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Q64514

- TPP2_MOUSE

UniProt

Q64514 - TPP2_MOUSE

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Protein

Tripeptidyl-peptidase 2

Gene

Tpp2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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-KW
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

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.
ExpressionAtlasiQ64514. baseline and differential.
GenevestigatoriQ64514.

Interactioni

Protein-protein interaction databases

IntActiQ64514. 1 interaction.
MINTiMINT-4138337.

Structurei

3D structure databases

ProteinModelPortaliQ64514.
SMRiQ64514. Positions 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

        10         20         30         40         50
MATAATEEPF PFHGLLPKKE TGASSFLCRY PEYDGRGVLI AVLDTGVDPG
60 70 80 90 100
APGMQVTTDG KPKIIDIIDT TGSGDVNTAT EVEPKDGEII GLSGRVLKIP
110 120 130 140 150
ANWTNPLGKY HIGIKNGYDF YPKALKERIQ KERKEKIWDP IHRVALAEAC
160 170 180 190 200
RKQEEFDIAN NGSSQANKLI KEELQSQVEL LNSFEKKYSD PGPVYDCLVW
210 220 230 240 250
HDGETWRACV DSNENGDLSK CAVLRNYKEA QEYSSFGTAE MLNYSVNIYD
260 270 280 290 300
DGNLLSIVTS GGAHGTHVAS IAAGHFPEEP ERNGVAPGAQ ILSIKIGDTR
310 320 330 340 350
LSTMETGTGL IRAMIEVINH KCDLVNYSYG EATHWPNSGR ICEVINEAVW
360 370 380 390 400
KHNTIYVSSA GNNGPCLSTV GCPGGTTSSV IGVGAYVSPD MMVAEYSLRE
410 420 430 440 450
KLPANQYTWS SRGPSADGAL GVSISAPGGA IASVPNWTLR GTQLMNGTSM
460 470 480 490 500
SSPNACGGIA LVLSGLKANN VDYTVHSVRR ALENTAIKAD NIEVFAQGHG
510 520 530 540 550
IIQVDKAYDY LIQNTSFANR LGFTVTVGNN RGIYLRDPVQ VAAPSDHGVG
560 570 580 590 600
IEPVFPENTE NSEKISFQLH LALTSNSSWV QCPSHLELMN QCRHINIRVD
610 620 630 640 650
PRGLREGLHY TEVCGYDIAS PNAGPLFRVP ITAVIAAKVN ESSHYDLAFT
660 670 680 690 700
DVHFKPGQIR RHFVEVPEGA TWAEVTVCSC SSEVSAKFVL HAVQLVKQRA
710 720 730 740 750
YRSHEFYKFC SLPEKGTLIE AFPVLGGKAI EFCIARWWAS LSDVNIDYTI
760 770 780 790 800
SFHGIVCTAP QLNIHASEGI NRFDVQSSLK YEDLAPCITL KSWVQTLRPV
810 820 830 840 850
NAKTRPLGSR DVLPNNRQLY EMVLTYSFHQ PKSGEVTPSC PLLCELLYES
860 870 880 890 900
EFDSQLWIIF DQNKRQMGSG DAYPHQYSLK LEKGDYTIRL QIRHEQISDL
910 920 930 940 950
DRLKDLPFIV SHRLSNTLSL DIHENHSLAL LGKKKSSSLT LPPKYNQPFF
960 970 980 990 1000
VTSLPDDKIP KGAGPGCYLA GSLTLSKTEL GKKAGQSAAK RQGKFKKDVI
1010 1020 1030 1040 1050
PVHYYLIPPP TKIKNGSKDK EKDSEKEKDL KEEFTEALRD LKIQWMTKLD
1060 1070 1080 1090 1100
STDIYNELKE TYPAYLPLYV ARLHQLDAEK ERMKRLNEIV DAANAVISHI
1110 1120 1130 1140 1150
DQTALAVYIA MKTDPRPDAA TIKNDMDKQK STLIDALCRK GCALADHLLH
1160 1170 1180 1190 1200
TQPHDGAAAG DAEAKEEEGE STMESLSETY WETTKWTDLF DTKVLIFAYK
1210 1220 1230 1240 1250
HALVNKMYGR GLKFATKLVE EKPTKENWKN CIQLMKLLGW THCASFTENW
1260
LPIMYPPDYC VF
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]
ENSMUST00000188313; ENSMUSP00000139918; ENSMUSG00000041763. [Q64514-2]
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 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 ]
ENSMUST00000188313 ; ENSMUSP00000139918 ; ENSMUSG00000041763 . [Q64514-2 ]
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.
ExpressionAtlasi Q64514. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 115 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