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Q9JLY7 (DUS14_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
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 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 names
Name:Dusp14
Synonyms:Mkp6
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length198 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

A phosphoprotein + H2O = a protein + phosphate.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class dual specificity subfamily.

Contains 1 tyrosine-protein phosphatase domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 198198Dual specificity protein phosphatase 14
PRO_0000094823

Regions

Domain91 – 15666Tyrosine-protein phosphatase

Sites

Active site1111Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue71Phosphoserine By similarity
Modified residue81Phosphothreonine By similarity

Experimental info

Sequence conflict381R → K in AAF28862. Ref.1
Sequence conflict1501P → H in AAF28862. Ref.1
Sequence conflict1601D → E in AAF28862. Ref.1
Sequence conflict1631S → R in AAF28862. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9JLY7 [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: 5C2B4210E886DFCF

FASTA19822,311
        10         20         30         40         50         60 
MSSRGHSTLP RTLMAPRMIS EGDIGGIAQI TSSLFLGRAS VASNWHLLQA RGITCVINAT 

        70         80         90        100        110        120 
IEIPNFNWPQ FEYVKVPLAD IPHAPIRLYF DTVADKIHSV SKKHGATLVH CAAGVSRSAT 

       130        140        150        160        170        180 
LCIAYLMKFH NLCLLEAYNW VKARRPVIRP NLGFWRQLID YESQLFGKSS VKMVQTPYGI 

       190 
IPDVYEKESR HLMPYWGI

« Hide

References

« Hide 'large scale' references
[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: 11123293] [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. expand/collapse author list , 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: 16141072] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF120113 mRNA. Translation: AAF28862.1.
AK009744 mRNA. Translation: BAB26474.1.
BC002130 mRNA. Translation: AAH02130.1.
IPIIPI00124876.
RefSeqNP_062793.2. NM_019819.3.
UniGeneMm.240885.
Mm.475342.

3D structure databases

ProteinModelPortalQ9JLY7.
SMRQ9JLY7. Positions 24-191.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9JLY7.

PTM databases

PhosphoSiteQ9JLY7.

Proteomic databases

PRIDEQ9JLY7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000018792; ENSMUSP00000018792; ENSMUSG00000018648.
ENSMUST00000100705; ENSMUSP00000098271; ENSMUSG00000018648.
ENSMUST00000108101; ENSMUSP00000103736; ENSMUSG00000018648.
ENSMUST00000164891; ENSMUSP00000130624; ENSMUSG00000018648.
GeneID56405.
KEGGmmu:56405.

Organism-specific databases

CTD11072.
MGIMGI:1927168. Dusp14.

Phylogenomic databases

GeneTreeENSGT00590000082789.
HOGENOMHBG717377.
HOVERGENHBG051422.
InParanoidQ9JLY7.
OMAHAWVKAR.
OrthoDBEOG48PMM7.
PhylomeDBQ9JLY7.

Gene expression databases

ArrayExpressQ9JLY7.
BgeeQ9JLY7.
CleanExMM_DUSP14.
GenevestigatorQ9JLY7.
GermOnlineENSMUSG00000018648. Mus musculus.

Family and domain databases

InterProIPR020417. Dual-sp_phosphatase.
IPR000340. Dual-sp_phosphatase_cat-dom.
IPR020420. Dual-sp_phosphatase_famB.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR000387. Tyr/Dual-specificity_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
KOK04459.
PfamPF00782. DSPc. 1 hit.
[Graphical view]
PRINTSPR01908. ADSPHPHTASE.
PR01910. ADSPHPHTASEB.
SMARTSM00195. DSPc. 1 hit.
[Graphical view]
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio312530.
SOURCESearch...

Entry information

Entry nameDUS14_MOUSE
AccessionPrimary (citable) accession number: Q9JLY7
Secondary accession number(s): Q9D715
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: January 23, 2002
Last modified: November 16, 2011
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents