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Q9BY84 (DUS16_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length665 AA.
Sequence statusComplete.
Protein existenceEvidence 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 protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 665665Dual specificity protein phosphatase 16
PRO_0000094826

Regions

Domain22 – 137116Rhodanese
Domain227 – 28963Tyrosine-protein phosphatase

Sites

Active site2441Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue4461Phosphoserine; by MAPK1 Ref.5
Modified residue5011Phosphoserine Ref.7

Natural variations

Natural variant231T → M.
Corresponds to variant rs36049447 [ dbSNP | Ensembl ].
VAR_051753
Natural variant3661V → M.
Corresponds to variant rs3809199 [ dbSNP | Ensembl ].
VAR_051754

Secondary structure

........................... 665
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9BY84 [UniParc].

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

FASTA66573,102
        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' 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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.
CCDSCCDS8650.1.
RefSeqNP_085143.1. NM_030640.2.
XP_006719218.1. XM_006719155.1.
UniGeneHs.536535.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2VSWX-ray2.20A/B5-150[»]
3TG3X-ray2.68A/B/C/D5-138[»]
ProteinModelPortalQ9BY84.
SMRQ9BY84. Positions 5-138, 158-328.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123321. 7 interactions.
IntActQ9BY84. 1 interaction.
STRING9606.ENSP00000228862.

PTM databases

PhosphoSiteQ9BY84.

Polymorphism databases

DMDM20137933.

Proteomic databases

MaxQBQ9BY84.
PaxDbQ9BY84.
PRIDEQ9BY84.

Protocols and materials databases

DNASU80824.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000228862; ENSP00000228862; ENSG00000111266.
GeneID80824.
KEGGhsa:80824.
UCSCuc001ran.2. human.

Organism-specific databases

CTD80824.
GeneCardsGC12M012628.
HGNCHGNC:17909. DUSP16.
HPAHPA020326.
MIM607175. gene.
neXtProtNX_Q9BY84.
PharmGKBPA38475.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2453.
HOGENOMHOG000082452.
HOVERGENHBG005541.
InParanoidQ9BY84.
KOK04459.
OMAQMEFGES.
OrthoDBEOG747PJD.
PhylomeDBQ9BY84.
TreeFamTF105122.

Enzyme and pathway databases

SignaLinkQ9BY84.

Gene expression databases

ArrayExpressQ9BY84.
BgeeQ9BY84.
CleanExHS_DUSP16.
GenevestigatorQ9BY84.

Family and domain databases

Gene3D3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProIPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR008343. MKP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR001763. Rhodanese-like_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PRINTSPR01764. MAPKPHPHTASE.
SMARTSM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMSSF52799. SSF52799. 1 hit.
SSF52821. SSF52821. 1 hit.
PROSITEPS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDUSP16. human.
EvolutionaryTraceQ9BY84.
GeneWikiDUSP16.
GenomeRNAi80824.
NextBio71232.
PROQ9BY84.
SOURCESearch...

Entry information

Entry nameDUS16_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

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

Human chromosome 12

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