306 , AF059307 , AF059308 Genomic DNA. Translation: AAD24414.1 .
AK056366 mRNA. Translation: BAG51690.1 .
AK096626 mRNA. Translation: BAC04829.1 .
AC011499 Genomic DNA. No translation available.
CH471139 Genomic DNA. Translation: EAW69151.1 .
CH471139 Genomic DNA. Translation: EAW69154.1 .
BC000235 mRNA. Translation: AAH00235.1 .
X74215 mRNA. Translation: CAA52291.1 . Different initiation.
X76040 mRNA. Translation: CAA53625.1 .
CCDSi CCDS12148.1. [P36776-1 ]
CCDS62507.1. [P36776-3 ]
CCDS62508.1. [P36776-2 ]
PIRi S42366.
S57342.
RefSeqi NP_001263408.1. NM_001276479.1. [P36776-2 ]
NP_001263409.1. NM_001276480.1. [P36776-3 ]
NP_004784.2. NM_004793.3. [P36776-1 ]
UniGenei Hs.350265.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2X36 X-ray 2.00 A/B/C/D/E/F 753-959 [» ]
ProteinModelPortali P36776.
SMRi P36776. Positions 288-408, 419-953.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114762. 33 interactions.
IntActi P36776. 21 interactions.
MINTi MINT-3014242.
STRINGi 9606.ENSP00000353826.

Protein family/group databases

MEROPSi S16.002.

PTM databases

PhosphoSitei P36776.

Polymorphism databases

DMDMi 12644239.

Proteomic databases

MaxQBi P36776.
PaxDbi P36776.
PRIDEi P36776.

Protocols and materials databases

DNASUi 9361.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000360614 ; ENSP00000353826 ; ENSG00000196365 . [P36776-1 ]
ENST00000540670 ; ENSP00000441523 ; ENSG00000196365 . [P36776-3 ]
ENST00000593119 ; ENSP00000468541 ; ENSG00000196365 . [P36776-2 ]
GeneIDi 9361.
KEGGi hsa:9361.
UCSCi uc002mcx.4. human. [P36776-1 ]
uc002mcy.3. human.

Organism-specific databases

CTDi 9361.
GeneCardsi GC19M005691.
HGNCi HGNC:9479. LONP1.
HPAi HPA002034.
HPA002192.
MIMi 605490. gene.
neXtProti NX_P36776.
PharmGKBi PA162394145.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0466.
GeneTreei ENSGT00530000063553.
HOGENOMi HOG000261409.
HOVERGENi HBG000798.
InParanoidi P36776.
KOi K08675.
OMAi QTLPWRA.
OrthoDBi EOG7HQN7C.
PhylomeDBi P36776.
TreeFami TF105001.

Enzyme and pathway databases

BRENDAi 3.4.21.53. 2681.

Miscellaneous databases

ChiTaRSi LONP1. human.
EvolutionaryTracei P36776.
GeneWikii LONP1.
GenomeRNAii 9361.
NextBioi 35055.
PROi P36776.
SOURCEi Search...

Gene expression databases

Bgeei P36776.
CleanExi HS_LONP1.
ExpressionAtlasi P36776. baseline and differential.
Genevestigatori P36776.

Family and domain databases

Gene3Di 3.30.230.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPi MF_03120. lonm_euk.
InterProi IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR004815. Lon_bac/euk-typ.
IPR027065. Lon_Prtase.
IPR027503. Lonm_euk.
IPR027417. P-loop_NTPase.
IPR008269. Pept_S16_C.
IPR003111. Pept_S16_N.
IPR008268. Peptidase_S16_AS.
IPR015947. PUA-like_domain.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
[Graphical view ]
PANTHERi PTHR10046. PTHR10046. 1 hit.
Pfami PF00004. AAA. 1 hit.
PF02190. LON. 1 hit.
PF05362. Lon_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF001174. Lon_proteas. 1 hit.
SMARTi SM00382. AAA. 1 hit.
SM00464. LON. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
SSF54211. SSF54211. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsi TIGR00763. lon. 1 hit.
PROSITEi PS01046. LON_SER. 1 hit.
[Graphical view ]
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Publicationsi

« Hide 'large scale' publications
  1. "A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease."
    Wang N., Gottesman S., Willingham M.C., Gottesman M.M., Maurizi M.R.
    Proc. Natl. Acad. Sci. U.S.A. 90:11247-11251(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
    Tissue: Brain.
  2. "Identification of rare DNA variants in mitochondrial disorders with improved array-based sequencing."
    Wang W., Shen P., Thiyagarajan S., Lin S., Palm C., Horvath R., Klopstock T., Cutler D., Pique L., Schrijver I., Davis R.W., Mindrinos M., Speed T.P., Scharfe C.
    Nucleic Acids Res. 39:44-58(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-911.
  3. "Chromosomal mapping and genomic organization of the ATP-dependent human LON protease gene."
    Huang N.N., Maurizi M.R., Torres R.R., Polymeropoulos M.H., Lennon G.G., Gottesman M.M.
    Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Tissue: Brain.
  5. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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).
    Tissue: Eye.
  8. "Cloning and sequence analysis of cDNA for a human homolog of eubacterial ATP-dependent Lon proteases."
    Amerik A.Y., Petukhova G.V., Grigorenko V.G., Lykov I.P., Yarovoi S.V., Lipkin V.M., Gorbalenya A.E.
    FEBS Lett. 340:25-28(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-959 (ISOFORM 1), VARIANT ILE-911.
    Tissue: Brain.
  9. "Synthesis, processing, and localization of human Lon protease."
    Wang N., Maurizi M.R., Emmert-Buck L., Gottesman M.M.
    J. Biol. Chem. 269:29308-29313(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  10. "The human LON protease binds to mitochondrial promoters in a single-stranded, site-specific, strand-specific manner."
    Fu G.K., Markovitz D.M.
    Biochemistry 37:1905-1909(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING.
  11. "Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism."
    Bota D.A., Davies K.J.
    Nat. Cell Biol. 4:674-680(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "DNA and RNA binding by the mitochondrial lon protease is regulated by nucleotide and protein substrate."
    Liu T., Lu B., Lee I., Ondrovicova G., Kutejova E., Suzuki C.K.
    J. Biol. Chem. 279:13902-13910(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING, MUTAGENESIS OF SER-855, SUBUNIT, INTERACTION WITH PEO1 AND POLG.
  13. "Cleavage site selection within a folded substrate by the ATP-dependent lon protease."
    Ondrovicova G., Liu T., Singh K., Tian B., Li H., Gakh O., Perecko D., Janata J., Granot Z., Orly J., Kutejova E., Suzuki C.K.
    J. Biol. Chem. 280:25103-25110(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Roles for the human ATP-dependent Lon protease in mitochondrial DNA maintenance."
    Lu B., Yadav S., Shah P.G., Liu T., Tian B., Pukszta S., Villaluna N., Kutejova E., Newlon C.S., Santos J.H., Suzuki C.K.
    J. Biol. Chem. 282:17363-17374(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING.
  15. "Turnover of mitochondrial steroidogenic acute regulatory (StAR) protein by Lon protease: the unexpected effect of proteasome inhibitors."
    Granot Z., Kobiler O., Melamed-Book N., Eimerl S., Bahat A., Lu B., Braun S., Maurizi M.R., Suzuki C.K., Oppenheim A.B., Orly J.
    Mol. Endocrinol. 21:2164-2177(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBSTRATE.
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Structure of the catalytic domain of the human mitochondrial Lon protease: proposed relation of oligomer formation and activity."
    Garcia-Nafria J., Ondrovicova G., Blagova E., Levdikov V.M., Bauer J.A., Suzuki C.K., Kutejova E., Wilkinson A.J., Wilson K.S.
    Protein Sci. 19:987-999(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 753-959, SUBUNIT.

Entry informationi

Entry nameiLONM_HUMAN
AccessioniPrimary (citable) accession number: P36776
Secondary accession number(s): B3KPH8
, D6W635, E5KMH8, F5GZ27, P36777, Q8N8K8, Q9UQ95
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: December 1, 2000
Last modified: November 26, 2014
This is version 147 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3