Q9BY84 (DUS16_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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)

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 Ref.7
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 inactivation of MAPK activity Traceable author statement Ref.1. Source: UniProtKB
Cellular component	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

63

Tyrosine-protein phosphatase

Sites

Active site

244

1

Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue

446

1

Phosphoserine; by MAPK1 Ref.5

Modified residue

501

1

Phosphoserine Ref.7

Natural variations

Natural variant

23

1

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

VAR_051753

Natural variant

366

1

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

VAR_051754

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

665

Helix Strand Turn

Details...

Beta strand

6 – 11

6

Helix

12 – 19

8

Beta strand

20 – 32

13

Helix

34 – 39

6

Beta strand

40 – 51

12

Helix

52 – 59

8

Beta strand

60 – 64

5

Helix

65 – 71

7

Beta strand

72 – 102

31

Helix

103 – 114

12

Beta strand

115 – 123

9

Helix

124 – 131

8

Sequences

	Sequence		Length	Mass (Da)
	Q9BY84 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 1BD853FF08460DFF	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

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: 11489891] [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: 14586399] [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: 11214970] [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: 15489334] [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: 12794087] [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: 15888437] [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: 18669648] [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 specifity 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	[»]

ProteinModelPortal

Q9BY84.

SMR

Q9BY84. Positions 5-300.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9BY84. 1 interaction.

STRING

Q9BY84.

PTM databases

PhosphoSite

Q9BY84.

Polymorphism databases

DMDM

20137933.

Proteomic databases

PRIDE

Q9BY84.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000228862; ENSP00000228862; ENSG00000111266.

GeneID

80824.

KEGG

hsa:80824.

UCSC

uc001rao.1. human.

Organism-specific databases

CTD

80824.

GeneCards

GC12M012628.

H-InvDB

HIX0010437.

HGNC

HGNC:17909. DUSP16.

HPA

HPA020326.

MIM

607175. gene.

neXtProt

NX_Q9BY84.

PharmGKB

PA38475.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00590000082869.

HOGENOM

HBG717224.

HOVERGEN

HBG005541.

InParanoid

Q9BY84.

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

InterPro

IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR008343. MAPK_phosph.
IPR001763. Rhodanese-like.
IPR000387. Tyr/Dual-specificity_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]

Gene3D

G3DSA:3.40.250.10. Rhodanese-like. 1 hit.

KO

K04459.

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

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:	January 25, 2012
This is version 96 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.