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Q64514

- TPP2_MOUSE

UniProt

Q64514 - TPP2_MOUSE

Protein

Tripeptidyl-peptidase 2

Gene

Tpp2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited By similarity. Stimulates adipogenesis.By similarity1 Publication

    Catalytic activityi

    Release of an N-terminal tripeptide from a polypeptide.PROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei44 – 441Charge relay systemBy similarity
    Active sitei264 – 2641Charge relay systemBy similarity
    Active sitei449 – 4491Charge relay systemBy similarity

    GO - Molecular functioni

    1. aminopeptidase activity Source: UniProtKB-KW
    2. peptide binding Source: Ensembl
    3. serine-type endopeptidase activity Source: RefGenome
    4. tripeptidyl-peptidase activity Source: Ensembl

    GO - Biological processi

    1. proteolysis Source: RefGenome

    Keywords - Molecular functioni

    Aminopeptidase, Hydrolase, Protease, Serine protease

    Enzyme and pathway databases

    ReactomeiREACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.

    Protein family/group databases

    MEROPSiS08.090.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tripeptidyl-peptidase 2 (EC:3.4.14.10)
    Short name:
    TPP-2
    Alternative name(s):
    Tripeptidyl aminopeptidase
    Tripeptidyl-peptidase II
    Short name:
    TPP-II
    Gene namesi
    Name:Tpp2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:102724. Tpp2.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Translocates to the nucleus in responce to gamma-irradiation.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Homozygous mutant mice die in utero before embryonic day 9.0. Heterozygous mice display normal food intake but appear lean with a significant reduction in body fat, smaller adipocytes, decreased plasma insulin levels and less white adipose tissue in the gonad, groin and mesenteric regions.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi44 – 441D → A: No effect on adipogenesis. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 12621261Tripeptidyl-peptidase 2PRO_0000076423Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei401 – 4011N6-acetyllysine1 Publication
    Cross-linki1018 – 1018Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki1026 – 1026Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiQ64514.
    PaxDbiQ64514.
    PRIDEiQ64514.

    PTM databases

    PhosphoSiteiQ64514.

    Expressioni

    Tissue specificityi

    Expressed in the brain, skeletal muscle, gonadal and mesenteric white adipose tissue and brown adipose tissues.1 Publication

    Gene expression databases

    BgeeiQ64514.
    CleanExiMM_TPP2.
    GenevestigatoriQ64514.

    Interactioni

    Protein-protein interaction databases

    IntActiQ64514. 1 interaction.
    MINTiMINT-4138337.

    Structurei

    3D structure databases

    ProteinModelPortaliQ64514.
    SMRiQ64514. Positions 21-77, 237-507.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini40 – 509470Peptidase S8Add
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase S8 family.Curated
    Contains 1 peptidase S8 domain.Curated

    Phylogenomic databases

    eggNOGiCOG1404.
    GeneTreeiENSGT00390000014623.
    HOGENOMiHOG000008178.
    HOVERGENiHBG017992.
    InParanoidiQ64514.
    KOiK01280.
    OMAiEVWRACI.
    OrthoDBiEOG786H2B.
    PhylomeDBiQ64514.
    TreeFamiTF105647.

    Family and domain databases

    Gene3Di3.40.50.200. 2 hits.
    InterProiIPR000209. Peptidase_S8/S53_dom.
    IPR022398. Peptidase_S8_His-AS.
    IPR023828. Peptidase_S8_Ser-AS.
    IPR015500. Peptidase_S8_subtilisin-rel.
    IPR022229. Peptidase_S8A_TPPII.
    [Graphical view]
    PANTHERiPTHR10795. PTHR10795. 1 hit.
    PfamiPF00082. Peptidase_S8. 1 hit.
    PF12580. TPPII. 1 hit.
    [Graphical view]
    PRINTSiPR00723. SUBTILISIN.
    SUPFAMiSSF52743. SSF52743. 2 hits.
    PROSITEiPS00137. SUBTILASE_HIS. 1 hit.
    PS00138. SUBTILASE_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 Long (identifier: Q64514-1) [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

    MATAATEEPF PFHGLLPKKE TGASSFLCRY PEYDGRGVLI AVLDTGVDPG     50
    APGMQVTTDG KPKIIDIIDT TGSGDVNTAT EVEPKDGEII GLSGRVLKIP 100
    ANWTNPLGKY HIGIKNGYDF YPKALKERIQ KERKEKIWDP IHRVALAEAC 150
    RKQEEFDIAN NGSSQANKLI KEELQSQVEL LNSFEKKYSD PGPVYDCLVW 200
    HDGETWRACV DSNENGDLSK CAVLRNYKEA QEYSSFGTAE MLNYSVNIYD 250
    DGNLLSIVTS GGAHGTHVAS IAAGHFPEEP ERNGVAPGAQ ILSIKIGDTR 300
    LSTMETGTGL IRAMIEVINH KCDLVNYSYG EATHWPNSGR ICEVINEAVW 350
    KHNTIYVSSA GNNGPCLSTV GCPGGTTSSV IGVGAYVSPD MMVAEYSLRE 400
    KLPANQYTWS SRGPSADGAL GVSISAPGGA IASVPNWTLR GTQLMNGTSM 450
    SSPNACGGIA LVLSGLKANN VDYTVHSVRR ALENTAIKAD NIEVFAQGHG 500
    IIQVDKAYDY LIQNTSFANR LGFTVTVGNN RGIYLRDPVQ VAAPSDHGVG 550
    IEPVFPENTE NSEKISFQLH LALTSNSSWV QCPSHLELMN QCRHINIRVD 600
    PRGLREGLHY TEVCGYDIAS PNAGPLFRVP ITAVIAAKVN ESSHYDLAFT 650
    DVHFKPGQIR RHFVEVPEGA TWAEVTVCSC SSEVSAKFVL HAVQLVKQRA 700
    YRSHEFYKFC SLPEKGTLIE AFPVLGGKAI EFCIARWWAS LSDVNIDYTI 750
    SFHGIVCTAP QLNIHASEGI NRFDVQSSLK YEDLAPCITL KSWVQTLRPV 800
    NAKTRPLGSR DVLPNNRQLY EMVLTYSFHQ PKSGEVTPSC PLLCELLYES 850
    EFDSQLWIIF DQNKRQMGSG DAYPHQYSLK LEKGDYTIRL QIRHEQISDL 900
    DRLKDLPFIV SHRLSNTLSL DIHENHSLAL LGKKKSSSLT LPPKYNQPFF 950
    VTSLPDDKIP KGAGPGCYLA GSLTLSKTEL GKKAGQSAAK RQGKFKKDVI 1000
    PVHYYLIPPP TKIKNGSKDK EKDSEKEKDL KEEFTEALRD LKIQWMTKLD 1050
    STDIYNELKE TYPAYLPLYV ARLHQLDAEK ERMKRLNEIV DAANAVISHI 1100
    DQTALAVYIA MKTDPRPDAA TIKNDMDKQK STLIDALCRK GCALADHLLH 1150
    TQPHDGAAAG DAEAKEEEGE STMESLSETY WETTKWTDLF DTKVLIFAYK 1200
    HALVNKMYGR GLKFATKLVE EKPTKENWKN CIQLMKLLGW THCASFTENW 1250
    LPIMYPPDYC VF 1262
    Length:1,262
    Mass (Da):139,879
    Last modified:January 23, 2007 - v3
    Checksum:iD50D22C85544B034
    GO
    Isoform Short (identifier: Q64514-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         985-997: Missing.

    Show »
    Length:1,249
    Mass (Da):138,463
    Checksum:iA4E59C8D6416EF88
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei985 – 99713Missing in isoform Short. 2 PublicationsVSP_005446Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X81323 mRNA. Translation: CAA57103.1.
    BC058239 mRNA. Translation: AAH58239.1.
    CCDSiCCDS14926.1. [Q64514-1]
    PIRiI48855.
    RefSeqiNP_033444.1. NM_009418.2. [Q64514-1]
    XP_006495948.1. XM_006495885.1. [Q64514-2]
    UniGeneiMm.401675.

    Genome annotation databases

    EnsembliENSMUST00000087933; ENSMUSP00000085244; ENSMUSG00000041763. [Q64514-1]
    GeneIDi22019.
    KEGGimmu:22019.
    UCSCiuc007avs.1. mouse. [Q64514-1]
    uc007avt.1. mouse. [Q64514-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X81323 mRNA. Translation: CAA57103.1 .
    BC058239 mRNA. Translation: AAH58239.1 .
    CCDSi CCDS14926.1. [Q64514-1 ]
    PIRi I48855.
    RefSeqi NP_033444.1. NM_009418.2. [Q64514-1 ]
    XP_006495948.1. XM_006495885.1. [Q64514-2 ]
    UniGenei Mm.401675.

    3D structure databases

    ProteinModelPortali Q64514.
    SMRi Q64514. Positions 21-77, 237-507.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q64514. 1 interaction.
    MINTi MINT-4138337.

    Chemistry

    ChEMBLi CHEMBL5512.

    Protein family/group databases

    MEROPSi S08.090.

    PTM databases

    PhosphoSitei Q64514.

    Proteomic databases

    MaxQBi Q64514.
    PaxDbi Q64514.
    PRIDEi Q64514.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000087933 ; ENSMUSP00000085244 ; ENSMUSG00000041763 . [Q64514-1 ]
    GeneIDi 22019.
    KEGGi mmu:22019.
    UCSCi uc007avs.1. mouse. [Q64514-1 ]
    uc007avt.1. mouse. [Q64514-2 ]

    Organism-specific databases

    CTDi 7174.
    MGIi MGI:102724. Tpp2.

    Phylogenomic databases

    eggNOGi COG1404.
    GeneTreei ENSGT00390000014623.
    HOGENOMi HOG000008178.
    HOVERGENi HBG017992.
    InParanoidi Q64514.
    KOi K01280.
    OMAi EVWRACI.
    OrthoDBi EOG786H2B.
    PhylomeDBi Q64514.
    TreeFami TF105647.

    Enzyme and pathway databases

    Reactomei REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.

    Miscellaneous databases

    NextBioi 301748.
    PROi Q64514.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q64514.
    CleanExi MM_TPP2.
    Genevestigatori Q64514.

    Family and domain databases

    Gene3Di 3.40.50.200. 2 hits.
    InterProi IPR000209. Peptidase_S8/S53_dom.
    IPR022398. Peptidase_S8_His-AS.
    IPR023828. Peptidase_S8_Ser-AS.
    IPR015500. Peptidase_S8_subtilisin-rel.
    IPR022229. Peptidase_S8A_TPPII.
    [Graphical view ]
    PANTHERi PTHR10795. PTHR10795. 1 hit.
    Pfami PF00082. Peptidase_S8. 1 hit.
    PF12580. TPPII. 1 hit.
    [Graphical view ]
    PRINTSi PR00723. SUBTILISIN.
    SUPFAMi SSF52743. SSF52743. 2 hits.
    PROSITEi PS00137. SUBTILASE_HIS. 1 hit.
    PS00138. SUBTILASE_SER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of cDNA for murine tripeptidyl-peptidase II reveals alternative splicing."
      Tomkinson B.
      Biochem. J. 304:517-523(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
      Strain: Leaden X A1.
    2. "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 SHORT).
      Tissue: Olfactory epithelium.
    3. "Tripeptidyl peptidase II promotes fat formation in a conserved fashion."
      McKay R.M., McKay J.P., Suh J.M., Avery L., Graff J.M.
      EMBO Rep. 8:1183-1189(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-44.
    4. "A role for nuclear translocation of tripeptidyl-peptidase II in reactive oxygen species-dependent DNA damage responses."
      Preta G., de Klark R., Glas R.
      Biochem. Biophys. Res. Commun. 389:575-579(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-401, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiTPP2_MOUSE
    AccessioniPrimary (citable) accession number: Q64514
    Secondary accession number(s): Q5D072
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 114 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The limitation of proteolytic products to tripeptides is achieved by tailoring the size of the substrate-binding cleft: the two negatively charged residues Glu-305 and Glu-331 that are blocking position P4 limit the number of residues that can be accommodated in the binding cleft and thus create a molecular ruler. At the same time, they orient substrates so that the tripeptides are removed exclusively from the N-terminus By similarity.By similarity

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3