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Q05922

- DUS2_MOUSE

UniProt

Q05922 - DUS2_MOUSE

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Protein

Dual specificity protein phosphatase 2

Gene

Dusp2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

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 sitei261 – 2611Phosphocysteine intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  1. MAP kinase tyrosine/serine/threonine phosphatase activity Source: InterPro
  2. mitogen-activated protein kinase binding Source: MGI
  3. phosphoprotein phosphatase activity Source: MGI
  4. protein tyrosine/serine/threonine phosphatase activity Source: RefGenome
  5. protein tyrosine phosphatase activity Source: UniProtKB-EC

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Names & Taxonomyi

Protein namesi
Recommended name:
Dual specificity protein phosphatase 2 (EC:3.1.3.16, EC:3.1.3.48)
Alternative name(s):
Dual specificity protein phosphatase PAC-1
Gene namesi
Name:Dusp2
Synonyms:Pac-1, Pac1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:101911. Dusp2.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 318318Dual specificity protein phosphatase 2PRO_0000094794Add
BLAST

Proteomic databases

PRIDEiQ05922.

PTM databases

PhosphoSiteiQ05922.

Expressioni

Tissue specificityi

In hematopoietic tissues such as spleen and thymus.

Inductioni

By mitogens.

Gene expression databases

BgeeiQ05922.
CleanExiMM_DUSP2.
GenevestigatoriQ05922.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
MAPK1P284822EBI-7898692,EBI-959949From a different organism.

Protein-protein interaction databases

BioGridi199340. 3 interactions.
IntActiQ05922. 2 interactions.
MINTiMINT-8214532.

Structurei

3D structure databases

ProteinModelPortaliQ05922.
SMRiQ05922. Positions 29-147, 174-318.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini27 – 148122RhodanesePROSITE-ProRule annotationAdd
BLAST
Domaini241 – 30666Tyrosine-protein phosphataseAdd
BLAST

Sequence similaritiesi

Contains 1 rhodanese domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG2453.
GeneTreeiENSGT00760000118902.
HOGENOMiHOG000294080.
HOVERGENiHBG007347.
InParanoidiQ05922.
KOiK04459.
OMAiCLAYLMQ.
OrthoDBiEOG75MVWD.
TreeFamiTF105122.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProiIPR020417. Atypical_DUSP.
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]
PANTHERiPTHR10159. PTHR10159. 1 hit.
PfamiPF00782. DSPc. 1 hit.
PF00581. Rhodanese. 1 hit.
[Graphical view]
PIRSFiPIRSF000939. MAPK_Ptase. 1 hit.
PRINTSiPR01908. ADSPHPHTASE.
PR01764. 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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q05922-1) [UniParc]FASTAAdd to Basket

Also known as: Long

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPIAMGLETA CELECAALGA LLREPREAER TLLLDCRPFL AFCRSHVRAA
60 70 80 90 100
RPVPWNALLR RRARGTPAAA LACLLPDRAL RARLGRGELA RAVVLDESSA
110 120 130 140 150
SVAELPPDGP AHLLLAALQH EMRGGPTTVC FLRGGFKSFQ TYCPDLCSEA
160 170 180 190 200
PAQALPPAGA ENSNSDPRVP IYDQGGPVEI LPYLYLGSCN HSSDLQGLQA
210 220 230 240 250
CGITAVLNVS ASCPNHFEGL FHYKSIPVED NQMVEISAWF QEAISFIDSV
260 270 280 290 300
KNSGGRVLVH CQAGISRSAT ICLAYLIQSH RVRLDEAFDF VKQRRGVISP
310
NFSFMGQLLQ LETQVLCH
Length:318
Mass (Da):34,576
Last modified:July 27, 2011 - v2
Checksum:iAAB6A01BA598C5C9
GO
Isoform 2 (identifier: Q05922-2) [UniParc]FASTAAdd to Basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     175-179: GGPVE → VSSDL
     180-318: Missing.

Show »
Length:179
Mass (Da):19,209
Checksum:iE10BE72F8835521A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 122CE → WQ in AAA85136. (PubMed:7896276)Curated
Sequence conflicti20 – 201A → V in AAA85136. (PubMed:7896276)Curated
Sequence conflicti64 – 641R → P in AAA19666. (PubMed:7681221)Curated
Sequence conflicti64 – 641R → P in AAA85136. (PubMed:7896276)Curated
Sequence conflicti103 – 1031A → T in AAA19666. (PubMed:7681221)Curated
Sequence conflicti103 – 1031A → T in AAA85136. (PubMed:7896276)Curated
Sequence conflicti156 – 1561P → A in AAA85136. (PubMed:7896276)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei175 – 1795GGPVE → VSSDL in isoform 2. CuratedVSP_005135
Alternative sequencei180 – 318139Missing in isoform 2. CuratedVSP_005136Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L11330 mRNA. Translation: AAA19666.1.
U09268 Genomic DNA. Translation: AAA85136.1.
AK134067 mRNA. Translation: BAE21999.1.
AL845368 Genomic DNA. Translation: CAM17446.1.
BC048696 mRNA. Translation: AAH48696.1.
CCDSiCCDS16699.1. [Q05922-1]
PIRiB57126.
RefSeqiNP_034220.2. NM_010090.2. [Q05922-1]
UniGeneiMm.4729.

Genome annotation databases

EnsembliENSMUST00000028846; ENSMUSP00000028846; ENSMUSG00000027368. [Q05922-1]
GeneIDi13537.
KEGGimmu:13537.
UCSCiuc008mff.1. mouse. [Q05922-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L11330 mRNA. Translation: AAA19666.1 .
U09268 Genomic DNA. Translation: AAA85136.1 .
AK134067 mRNA. Translation: BAE21999.1 .
AL845368 Genomic DNA. Translation: CAM17446.1 .
BC048696 mRNA. Translation: AAH48696.1 .
CCDSi CCDS16699.1. [Q05922-1 ]
PIRi B57126.
RefSeqi NP_034220.2. NM_010090.2. [Q05922-1 ]
UniGenei Mm.4729.

3D structure databases

ProteinModelPortali Q05922.
SMRi Q05922. Positions 29-147, 174-318.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199340. 3 interactions.
IntActi Q05922. 2 interactions.
MINTi MINT-8214532.

PTM databases

PhosphoSitei Q05922.

Proteomic databases

PRIDEi Q05922.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000028846 ; ENSMUSP00000028846 ; ENSMUSG00000027368 . [Q05922-1 ]
GeneIDi 13537.
KEGGi mmu:13537.
UCSCi uc008mff.1. mouse. [Q05922-1 ]

Organism-specific databases

CTDi 1844.
MGIi MGI:101911. Dusp2.

Phylogenomic databases

eggNOGi COG2453.
GeneTreei ENSGT00760000118902.
HOGENOMi HOG000294080.
HOVERGENi HBG007347.
InParanoidi Q05922.
KOi K04459.
OMAi CLAYLMQ.
OrthoDBi EOG75MVWD.
TreeFami TF105122.

Miscellaneous databases

ChiTaRSi DUSP2. mouse.
NextBioi 284136.
PROi Q05922.
SOURCEi Search...

Gene expression databases

Bgeei Q05922.
CleanExi MM_DUSP2.
Genevestigatori Q05922.

Family and domain databases

Gene3Di 3.40.250.10. 1 hit.
3.90.190.10. 1 hit.
InterProi IPR020417. Atypical_DUSP.
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 PR01908. ADSPHPHTASE.
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

« Hide 'large scale' publications
  1. "PAC-1: a mitogen-induced nuclear protein tyrosine phosphatase."
    Rohan P., Davis P., Moskaluk C.A., Kearns M., Krutzsch H., Siebenlist U., Kelly K.
    Science 259:1763-1766(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Structure of the gene encoding the murine dual specificity tyrosine-threonine phosphatase PAC1."
    Gerondakis S., Economou C., Grumont R.J.
    Genomics 24:182-184(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2).
    Strain: 129.
  3. "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] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Thymus.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "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] (ISOFORM 1).
    Tissue: Limb.

Entry informationi

Entry nameiDUS2_MOUSE
AccessioniPrimary (citable) accession number: Q05922
Secondary accession number(s): Q60640, Q80ZN1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 131 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