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Q9BY84

- DUS16_HUMAN

UniProt

Q9BY84 - DUS16_HUMAN

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Protein
Dual specificity protein phosphatase 16
Gene
DUSP16, KIAA1700, MKP7
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Dual specificity protein phosphatase involved in the inactivation of MAP kinases. Dephosphorylates MAPK10 bound to ARRB2.2 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei244 – 2441Phosphocysteine intermediate By similarity

GO - Molecular functioni

  1. MAP kinase tyrosine/serine/threonine phosphatase activity Source: InterPro
  2. phosphoprotein phosphatase activity Source: UniProtKB
  3. protein tyrosine phosphatase activity Source: UniProtKB-EC
  4. protein tyrosine/serine/threonine phosphatase activity Source: RefGenome
Complete GO annotation...

GO - Biological processi

  1. MAPK export from nucleus Source: UniProtKB
  2. MAPK phosphatase export from nucleus, leptomycin B sensitive Source: UniProtKB
  3. dephosphorylation Source: UniProtKB
  4. inactivation of MAPK activity Source: UniProtKB
  5. protein dephosphorylation Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

SignaLinkiQ9BY84.

Names & Taxonomyi

Protein namesi
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 namesi
Name:DUSP16
Synonyms:KIAA1700, MKP7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:17909. DUSP16.

Subcellular locationi

Cytoplasm. Nucleus. Cytoplasmic vesicle
Note: After dissociation upon AGTR stimulation, re-associates with ARRB2 on endocytic vesicles.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38475.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 665665Dual specificity protein phosphatase 16
PRO_0000094826Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei446 – 4461Phosphoserine; by MAPK11 Publication
Modified residuei501 – 5011Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated at Ser-446 by MAPK1/ERK2, which prevents its degradation, and thereby stabilizes it and blocks JNK MAPK activity.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9BY84.
PaxDbiQ9BY84.
PRIDEiQ9BY84.

PTM databases

PhosphoSiteiQ9BY84.

Expressioni

Gene expression databases

ArrayExpressiQ9BY84.
BgeeiQ9BY84.
CleanExiHS_DUSP16.
GenevestigatoriQ9BY84.

Organism-specific databases

HPAiHPA020326.

Interactioni

Subunit structurei

Interacts with ARRB2.1 Publication

Protein-protein interaction databases

BioGridi123321. 7 interactions.
IntActiQ9BY84. 1 interaction.
STRINGi9606.ENSP00000228862.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 103
Helixi12 – 198
Beta strandi21 – 244
Beta strandi26 – 305
Helixi34 – 396
Helixi52 – 598
Helixi65 – 717
Beta strandi83 – 886
Helixi95 – 973
Helixi103 – 11412
Beta strandi118 – 1214
Helixi124 – 1318
Helixi133 – 1353

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2VSWX-ray2.20A/B5-150[»]
3TG3X-ray2.68A/B/C/D5-138[»]
ProteinModelPortaliQ9BY84.
SMRiQ9BY84. Positions 5-138, 158-328.

Miscellaneous databases

EvolutionaryTraceiQ9BY84.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 137116Rhodanese
Add
BLAST
Domaini227 – 28963Tyrosine-protein phosphatase
Add
BLAST

Sequence similaritiesi

Contains 1 rhodanese domain.

Phylogenomic databases

eggNOGiCOG2453.
HOGENOMiHOG000082452.
HOVERGENiHBG005541.
InParanoidiQ9BY84.
KOiK04459.
OMAiQMEFGES.
OrthoDBiEOG747PJD.
PhylomeDBiQ9BY84.
TreeFamiTF105122.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR000340. 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]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PRINTSiPR01764. MAPKPHPHTASE.
SMARTiSM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
SSF52821. SSF52821. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9BY84-1 [UniParc]FASTAAdd to Basket

« Hide

MAHEMIGTQI VTERLVALLE SGTEKVLLID SRPFVEYNTS HILEAININC    50
SKLMKRRLQQ DKVLITELIQ HSAKHKVDID CSQKVVVYDQ SSQDVASLSS 100
DCFLTVLLGK LEKSFNSVHL LAGGFAEFSR CFPGLCEGKS TLVPTCISQP 150
CLPVANIGPT RILPNLYLGC QRDVLNKELM QQNGIGYVLN ASNTCPKPDF 200
IPESHFLRVP VNDSFCEKIL PWLDKSVDFI EKAKASNGCV LVHCLAGISR 250
SATIAIAYIM KRMDMSLDEA YRFVKEKRPT ISPNFNFLGQ LLDYEKKIKN 300
QTGASGPKSK LKLLHLEKPN EPVPAVSEGG QKSETPLSPP CADSATSEAA 350
GQRPVHPASV PSVPSVQPSL LEDSPLVQAL SGLHLSADRL EDSNKLKRSF 400
SLDIKSVSYS ASMAASLHGF SSSEDALEYY KPSTTLDGTN KLCQFSPVQE 450
LSEQTPETSP DKEEASIPKK LQTARPSDSQ SKRLHSVRTS SSGTAQRSLL 500
SPLHRSGSVE DNYHTSFLFG LSTSQQHLTK SAGLGLKGWH SDILAPQTST 550
PSLTSSWYFA TESSHFYSAS AIYGGSASYS AYSCSQLPTC GDQVYSVRRR 600
QKPSDRADSR RSWHEESPFE KQFKRRSCQM EFGESIMSEN RSREELGKVG 650
SQSSFSGSME IIEVS 665
Length:665
Mass (Da):73,102
Last modified:June 1, 2001 - v1
Checksum:i1BD853FF08460DFF
GO

Sequence cautioni

The sequence BAB21791.1 differs from that shown. Reason: Erroneous initiation.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti23 – 231T → M.
Corresponds to variant rs36049447 [ dbSNP | Ensembl ].
VAR_051753
Natural varianti366 – 3661V → M.
Corresponds to variant rs3809199 [ dbSNP | Ensembl ].
VAR_051754

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB052156 mRNA. Translation: BAB40814.1.
AF506796 mRNA. Translation: AAN75120.1.
AB051487 mRNA. Translation: BAB21791.1. Different initiation.
BC109235 mRNA. Translation: AAI09236.1.
CCDSiCCDS8650.1.
RefSeqiNP_085143.1. NM_030640.2.
XP_006719218.1. XM_006719155.1.
UniGeneiHs.536535.

Genome annotation databases

EnsembliENST00000228862; ENSP00000228862; ENSG00000111266.
GeneIDi80824.
KEGGihsa:80824.
UCSCiuc001ran.2. human.

Polymorphism databases

DMDMi20137933.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB052156 mRNA. Translation: BAB40814.1 .
AF506796 mRNA. Translation: AAN75120.1 .
AB051487 mRNA. Translation: BAB21791.1 . Different initiation.
BC109235 mRNA. Translation: AAI09236.1 .
CCDSi CCDS8650.1.
RefSeqi NP_085143.1. NM_030640.2.
XP_006719218.1. XM_006719155.1.
UniGenei Hs.536535.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali Q9BY84.
SMRi Q9BY84. Positions 5-138, 158-328.
ModBasei Search...

Protein-protein interaction databases

BioGridi 123321. 7 interactions.
IntActi Q9BY84. 1 interaction.
STRINGi 9606.ENSP00000228862.

PTM databases

PhosphoSitei Q9BY84.

Polymorphism databases

DMDMi 20137933.

Proteomic databases

MaxQBi Q9BY84.
PaxDbi Q9BY84.
PRIDEi Q9BY84.

Protocols and materials databases

DNASUi 80824.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000228862 ; ENSP00000228862 ; ENSG00000111266 .
GeneIDi 80824.
KEGGi hsa:80824.
UCSCi uc001ran.2. human.

Organism-specific databases

CTDi 80824.
GeneCardsi GC12M012628.
HGNCi HGNC:17909. DUSP16.
HPAi HPA020326.
MIMi 607175. gene.
neXtProti NX_Q9BY84.
PharmGKBi PA38475.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2453.
HOGENOMi HOG000082452.
HOVERGENi HBG005541.
InParanoidi Q9BY84.
KOi K04459.
OMAi QMEFGES.
OrthoDBi EOG747PJD.
PhylomeDBi Q9BY84.
TreeFami TF105122.

Enzyme and pathway databases

SignaLinki Q9BY84.

Miscellaneous databases

ChiTaRSi DUSP16. human.
EvolutionaryTracei Q9BY84.
GeneWikii DUSP16.
GenomeRNAii 80824.
NextBioi 71232.
PROi Q9BY84.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9BY84.
Bgeei Q9BY84.
CleanExi HS_DUSP16.
Genevestigatori Q9BY84.

Family and domain databases

Gene3Di 3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProi IPR000340. 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 ]
PANTHERi PTHR10159. PTHR10159. 1 hit.
Pfami PF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view ]
PRINTSi PR01764. MAPKPHPHTASE.
SMARTi SM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
SSF52821. SSF52821. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiDUS16_HUMAN
AccessioniPrimary (citable) accession number: Q9BY84
Secondary accession number(s): Q547C7, Q9C0G3
Entry historyi
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 statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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