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P36776

- LONM_HUMAN

UniProt

P36776 - LONM_HUMAN

Protein

Lon protease homolog, mitochondrial

Gene

LONP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (01 Dec 2000)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    9. sequence-specific DNA binding Source: UniProtKB
    10. serine-type endopeptidase activity Source: UniProtKB-HAMAP
    11. single-stranded DNA binding Source: Ensembl
    12. 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

    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

    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

    ArrayExpressiP36776.
    BgeeiP36776.
    CleanExiHS_LONP1.
    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. 29 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 – 78623
    Beta strandi799 – 8046
    Helixi808 – 82821
    Helixi834 – 8374
    Beta strandi839 – 8435
    Turni850 – 8523
    Helixi853 – 8564
    Helixi857 – 86913
    Beta strandi877 – 8793
    Beta strandi887 – 8904
    Helixi895 – 90410
    Beta strandi909 – 9135
    Helixi914 – 9163
    Helixi917 – 9215
    Helixi925 – 9284
    Beta strandi932 – 9387
    Helixi939 – 9468

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MAASTGYVRL WGAARCWVLR RPMLAAAGGR VPTAAGAWLL RGQRTCDASP    50
    PWALWGRGPA IGGQWRGFWE ASSRGGGAFS GGEDASEGGA EEGAGGAGGS 100
    AGAGEGPVIT ALTPMTIPDV FPHLPLIAIT RNPVFPRFIK IIEVKNKKLV 150
    ELLRRKVRLA QPYVGVFLKR DDSNESDVVE SLDEIYHTGT FAQIHEMQDL 200
    GDKLRMIVMG HRRVHISRQL EVEPEEPEAE NKHKPRRKSK RGKKEAEDEL 250
    SARHPAELAM EPTPELPAEV LMVEVENVVH EDFQVTEEVK ALTAEIVKTI 300
    RDIIALNPLY RESVLQMMQA GQRVVDNPIY LSDMGAALTG AESHELQDVL 350
    EETNIPKRLY KALSLLKKEF ELSKLQQRLG REVEEKIKQT HRKYLLQEQL 400
    KIIKKELGLE KDDKDAIEEK FRERLKELVV PKHVMDVVDE ELSKLGLLDN 450
    HSSEFNVTRN YLDWLTSIPW GKYSNENLDL ARAQAVLEED HYGMEDVKKR 500
    ILEFIAVSQL RGSTQGKILC FYGPPGVGKT SIARSIARAL NREYFRFSVG 550
    GMTDVAEIKG HRRTYVGAMP GKIIQCLKKT KTENPLILID EVDKIGRGYQ 600
    GDPSSALLEL LDPEQNANFL DHYLDVPVDL SKVLFICTAN VTDTIPEPLR 650
    DRMEMINVSG YVAQEKLAIA ERYLVPQARA LCGLDESKAK LSSDVLTLLI 700
    KQYCRESGVR NLQKQVEKVL RKSAYKIVSG EAESVEVTPE NLQDFVGKPV 750
    FTVERMYDVT PPGVVMGLAW TAMGGSTLFV ETSLRRPQDK DAKGDKDGSL 800
    EVTGQLGEVM KESARIAYTF ARAFLMQHAP ANDYLVTSHI HLHVPEGATP 850
    KDGPSAGCTI VTALLSLAMG RPVRQNLAMT GEVSLTGKIL PVGGIKEKTI 900
    AAKRAGVTCI VLPAENKKDF YDLAAFITEG LEVHFVEHYR EIFDIAFPDE 950
    QAEALAVER 959
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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.
    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]

    Polymorphism databases

    DMDMi12644239.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    NP_004784.2. NM_004793.3. [P36776-1 ]
    UniGenei Hs.350265.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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. 29 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 ]

    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.
    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

    ArrayExpressi P36776.
    Bgeei P36776.
    CleanExi HS_LONP1.
    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 ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 145 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