DUSP5

Functionⁱ

Dual specificity protein phosphatase; active with phosphotyrosine, phosphoserine and phosphothreonine residues. The highest relative activity is toward ERK1.1 Publication

Catalytic activityⁱ

H₂O
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
O-phospho-L-seryl-[protein]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
=
L-seryl-[protein]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+
phosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.1
  "A novel dual specificity phosphatase induced by serum stimulation and heat shock."
  Ishibashi T., Bottaro D.P., Michieli P., Kelley C.A., Aaronson S.A.
  J. Biol. Chem. 269:29897-29902(1994) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY.
EC:3.1.3.16
1 Publication
Manual assertion based on experiment inⁱ
- Ref.1
  "A novel dual specificity phosphatase induced by serum stimulation and heat shock."
  Ishibashi T., Bottaro D.P., Michieli P., Kelley C.A., Aaronson S.A.
  J. Biol. Chem. 269:29897-29902(1994) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
H₂O
zoom
+
O-phospho-L-seryl-[protein]
O-phospho-L-serine residue
zoom
=
L-seryl-[protein]
L-serine residue
zoom
+
phosphate
zoom
H₂O
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
O-phospho-L-threonyl-[protein]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
=
L-threonyl-[protein]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+
phosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
1 Publication
Manual assertion based on experiment inⁱ
- Ref.1
  "A novel dual specificity phosphatase induced by serum stimulation and heat shock."
  Ishibashi T., Bottaro D.P., Michieli P., Kelley C.A., Aaronson S.A.
  J. Biol. Chem. 269:29897-29902(1994) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY.
EC:3.1.3.16
1 Publication
Manual assertion based on experiment inⁱ
- Ref.1
  "A novel dual specificity phosphatase induced by serum stimulation and heat shock."
  Ishibashi T., Bottaro D.P., Michieli P., Kelley C.A., Aaronson S.A.
  J. Biol. Chem. 269:29897-29902(1994) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
H₂O
zoom
+
O-phospho-L-threonyl-[protein]
O-phospho-L-threonine residue
zoom
=
L-threonyl-[protein]
L-threonine residue
zoom
+
phosphate
zoom
H₂O
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
O-phospho-L-tyrosyl-[protein]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
=
L-tyrosyl-[protein]
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
+
phosphate
Search proteins in UniProtKB for this molecule.
Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
PROSITE-ProRule annotation
Manual assertion according to rulesⁱ
- PROSITE-ProRule:PRU10044
1 Publication
Manual assertion based on experiment inⁱ
- Ref.1
  "A novel dual specificity phosphatase induced by serum stimulation and heat shock."
  Ishibashi T., Bottaro D.P., Michieli P., Kelley C.A., Aaronson S.A.
  J. Biol. Chem. 269:29897-29902(1994) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY.
EC:3.1.3.48
PROSITE-ProRule annotation
Manual assertion according to rulesⁱ
- PROSITE-ProRule:PRU10044
1 Publication
Manual assertion based on experiment inⁱ
- Ref.1
  "A novel dual specificity phosphatase induced by serum stimulation and heat shock."
  Ishibashi T., Bottaro D.P., Michieli P., Kelley C.A., Aaronson S.A.
  J. Biol. Chem. 269:29897-29902(1994) [PubMed] [Europe PMC] [Abstract]
  Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
. Show »« Hide
H₂O
zoom
+
O-phospho-L-tyrosyl-[protein]
L-tyrosine-phosphate residue
zoom
=
L-tyrosyl-[protein]
L-tyrosine residue
zoom
+
phosphate
zoom

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Active siteⁱ	263	Phosphocysteine intermediatePROSITE-ProRule annotation1 Publication		1

GO - Molecular functionⁱ

MAP kinase tyrosine/serine/threonine phosphatase activity
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
phosphatase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 24531476
protein tyrosine/serine/threonine phosphatase activity
Source: UniProtKB
Inferred from direct assayⁱ
- 7961985
protein tyrosine phosphatase activity
Source: ProtInc
Traceable author statementⁱ
- 7961985

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

activation of MAPK activity Source: Reactome
dephosphorylation
Source: UniProtKB
Inferred from direct assayⁱ
- 24531476
inactivation of MAPK activity
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635
MAPK cascade Source: Reactome
peptidyl-threonine dephosphorylation
Source: UniProtKB
Inferred from direct assayⁱ
- 7961985
peptidyl-tyrosine dephosphorylation
Source: UniProtKB
Inferred from direct assayⁱ
- 7961985
protein dephosphorylation
Source: ProtInc
Traceable author statementⁱ
- 7961985

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase, Protein phosphatase

Molecular function

Hydrolase, Protein phosphatase

Enzyme and pathway databases

Reactomeⁱ	R-HSA-112409 RAF-independent MAPK1/3 activation R-HSA-5675221 Negative regulation of MAPK pathway
SignaLinkⁱ	Q16690
SIGNORⁱ	Q16690

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Dual specificity protein phosphatase 5 (EC:3.1.3.161 Publication, EC:3.1.3.481 Publication) Alternative name(s): Dual specificity protein phosphatase hVH3
Gene namesⁱ	Name:DUSP5 Synonyms:VH3
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 10

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000138166.5
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:3071 DUSP5
MIMⁱ	603069 gene
neXtProtⁱ	NX_Q16690

Keywords - Cellular componentⁱ

Nucleus

Pathology & Biotechⁱ

Organism-specific databases

DisGeNET More...DisGeNETⁱ	1847
Open Targets More...OpenTargetsⁱ	ENSG00000138166
PharmGKBⁱ	PA27528

Chemistry databases

ChEMBLⁱ	CHEMBL1250380

ChEMBLⁱ

CHEMBL1250380

Polymorphism and mutation databases

BioMutaⁱ	DUSP5
DMDMⁱ	215273975

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000094802	1 – 384	Dual specificity protein phosphatase 5Add BLAST		384

Proteomic databases

EPDⁱ	Q16690
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	Q16690
PaxDbⁱ	Q16690
PeptideAtlas More...PeptideAtlasⁱ	Q16690
PRIDEⁱ	Q16690
ProteomicsDBⁱ	61034

PTM databases

DEPODⁱ	Q16690
iPTMnetⁱ	Q16690
PhosphoSitePlusⁱ	Q16690

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000138166 Expressed in 196 organ(s), highest expression level in ectocervix
CleanExⁱ	HS_DUSP5
Genevisibleⁱ	Q16690 HS

Interactionⁱ

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
MAPK1	P28482	3	EBI-7487376,EBI-959949

With

Entry

#Exp.

IntAct

Notes

MAPK1

P28482

3

EBI-7487376,EBI-959949

Protein-protein interaction databases

BioGridⁱ	108180, 17 interactors
IntActⁱ	Q16690, 1 interactor
Molecular INTeraction database More...MINTⁱ	Q16690
STRINGⁱ	9606.ENSP00000358596

Chemistry databases

BindingDBⁱ

Q16690

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	180 – 183	Combined sources	4
Beta strandⁱ	186 – 190	Combined sources	5
Helixⁱ	191 – 194	Combined sources	4
Helixⁱ	197 – 203	Combined sources	7
Beta strandⁱ	207 – 210	Combined sources	4
Beta strandⁱ	223 – 227	Combined sources	5
Helixⁱ	239 – 241	Combined sources	3
Helixⁱ	242 – 254	Combined sources	13
Beta strandⁱ	259 – 268	Combined sources	10
Helixⁱ	269 – 282	Combined sources	14
Helixⁱ	286 – 296	Combined sources	11
Helixⁱ	304 – 317	Combined sources	14

Show more details

3D structure databases

ProteinModelPortalⁱ	Q16690
SMRⁱ	Q16690
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q16690

EvolutionaryTraceⁱ

Q16690

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	19 – 141	RhodanesePROSITE-ProRule annotationAdd BLAST		123
Domainⁱ	180 – 384	Tyrosine-protein phosphataseAdd BLAST		205

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	53 – 74	Nuclear localization signalSequence analysisAdd BLAST		22

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	79 – 82	Poly-Gly		4

Sequence similaritiesⁱ

Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.Curated

Phylogenomic databases

eggNOGⁱ	KOG1716 Eukaryota COG2453 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00940000159529
HOVERGENⁱ	HBG007347
InParanoidⁱ	Q16690
KEGG Orthology (KO) More...KOⁱ	K04459
OMAⁱ	CVREKGG
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0249
PhylomeDBⁱ	Q16690
TreeFamⁱ	TF105122

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00127 DSPc, 1 hit
Gene3Dⁱ	3.40.250.10, 1 hit 3.90.190.10, 1 hit
InterProⁱ	View protein in InterPro IPR000340 Dual-sp_phosphatase_cat-dom IPR024950 DUSP IPR008343 MKP IPR029021 Prot-tyrosine_phosphatase-like IPR001763 Rhodanese-like_dom IPR036873 Rhodanese-like_dom_sf IPR016130 Tyr_Pase_AS IPR003595 Tyr_Pase_cat IPR000387 TYR_PHOSPHATASE_dom IPR020422 TYR_PHOSPHATASE_DUAL_dom
PANTHERⁱ	PTHR10159 PTHR10159, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00782 DSPc, 1 hit PF00581 Rhodanese, 1 hit
PIRSFⁱ	PIRSF000939 MAPK_Ptase, 1 hit
PRINTSⁱ	PR01764 MAPKPHPHTASE
SMARTⁱ	View protein in SMART SM00195 DSPc, 1 hit SM00404 PTPc_motif, 1 hit SM00450 RHOD, 1 hit
SUPFAMⁱ	SSF52799 SSF52799, 1 hit SSF52821 SSF52821, 1 hit
PROSITEⁱ	View protein in PROSITE PS50206 RHODANESE_3, 1 hit PS00383 TYR_PHOSPHATASE_1, 1 hit PS50056 TYR_PHOSPHATASE_2, 1 hit PS50054 TYR_PHOSPHATASE_DUAL, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Q16690-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MKVTSLDGRQ LRKMLRKEAA ARCVVLDCRP YLAFAASNVR GSLNVNLNSV 
        60         70         80         90        100
VLRRARGGAV SARYVLPDEA ARARLLQEGG GGVAAVVVLD QGSRHWQKLR 
       110        120        130        140        150
EESAARVVLT SLLACLPAGP RVYFLKGGYE TFYSEYPECC VDVKPISQEK 
       160        170        180        190        200
IESERALISQ CGKPVVNVSY RPAYDQGGPV EILPFLYLGS AYHASKCEFL 
       210        220        230        240        250
ANLHITALLN VSRRTSEACA THLHYKWIPV EDSHTADISS HFQEAIDFID 
       260        270        280        290        300
CVREKGGKVL VHCEAGISRS PTICMAYLMK TKQFRLKEAF DYIKQRRSMV 
       310        320        330        340        350
SPNFGFMGQL LQYESEILPS TPNPQPPSCQ GEAAGSSLIG HLQTLSPDMQ 
       360        370        380 
GAYCTFPASV LAPVPTHSTV SELSRSPVAT ATSC

Length:384

Mass (Da):42,047

Last modified:November 25, 2008 - v2

Checksum:ⁱ2E4B2938F886CB4E

GO

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	9 – 11	RQL → GHV in AAA64693 (PubMed:7961985).Curated	3
Sequence conflictⁱ	71	A → R in AAA64693 (PubMed:7961985).Curated	1
Sequence conflictⁱ	105 – 106	AR → F in AAA64693 (PubMed:7961985).Curated	2
Sequence conflictⁱ	220	A → M in AAA64693 (PubMed:7961985).Curated	1
Sequence conflictⁱ	220	A → M in AAB06261 (PubMed:7836374).Curated	1
Sequence conflictⁱ	220	A → M in AAH62545 (PubMed:15489334).Curated	1
Sequence conflictⁱ	382	T → Q in AAA64693 (PubMed:7961985).Curated	1

Natural variant

Feature key	Position(s)	DescriptionActions	Length
Natural variantⁱVAR_020298	154	E → D. Corresponds to variant dbSNP:rs2282238Ensembl.	1
Natural variantⁱVAR_059777	220	A → T. Corresponds to variant dbSNP:rs1889566Ensembl.	1
Natural variantⁱVAR_059778	220	A → V. Corresponds to variant dbSNP:rs1889565Ensembl.	1
Natural variantⁱVAR_047368	322	P → L. Corresponds to variant dbSNP:rs35101549Ensembl.	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U15932 mRNA Translation: AAA64693.2 U16996 mRNA Translation: AAB06261.1 AL355512 Genomic DNA No translation available. BC062545 mRNA Translation: AAH62545.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS7566.1
PIRⁱ	I38890
NCBI Reference Sequences More...RefSeqⁱ	NP_004410.3, NM_004419.3
UniGeneⁱ	Hs.2128

Genome annotation databases

Ensemblⁱ	ENST00000369583; ENSP00000358596; ENSG00000138166
GeneIDⁱ	1847
KEGGⁱ	hsa:1847
UCSC genome browser More...UCSCⁱ	uc001kzd.4 human

Keywords - Coding sequence diversityⁱ

Polymorphism

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q16690	Dual specificity protein phosphatase		MACMU		384	UniRef90_Q16690
Dual specificity protein phosphatase		CERAT		384
Dual specificity protein phosphatase		GORGO		384
Dual specificity protein phosphatase		PONAB		384
Dual specificity protein phosphatase		MACNE		384
+6

Protein	Similar proteins		Species	Score	Length	Source
Q16690	Dual specificity protein phosphatase		PONAB		384	UniRef50_Q16690
Dual specificity protein phosphatase		MACMU		384
Dual specificity protein phosphatase		MACNE		384
Dual specificity protein phosphatase		NOMLE		384
Dual specificity protein phosphatase		MACFA		384
+19

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U15932 mRNA Translation: AAA64693.2 U16996 mRNA Translation: AAB06261.1 AL355512 Genomic DNA No translation available. BC062545 mRNA Translation: AAH62545.1
CCDSⁱ	CCDS7566.1
PIRⁱ	I38890
RefSeqⁱ	NP_004410.3, NM_004419.3
UniGeneⁱ	Hs.2128

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	2G6Z	X-ray	2.70	A/B/C	178-384	[»]
ProteinModelPortalⁱ	Q16690
SMRⁱ	Q16690
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	108180, 17 interactors
IntActⁱ	Q16690, 1 interactor
MINTⁱ	Q16690
STRINGⁱ	9606.ENSP00000358596

Chemistry databases

BindingDBⁱ	Q16690
ChEMBLⁱ	CHEMBL1250380

PTM databases

DEPODⁱ	Q16690
iPTMnetⁱ	Q16690
PhosphoSitePlusⁱ	Q16690

Polymorphism and mutation databases

BioMutaⁱ	DUSP5
DMDMⁱ	215273975

Proteomic databases

EPDⁱ	Q16690
MaxQBⁱ	Q16690
PaxDbⁱ	Q16690
PeptideAtlasⁱ	Q16690
PRIDEⁱ	Q16690
ProteomicsDBⁱ	61034

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	1847
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000369583; ENSP00000358596; ENSG00000138166
GeneIDⁱ	1847
KEGGⁱ	hsa:1847
UCSCⁱ	uc001kzd.4 human

Organism-specific databases

CTDⁱ	1847
DisGeNETⁱ	1847
EuPathDBⁱ	HostDB:ENSG00000138166.5
GeneCardsⁱ	DUSP5
H-InvDBⁱ	HIX0001673
HGNCⁱ	HGNC:3071 DUSP5
MIMⁱ	603069 gene
neXtProtⁱ	NX_Q16690
OpenTargetsⁱ	ENSG00000138166
PharmGKBⁱ	PA27528
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG1716 Eukaryota COG2453 LUCA
GeneTreeⁱ	ENSGT00940000159529
HOVERGENⁱ	HBG007347
InParanoidⁱ	Q16690
KOⁱ	K04459
OMAⁱ	CVREKGG
OrthoDBⁱ	EOG091G0249
PhylomeDBⁱ	Q16690
TreeFamⁱ	TF105122

Enzyme and pathway databases

Reactomeⁱ	R-HSA-112409 RAF-independent MAPK1/3 activation R-HSA-5675221 Negative regulation of MAPK pathway
SignaLinkⁱ	Q16690
SIGNORⁱ	Q16690

Miscellaneous databases

ChiTaRSⁱ	DUSP5 human
EvolutionaryTraceⁱ	Q16690
GeneWikiⁱ	DUSP5
GenomeRNAiⁱ	1847
Protein Ontology More...PROⁱ	PR:Q16690
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000138166 Expressed in 196 organ(s), highest expression level in ectocervix
CleanExⁱ	HS_DUSP5
Genevisibleⁱ	Q16690 HS

Family and domain databases

CDDⁱ	cd00127 DSPc, 1 hit
Gene3Dⁱ	3.40.250.10, 1 hit 3.90.190.10, 1 hit
InterProⁱ	View protein in InterPro IPR000340 Dual-sp_phosphatase_cat-dom IPR024950 DUSP IPR008343 MKP IPR029021 Prot-tyrosine_phosphatase-like IPR001763 Rhodanese-like_dom IPR036873 Rhodanese-like_dom_sf IPR016130 Tyr_Pase_AS IPR003595 Tyr_Pase_cat IPR000387 TYR_PHOSPHATASE_dom IPR020422 TYR_PHOSPHATASE_DUAL_dom
PANTHERⁱ	PTHR10159 PTHR10159, 1 hit
Pfamⁱ	View protein in Pfam PF00782 DSPc, 1 hit PF00581 Rhodanese, 1 hit
PIRSFⁱ	PIRSF000939 MAPK_Ptase, 1 hit
PRINTSⁱ	PR01764 MAPKPHPHTASE
SMARTⁱ	View protein in SMART SM00195 DSPc, 1 hit SM00404 PTPc_motif, 1 hit SM00450 RHOD, 1 hit
SUPFAMⁱ	SSF52799 SSF52799, 1 hit SSF52821 SSF52821, 1 hit
PROSITEⁱ	View protein in PROSITE PS50206 RHODANESE_3, 1 hit PS00383 TYR_PHOSPHATASE_1, 1 hit PS50056 TYR_PHOSPHATASE_2, 1 hit PS50054 TYR_PHOSPHATASE_DUAL, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	DUS5_HUMAN
Accessionⁱ	Q16690Primary (citable) accession number: Q16690 Secondary accession number(s): Q12997, Q5T603
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
	Last sequence update:	November 25, 2008
	Last modified:	December 5, 2018
	This is version 170 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program
Disclaimer	Any 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

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

PDB cross-references
Index of Protein Data Bank (PDB) cross-references
SIMILARITY comments
Index of protein domains and families
Human chromosome 10
Human chromosome 10: entries, gene names and cross-references to MIM
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q16690 (DUS5_HUMAN)

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Dual specificity protein phosphatase 5

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Nucleus

Nucleus

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Motif

Compositional bias

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Experimental Info

Natural variant

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Catalytic activityⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ