Dual specificity protein phosphatase 16

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Q9BY84 (DUS16_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 108. History...

Clusters with 100%, 90%, 50% identity |

Documents (6) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Dual specificity protein phosphatase 16
EC=3.1.3.16
EC=3.1.3.48

Alternative name(s):
Mitogen-activated protein kinase phosphatase 7
Short name=MAP kinase phosphatase 7
Short name=MKP-7

Gene names

Name:	DUSP16
Synonyms:	KIAA1700, MKP7

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	665 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Dual specificity protein phosphatase involved in the inactivation of MAP kinases. Dephosphorylates MAPK10 bound to ARRB2. Ref.1 Ref.6
Catalytic activity	Protein tyrosine phosphate + H₂O = protein tyrosine + phosphate. A phosphoprotein + H₂O = a protein + phosphate.
Subunit structure	Interacts with ARRB2. Ref.6
Subcellular location	Cytoplasm. Nucleus. Cytoplasmic vesicle. Note: After dissociation upon AGTR stimulation, re-associates with ARRB2 on endocytic vesicles. Ref.1 Ref.6
Post-translational modification	Phosphorylated at Ser-446 by MAPK1/ERK2, which prevents its degradation, and thereby stabilizes it and blocks JNK MAPK activity. Ref.5
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily. Contains 1 rhodanese domain. Contains 1 tyrosine-protein phosphatase domain.
Sequence caution	The sequence BAB21791.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoplasmic vesicle Nucleus
Coding sequence diversity	Polymorphism
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	MAPK export from nucleus Traceable author statement Ref.1. Source: UniProtKB MAPK phosphatase export from nucleus, leptomycin B sensitive Traceable author statement Ref.1. Source: UniProtKB peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Traceable author statement Ref.1. Source: UniProtKB cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Traceable author statement Ref.1. Source: UniProtKB
Molecular_function	MAP kinase tyrosine/serine/threonine phosphatase activity Inferred from Biological aspect of Ancestor. Source: RefGenome protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 665

665

Dual specificity protein phosphatase 16

PRO_0000094826

Regions

Domain

22 – 137

116

Rhodanese

Domain

227 – 289

Tyrosine-protein phosphatase

Sites

Active site

244

Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue

446

Phosphoserine; by MAPK1 Ref.5

Modified residue

501

Phosphoserine Ref.7

Natural variations

Natural variant

T → M.
Corresponds to variant rs36049447 [ dbSNP | Ensembl ].

VAR_051753

Natural variant

366

V → M.
Corresponds to variant rs3809199 [ dbSNP | Ensembl ].

VAR_051754

Secondary structure

665

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q9BY84 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 1BD853FF08460DFF
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FASTA

665

73,102

        10         20         30         40         50         60 
MAHEMIGTQI VTERLVALLE SGTEKVLLID SRPFVEYNTS HILEAININC SKLMKRRLQQ 

        70         80         90        100        110        120 
DKVLITELIQ HSAKHKVDID CSQKVVVYDQ SSQDVASLSS DCFLTVLLGK LEKSFNSVHL 

       130        140        150        160        170        180 
LAGGFAEFSR CFPGLCEGKS TLVPTCISQP CLPVANIGPT RILPNLYLGC QRDVLNKELM 

       190        200        210        220        230        240 
QQNGIGYVLN ASNTCPKPDF IPESHFLRVP VNDSFCEKIL PWLDKSVDFI EKAKASNGCV 

       250        260        270        280        290        300 
LVHCLAGISR SATIAIAYIM KRMDMSLDEA YRFVKEKRPT ISPNFNFLGQ LLDYEKKIKN 

       310        320        330        340        350        360 
QTGASGPKSK LKLLHLEKPN EPVPAVSEGG QKSETPLSPP CADSATSEAA GQRPVHPASV 

       370        380        390        400        410        420 
PSVPSVQPSL LEDSPLVQAL SGLHLSADRL EDSNKLKRSF SLDIKSVSYS ASMAASLHGF 

       430        440        450        460        470        480 
SSSEDALEYY KPSTTLDGTN KLCQFSPVQE LSEQTPETSP DKEEASIPKK LQTARPSDSQ 

       490        500        510        520        530        540 
SKRLHSVRTS SSGTAQRSLL SPLHRSGSVE DNYHTSFLFG LSTSQQHLTK SAGLGLKGWH 

       550        560        570        580        590        600 
SDILAPQTST PSLTSSWYFA TESSHFYSAS AIYGGSASYS AYSCSQLPTC GDQVYSVRRR 

       610        620        630        640        650        660 
QKPSDRADSR RSWHEESPFE KQFKRRSCQM EFGESIMSEN RSREELGKVG SQSSFSGSME 


IIEVS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"MKP-7, a novel mitogen-activated protein kinase phosphatase, functions as a shuttle protein." Masuda K., Shima H., Watanabe M., Kikuchi K. J. Biol. Chem. 276:39002-39011(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION.
[2]	"MAPK phosphatase DUSP16/MKP-7, a candidate tumor suppressor for chromosome region 12p12-13, reduces BCR-ABL-induced transformation." Hoornaert I., Marynen P., Goris J., Sciot R., Baens M. Oncogene 22:7728-7736(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Bone marrow.
[3]	"Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O. DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	"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].
[5]	"Activation of ERK induces phosphorylation of MAPK phosphatase-7, a JNK specific phosphatase, at Ser-446." Masuda K., Shima H., Katagiri C., Kikuchi K. J. Biol. Chem. 278:32448-32456(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-446.
[6]	"Dynamic interaction between the dual specificity phosphatase MKP7 and the JNK3 scaffold protein beta-arrestin 2." Willoughby E.A., Collins M.K. J. Biol. Chem. 280:25651-25658(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ARRB2.
[7]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-501, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"The structure of the rhodanese domain of the human 2 dual specificity phosphatase 16." Structural genomics consortium (SGC) Submitted (JUN-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 5-150.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AB052156 mRNA. Translation: BAB40814.1.
AF506796 mRNA. Translation: AAN75120.1.
AB051487 mRNA. Translation: BAB21791.1. Different initiation.
BC109235 mRNA. Translation: AAI09236.1.

IPI

IPI00028428.

RefSeq

NP_085143.1. NM_030640.2.

UniGene

Hs.536535.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2VSW	X-ray	2.20	A/B	5-150	[»]
3TG3	X-ray	2.68	A/B/C/D	5-138	[»]

ProteinModelPortal

Q9BY84.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9BY84. 1 interaction.

STRING

9606.ENSP00000228862.

PTM databases

PhosphoSite

Q9BY84.

Polymorphism databases

DMDM

20137933.

Proteomic databases

PaxDb

Q9BY84.

PRIDE

Q9BY84.

Protocols and materials databases

DNASU

80824.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000228862; ENSP00000228862; ENSG00000111266.

GeneID

80824.

KEGG

hsa:80824.

UCSC

uc001ran.2. human.

Organism-specific databases

CTD

80824.

GeneCards

GC12M012628.

HGNC

HGNC:17909. DUSP16.

HPA

HPA020326.

MIM

607175. gene.

neXtProt

NX_Q9BY84.

PharmGKB

PA38475.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2453.

HOGENOM

HOG000082452.

HOVERGEN

HBG005541.

InParanoid

Q9BY84.

K04459.

OMA

KLCQFSP.

OrthoDB

EOG434W69.

PhylomeDB

Q9BY84.

Enzyme and pathway databases

Pathway_Interaction_DB

p38alphabetapathway. Regulation of p38-alpha and p38-beta.

Gene expression databases

ArrayExpress

Q9BY84.

Bgee

Q9BY84.

CleanEx

HS_DUSP16.

Genevestigator

Q9BY84.

GermOnline

ENSG00000111266. Homo sapiens.

Family and domain databases

Gene3D

3.40.250.10. 1 hit.

InterPro

IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR008343. MKP.
IPR001763. Rhodanese-like_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]

PANTHER

PTHR10159. PTHR10159. 1 hit.

Pfam

PF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]

PRINTS

PR01764. MAPKPHPHTASE.

SMART

SM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view]

SUPFAM

SSF52821. Rhodanese-like. 1 hit.

PROSITE

PS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

DUSP16. human.

EvolutionaryTrace

Q9BY84.

GenomeRNAi

80824.

NextBio

71232.

SOURCE

Search...

Entry information

Entry name

DUS16_HUMAN

Accession

Primary (citable) accession number: Q9BY84
Secondary accession number(s): Q547C7, Q9C0G3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 23, 2002
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 108 of the entry and version 1 of the sequence. [Complete history]

Entry status

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.

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Human chromosome 12: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Natural variations

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents