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Q64514 (TPP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tripeptidyl-peptidase 2

Short name=TPP-2
EC=3.4.14.10
Alternative name(s):
Tripeptidyl aminopeptidase
Tripeptidyl-peptidase II
Short name=TPP-II
Gene names
Name:Tpp2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1262 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

Release of an N-terminal tripeptide from a polypeptide.

Subcellular location

Cytoplasm. Nucleus. Note: Translocates to the nucleus in responce to gamma-irradiation. Ref.3

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.

Sequence similarities

Belongs to the peptidase S8 family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: Q64514-1)

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.
Isoform Short (identifier: Q64514-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 12621261Tripeptidyl-peptidase 2
PRO_0000076423

Sites

Active site441Charge relay system By similarity
Active site2641Charge relay system By similarity
Active site4491Charge relay system By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue4011N6-acetyllysine Ref.4
Cross-link1018Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link1026Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Natural variations

Alternative sequence985 – 99713Missing in isoform Short.
VSP_005446

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: D50D22C85544B034

FASTA1,262139,879
        10         20         30         40         50         60 
MATAATEEPF PFHGLLPKKE TGASSFLCRY PEYDGRGVLI AVLDTGVDPG APGMQVTTDG 

        70         80         90        100        110        120 
KPKIIDIIDT TGSGDVNTAT EVEPKDGEII GLSGRVLKIP ANWTNPLGKY HIGIKNGYDF 

       130        140        150        160        170        180 
YPKALKERIQ KERKEKIWDP IHRVALAEAC RKQEEFDIAN NGSSQANKLI KEELQSQVEL 

       190        200        210        220        230        240 
LNSFEKKYSD PGPVYDCLVW HDGETWRACV DSNENGDLSK CAVLRNYKEA QEYSSFGTAE 

       250        260        270        280        290        300 
MLNYSVNIYD DGNLLSIVTS GGAHGTHVAS IAAGHFPEEP ERNGVAPGAQ ILSIKIGDTR 

       310        320        330        340        350        360 
LSTMETGTGL IRAMIEVINH KCDLVNYSYG EATHWPNSGR ICEVINEAVW KHNTIYVSSA 

       370        380        390        400        410        420 
GNNGPCLSTV GCPGGTTSSV IGVGAYVSPD MMVAEYSLRE KLPANQYTWS SRGPSADGAL 

       430        440        450        460        470        480 
GVSISAPGGA IASVPNWTLR GTQLMNGTSM SSPNACGGIA LVLSGLKANN VDYTVHSVRR 

       490        500        510        520        530        540 
ALENTAIKAD NIEVFAQGHG IIQVDKAYDY LIQNTSFANR LGFTVTVGNN RGIYLRDPVQ 

       550        560        570        580        590        600 
VAAPSDHGVG IEPVFPENTE NSEKISFQLH LALTSNSSWV QCPSHLELMN QCRHINIRVD 

       610        620        630        640        650        660 
PRGLREGLHY TEVCGYDIAS PNAGPLFRVP ITAVIAAKVN ESSHYDLAFT DVHFKPGQIR 

       670        680        690        700        710        720 
RHFVEVPEGA TWAEVTVCSC SSEVSAKFVL HAVQLVKQRA YRSHEFYKFC SLPEKGTLIE 

       730        740        750        760        770        780 
AFPVLGGKAI EFCIARWWAS LSDVNIDYTI SFHGIVCTAP QLNIHASEGI NRFDVQSSLK 

       790        800        810        820        830        840 
YEDLAPCITL KSWVQTLRPV NAKTRPLGSR DVLPNNRQLY EMVLTYSFHQ PKSGEVTPSC 

       850        860        870        880        890        900 
PLLCELLYES EFDSQLWIIF DQNKRQMGSG DAYPHQYSLK LEKGDYTIRL QIRHEQISDL 

       910        920        930        940        950        960 
DRLKDLPFIV SHRLSNTLSL DIHENHSLAL LGKKKSSSLT LPPKYNQPFF VTSLPDDKIP 

       970        980        990       1000       1010       1020 
KGAGPGCYLA GSLTLSKTEL GKKAGQSAAK RQGKFKKDVI PVHYYLIPPP TKIKNGSKDK 

      1030       1040       1050       1060       1070       1080 
EKDSEKEKDL KEEFTEALRD LKIQWMTKLD STDIYNELKE TYPAYLPLYV ARLHQLDAEK 

      1090       1100       1110       1120       1130       1140 
ERMKRLNEIV DAANAVISHI DQTALAVYIA MKTDPRPDAA TIKNDMDKQK STLIDALCRK 

      1150       1160       1170       1180       1190       1200 
GCALADHLLH TQPHDGAAAG DAEAKEEEGE STMESLSETY WETTKWTDLF DTKVLIFAYK 

      1210       1220       1230       1240       1250       1260 
HALVNKMYGR GLKFATKLVE EKPTKENWKN CIQLMKLLGW THCASFTENW LPIMYPPDYC 


VF 

« Hide

Isoform Short [UniParc].

Checksum: A4E59C8D6416EF88
Show »

FASTA1,249138,463

References

« Hide 'large scale' references
[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]"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.
[4]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X81323 mRNA. Translation: CAA57103.1.
BC058239 mRNA. Translation: AAH58239.1.
CCDSCCDS14926.1. [Q64514-1]
PIRI48855.
RefSeqNP_033444.1. NM_009418.2. [Q64514-1]
XP_006495948.1. XM_006495885.1. [Q64514-2]
UniGeneMm.401675.

3D structure databases

ProteinModelPortalQ64514.
SMRQ64514. Positions 21-77, 237-507.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ64514. 1 interaction.
MINTMINT-4138337.

Chemistry

ChEMBLCHEMBL5512.

Protein family/group databases

MEROPSS08.090.

PTM databases

PhosphoSiteQ64514.

Proteomic databases

MaxQBQ64514.
PaxDbQ64514.
PRIDEQ64514.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000087933; ENSMUSP00000085244; ENSMUSG00000041763. [Q64514-1]
GeneID22019.
KEGGmmu:22019.
UCSCuc007avs.1. mouse. [Q64514-1]
uc007avt.1. mouse. [Q64514-2]

Organism-specific databases

CTD7174.
MGIMGI:102724. Tpp2.

Phylogenomic databases

eggNOGCOG1404.
GeneTreeENSGT00390000014623.
HOGENOMHOG000008178.
HOVERGENHBG017992.
InParanoidQ64514.
KOK01280.
OMAEVWRACI.
OrthoDBEOG786H2B.
PhylomeDBQ64514.
TreeFamTF105647.

Gene expression databases

BgeeQ64514.
CleanExMM_TPP2.
GenevestigatorQ64514.

Family and domain databases

Gene3D3.40.50.200. 2 hits.
InterProIPR000209. 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]
PANTHERPTHR10795. PTHR10795. 1 hit.
PfamPF00082. Peptidase_S8. 1 hit.
PF12580. TPPII. 1 hit.
[Graphical view]
PRINTSPR00723. SUBTILISIN.
SUPFAMSSF52743. SSF52743. 2 hits.
PROSITEPS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio301748.
PROQ64514.
SOURCESearch...

Entry information

Entry nameTPP2_MOUSE
AccessionPrimary (citable) accession number: Q64514
Secondary accession number(s): Q5D072
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 112 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot