Q64514 (TPP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 101.
History...
Clusters with 
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended 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 |
| ||
| Organism | Mus musculus (Mouse) [Reference proteome] | ||
| Taxonomic identifier | 10090 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus |
Protein attributes
| Sequence length | 1262 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript 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. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Nucleus |
| Coding sequence diversity | Alternative splicing |
| Molecular function | Aminopeptidase Hydrolase Protease Serine protease |
| PTM | Acetylation Isopeptide bond Ubl conjugation |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | proteolysis Inferred from Biological aspect of Ancestor. Source: RefGenome |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleusInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | aminopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activityInferred from Biological aspect of Ancestor. Source: RefGenome |
| Complete GO annotation... | |
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 key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 1262 | 1261 | Tripeptidyl-peptidase 2 | PRO_0000076423 | |||||
Sites | |||||||||
| Active site | 44 | 1 | Charge relay system By similarity | ||||||
| Active site | 264 | 1 | Charge relay system By similarity | ||||||
| Active site | 449 | 1 | Charge relay system By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine By similarity | ||||||
| Cross-link | 1018 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity | |||||||
| Cross-link | 1026 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity | |||||||
Natural variations | |||||||||
| Alternative sequence | 985 – 997 | 13 | Missing in isoform Short. | VSP_005446 | |||||
Sequences
| ||||||||||||||||||||||||
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. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X81323 mRNA. Translation: CAA57103.1. BC058239 mRNA. Translation: AAH58239.1. |
| IPI | IPI00227843. IPI00469194. |
| PIR | I48855. |
| RefSeq | NP_033444.1. NM_009418.2. |
| UniGene | Mm.401675. |
3D structure databases | |
| ProteinModelPortal | Q64514. |
| SMR | Q64514. Positions 237-507. |
| ModBase | Search... |
Protein-protein interaction databases | |
| MINT | MINT-4138337. |
Protein family/group databases | |
| MEROPS | S08.090. |
PTM databases | |
| PhosphoSite | Q64514. |
Proteomic databases | |
| PaxDb | Q64514. |
| PRIDE | Q64514. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000087933; ENSMUSP00000085244; ENSMUSG00000041763. |
| GeneID | 22019. |
| KEGG | mmu:22019. |
| UCSC | uc007avs.1. mouse. uc007avt.1. mouse. |
Organism-specific databases | |
| CTD | 7174. |
| MGI | MGI:102724. Tpp2. |
Phylogenomic databases | |
| eggNOG | COG1404. |
| GeneTree | ENSGT00390000014623. |
| HOGENOM | HOG000008178. |
| HOVERGEN | HBG017992. |
| InParanoid | Q64514. |
| KO | K01280. |
| OMA | EVWRACI. |
| OrthoDB | EOG4H462Z. |
Gene expression databases | |
| Bgee | Q64514. |
| CleanEx | MM_TPP2. |
| Genevestigator | Q64514. |
| GermOnline | ENSMUSG00000041763. Mus musculus. |
Family and domain databases | |
| Gene3D | 3.40.50.200. 2 hits. |
| InterPro | 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] |
| PANTHER | PTHR10795. PTHR10795. 1 hit. |
| Pfam | PF00082. Peptidase_S8. 1 hit. PF12580. TPPII. 1 hit. [Graphical view] |
| PRINTS | PR00723. SUBTILISIN. |
| SUPFAM | SSF52743. Pept_S8_S53. 1 hit. |
| PROSITE | PS00136. SUBTILASE_ASP. False negative. PS00137. SUBTILASE_HIS. 1 hit. PS00138. SUBTILASE_SER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChEMBL | CHEMBL5512. |
| NextBio | 301748. |
| SOURCE | Search... |
Entry information
| Entry name | TPP2_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q64514 Secondary accession number(s): Q5D072 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| Peptidase families Classification of peptidase families and list of entries |
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |