Q9H0I9 · TKTL2_HUMAN
- ProteinTransketolase-like protein 2
- GeneTKTL2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids626 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Plays an essential role in total transketolase activity and cell proliferation in cancer cells; after transfection with anti-TKTL1 siRNA, total transketolase activity dramatically decreases and proliferation was significantly inhibited in cancer cells. Plays a pivotal role in carcinogenesis.
Catalytic activity
- D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate
Cofactor
Protein has several cofactor binding sites:
Ca2+ (UniProtKB | Rhea| CHEBI:29108 )
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Co2+ (UniProtKB | Rhea| CHEBI:48828 )
Note: Binds 1 Mg2+ ion per subunit. Can also utilize other divalent metal cations, such as Ca2+, Mn2+ and Co2+.
Note: Binds 1 thiamine pyrophosphate per subunit.
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 41 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 78 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 124-126 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: GSL | ||||||
Binding site | 156 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 157 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 186 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 186 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 188 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 248 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 262 | substrate | ||||
Sequence: H | ||||||
Binding site | 262 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Site | 262 | Important for catalytic activity | ||||
Sequence: H | ||||||
Binding site | 349 | substrate | ||||
Sequence: S | ||||||
Active site | 370 | Proton donor | ||||
Sequence: E | ||||||
Binding site | 370 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 396 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 420 | substrate | ||||
Sequence: H | ||||||
Binding site | 428 | substrate | ||||
Sequence: D | ||||||
Binding site | 432 | thiamine diphosphate (UniProtKB | ChEBI) | ||||
Sequence: Q |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | metal ion binding | |
Molecular Function | thiamine pyrophosphate binding | |
Molecular Function | transketolase activity |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTransketolase-like protein 2
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9H0I9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_031990 | 442 | in dbSNP:rs3811750 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_031991 | 590 | in dbSNP:rs11735477 | |||
Sequence: Q → H |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 868 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000285200 | 1-626 | Transketolase-like protein 2 | |||
Sequence: MMANDAKPDVKTVQVLRDTANRLRIHSIRATCASGSGQLTSCCSAAEVVSVLFFHTMKYKQTDPEHPDNDRFILSRGHAAPILYAAWVEVGDISESDLLNLRKLHSDLERHPTPRLPFVDVATGSLGQGLGTACGMAYTGKYLDKASYRVFCLMGDGESSEGSVWEAFAFASHYNLDNLVAVFDVNRLGQSGPAPLEHGADIYQNCCEAFGWNTYLVDGHDVEALCQAFWQASQVKNKPTAIVAKTFKGRGIPNIEDAENWHGKPVPKERADAIVKLIESQIQTNENLIPKSPVEDSPQISITDIKMTSPPAYKVGDKIATQKTYGLALAKLGRANERVIVLSGDTMNSTFSEIFRKEHPERFIECIIAEQNMVSVALGCATRGRTIAFAGAFAAFFTRAFDQLRMGAISQANINLIGSHCGVSTGEDGVSQMALEDLAMFRSIPNCTVFYPSDAISTEHAIYLAANTKGMCFIRTSQPETAVIYTPQENFEIGQAKVVRHGVNDKVTVIGAGVTLHEALEAADHLSQQGISVRVIDPFTIKPLDAATIISSAKATGGRVITVEDHYREGGIGEAVCAAVSREPDILVHQLAVSGVPQRGKTSELLDMFGISTRHIIAAVTLTLMK |
Proteomic databases
PTM databases
Expression
Tissue specificity
Overexpressed in hepatoma cancer cells.
Gene expression databases
Organism-specific databases
Structure
Sequence
- Sequence statusComplete
- Length626
- Mass (Da)67,877
- Last updated2001-03-01 v1
- Checksum446C4EC81EDC0EA4
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 54 | in Ref. 2; BAB71427 | ||||
Sequence: F → L | ||||||
Sequence conflict | 302 | in Ref. 4; AAH28707 | ||||
Sequence: I → V | ||||||
Sequence conflict | 311 | in Ref. 4; AAH28707 | ||||
Sequence: P → H | ||||||
Sequence conflict | 406 | in Ref. 2; BAB71427 | ||||
Sequence: M → I |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL136779 EMBL· GenBank· DDBJ | CAB66713.1 EMBL· GenBank· DDBJ | mRNA | ||
AK057325 EMBL· GenBank· DDBJ | BAB71427.1 EMBL· GenBank· DDBJ | mRNA | ||
CR533560 EMBL· GenBank· DDBJ | CAG38591.1 EMBL· GenBank· DDBJ | mRNA | ||
BC028707 EMBL· GenBank· DDBJ | AAH28707.4 EMBL· GenBank· DDBJ | mRNA | ||
BC125101 EMBL· GenBank· DDBJ | AAI25102.1 EMBL· GenBank· DDBJ | mRNA | ||
BC142943 EMBL· GenBank· DDBJ | AAI42944.1 EMBL· GenBank· DDBJ | mRNA |