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General Information
Symbol
Dmel\TppII
Species
D. melanogaster
Name
Tripeptidyl-peptidase II
Annotation Symbol
CG3991
Feature Type
FlyBase ID
FBgn0020370
Gene Model Status
Stock Availability
Enzyme Name (EC)
Tripeptidyl-peptidase II (3.4.14.10)
Tripeptidyl-peptidase I (3.4.14.9)
Acylaminoacyl-peptidase (3.4.19.1)
Chymotrypsin (3.4.21.1)
Acrosin (3.4.21.10)
C-terminal processing peptidase (3.4.21.102)
Cathepsin G (3.4.21.20)
Coagulation factor VIIa (3.4.21.21)
Coagulation factor IXa (3.4.21.22)
Prolyl oligopeptidase (3.4.21.26)
Coagulation factor XIa (3.4.21.27)
Plasma kallikrein (3.4.21.34)
Tissue kallikrein (3.4.21.35)
Pancreatic elastase (3.4.21.36)
Coagulation factor XIIa (3.4.21.38)
Chymase (3.4.21.39)
Trypsin (3.4.21.4)
Complement subcomponent C1r (3.4.21.41)
Complement subcomponent C1s (3.4.21.42)
Classical-complement-pathway C3/C5 convertase (3.4.21.43)
Complement factor I (3.4.21.45)
Complement factor D (3.4.21.46)
Alternative-complement-pathway C3/C5 convertase (3.4.21.47)
Cerevisin (3.4.21.48)
Thrombin (3.4.21.5)
Endopeptidase La (3.4.21.53)
Gamma-renin (3.4.21.54)
Tryptase (3.4.21.59)
Coagulation factor Xa (3.4.21.6)
Kexin (3.4.21.61)
Subtilisin (3.4.21.62)
T-plasminogen activator (3.4.21.68)
Protein C (activated) (3.4.21.69)
Plasmin (3.4.21.7)
Pancreatic elastase II (3.4.21.71)
U-plasminogen activator (3.4.21.73)
Furin (3.4.21.75)
Granzyme A (3.4.21.78)
Granzyme B (3.4.21.79)
Oligopeptidase B (3.4.21.83)
Repressor LexA (3.4.21.88)
Signal peptidase I (3.4.21.89)
Enteropeptidase (3.4.21.9)
Endopeptidase Clp (3.4.21.92)
Proprotein convertase 1 (3.4.21.93)
Proprotein convertase 2 (3.4.21.94)
Microbial collagenase (3.4.24.3)
Neutrophil collagenase (3.4.24.34)
Interstitial collagenase (3.4.24.7)
Gene Snapshot
tripeptidyl-peptidase II (TppII) encodes an exopeptidase that removes tripeptides from the free N-terminus of longer peptides. [Date last reviewed: 2018-10-04]
Also Known As

TPP II, dTPPII, dTPP II

Key Links
Genomic Location
Cytogenetic map
Sequence location
2R:13,152,885..13,159,141 [-]
Recombination map

2-68

RefSeq locus
NT_033778 REGION:13152885..13159141
Sequence
Other Genome Views
The following external sites may use different assemblies or annotations than FlyBase.
Function
GO Summary Ribbons
Gene Ontology (GO) Annotations (6 terms)
Molecular Function (3 terms)
Terms Based on Experimental Evidence (2 terms)
CV Term
Evidence
References
inferred from physical interaction with UniProtKB:Q9V6K1
(assigned by UniProt )
Terms Based on Predictions or Assertions (2 terms)
CV Term
Evidence
References
inferred from electronic annotation with InterPro:IPR000209
(assigned by InterPro )
inferred from biological aspect of ancestor with PANTHER:PTN000083315
(assigned by GO_Central )
Biological Process (1 term)
Terms Based on Experimental Evidence (1 term)
CV Term
Evidence
References
inferred from direct assay
Terms Based on Predictions or Assertions (0 terms)
Cellular Component (2 terms)
Terms Based on Experimental Evidence (2 terms)
CV Term
Evidence
References
inferred from direct assay
inferred from direct assay
(assigned by UniProt )
Terms Based on Predictions or Assertions (1 term)
CV Term
Evidence
References
inferred from biological aspect of ancestor with PANTHER:PTN000083315
(assigned by GO_Central )
Gene Group (FlyBase)
Protein Family (UniProt)
Belongs to the peptidase S8 family. (Q9V6K1)
Catalytic Activity (EC)
Experimental Evidence
Release of an N-terminal tripeptide from a polypeptide (3.4.14.10)
Release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity (3.4.14.9)
Predictions / Assertions
Release of an N-terminal tripeptide from a polypeptide (3.4.14.10)
Release of an N-terminal tripeptide from a polypeptide, but also has endopeptidase activity (3.4.14.9)
Cleavage of an N-acetyl or N-formyl amino acid from the N-terminus of a polypeptide (3.4.19.1)
Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa (3.4.21.1)
Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa (3.4.21.10)
The enzyme shows specific recognition of a C-terminal tripeptide, Xaa- Yaa-Zaa, in which Xaa is preferably Ala or Leu, Yaa is preferably Ala or Tyr, and Zaa is preferably Ala, but then cleaves at a variable distance from the C-terminus (3.4.21.102)
A typical cleavage is -Ala-Ala-|-Arg-Ala-Ala- Lys-Glu-Asn-Tyr-Ala-Leu-Ala-Ala (3.4.21.102)
Specificity similar to chymotrypsin C (3.4.21.20)
Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa (3.4.21.21)
Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa (3.4.21.22)
Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides (3.4.21.26)
Selective cleavage of Arg-|-Ala and Arg-|-Val bonds in factor IX to form factor IXa (3.4.21.27)
Cleaves selectively Arg-|-Xaa and Lys-|-Xaa bonds, including Lys-|-Arg and Arg-|-Ser bonds in (human) kininogen to release bradykinin (3.4.21.34)
Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates (3.4.21.35)
Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa (3.4.21.35)
Hydrolysis of proteins, including elastin (3.4.21.36)
Preferential cleavage: Ala-|-Xaa (3.4.21.36)
Selective cleavage of Arg-|-Ile bonds in factor VII to form factor VIIa and factor XI to form factor XIa (3.4.21.38)
Preferential cleavage: Phe-|-Xaa > Tyr-|-Xaa > Trp-|-Xaa > Leu-|-Xaa (3.4.21.39)
Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa (3.4.21.4)
Selective cleavage of Lys(or Arg)-|-Ile bond in complement subcomponent C1s to form the active form of C1s (EC 3 (3.4.21.41)
21 (3.4.21.41)
42) (3.4.21.41)
Cleavage of Arg-|-Ala bond in complement component C4 to form C4a and C4b, and Lys(or Arg)-|-Lys bond in complement component C2 to form C2a and C2b: the 'classical' pathway C3 convertase (3.4.21.42)
Selective cleavage of Arg-|-Ser bond in complement component C3 alpha- chain to form C3a and C3b, and Arg-|-Xaa bond in complement component C5 alpha-chain to form C5a and C5b (3.4.21.43)
Inactivates complement subcomponents C3b, iC3b and C4b by proteolytic cleavage (3.4.21.45)
Selective cleavage of Arg-|-Lys bond in complement factor B when in complex with complement subcomponent C3b or with cobra venom factor (3.4.21.46)
Cleavage of Arg-|-Ser bond in complement component C3 alpha-chain to yield C3a and C3b, and Arg-|-Xaa bond in complement component C5 alpha- chain to yield C5a and C5b (3.4.21.47)
Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt > Ac-Tyr-OEt (3.4.21.48)
Does not hydrolyze peptide amides (3.4.21.48)
Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B (3.4.21.5)
Hydrolysis of proteins in presence of ATP (3.4.21.53)
Cleavage of the Leu-|-Leu bond in synthetic tetradecapeptide renin substrate, to produce angiotensin I, but not active on natural angiotensinogen (3.4.21.54)
Also hydrolyzes Bz-Arg-p-nitroanilide (3.4.21.54)
Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa, but with more restricted specificity than trypsin (3.4.21.59)
Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin (3.4.21.6)
Cleavage of -Lys-Arg-|-Xaa- and -Arg-Arg-|-Xaa- bonds to process yeast alpha-factor pheromone and killer toxin precursors (3.4.21.61)
Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1 (3.4.21.62)
Hydrolyzes peptide amides (3.4.21.62)
Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin (3.4.21.68)
Degradation of blood coagulation factors Va and VIIIa (3.4.21.69)
Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa, higher selectivity than trypsin (3.4.21.7)
Converts fibrin into soluble products (3.4.21.7)
Preferential cleavage: Leu-|-Xaa, Met-|-Xaa and Phe-|-Xaa (3.4.21.71)
Hydrolyzes elastin (3.4.21.71)
Specific cleavage of Arg-|-Val bond in plasminogen to form plasmin (3.4.21.73)
Release of mature proteins from their proproteins by cleavage of -Arg- Xaa-Yaa-Arg-|-Zaa- bonds, where Xaa can be any amino acid and Yaa is Arg or Lys (3.4.21.75)
Releases albumin, complement component C3 and von Willebrand factor from their respective precursors (3.4.21.75)
Hydrolysis of proteins, including fibronectin, type IV collagen and nucleolin (3.4.21.78)
Preferential cleavage: -Arg-|-Xaa-, -Lys-|-Xaa- >> -Phe-|- Xaa- in small molecule substrates (3.4.21.78)
Preferential cleavage: -Asp-|-Xaa- >> -Asn-|-Xaa- > -Met-|-Xaa-, -Ser-|-Xaa- (3.4.21.79)
Hydrolysis of -Arg-|-Xaa- and -Lys-|-Xaa- bonds in oligopeptides, even when P1' residue is proline (3.4.21.83)
Hydrolysis of Ala-|-Gly bond in repressor LexA (3.4.21.88)
Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins (3.4.21.89)
Activation of trypsinogen by selective cleavage of 6-Lys-|-Ile-7 bond (3.4.21.9)
Hydrolysis of proteins to small peptides in the presence of ATP and magnesium (3.4.21.92)
Alpha-casein is the usual test substrate (3.4.21.92)
In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs) (3.4.21.92)
Release of protein hormones, neuropeptides and renin from their precursors, generally by hydrolysis of -Lys-Arg-|- bonds (3.4.21.93)
Release of protein hormones and neuropeptides from their precursors, generally by hydrolysis of -Lys-Arg-|- bonds (3.4.21.94)
Digestion of native collagen in the triple helical region at Xaa-|-Gly bonds (3.4.24.3)
With synthetic peptides, a preference is shown for Gly at P3 and P1', Pro and Ala at P2 and P2', and hydroxyproline, Ala or Arg at P3' (3.4.24.3)
Cleavage of interstitial collagens in the triple helical domain (3.4.24.34)
Unlike EC 3 (3.4.24.34)
24 (3.4.24.34)
7, this enzyme cleaves type III collagen more slowly than type I (3.4.24.34)
Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha-1(I) chain (3.4.24.7)
Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue (3.4.24.7)
Summaries
Gene Group (FlyBase)
TRIPEPTIDYL PEPTIDASES -
The huge exopeptidase, tripeptidyl-peptidase II, is a large homooligomeric complex involved in a large number of important biological processes. It is present in the cytosol of most eukaryotic cells, where it removes tripeptides from free amino termini of longer peptides with a broad specificity. Its main role appears to be general protein degradation, together with the proteasome. (Adapted from PMID:31108122.)
Protein Function (UniProtKB)
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). Efficiently cleaves Ala-Ala-Ala-polypeptide and Pro-Pro-Ala-polypeptide, Val-Leu-Lys-polypeptide only at high concentration. Does not cleave Ala-Phe-Pro-polypeptide nor Pro-Leu-Gly-polypeptide.
(UniProt, Q9V6K1)
Gene Model and Products
Number of Transcripts
4
Number of Unique Polypeptides
3

Please see the JBrowse view of Dmel\TppII for information on other features

To submit a correction to a gene model please use the Contact FlyBase form

Protein Domains (via Pfam)
Isoform displayed:
Pfam protein domains
InterPro name
classification
start
end
Protein Domains (via SMART)
Isoform displayed:
SMART protein domains
InterPro name
classification
start
end
Comments on Gene Model

Gene model reviewed during 5.49

Low-frequency RNA-Seq exon junction(s) not annotated.

Gene model reviewed during 5.53

Sequence Ontology: Class of Gene
Transcript Data
Annotated Transcripts
Name
FlyBase ID
RefSeq ID
Length (nt)
Assoc. CDS (aa)
FBtr0087775
4287
1354
FBtr0087774
4641
1441
FBtr0339755
4350
1375
FBtr0344199
4375
1354
Additional Transcript Data and Comments
Reported size (kB)
Comments
External Data
Crossreferences
Polypeptide Data
Annotated Polypeptides
Name
FlyBase ID
Predicted MW (kDa)
Length (aa)
Theoretical pI
RefSeq ID
GenBank
FBpp0086888
148.9
1354
6.98
FBpp0086887
158.7
1441
7.64
FBpp0308802
151.1
1375
7.18
FBpp0310608
148.9
1354
6.98
Polypeptides with Identical Sequences

The group(s) of polypeptides indicated below share identical sequence to each other.

1354 aa isoforms: TppII-PA, TppII-PF
Additional Polypeptide Data and Comments
Reported size (kDa)
Comments
External Data
Subunit Structure (UniProtKB)

Homooligomer; forms a complex of 6 MDa probably composed of 40 subunits. Forms a structure consisting of 2 segmented and twisted strands that form a spindle-shaped structure. Each strand is composed of 10 segments (a segment being a homodimer oriented head to head), stacking of these segments leads to the formation of a twisted single strand. 2 strands compose the fully assembled spindle.

(UniProt, Q9V6K1)
Linkouts
Sequences Consistent with the Gene Model
Nucleotide / Polypeptide Records
 
Mapped Features

Click to get a list of regulatory features (enhancers, TFBS, etc.) and gene disruptions (point mutations, indels, etc.) within or overlapping Dmel\TppII using the Feature Mapper tool.

External Data
Crossreferences
Eukaryotic Promoter Database - A collection of databases of experimentally validated promoters for selected model organisms.
Linkouts
Expression Data
Expression Summary Ribbons
Colored tiles in ribbon indicate that expression data has been curated by FlyBase for that anatomical location. Colorless tiles indicate that there is no curated data for that location.
For complete stage-specific expression data, view the modENCODE Development RNA-Seq section under High-Throughput Expression below.
Transcript Expression
Polypeptide Expression
mass spectroscopy
Stage
Tissue/Position (including subcellular localization)
Reference
Additional Descriptive Data
Marker for
 
Subcellular Localization
CV Term
Evidence
References
inferred from direct assay
inferred from direct assay
(assigned by UniProt )
Expression Deduced from Reporters
High-Throughput Expression Data
Associated Tools

GBrowse - Visual display of RNA-Seq signals

View Dmel\TppII in GBrowse 2
RNA-Seq by Region - Search RNA-Seq expression levels by exon or genomic region
Reference
See Gelbart and Emmert, 2013 for analysis details and data files for all genes.
Developmental Proteome: Life Cycle
Developmental Proteome: Embryogenesis
External Data and Images
Linkouts
BDGP expression data - Patterns of gene expression in Drosophila embryogenesis
FLIGHT - Cell culture data for RNAi and other high-throughput technologies
FlyAtlas - Adult expression by tissue, using Affymetrix Dros2 array
Fly-FISH - A database of Drosophila embryo and larvae mRNA localization patterns
Flygut - An atlas of the Drosophila adult midgut
Images
FlyExpress - Embryonic expression images (BDGP data)
  • Stages(s) 4-6
  • Stages(s) 7-8
  • Stages(s) 9-10
  • Stages(s) 11-12
  • Stages(s) 13-16
Alleles, Insertions, and Transgenic Constructs
Classical and Insertion Alleles ( 10 )
For All Classical and Insertion Alleles Show
 
Other relevant insertions
Transgenic Constructs ( 4 )
For All Alleles Carried on Transgenic Constructs Show
Transgenic constructs containing/affecting coding region of TppII
Transgenic constructs containing regulatory region of TppII
Deletions and Duplications ( 1 )
Phenotypes
For more details about a specific phenotype click on the relevant allele symbol.
Lethality
Allele
Other Phenotypes
Allele
Phenotype manifest in
Allele
Orthologs
Human Orthologs (via DIOPT v8.0)
Homo sapiens (Human) (15)
Species\Gene Symbol
Score
Best Score
Best Reverse Score
Alignment
Complementation?
Transgene?
15 of 15
Yes
Yes
1 of 15
No
No
1 of 15
No
No
1  
1 of 15
No
No
1 of 15
No
No
1  
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
Yes
1 of 15
No
Yes
1 of 15
No
Yes
1 of 15
No
Yes
Model Organism Orthologs (via DIOPT v8.0)
Mus musculus (laboratory mouse) (15)
Species\Gene Symbol
Score
Best Score
Best Reverse Score
Alignment
Complementation?
Transgene?
14 of 15
Yes
Yes
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
Yes
1 of 15
No
Yes
1 of 15
No
Yes
1 of 15
No
Yes
Rattus norvegicus (Norway rat) (15)
10 of 13
Yes
Yes
1 of 13
No
Yes
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
No
1 of 13
No
Yes
1 of 13
No
Yes
1 of 13
No
Yes
1 of 13
No
Yes
Xenopus tropicalis (Western clawed frog) (13)
9 of 12
Yes
Yes
1 of 12
No
No
1 of 12
No
No
1 of 12
No
No
1 of 12
No
No
1 of 12
No
No
1 of 12
No
No
1 of 12
No
No
1 of 12
No
No
1 of 12
No
No
1 of 12
No
No
1 of 12
No
Yes
1 of 12
No
Yes
Danio rerio (Zebrafish) (16)
14 of 15
Yes
Yes
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
1 of 15
No
Yes
1 of 15
No
Yes
1 of 15
No
Yes
1 of 15
No
Yes
Caenorhabditis elegans (Nematode, roundworm) (4)
14 of 15
Yes
Yes
1 of 15
No
No
1 of 15
No
No
1 of 15
No
No
Arabidopsis thaliana (thale-cress) (1)
7 of 9
Yes
Yes
Saccharomyces cerevisiae (Brewer's yeast) (4)
3 of 15
Yes
No
3 of 15
Yes
No
2 of 15
No
No
1 of 15
No
No
Schizosaccharomyces pombe (Fission yeast) (1)
10 of 12
Yes
Yes
Ortholog(s) in Drosophila Species (via OrthoDB v9.1) ( EOG091900ML )
Organism
Common Name
Gene
AAA Syntenic Ortholog
Multiple Dmel Genes in this Orthologous Group
Drosophila suzukii
Spotted wing Drosophila
Drosophila simulans
Drosophila sechellia
Drosophila erecta
Drosophila yakuba
Drosophila ananassae
Drosophila pseudoobscura pseudoobscura
Drosophila persimilis
Drosophila willistoni
Drosophila virilis
Drosophila mojavensis
Drosophila grimshawi
Orthologs in non-Drosophila Dipterans (via OrthoDB v9.1) ( EOG091501DE )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Musca domestica
House fly
Glossina morsitans
Tsetse fly
Mayetiola destructor
Hessian fly
Aedes aegypti
Yellow fever mosquito
Aedes aegypti
Yellow fever mosquito
Anopheles darlingi
American malaria mosquito
Anopheles gambiae
Malaria mosquito
Culex quinquefasciatus
Southern house mosquito
Orthologs in non-Dipteran Insects (via OrthoDB v9.1) ( EOG090W00X2 )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Bombyx mori
Silkmoth
Danaus plexippus
Monarch butterfly
Heliconius melpomene
Postman butterfly
Apis florea
Little honeybee
Apis mellifera
Western honey bee
Bombus impatiens
Common eastern bumble bee
Bombus terrestris
Buff-tailed bumblebee
Linepithema humile
Argentine ant
Megachile rotundata
Alfalfa leafcutting bee
Nasonia vitripennis
Parasitic wasp
Dendroctonus ponderosae
Mountain pine beetle
Tribolium castaneum
Red flour beetle
Pediculus humanus
Human body louse
Rhodnius prolixus
Kissing bug
Cimex lectularius
Bed bug
Acyrthosiphon pisum
Pea aphid
Acyrthosiphon pisum
Pea aphid
Zootermopsis nevadensis
Nevada dampwood termite
Orthologs in non-Insect Arthropods (via OrthoDB v9.1) ( EOG090X00VF )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Strigamia maritima
European centipede
Ixodes scapularis
Black-legged tick
Stegodyphus mimosarum
African social velvet spider
Stegodyphus mimosarum
African social velvet spider
Tetranychus urticae
Two-spotted spider mite
Daphnia pulex
Water flea
Orthologs in non-Arthropod Metazoa (via OrthoDB v9.1) ( EOG091G00P0 )
Organism
Common Name
Gene
Multiple Dmel Genes in this Orthologous Group
Strongylocentrotus purpuratus
Purple sea urchin
Ciona intestinalis
Vase tunicate
Gallus gallus
Domestic chicken
Paralogs
Paralogs (via DIOPT v8.0)
Drosophila melanogaster (Fruit fly) (4)
3 of 10
2 of 10
2 of 10
1 of 10
Human Disease Associations
FlyBase Human Disease Model Reports
    Disease Model Summary Ribbon
    Disease Ontology (DO) Annotations
    Models Based on Experimental Evidence ( 0 )
    Allele
    Disease
    Evidence
    References
    Potential Models Based on Orthology ( 0 )
    Human Ortholog
    Disease
    Evidence
    References
    Modifiers Based on Experimental Evidence ( 0 )
    Allele
    Disease
    Interaction
    References
    Disease Associations of Human Orthologs (via DIOPT v8.0 and OMIM)
    Note that ortholog calls supported by only 1 or 2 algorithms (DIOPT score < 3) are not shown.
    Homo sapiens (Human)
    Gene name
    Score
    OMIM
    OMIM Phenotype
    DO term
    Complementation?
    Transgene?
    Functional Complementation Data
    Functional complementation data is computed by FlyBase using a combination of the orthology data obtained from DIOPT and OrthoDB and the allele-level genetic interaction data curated from the literature.
    Interactions
    Summary of Physical Interactions
    esyN Network Diagram
    Show neighbor-neighbor interactions:
    Select Layout:
    Legend:
    Protein
    RNA
    Selected Interactor(s)
    Interactions Browser

    Please see the Physical Interaction reports below for full details
    protein-protein
    Physical Interaction
    Assay
    References
    Summary of Genetic Interactions
    esyN Network Diagram
    Starting gene(s)
    Interaction type
    Interacting gene(s)
    Reference
    Starting gene(s)
    Interaction type
    Interacting gene(s)
    Reference
    External Data
    Subunit Structure (UniProtKB)
    Homooligomer; forms a complex of 6 MDa probably composed of 40 subunits. Forms a structure consisting of 2 segmented and twisted strands that form a spindle-shaped structure. Each strand is composed of 10 segments (a segment being a homodimer oriented head to head), stacking of these segments leads to the formation of a twisted single strand. 2 strands compose the fully assembled spindle.
    (UniProt, Q9V6K1 )
    Linkouts
    BioGRID - A database of protein and genetic interactions.
    DroID - A comprehensive database of gene and protein interactions.
    InterologFinder - Protein-protein interactions (PPI) from both known and predicted PPI data sets.
    MIST (protein-protein) - An integrated Molecular Interaction Database
    Pathways
    Signaling Pathways (FlyBase)
    Metabolic Pathways
    External Data
    Linkouts
    Reactome - An open-source, open access, manually curated and peer-reviewed pathway database.
    Genomic Location and Detailed Mapping Data
    Chromosome (arm)
    2R
    Recombination map

    2-68

    Cytogenetic map
    Sequence location
    2R:13,152,885..13,159,141 [-]
    FlyBase Computed Cytological Location
    Cytogenetic map
    Evidence for location
    49F4-49F4
    Limits computationally determined from genome sequence between P{lacW}Psck07834&P{lacW}Su(z)2k06344 and P{EP}EP873EP873
    Experimentally Determined Cytological Location
    Cytogenetic map
    Notes
    References
    49F7-49F8
    49F-49F
    (determined by in situ hybridisation)
    49F7-49F8
    (determined by in situ hybridisation)
    Experimentally Determined Recombination Data
    Location
    Left of (cM)
    Right of (cM)
    Notes
    Stocks and Reagents
    Stocks (13)
    Genomic Clones (14)
     

    Please Note FlyBase no longer curates genomic clone accessions so this list may not be complete

    cDNA Clones (215)
     

    Please Note This section lists cDNAs and ESTs that fall within the genomic extent of the gene model, which may include cDNAs and ESTs of genes within introns, or of overlapping genes. Please see GBrowse for alignment of the cDNAs and ESTs to the gene model.

    cDNA clones, fully sequenced
    BDGP DGC clones
    Other clones
    Drosophila Genomics Resource Center cDNA clones

    For each fully sequenced cDNA the DGRC maintains various forms of the cDNA (e.g tagged or untagged) in several different host vectors for subsequent cloning and expression in Drosophila and Drosophila cell lines.

    cDNA Clones, End Sequenced (ESTs)
    RNAi and Array Information
    Linkouts
    DRSC - Results frm RNAi screens
    GenomeRNAi - A database for cell-based and in vivo RNAi phenotypes and reagents
    Antibody Information
    Laboratory Generated Antibodies
     
    Commercially Available Antibodies
     
    Other Information
    Relationship to Other Genes
    Source for database identify of
    Source for database merge of

    Source for merge of: TppII anon-WO0118547.127

    Additional comments

    Source for merge of TppII anon-WO0118547.127 was sequence comparison ( date:051113 ).

    Other Comments

    TppII proteins assemble into a giant proteolytic copmplex of 6 MDa, with a remarkable architecture consisting of two segmented and twisted strands that form a spindle-shaped structure. The building blocks of this complex are dimers, within which the 150kDa monomers are oriented head to head. Stacking of these dimers leads to the formation of twisted single strands, two of which comprise the fully assembled spindle. Reciprocal interactions of the N-terminal part of subunits from neighboring strands are probably involved in the formation of the native quaternary structure, lending the TppII spindle a stability higher than that of single strands.

    Area matching Drosophila EST AA978904.

    TppII has been cloned and characterised.

    Origin and Etymology
    Discoverer
    Etymology
    Identification
    External Crossreferences and Linkouts ( 60 )
    Sequence Crossreferences
    NCBI Gene - Gene integrates information from a wide range of species. A record may include nomenclature, Reference Sequences (RefSeqs), maps, pathways, variations, phenotypes, and links to genome-, phenotype-, and locus-specific resources worldwide.
    GenBank Nucleotide - A collection of sequences from several sources, including GenBank, RefSeq, TPA, and PDB.
    GenBank Protein - A collection of sequences from several sources, including translations from annotated coding regions in GenBank, RefSeq and TPA, as well as records from SwissProt, PIR, PRF, and PDB.
    RefSeq - A comprehensive, integrated, non-redundant, well-annotated set of reference sequences including genomic, transcript, and protein.
    UniProt/Swiss-Prot - Manually annotated and reviewed records of protein sequence and functional information
    UniProt/TrEMBL - Automatically annotated and unreviewed records of protein sequence and functional information
    Other crossreferences
    BDGP expression data - Patterns of gene expression in Drosophila embryogenesis
    Drosophila Genomics Resource Center - Drosophila Genomics Resource Center (DGRC) cDNA clones
    Eukaryotic Promoter Database - A collection of databases of experimentally validated promoters for selected model organisms.
    Fly-FISH - A database of Drosophila embryo and larvae mRNA localization patterns
    Flygut - An atlas of the Drosophila adult midgut
    GenomeRNAi - A database for cell-based and in vivo RNAi phenotypes and reagents
    iBeetle-Base - RNAi phenotypes in the red flour beetle (Tribolium castaneum)
    KEGG Genes - Molecular building blocks of life in the genomic space.
    modMine - A data warehouse for the modENCODE project
    SignaLink - A signaling pathway resource with multi-layered regulatory networks.
    Linkouts
    BioGRID - A database of protein and genetic interactions.
    DroID - A comprehensive database of gene and protein interactions.
    DRSC - Results frm RNAi screens
    FLIGHT - Cell culture data for RNAi and other high-throughput technologies
    FlyAtlas - Adult expression by tissue, using Affymetrix Dros2 array
    FlyCyc Genes - Genes from a BioCyc PGDB for Dmel
    FlyMine - An integrated database for Drosophila genomics
    InterologFinder - Protein-protein interactions (PPI) from both known and predicted PPI data sets.
    MIST (protein-protein) - An integrated Molecular Interaction Database
    Reactome - An open-source, open access, manually curated and peer-reviewed pathway database.
    Synonyms and Secondary IDs (13)
    Datasets (0)
    Study focus (0)
    Experimental Role
    Project
    Project Type
    Title
    References (69)