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Q86WA8

- LONP2_HUMAN

UniProt

Q86WA8 - LONP2_HUMAN

Protein

Lon protease homolog 2, peroxisomal

Gene

LONP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    Functioni

    ATP-dependent serine protease that mediates the selective degradation of misfolded and unassembled polypeptides in the peroxisomal matrix. Necessary for type 2 peroxisome targeting signal (PTS2)-containing protein processing and facilitates peroxisome matrix protein import By similarity. May indirectly regulate peroxisomal fatty acid beta-oxidation through degradation of the self-processed forms of TYSND1.1 PublicationUniRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei743 – 7431UniRule annotation
    Active sitei786 – 7861UniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi375 – 3828ATPUniRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-HAMAP
    2. ATP-dependent peptidase activity Source: RefGenome
    3. enzyme binding Source: UniProtKB
    4. peptidase activity Source: UniProtKB
    5. protease binding Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. receptor binding Source: UniProtKB
    8. serine-type endopeptidase activity Source: UniProtKB-HAMAP

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. misfolded or incompletely synthesized protein catabolic process Source: RefGenome
    3. peroxisome organization Source: UniProtKB
    4. protein import into peroxisome matrix Source: UniProtKB-HAMAP
    5. protein processing Source: UniProtKB
    6. protein targeting to peroxisome Source: UniProtKB
    7. regulation of fatty acid beta-oxidation Source: UniProtKB
    8. response to organic cyclic compound Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Protease, Serine protease

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_16907. Association of TriC/CCT with target proteins during biosynthesis.

    Protein family/group databases

    MEROPSiS16.006.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lon protease homolog 2, peroxisomalUniRule annotation (EC:3.4.21.-UniRule annotation)
    Alternative name(s):
    Lon protease-like protein 2UniRule annotation
    Short name:
    Lon protease 2UniRule annotation
    Peroxisomal Lon proteaseUniRule annotation
    Gene namesi
    Name:LONP2UniRule annotation
    Synonyms:LONP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:20598. LONP2.

    Subcellular locationi

    Peroxisome matrix 2 PublicationsUniRule annotation

    GO - Cellular componenti

    1. membrane Source: UniProtKB
    2. nucleus Source: Ensembl
    3. peroxisomal matrix Source: RefGenome
    4. peroxisome Source: UniProtKB

    Keywords - Cellular componenti

    Peroxisome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi743 – 7431S → A: Reduces degradation of self-processed forms of TYSND1. 1 Publication

    Organism-specific databases

    PharmGKBiPA162394186.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 852851Lon protease homolog 2, peroxisomalPRO_0000287640Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ86WA8.
    PaxDbiQ86WA8.
    PRIDEiQ86WA8.

    PTM databases

    PhosphoSiteiQ86WA8.

    Expressioni

    Gene expression databases

    ArrayExpressiQ86WA8.
    BgeeiQ86WA8.
    CleanExiHS_LONP2.
    GenevestigatoriQ86WA8.

    Organism-specific databases

    HPAiHPA008862.

    Interactioni

    Subunit structurei

    Interacts with PEX5. Interacts with TYSND1.1 PublicationUniRule annotation

    Protein-protein interaction databases

    BioGridi123755. 5 interactions.
    IntActiQ86WA8. 5 interactions.
    STRINGi9606.ENSP00000285737.

    Structurei

    3D structure databases

    ProteinModelPortaliQ86WA8.
    SMRiQ86WA8. Positions 269-835.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini13 – 219207LonUniRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi850 – 8523Microbody targeting signalUniRule annotation

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0466.
    HOGENOMiHOG000261408.
    HOVERGENiHBG000798.
    InParanoidiQ86WA8.
    KOiK01338.
    OMAiDQREYFL.
    OrthoDBiEOG77T13V.
    PhylomeDBiQ86WA8.
    TreeFamiTF317215.

    Family and domain databases

    Gene3Di3.30.230.10. 1 hit.
    3.40.50.300. 1 hit.
    HAMAPiMF_03121. lonp2_euk.
    InterProiIPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR004815. Lon_bac/euk-typ.
    IPR027065. Lon_Prtase.
    IPR027501. Lonp2_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.
    [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 (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q86WA8-1) [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

    MSSVSPIQIP SRLPLLLTHE GVLLPGSTMR TSVDSARNLQ LVRSRLLKGT    50
    SLQSTILGVI PNTPDPASDA QDLPPLHRIG TAALAVQVVG SNWPKPHYTL 100
    LITGLCRFQI VQVLKEKPYP IAEVEQLDRL EEFPNTCKMR EELGELSEQF 150
    YKYAVQLVEM LDMSVPAVAK LRRLLDSLPR EALPDILTSI IRTSNKEKLQ 200
    ILDAVSLEER FKMTIPLLVR QIEGLKLLQK TRKPKQDDDK RVIAIRPIRR 250
    ITHISGTLED EDEDEDNDDI VMLEKKIRTS SMPEQAHKVC VKEIKRLKKM 300
    PQSMPEYALT RNYLELMVEL PWNKSTTDRL DIRAARILLD NDHYAMEKLK 350
    KRVLEYLAVR QLKNNLKGPI LCFVGPPGVG KTSVGRSVAK TLGREFHRIA 400
    LGGVCDQSDI RGHRRTYVGS MPGRIINGLK TVGVNNPVFL LDEVDKLGKS 450
    LQGDPAAALL EVLDPEQNHN FTDHYLNVAF DLSQVLFIAT ANTTATIPAA 500
    LLDRMEIIQV PGYTQEEKIE IAHRHLIPKQ LEQHGLTPQQ IQIPQVTTLD 550
    IITRYTREAG VRSLDRKLGA ICRAVAVKVA EGQHKEAKLD RSDVTEREGC 600
    REHILEDEKP ESISDTTDLA LPPEMPILID FHALKDILGP PMYEMEVSQR 650
    LSQPGVAIGL AWTPLGGEIM FVEASRMDGE GQLTLTGQLG DVMKESAHLA 700
    ISWLRSNAKK YQLTNAFGSF DLLDNTDIHL HFPAGAVTKD GPSAGVTIVT 750
    CLASLFSGRL VRSDVAMTGE ITLRGLVLPV GGIKDKVLAA HRAGLKQVII 800
    PRRNEKDLEG IPGNVRQDLS FVTASCLDEV LNAAFDGGFT VKTRPGLLNS 850
    KL 852
    Length:852
    Mass (Da):94,617
    Last modified:June 1, 2003 - v1
    Checksum:i00444E4FF47417AC
    GO
    Isoform 2 (identifier: Q86WA8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         156-199: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:808
    Mass (Da):89,660
    Checksum:iA3BF87CB9C823DA1
    GO

    Sequence cautioni

    The sequence BAB55278.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti255 – 2551S → A in AAI10435. (PubMed:15489334)Curated
    Sequence conflicti628 – 6281L → F in BAC11201. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei156 – 19944Missing in isoform 2. 1 PublicationVSP_056190Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ548761 mRNA. Translation: CAD68987.1.
    AK027666 mRNA. Translation: BAB55278.1. Different initiation.
    AK074775 mRNA. Translation: BAC11201.1.
    AC007600 Genomic DNA. No translation available.
    AC023818 Genomic DNA. No translation available.
    BC093910 mRNA. Translation: AAH93910.1.
    BC093912 mRNA. Translation: AAH93912.1.
    BC110434 mRNA. Translation: AAI10435.1.
    BC143246 mRNA. Translation: AAI43247.1.
    AL834201 mRNA. Translation: CAD38889.1.
    CCDSiCCDS10734.1.
    RefSeqiNP_113678.2. NM_031490.2.
    XP_005256248.1. XM_005256191.1.
    UniGeneiHs.731827.

    Genome annotation databases

    EnsembliENST00000285737; ENSP00000285737; ENSG00000102910.
    ENST00000535754; ENSP00000445426; ENSG00000102910.
    GeneIDi83752.
    KEGGihsa:83752.
    UCSCiuc002efi.1. human.

    Polymorphism databases

    DMDMi74727668.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ548761 mRNA. Translation: CAD68987.1 .
    AK027666 mRNA. Translation: BAB55278.1 . Different initiation.
    AK074775 mRNA. Translation: BAC11201.1 .
    AC007600 Genomic DNA. No translation available.
    AC023818 Genomic DNA. No translation available.
    BC093910 mRNA. Translation: AAH93910.1 .
    BC093912 mRNA. Translation: AAH93912.1 .
    BC110434 mRNA. Translation: AAI10435.1 .
    BC143246 mRNA. Translation: AAI43247.1 .
    AL834201 mRNA. Translation: CAD38889.1 .
    CCDSi CCDS10734.1.
    RefSeqi NP_113678.2. NM_031490.2.
    XP_005256248.1. XM_005256191.1.
    UniGenei Hs.731827.

    3D structure databases

    ProteinModelPortali Q86WA8.
    SMRi Q86WA8. Positions 269-835.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123755. 5 interactions.
    IntActi Q86WA8. 5 interactions.
    STRINGi 9606.ENSP00000285737.

    Protein family/group databases

    MEROPSi S16.006.

    PTM databases

    PhosphoSitei Q86WA8.

    Polymorphism databases

    DMDMi 74727668.

    Proteomic databases

    MaxQBi Q86WA8.
    PaxDbi Q86WA8.
    PRIDEi Q86WA8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000285737 ; ENSP00000285737 ; ENSG00000102910 .
    ENST00000535754 ; ENSP00000445426 ; ENSG00000102910 .
    GeneIDi 83752.
    KEGGi hsa:83752.
    UCSCi uc002efi.1. human.

    Organism-specific databases

    CTDi 83752.
    GeneCardsi GC16P048278.
    H-InvDB HIX0173249.
    HGNCi HGNC:20598. LONP2.
    HPAi HPA008862.
    neXtProti NX_Q86WA8.
    PharmGKBi PA162394186.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0466.
    HOGENOMi HOG000261408.
    HOVERGENi HBG000798.
    InParanoidi Q86WA8.
    KOi K01338.
    OMAi DQREYFL.
    OrthoDBi EOG77T13V.
    PhylomeDBi Q86WA8.
    TreeFami TF317215.

    Enzyme and pathway databases

    Reactomei REACT_16907. Association of TriC/CCT with target proteins during biosynthesis.

    Miscellaneous databases

    GenomeRNAii 83752.
    NextBioi 72777.
    PROi Q86WA8.

    Gene expression databases

    ArrayExpressi Q86WA8.
    Bgeei Q86WA8.
    CleanExi HS_LONP2.
    Genevestigatori Q86WA8.

    Family and domain databases

    Gene3Di 3.30.230.10. 1 hit.
    3.40.50.300. 1 hit.
    HAMAPi MF_03121. lonp2_euk.
    InterProi IPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR004815. Lon_bac/euk-typ.
    IPR027065. Lon_Prtase.
    IPR027501. Lonp2_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.
    [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 mammalian peroxisomal lon protease: cloning and characterization."
      De Walque S., Van Veldhoven P.P.
      Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "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] (ISOFORM 1).
      Tissue: Teratocarcinoma.
    3. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORMS 1 AND 2).
      Tissue: Brain and Uterus.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 138-852 (ISOFORM 1).
      Tissue: Melanoma.
    6. "Proteomic analysis of rat liver peroxisome: presence of peroxisome-specific isozyme of Lon protease."
      Kikuchi M., Hatano N., Yokota S., Shimozawa N., Imanaka T., Taniguchi H.
      J. Biol. Chem. 279:421-428(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Two proteases, trypsin domain-containing 1 (Tysnd1) and peroxisomal lon protease (PsLon), cooperatively regulate fatty acid beta-oxidation in peroxisomal matrix."
      Okumoto K., Kametani Y., Fujiki Y.
      J. Biol. Chem. 286:44367-44379(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PEX5 AND TYSND1, MUTAGENESIS OF SER-743.
    9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiLONP2_HUMAN
    AccessioniPrimary (citable) accession number: Q86WA8
    Secondary accession number(s): B7ZKL7
    , Q0D2H6, Q8N3B9, Q8NCE9, Q96K43
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 15, 2007
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 107 of the entry and version 1 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3