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Protein

Dual specificity protein phosphatase 4

Gene

Dusp4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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.PROSITE-ProRule annotation
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei284 – 2841Phosphocysteine intermediatePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

ReactomeiREACT_299247. 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 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:2442191. Dusp4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

MaxQBiQ8BFV3.
PRIDEiQ8BFV3.

PTM databases

PhosphoSiteiQ8BFV3.

Expressioni

Gene expression databases

BgeeiQ8BFV3.
CleanExiMM_DUSP4.
GenevisibleiQ8BFV3. MM.

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.
STRINGi10090.ENSMUSP00000033930.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 163119RhodanesePROSITE-ProRule annotationAdd
BLAST
Domaini201 – 398198Tyrosine-protein phosphataseAdd
BLAST

Sequence similaritiesi

Contains 1 rhodanese domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118902.
HOGENOMiHOG000294080.
HOVERGENiHBG007347.
InParanoidiQ8BFV3.
KOiK04459.
OMAiHKEDISC.
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

        10         20         30         40         50
MVTMEELREM DCSVLKRLMN RDENGGGGSA GGNGSGSHGA LGLLSGGKCL
60 70 80 90 100
LLDCRPFLAH SAGYIRGSVN VRCNTIVRRR AKGSVSLEQI LPAEEEVRAR
110 120 130 140 150
LRSGLYSAVI VYDERSPRAE SLREDSTVSL VVQALRRNAE RTDICLLKGG
160 170 180 190 200
YERFSSEYPE FCSKTKALAA IPPPVPPSTN ESLDLGCSSC GTPLHDQGGP
210 220 230 240 250
VEILPFLYLG SAYHAARRDM LDALGITALL NVSSDCPNHF EGHYQYKCIP
260 270 280 290 300
VEDNHKADIS SWFMEAIEYI DAVKDCRGRV LVHCQAGISR SATICLAYLM
310 320 330 340 350
MKKRVRLEEA FEFVKQRRSI ISPNFSFMGQ LLQFESQVLT TSCAAEAASP
360 370 380 390
SGPLRERGKA TPTPTSQFVF SFPVSVGVHA APSNLPYLHS PITTSPSC
Length:398
Mass (Da):43,372
Last modified:March 1, 2003 - v1
Checksum:iE9542B1ACD48097B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AK053746 mRNA. Translation: BAC35504.1.
AK080964 mRNA. Translation: BAC38097.1.
CCDSiCCDS22241.1.
RefSeqiNP_795907.1. NM_176933.4.
UniGeneiMm.170276.
Mm.392187.

3D structure databases

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

Protein-protein interaction databases

BioGridi235330. 2 interactions.
IntActiQ8BFV3. 2 interactions.
STRINGi10090.ENSMUSP00000033930.

PTM databases

PhosphoSiteiQ8BFV3.

Proteomic databases

MaxQBiQ8BFV3.
PRIDEiQ8BFV3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1846.
MGIiMGI:2442191. Dusp4.

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118902.
HOGENOMiHOG000294080.
HOVERGENiHBG007347.
InParanoidiQ8BFV3.
KOiK04459.
OMAiHKEDISC.
OrthoDBiEOG75MVWD.
PhylomeDBiQ8BFV3.
TreeFamiTF105122.

Enzyme and pathway databases

ReactomeiREACT_299247. ERKs are inactivated.

Miscellaneous databases

ChiTaRSiDusp4. mouse.
NextBioi394902.
PROiQ8BFV3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BFV3.
CleanExiMM_DUSP4.
GenevisibleiQ8BFV3. MM.

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]
ProtoNetiSearch...

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: July 22, 2015
This is version 104 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

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.