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P29144

- TPP2_HUMAN

UniProt

P29144 - TPP2_HUMAN

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Protein

Tripeptidyl-peptidase 2

Gene
TPP2
Organism
Homo sapiens (Human)
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. Stimulates adipogenesis By similarity.

Catalytic activityi

Release of an N-terminal tripeptide from a polypeptide.

Sites

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

GO - Molecular functioni

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

GO - Biological processi

  1. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  2. protein polyubiquitination Source: Reactome
  3. proteolysis Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Protease, Serine protease

Enzyme and pathway databases

ReactomeiREACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinkiP29144.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:12016. TPP2.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. cytosol Source: Reactome
  3. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36695.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 12491248Tripeptidyl-peptidase 2PRO_0000076422Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei401 – 4011N6-acetyllysine By similarity
Cross-linki1005 – 1005Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki1013 – 1013Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiP29144.
PaxDbiP29144.
PeptideAtlasiP29144.
PRIDEiP29144.

PTM databases

PhosphoSiteiP29144.

Expressioni

Gene expression databases

ArrayExpressiP29144.
BgeeiP29144.
CleanExiHS_TPP2.
GenevestigatoriP29144.

Organism-specific databases

HPAiHPA021069.

Interactioni

Protein-protein interaction databases

BioGridi113027. 7 interactions.
DIPiDIP-50761N.
STRINGi9606.ENSP00000365233.

Structurei

3D structure databases

ProteinModelPortaliP29144.
SMRiP29144. Positions 20-55, 237-507.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S8 family.

Phylogenomic databases

eggNOGiCOG1404.
HOGENOMiHOG000008178.
HOVERGENiHBG017992.
KOiK01280.
OrthoDBiEOG786H2B.
PhylomeDBiP29144.
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]

Sequencei

Sequence statusi: Complete.

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

P29144-1 [UniParc]FASTAAdd to Basket

« Hide

MATAATEEPF PFHGLLPKKE TGAASFLCRY PEYDGRGVLI AVLDTGVDPG     50
APGMQVTTDG KPKIVDIIDT TGSGDVNTAT EVEPKDGEIV GLSGRVLKIP 100
ASWTNPSGKY HIGIKNGYDF YPKALKERIQ KERKEKIWDP VHRVALAEAC 150
RKQEEFDVAN NGSSQANKLI KEELQSQVEL LNSFEKKYSD PGPVYDCLVW 200
HDGEVWRACI DSNEDGDLSK STVLRNYKEA QEYGSFGTAE MLNYSVNIYD 250
DGNLLSIVTS GGAHGTHVAS IAAGHFPEEP ERNGVAPGAQ ILSIKIGDTR 300
LSTMETGTGL IRAMIEVINH KCDLVNYSYG EATHWPNSGR ICEVINEAVW 350
KHNIIYVSSA GNNGPCLSTV GCPGGTTSSV IGVGAYVSPD MMVAEYSLRE 400
KLPANQYTWS SRGPSADGAL GVSISAPGGA IASVPNWTLR GTQLMNGTSM 450
SSPNACGGIA LILSGLKANN IDYTVHSVRR ALENTAVKAD NIEVFAQGHG 500
IIQVDKAYDY LVQNTSFANK LGFTVTVGNN RGIYLRDPVQ VAAPSDHGVG 550
IEPVFPENTE NSEKISLQLH LALTSNSSWV QCPSHLELMN QCRHINIRVD 600
PRGLREGLHY TEVCGYDIAS PNAGPLFRVP ITAVIAAKVN ESSHYDLAFT 650
DVHFKPGQIR RHFIEVPEGA TWAEVTVCSC SSEVSAKFVL HAVQLVKQRA 700
YRSHEFYKFC SLPEKGTLTE AFPVLGGKAI EFCIARWWAS LSDVNIDYTI 750
SFHGIVCTAP QLNIHASEGI NRFDVQSSLK YEDLAPCITL KNWVQTLRPV 800
SAKTKPLGSR DVLPNNRQLY EMVLTYNFHQ PKSGEVTPSC PLLCELLYES 850
EFDSQLWIIF DQNKRQMGSG DAYPHQYSLK LEKGDYTIRL QIRHEQISDL 900
ERLKDLPFIV SHRLSNTLSL DIHENHSFAL LGKKKSSNLT LPPKYNQPFF 950
VTSLPDDKIP KGAGPGCYLA GSLTLSKTEL GKKADVIPVH YYLIPPPTKT 1000
KNGSKDKEKD SEKEKDLKEE FTEALRDLKI QWMTKLDSSD IYNELKETYP 1050
NYLPLYVARL HQLDAEKERM KRLNEIVDAA NAVISHIDQT ALAVYIAMKT 1100
DPRPDAATIK NDMDKQKSTL VDALCRKGCA LADHLLHTQA QDGAISTDAE 1150
GKEEEGESPL DSLAETFWET TKWTDLFDNK VLTFAYKHAL VNKMYGRGLK 1200
FATKLVEEKP TKENWKNCIQ LMKLLGWTHC ASFTENWLPI MYPPDYCVF 1249
Length:1,249
Mass (Da):138,350
Last modified:January 23, 2007 - v4
Checksum:iA26A6249DBF7F3DD
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti252 – 2521G → R in AAA36760. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL158063 Genomic DNA. Translation: CAH72179.1.
CH471085 Genomic DNA. Translation: EAX09059.1.
BC039905 mRNA. Translation: AAH39905.1.
M73047 mRNA. Translation: AAA36760.1.
M55169 mRNA. Translation: AAA63263.1.
CCDSiCCDS9502.1.
PIRiS54376.
RefSeqiNP_003282.2. NM_003291.2.
UniGeneiHs.432424.

Genome annotation databases

EnsembliENST00000376065; ENSP00000365233; ENSG00000134900.
GeneIDi7174.
KEGGihsa:7174.
UCSCiuc001vpi.4. human.

Polymorphism databases

DMDMi34223721.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL158063 Genomic DNA. Translation: CAH72179.1 .
CH471085 Genomic DNA. Translation: EAX09059.1 .
BC039905 mRNA. Translation: AAH39905.1 .
M73047 mRNA. Translation: AAA36760.1 .
M55169 mRNA. Translation: AAA63263.1 .
CCDSi CCDS9502.1.
PIRi S54376.
RefSeqi NP_003282.2. NM_003291.2.
UniGenei Hs.432424.

3D structure databases

ProteinModelPortali P29144.
SMRi P29144. Positions 20-55, 237-507.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 113027. 7 interactions.
DIPi DIP-50761N.
STRINGi 9606.ENSP00000365233.

Chemistry

ChEMBLi CHEMBL6156.

Protein family/group databases

MEROPSi S08.090.

PTM databases

PhosphoSitei P29144.

Polymorphism databases

DMDMi 34223721.

Proteomic databases

MaxQBi P29144.
PaxDbi P29144.
PeptideAtlasi P29144.
PRIDEi P29144.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000376065 ; ENSP00000365233 ; ENSG00000134900 .
GeneIDi 7174.
KEGGi hsa:7174.
UCSCi uc001vpi.4. human.

Organism-specific databases

CTDi 7174.
GeneCardsi GC13P103249.
HGNCi HGNC:12016. TPP2.
HPAi HPA021069.
MIMi 190470. gene.
neXtProti NX_P29144.
PharmGKBi PA36695.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1404.
HOGENOMi HOG000008178.
HOVERGENi HBG017992.
KOi K01280.
OrthoDBi EOG786H2B.
PhylomeDBi P29144.
TreeFami TF105647.

Enzyme and pathway databases

Reactomei REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
SignaLinki P29144.

Miscellaneous databases

GeneWikii Tripeptidyl_peptidase_II.
GenomeRNAii 7174.
NextBioi 28124.
PROi P29144.
SOURCEi Search...

Gene expression databases

ArrayExpressi P29144.
Bgeei P29144.
CleanExi HS_TPP2.
Genevestigatori P29144.

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. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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].
    Tissue: Testis.
  4. "Nucleotide sequence of cDNA covering the N-terminus of human tripeptidyl peptidase II."
    Tomkinson B.
    Biomed. Biochim. Acta 50:727-729(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-55, PROTEIN SEQUENCE OF 6-26.
  5. "Characterization of cDNA for human tripeptidyl peptidase II: the N-terminal part of the enzyme is similar to subtilisin."
    Tomkinson B., Jonsson A.-K.
    Biochemistry 30:168-174(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 56-1249.
    Tissue: Lymphocyte.
  6. Bienvenut W.V., Quadroni M.
    Submitted (JUL-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-18 AND 1036-1046, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  7. "Immunological cross-reactivity between human tripeptidyl peptidase II and fibronectin."
    Tomkinson B., Zetterqvist O.
    Biochem. J. 267:149-154(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 13-26; 1099-1118 AND 440-450.
  8. "Active site of tripeptidyl peptidase II from human erythrocytes is of the subtilisin type."
    Tomkinson B., Wernstedt C., Hellman U., Zetterqvist O.
    Proc. Natl. Acad. Sci. U.S.A. 84:7508-7512(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 441-450.
  9. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
    Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
    Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-1005 AND LYS-1013.
    Tissue: Mammary cancer.
  10. "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.
  11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTPP2_HUMAN
AccessioniPrimary (citable) accession number: P29144
Secondary accession number(s): Q5VZU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 131 of the entry and version 4 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

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.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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