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Q9JLY7

- DUS14_MOUSE

UniProt

Q9JLY7 - DUS14_MOUSE

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Protein

Dual specificity protein phosphatase 14

Gene

Dusp14

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

  1. MAP kinase tyrosine/serine/threonine phosphatase activity Source: InterPro
  2. poly(A) RNA binding Source: Ensembl
  3. protein tyrosine/serine/threonine phosphatase activity Source: RefGenome
  4. protein tyrosine phosphatase activity Source: UniProtKB-EC

GO - Biological processi

  1. peptidyl-tyrosine dephosphorylation Source: RefGenome
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: Chromosome 11

Organism-specific databases

MGIiMGI:1927168. Dusp14.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. 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.
GenevestigatoriQ9JLY7.

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.
OMAiRSQGFFH.
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_006533796.1.
XP_006533860.1. XM_006533797.1.
XP_006533861.1. XM_006533798.1.
XP_006533862.1. XM_006533799.1.
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 .
CCDSi CCDS25182.1.
RefSeqi NP_062793.2. NM_019819.3.
XP_006533859.1. XM_006533796.1.
XP_006533860.1. XM_006533797.1.
XP_006533861.1. XM_006533798.1.
XP_006533862.1. XM_006533799.1.
UniGenei Mm.240885.
Mm.475342.

3D structure databases

ProteinModelPortali Q9JLY7.
SMRi Q9JLY7. Positions 24-191.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q9JLY7.

Proteomic databases

MaxQBi Q9JLY7.
PaxDbi Q9JLY7.
PRIDEi Q9JLY7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000018792 ; ENSMUSP00000018792 ; ENSMUSG00000018648 .
ENSMUST00000100705 ; ENSMUSP00000098271 ; ENSMUSG00000018648 .
ENSMUST00000108101 ; ENSMUSP00000103736 ; ENSMUSG00000018648 .
ENSMUST00000164891 ; ENSMUSP00000130624 ; ENSMUSG00000018648 .
GeneIDi 56405.
KEGGi mmu:56405.
UCSCi uc007kqc.1. mouse.

Organism-specific databases

CTDi 11072.
MGIi MGI:1927168. Dusp14.

Phylogenomic databases

eggNOGi COG2453.
GeneTreei ENSGT00760000118853.
HOGENOMi HOG000233766.
HOVERGENi HBG051422.
InParanoidi Q9JLY7.
KOi K14165.
OMAi RSQGFFH.
OrthoDBi EOG7PK90H.
PhylomeDBi Q9JLY7.
TreeFami TF316009.

Miscellaneous databases

ChiTaRSi Dusp14. mouse.
NextBioi 312530.
PROi Q9JLY7.
SOURCEi Search...

Gene expression databases

Bgeei Q9JLY7.
CleanExi MM_DUSP14.
ExpressionAtlasi Q9JLY7. baseline and differential.
Genevestigatori Q9JLY7.

Family and domain databases

Gene3Di 3.90.190.10. 1 hit.
InterProi IPR020417. 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 ]
PANTHERi PTHR10159. PTHR10159. 1 hit.
Pfami PF00782. DSPc. 1 hit.
[Graphical view ]
PRINTSi PR01908. ADSPHPHTASE.
PR01910. ADSPHPHTASEB.
SMARTi SM00195. DSPc. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
PROSITEi 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. "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: November 26, 2014
This is version 108 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