Q9BY84 · DUS16_HUMAN
- ProteinDual specificity protein phosphatase 16
- GeneDUSP16
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids665 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Dual specificity protein phosphatase involved in the inactivation of MAP kinases. Dephosphorylates MAPK10 bound to ARRB2.
Catalytic activity
- H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 244 | Phosphocysteine intermediate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytoplasmic vesicle | |
Cellular Component | cytosol | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | JUN kinase binding | |
Molecular Function | MAP kinase tyrosine phosphatase activity | |
Molecular Function | MAP kinase tyrosine/serine/threonine phosphatase activity | |
Molecular Function | mitogen-activated protein kinase binding | |
Molecular Function | mitogen-activated protein kinase p38 binding | |
Molecular Function | myosin phosphatase activity | |
Molecular Function | phosphatase activity | |
Molecular Function | phosphoprotein phosphatase activity | |
Molecular Function | protein carrier chaperone | |
Molecular Function | protein tyrosine/threonine phosphatase activity | |
Biological Process | dephosphorylation | |
Biological Process | negative regulation of MAPK cascade |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDual specificity protein phosphatase 16
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9BY84
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: After dissociation upon AGTR stimulation, re-associates with ARRB2 on endocytic vesicles.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_051753 | 23 | in dbSNP:rs36049447 | |||
Sequence: T → M | ||||||
Natural variant | VAR_051754 | 366 | in dbSNP:rs3809199 | |||
Sequence: V → M |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,189 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, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000094826 | 1-665 | UniProt | Dual specificity protein phosphatase 16 | |||
Sequence: MAHEMIGTQIVTERLVALLESGTEKVLLIDSRPFVEYNTSHILEAININCSKLMKRRLQQDKVLITELIQHSAKHKVDIDCSQKVVVYDQSSQDVASLSSDCFLTVLLGKLEKSFNSVHLLAGGFAEFSRCFPGLCEGKSTLVPTCISQPCLPVANIGPTRILPNLYLGCQRDVLNKELMQQNGIGYVLNASNTCPKPDFIPESHFLRVPVNDSFCEKILPWLDKSVDFIEKAKASNGCVLVHCLAGISRSATIAIAYIMKRMDMSLDEAYRFVKEKRPTISPNFNFLGQLLDYEKKIKNQTGASGPKSKLKLLHLEKPNEPVPAVSEGGQKSETPLSPPCADSATSEAAGQRPVHPASVPSVPSVQPSLLEDSPLVQALSGLHLSADRLEDSNKLKRSFSLDIKSVSYSASMAASLHGFSSSEDALEYYKPSTTLDGTNKLCQFSPVQELSEQTPETSPDKEEASIPKKLQTARPSDSQSKRLHSVRTSSSGTAQRSLLSPLHRSGSVEDNYHTSFLFGLSTSQQHLTKSAGLGLKGWHSDILAPQTSTPSLTSSWYFATESSHFYSASAIYGGSASYSAYSCSQLPTCGDQVYSVRRRQKPSDRADSRRSWHEESPFEKQFKRRSCQMEFGESIMSENRSREELGKVGSQSSFSGSMEIIEVS | |||||||
Modified residue | 55 | UniProt | (Microbial infection) N6-acetyllysine; by EIS | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 401 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 446 | UniProt | Phosphoserine; by MAPK1 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 446 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 501 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 501 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 506 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 612 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 627 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylated at Ser-446 by MAPK1/ERK2, which prevents its degradation, and thereby stabilizes it and blocks JNK MAPK activity.
(Microbial infection) Acetylated at Lys-55 by the M.tuberculosis Eis protein; this leads to the inhibition of JNK-dependent autophagy, phagosome maturation, and ROS (reactive oxygen species) generation for enhanced intracellular survival of M.tuberculosis.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with ARRB2.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9BY84 | MAPK14 Q16539 | 3 | EBI-3443956, EBI-73946 | |
BINARY | Q9BY84 | MAPK8 P45983-4 | 3 | EBI-3443956, EBI-18121963 | |
BINARY | Q9BY84 | MAPK9 P45984 | 8 | EBI-3443956, EBI-713568 | |
BINARY | Q9BY84 | WFS1 O76024 | 3 | EBI-3443956, EBI-720609 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 22-137 | Rhodanese | ||||
Sequence: GTEKVLLIDSRPFVEYNTSHILEAININCSKLMKRRLQQDKVLITELIQHSAKHKVDIDCSQKVVVYDQSSQDVASLSSDCFLTVLLGKLEKSFNSVHLLAGGFAEFSRCFPGLCE | ||||||
Domain | 158-300 | Tyrosine-protein phosphatase | ||||
Sequence: GPTRILPNLYLGCQRDVLNKELMQQNGIGYVLNASNTCPKPDFIPESHFLRVPVNDSFCEKILPWLDKSVDFIEKAKASNGCVLVHCLAGISRSATIAIAYIMKRMDMSLDEAYRFVKEKRPTISPNFNFLGQLLDYEKKIKN | ||||||
Region | 321-368 | Disordered | ||||
Sequence: EPVPAVSEGGQKSETPLSPPCADSATSEAAGQRPVHPASVPSVPSVQP | ||||||
Region | 449-505 | Disordered | ||||
Sequence: QELSEQTPETSPDKEEASIPKKLQTARPSDSQSKRLHSVRTSSSGTAQRSLLSPLHR | ||||||
Compositional bias | 472-505 | Polar residues | ||||
Sequence: QTARPSDSQSKRLHSVRTSSSGTAQRSLLSPLHR | ||||||
Region | 597-665 | Disordered | ||||
Sequence: VRRRQKPSDRADSRRSWHEESPFEKQFKRRSCQMEFGESIMSENRSREELGKVGSQSSFSGSMEIIEVS | ||||||
Compositional bias | 598-628 | Basic and acidic residues | ||||
Sequence: RRRQKPSDRADSRRSWHEESPFEKQFKRRSC | ||||||
Compositional bias | 647-665 | Polar residues | ||||
Sequence: GKVGSQSSFSGSMEIIEVS |
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9BY84-1
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.
- Name1
- Length665
- Mass (Da)73,102
- Last updated2001-06-01 v1
- Checksum1BD853FF08460DFF
Q9BY84-2
- Name2
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F5H5X4 | F5H5X4_HUMAN | DUSP16 | 25 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_056981 | 124-143 | in isoform 2 | |||
Sequence: GFAEFSRCFPGLCEGKSTLV → ADAAEWDWLCVKCQQYLSKA | ||||||
Alternative sequence | VSP_056982 | 144-665 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 472-505 | Polar residues | ||||
Sequence: QTARPSDSQSKRLHSVRTSSSGTAQRSLLSPLHR | ||||||
Compositional bias | 598-628 | Basic and acidic residues | ||||
Sequence: RRRQKPSDRADSRRSWHEESPFEKQFKRRSC | ||||||
Compositional bias | 647-665 | Polar residues | ||||
Sequence: GKVGSQSSFSGSMEIIEVS |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB052156 EMBL· GenBank· DDBJ | BAB40814.1 EMBL· GenBank· DDBJ | mRNA | ||
AF506796 EMBL· GenBank· DDBJ | AAN75120.1 EMBL· GenBank· DDBJ | mRNA | ||
AY038927 EMBL· GenBank· DDBJ | AAK69770.1 EMBL· GenBank· DDBJ | mRNA | ||
AB051487 EMBL· GenBank· DDBJ | BAB21791.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC007619 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC092824 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC109235 EMBL· GenBank· DDBJ | AAI09236.1 EMBL· GenBank· DDBJ | mRNA |