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Q8BFV3 (DUS4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 92. 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

Names and origin

Protein namesRecommended name:
Dual specificity protein phosphatase 4

EC=3.1.3.16
EC=3.1.3.48
Gene names
Name:Dusp4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length398 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Regulates mitogenic signal transduction by dephosphorylating both Thr and Tyr residues on MAP kinases ERK1 and ERK2 By similarity.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

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

Subunit structure

Hollow spherical complex composed of 24 subunits with pseudooctahedral symmetry, has a tetramer as the basic unit By similarity.

Subcellular location

Nucleus By similarity.

Post-translational modification

Phosphorylation in the C-terminus by ERK1/2 inhibits proteasomal degradation and stabilizes the protein By similarity.

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 398398Dual specificity protein phosphatase 4
PRO_0000094799

Regions

Domain45 – 163119Rhodanese
Domain201 – 398198Tyrosine-protein phosphatase

Sites

Active site2841Phosphocysteine intermediate By similarity

Amino acid modifications

Modified residue3901Phosphoserine; by MAPK By similarity
Modified residue3951Phosphoserine; by MAPK By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8BFV3 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: E9542B1ACD48097B

FASTA39843,372
        10         20         30         40         50         60 
MVTMEELREM DCSVLKRLMN RDENGGGGSA GGNGSGSHGA LGLLSGGKCL LLDCRPFLAH 

        70         80         90        100        110        120 
SAGYIRGSVN VRCNTIVRRR AKGSVSLEQI LPAEEEVRAR LRSGLYSAVI VYDERSPRAE 

       130        140        150        160        170        180 
SLREDSTVSL VVQALRRNAE RTDICLLKGG YERFSSEYPE FCSKTKALAA IPPPVPPSTN 

       190        200        210        220        230        240 
ESLDLGCSSC GTPLHDQGGP VEILPFLYLG SAYHAARRDM LDALGITALL NVSSDCPNHF 

       250        260        270        280        290        300 
EGHYQYKCIP VEDNHKADIS SWFMEAIEYI DAVKDCRGRV LVHCQAGISR SATICLAYLM 

       310        320        330        340        350        360 
MKKRVRLEEA FEFVKQRRSI ISPNFSFMGQ LLQFESQVLT TSCAAEAASP SGPLRERGKA 

       370        380        390 
TPTPTSQFVF SFPVSVGVHA APSNLPYLHS PITTSPSC 

« Hide

References

[1]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Adipose tissue and Eye.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK053746 mRNA. Translation: BAC35504.1.
AK080964 mRNA. Translation: BAC38097.1.
RefSeqNP_795907.1. NM_176933.4.
UniGeneMm.170276.
Mm.392187.

3D structure databases

ProteinModelPortalQ8BFV3.
SMRQ8BFV3. Positions 10-164, 198-339.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid235330. 2 interactions.
IntActQ8BFV3. 2 interactions.

PTM databases

PhosphoSiteQ8BFV3.

Proteomic databases

PRIDEQ8BFV3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033930; ENSMUSP00000033930; ENSMUSG00000031530.
GeneID319520.
KEGGmmu:319520.
UCSCuc009lks.1. mouse.

Organism-specific databases

CTD1846.
MGIMGI:2442191. Dusp4.

Phylogenomic databases

eggNOGCOG2453.
GeneTreeENSGT00700000104321.
HOGENOMHOG000294080.
HOVERGENHBG007347.
InParanoidQ8BFV3.
KOK04459.
OMAHHSPITT.
OrthoDBEOG75MVWD.
PhylomeDBQ8BFV3.
TreeFamTF105122.

Gene expression databases

BgeeQ8BFV3.
CleanExMM_DUSP4.
GenevestigatorQ8BFV3.

Family and domain databases

Gene3D3.40.250.10. 1 hit.
InterProIPR000340. Dual-sp_phosphatase_cat-dom.
IPR020422. Dual-sp_phosphatase_subgr_cat.
IPR024950. DUSP.
IPR008343. MKP.
IPR001763. Rhodanese-like_dom.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
[Graphical view]
PANTHERPTHR10159. PTHR10159. 1 hit.
PfamPF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PIRSFPIRSF000939. MAPK_Ptase. 1 hit.
PRINTSPR01764. MAPKPHPHTASE.
SMARTSM00195. DSPc. 1 hit.
SM00450. RHOD. 1 hit.
[Graphical view]
SUPFAMSSF52821. SSF52821. 1 hit.
PROSITEPS50206. RHODANESE_3. 1 hit.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDUSP4. mouse.
NextBio394902.
PROQ8BFV3.
SOURCESearch...

Entry information

Entry nameDUS4_MOUSE
AccessionPrimary (citable) accession number: Q8BFV3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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