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Protein

Dual specificity protein phosphatase 14

Gene

Dusp14

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Involved in the inactivation of MAP kinases. Dephosphorylates ERK, JNK and p38 MAP-kinases.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei111 – 1111Phosphocysteine intermediatePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity protein phosphatase 14 (EC:3.1.3.16, EC:3.1.3.48)
Alternative name(s):
Mitogen-activated protein kinase phosphatase 6
Short name:
MAP kinase phosphatase 6
Short name:
MKP-6
Gene namesi
Name:Dusp14
Synonyms:Mkp6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1927168. Dusp14.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • nucleus Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 198198Dual specificity protein phosphatase 14PRO_0000094823Add
BLAST

Proteomic databases

MaxQBiQ9JLY7.
PaxDbiQ9JLY7.
PRIDEiQ9JLY7.

PTM databases

PhosphoSiteiQ9JLY7.

Expressioni

Gene expression databases

BgeeiQ9JLY7.
CleanExiMM_DUSP14.
ExpressionAtlasiQ9JLY7. baseline and differential.
GenevisibleiQ9JLY7. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000018792.

Structurei

3D structure databases

ProteinModelPortaliQ9JLY7.
SMRiQ9JLY7. Positions 24-191.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini91 – 15666Tyrosine-protein phosphataseAdd
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118853.
HOGENOMiHOG000233766.
HOVERGENiHBG051422.
InParanoidiQ9JLY7.
KOiK14165.
OMAiHVEYVKV.
OrthoDBiEOG7PK90H.
PhylomeDBiQ9JLY7.
TreeFamiTF316009.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR020417. Atypical_DUSP.
IPR020420. Atypical_DUSP_famB.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSiPR01908. ADSPHPHTASE.
PR01910. ADSPHPHTASEB.
SMARTiSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9JLY7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSRGHSTLP RTLMAPRMIS EGDIGGIAQI TSSLFLGRAS VASNWHLLQA
60 70 80 90 100
RGITCVINAT IEIPNFNWPQ FEYVKVPLAD IPHAPIRLYF DTVADKIHSV
110 120 130 140 150
SKKHGATLVH CAAGVSRSAT LCIAYLMKFH NLCLLEAYNW VKARRPVIRP
160 170 180 190
NLGFWRQLID YESQLFGKSS VKMVQTPYGI IPDVYEKESR HLMPYWGI
Length:198
Mass (Da):22,311
Last modified:January 23, 2002 - v2
Checksum:i5C2B4210E886DFCF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 381R → K in AAF28862 (PubMed:11123293).Curated
Sequence conflicti150 – 1501P → H in AAF28862 (PubMed:11123293).Curated
Sequence conflicti160 – 1601D → E in AAF28862 (PubMed:11123293).Curated
Sequence conflicti163 – 1631S → R in AAF28862 (PubMed:11123293).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF120113 mRNA. Translation: AAF28862.1.
AK009744 mRNA. Translation: BAB26474.1.
BC002130 mRNA. Translation: AAH02130.1.
CCDSiCCDS25182.1.
RefSeqiNP_062793.2. NM_019819.3.
XP_006533859.1. XM_006533796.2.
XP_006533860.1. XM_006533797.2.
XP_006533861.1. XM_006533798.2.
XP_006533862.1. XM_006533799.2.
UniGeneiMm.240885.
Mm.475342.

Genome annotation databases

EnsembliENSMUST00000018792; ENSMUSP00000018792; ENSMUSG00000018648.
ENSMUST00000100705; ENSMUSP00000098271; ENSMUSG00000018648.
ENSMUST00000108101; ENSMUSP00000103736; ENSMUSG00000018648.
ENSMUST00000164891; ENSMUSP00000130624; ENSMUSG00000018648.
GeneIDi56405.
KEGGimmu:56405.
UCSCiuc007kqc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF120113 mRNA. Translation: AAF28862.1.
AK009744 mRNA. Translation: BAB26474.1.
BC002130 mRNA. Translation: AAH02130.1.
CCDSiCCDS25182.1.
RefSeqiNP_062793.2. NM_019819.3.
XP_006533859.1. XM_006533796.2.
XP_006533860.1. XM_006533797.2.
XP_006533861.1. XM_006533798.2.
XP_006533862.1. XM_006533799.2.
UniGeneiMm.240885.
Mm.475342.

3D structure databases

ProteinModelPortaliQ9JLY7.
SMRiQ9JLY7. Positions 24-191.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000018792.

PTM databases

PhosphoSiteiQ9JLY7.

Proteomic databases

MaxQBiQ9JLY7.
PaxDbiQ9JLY7.
PRIDEiQ9JLY7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000018792; ENSMUSP00000018792; ENSMUSG00000018648.
ENSMUST00000100705; ENSMUSP00000098271; ENSMUSG00000018648.
ENSMUST00000108101; ENSMUSP00000103736; ENSMUSG00000018648.
ENSMUST00000164891; ENSMUSP00000130624; ENSMUSG00000018648.
GeneIDi56405.
KEGGimmu:56405.
UCSCiuc007kqc.1. mouse.

Organism-specific databases

CTDi11072.
MGIiMGI:1927168. Dusp14.

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118853.
HOGENOMiHOG000233766.
HOVERGENiHBG051422.
InParanoidiQ9JLY7.
KOiK14165.
OMAiHVEYVKV.
OrthoDBiEOG7PK90H.
PhylomeDBiQ9JLY7.
TreeFamiTF316009.

Miscellaneous databases

ChiTaRSiDusp14. mouse.
NextBioi312530.
PROiQ9JLY7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JLY7.
CleanExiMM_DUSP14.
ExpressionAtlasiQ9JLY7. baseline and differential.
GenevisibleiQ9JLY7. MM.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR020417. Atypical_DUSP.
IPR020420. Atypical_DUSP_famB.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSiPR01908. ADSPHPHTASE.
PR01910. ADSPHPHTASEB.
SMARTiSM00195. DSPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Negative-feedback regulation of CD28 costimulation by a novel mitogen-activated protein kinase phosphatase, MKP6."
    Marti F., Krause A., Post N.H., Lyddane C., Dupont B., Sadelain M., King P.D.
    J. Immunol. 166:197-206(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Tongue.
  3. "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].

Entry informationi

Entry nameiDUS14_MOUSE
AccessioniPrimary (citable) accession number: Q9JLY7
Secondary accession number(s): Q9D715
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: January 23, 2002
Last modified: June 24, 2015
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.