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Q8BFV3

- DUS4_MOUSE

UniProt

Q8BFV3 - DUS4_MOUSE

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Protein
Dual specificity protein phosphatase 4
Gene
Dusp4
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

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

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 sitei284 – 2841Phosphocysteine intermediate By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. endoderm formation Source: RefGenome
  2. protein dephosphorylation Source: RefGenome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

ReactomeiREACT_210064. ERKs are inactivated.

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity protein phosphatase 4 (EC:3.1.3.16, EC:3.1.3.48)
Gene namesi
Name:Dusp4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:2442191. Dusp4.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 398398Dual specificity protein phosphatase 4
PRO_0000094799Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei390 – 3901Phosphoserine; by MAPK By similarity
Modified residuei395 – 3951Phosphoserine; by MAPK By similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ8BFV3.

PTM databases

PhosphoSiteiQ8BFV3.

Expressioni

Gene expression databases

BgeeiQ8BFV3.
CleanExiMM_DUSP4.
GenevestigatoriQ8BFV3.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi235330. 2 interactions.
IntActiQ8BFV3. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ8BFV3.
SMRiQ8BFV3. Positions 41-162, 198-339.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 163119Rhodanese
Add
BLAST
Domaini201 – 398198Tyrosine-protein phosphatase
Add
BLAST

Sequence similaritiesi

Contains 1 rhodanese domain.

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00700000104321.
HOGENOMiHOG000294080.
HOVERGENiHBG007347.
InParanoidiQ8BFV3.
KOiK04459.
OMAiHHSPITT.
OrthoDBiEOG75MVWD.
PhylomeDBiQ8BFV3.
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]
PIRSFiPIRSF000939. MAPK_Ptase. 1 hit.
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.

Q8BFV3-1 [UniParc]FASTAAdd to Basket

« Hide

MVTMEELREM DCSVLKRLMN RDENGGGGSA GGNGSGSHGA LGLLSGGKCL    50
LLDCRPFLAH SAGYIRGSVN VRCNTIVRRR AKGSVSLEQI LPAEEEVRAR 100
LRSGLYSAVI VYDERSPRAE SLREDSTVSL VVQALRRNAE RTDICLLKGG 150
YERFSSEYPE FCSKTKALAA IPPPVPPSTN ESLDLGCSSC GTPLHDQGGP 200
VEILPFLYLG SAYHAARRDM LDALGITALL NVSSDCPNHF EGHYQYKCIP 250
VEDNHKADIS SWFMEAIEYI DAVKDCRGRV LVHCQAGISR SATICLAYLM 300
MKKRVRLEEA FEFVKQRRSI ISPNFSFMGQ LLQFESQVLT TSCAAEAASP 350
SGPLRERGKA TPTPTSQFVF SFPVSVGVHA APSNLPYLHS PITTSPSC 398
Length:398
Mass (Da):43,372
Last modified:March 1, 2003 - v1
Checksum:iE9542B1ACD48097B
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK053746 mRNA. Translation: BAC35504.1.
AK080964 mRNA. Translation: BAC38097.1.
CCDSiCCDS22241.1.
RefSeqiNP_795907.1. NM_176933.4.
UniGeneiMm.170276.
Mm.392187.

Genome annotation databases

EnsembliENSMUST00000033930; ENSMUSP00000033930; ENSMUSG00000031530.
GeneIDi319520.
KEGGimmu:319520.
UCSCiuc009lks.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK053746 mRNA. Translation: BAC35504.1 .
AK080964 mRNA. Translation: BAC38097.1 .
CCDSi CCDS22241.1.
RefSeqi NP_795907.1. NM_176933.4.
UniGenei Mm.170276.
Mm.392187.

3D structure databases

ProteinModelPortali Q8BFV3.
SMRi Q8BFV3. Positions 41-162, 198-339.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 235330. 2 interactions.
IntActi Q8BFV3. 2 interactions.

PTM databases

PhosphoSitei Q8BFV3.

Proteomic databases

PRIDEi Q8BFV3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000033930 ; ENSMUSP00000033930 ; ENSMUSG00000031530 .
GeneIDi 319520.
KEGGi mmu:319520.
UCSCi uc009lks.1. mouse.

Organism-specific databases

CTDi 1846.
MGIi MGI:2442191. Dusp4.

Phylogenomic databases

eggNOGi COG2453.
GeneTreei ENSGT00700000104321.
HOGENOMi HOG000294080.
HOVERGENi HBG007347.
InParanoidi Q8BFV3.
KOi K04459.
OMAi HHSPITT.
OrthoDBi EOG75MVWD.
PhylomeDBi Q8BFV3.
TreeFami TF105122.

Enzyme and pathway databases

Reactomei REACT_210064. ERKs are inactivated.

Miscellaneous databases

ChiTaRSi DUSP4. mouse.
NextBioi 394902.
PROi Q8BFV3.
SOURCEi Search...

Gene expression databases

Bgeei Q8BFV3.
CleanExi MM_DUSP4.
Genevestigatori Q8BFV3.

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 ]
PIRSFi PIRSF000939. MAPK_Ptase. 1 hit.
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

  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.
    , 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.

Entry informationi

Entry nameiDUS4_MOUSE
AccessioniPrimary (citable) accession number: Q8BFV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: March 1, 2003
Last modified: September 3, 2014
This is version 95 of the entry and version 1 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

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