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Q13115

- DUS4_HUMAN

UniProt

Q13115 - DUS4_HUMAN

Protein

Dual specificity protein phosphatase 4

Gene

DUSP4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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 sitei280 – 2801Phosphocysteine intermediatePROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. endoderm formation Source: RefGenome
    2. innate immune response Source: Reactome
    3. MAPK cascade Source: ProtInc
    4. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    5. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    6. neurotrophin TRK receptor signaling pathway Source: Reactome
    7. protein dephosphorylation Source: RefGenome
    8. stress-activated MAPK cascade Source: Reactome
    9. toll-like receptor 10 signaling pathway Source: Reactome
    10. toll-like receptor 2 signaling pathway Source: Reactome
    11. toll-like receptor 3 signaling pathway Source: Reactome
    12. toll-like receptor 4 signaling pathway Source: Reactome
    13. toll-like receptor 5 signaling pathway Source: Reactome
    14. toll-like receptor 9 signaling pathway Source: Reactome
    15. toll-like receptor signaling pathway Source: Reactome
    16. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    17. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
    18. TRIF-dependent toll-like receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    ReactomeiREACT_12436. ERKs are inactivated.
    SignaLinkiQ13115.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity protein phosphatase 4 (EC:3.1.3.16, EC:3.1.3.48)
    Alternative name(s):
    Dual specificity protein phosphatase hVH2
    Mitogen-activated protein kinase phosphatase 2
    Short name:
    MAP kinase phosphatase 2
    Short name:
    MKP-2
    Gene namesi
    Name:DUSP4
    Synonyms:MKP2, VH2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:3070. DUSP4.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleoplasm Source: Reactome
    2. nucleus Source: ProtInc

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27527.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 394394Dual specificity protein phosphatase 4PRO_0000094798Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei386 – 3861Phosphoserine; by MAPK1 Publication
    Modified residuei391 – 3911Phosphoserine; by MAPK1 Publication

    Post-translational modificationi

    Phosphorylation in the C-terminus by ERK1/2 inhibits proteasomal degradation and stabilizes the protein.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ13115.
    PaxDbiQ13115.
    PRIDEiQ13115.

    PTM databases

    PhosphoSiteiQ13115.

    Expressioni

    Gene expression databases

    BgeeiQ13115.
    CleanExiHS_DUSP4.
    GenevestigatoriQ13115.

    Interactioni

    Subunit structurei

    Hollow spherical complex composed of 24 subunits with pseudooctahedral symmetry, has a tetramer as the basic unit.1 Publication

    Protein-protein interaction databases

    BioGridi108179. 7 interactions.
    IntActiQ13115. 5 interactions.
    MINTiMINT-8217030.
    STRINGi9606.ENSP00000240100.

    Structurei

    Secondary structure

    1
    394
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi197 – 2004
    Beta strandi203 – 2075
    Helixi208 – 2114
    Helixi214 – 2196
    Beta strandi224 – 2274
    Beta strandi229 – 2313
    Turni235 – 2395
    Beta strandi240 – 2445
    Beta strandi249 – 2524
    Turni255 – 2584
    Helixi259 – 27113
    Beta strandi276 – 28510
    Helixi286 – 29914
    Helixi303 – 3119
    Helixi321 – 33515

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3EZZX-ray2.90A/B/C/D/E/F194-336[»]
    ProteinModelPortaliQ13115.
    SMRiQ13115. Positions 44-158, 194-336.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ13115.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini41 – 159119RhodanesePROSITE-ProRule annotationAdd
    BLAST
    Domaini197 – 394198Tyrosine-protein phosphataseAdd
    BLAST

    Sequence similaritiesi

    Contains 1 rhodanese domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG2453.
    HOVERGENiHBG007347.
    InParanoidiQ13115.
    KOiK04459.
    OMAiHHSPITT.
    OrthoDBiEOG75MVWD.
    PhylomeDBiQ13115.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q13115-1) [UniParc]FASTAAdd to Basket

    Also known as: MKP-2-L

    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

    MVTMEELREM DCSVLKRLMN RDENGGGAGG SGSHGTLGLP SGGKCLLLDC    50
    RPFLAHSAGY ILGSVNVRCN TIVRRRAKGS VSLEQILPAE EEVRARLRSG 100
    LYSAVIVYDE RSPRAESLRE DSTVSLVVQA LRRNAERTDI CLLKGGYERF 150
    SSEYPEFCSK TKALAAIPPP VPPSATEPLD LGCSSCGTPL HDQGGPVEIL 200
    PFLYLGSAYH AARRDMLDAL GITALLNVSS DCPNHFEGHY QYKCIPVEDN 250
    HKADISSWFM EAIEYIDAVK DCRGRVLVHC QAGISRSATI CLAYLMMKKR 300
    VRLEEAFEFV KQRRSIISPN FSFMGQLLQF ESQVLATSCA AEAASPSGPL 350
    RERGKTPATP TSQFVFSFPV SVGVHSAPSS LPYLHSPITT SPSC 394
    Length:394
    Mass (Da):42,953
    Last modified:November 1, 1996 - v1
    Checksum:i0603971759B6952E
    GO
    Isoform 2 (identifier: Q13115-2) [UniParc]FASTAAdd to Basket

    Also known as: MKP-2-S

    The sequence of this isoform differs from the canonical sequence as follows:
         1-53: MVTMEELREM...KCLLLDCRPF → MGRKVHSNGS...RSRCLCSESQ
         54-144: Missing.

    Note: Does not bind to JNK or ERK, and is more susceptible to proteosomal degradation.

    Show »
    Length:303
    Mass (Da):32,993
    Checksum:i3BFB1126F4CF000A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti111 – 1111R → G in AAC50452. (PubMed:8626452)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5353MVTME…DCRPF → MGRKVHSNGSQFAEHSRSPR RTGRDCKPVRAPSMALGVSQ LAGRSRCLCSESQ in isoform 2. 1 PublicationVSP_044667Add
    BLAST
    Alternative sequencei54 – 14491Missing in isoform 2. 1 PublicationVSP_044668Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U21108 mRNA. Translation: AAA85119.1.
    U48807 mRNA. Translation: AAC50452.1.
    AK314820 mRNA. Translation: BAG37342.1.
    AL137704 mRNA. No translation available.
    AC084262 Genomic DNA. No translation available.
    CH471080 Genomic DNA. Translation: EAW63481.1.
    CH471080 Genomic DNA. Translation: EAW63482.1.
    CH471080 Genomic DNA. Translation: EAW63483.1.
    CH471080 Genomic DNA. Translation: EAW63484.1.
    BC002671 mRNA. Translation: AAH02671.1.
    BC014565 mRNA. Translation: AAH14565.1.
    CCDSiCCDS6072.1. [Q13115-1]
    CCDS6073.1. [Q13115-2]
    RefSeqiNP_001385.1. NM_001394.6. [Q13115-1]
    NP_476499.1. NM_057158.3. [Q13115-2]
    UniGeneiHs.417962.

    Genome annotation databases

    EnsembliENST00000240100; ENSP00000240100; ENSG00000120875. [Q13115-1]
    ENST00000240101; ENSP00000240101; ENSG00000120875. [Q13115-2]
    GeneIDi1846.
    KEGGihsa:1846.
    UCSCiuc003xhl.3. human.
    uc003xhm.3. human. [Q13115-1]

    Polymorphism databases

    DMDMi2499745.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U21108 mRNA. Translation: AAA85119.1 .
    U48807 mRNA. Translation: AAC50452.1 .
    AK314820 mRNA. Translation: BAG37342.1 .
    AL137704 mRNA. No translation available.
    AC084262 Genomic DNA. No translation available.
    CH471080 Genomic DNA. Translation: EAW63481.1 .
    CH471080 Genomic DNA. Translation: EAW63482.1 .
    CH471080 Genomic DNA. Translation: EAW63483.1 .
    CH471080 Genomic DNA. Translation: EAW63484.1 .
    BC002671 mRNA. Translation: AAH02671.1 .
    BC014565 mRNA. Translation: AAH14565.1 .
    CCDSi CCDS6072.1. [Q13115-1 ]
    CCDS6073.1. [Q13115-2 ]
    RefSeqi NP_001385.1. NM_001394.6. [Q13115-1 ]
    NP_476499.1. NM_057158.3. [Q13115-2 ]
    UniGenei Hs.417962.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3EZZ X-ray 2.90 A/B/C/D/E/F 194-336 [» ]
    ProteinModelPortali Q13115.
    SMRi Q13115. Positions 44-158, 194-336.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108179. 7 interactions.
    IntActi Q13115. 5 interactions.
    MINTi MINT-8217030.
    STRINGi 9606.ENSP00000240100.

    Chemistry

    ChEMBLi CHEMBL2146343.

    PTM databases

    PhosphoSitei Q13115.

    Polymorphism databases

    DMDMi 2499745.

    Proteomic databases

    MaxQBi Q13115.
    PaxDbi Q13115.
    PRIDEi Q13115.

    Protocols and materials databases

    DNASUi 1846.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000240100 ; ENSP00000240100 ; ENSG00000120875 . [Q13115-1 ]
    ENST00000240101 ; ENSP00000240101 ; ENSG00000120875 . [Q13115-2 ]
    GeneIDi 1846.
    KEGGi hsa:1846.
    UCSCi uc003xhl.3. human.
    uc003xhm.3. human. [Q13115-1 ]

    Organism-specific databases

    CTDi 1846.
    GeneCardsi GC08M029190.
    HGNCi HGNC:3070. DUSP4.
    MIMi 602747. gene.
    neXtProti NX_Q13115.
    PharmGKBi PA27527.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2453.
    HOVERGENi HBG007347.
    InParanoidi Q13115.
    KOi K04459.
    OMAi HHSPITT.
    OrthoDBi EOG75MVWD.
    PhylomeDBi Q13115.
    TreeFami TF105122.

    Enzyme and pathway databases

    Reactomei REACT_12436. ERKs are inactivated.
    SignaLinki Q13115.

    Miscellaneous databases

    EvolutionaryTracei Q13115.
    GeneWikii DUSP4.
    GenomeRNAii 1846.
    NextBioi 7559.
    PROi Q13115.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q13115.
    CleanExi HS_DUSP4.
    Genevestigatori Q13115.

    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. "Isolation and characterization of a novel dual specific phosphatase, HVH2, which selectively dephosphorylates the mitogen-activated protein kinase."
      Guan K.-L., Butch E.
      J. Biol. Chem. 270:7197-7203(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "The mitogen-activated protein kinase phosphatases PAC1, MKP-1, and MKP-2 have unique substrate specificities and reduced activity in vivo toward the ERK2 sevenmaker mutation."
      Chu Y., Solski P.A., Khosravi-Far R., Der C.J., Kelly K.
      J. Biol. Chem. 271:6497-6501(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Testis.
    5. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Skin and Uterus.
    8. "Post-translational regulation of mitogen-activated protein kinase phosphatase-2 (MKP-2) by ERK."
      Peng D.J., Zhou J.Y., Wu G.S.
      Cell Cycle 9:4650-4655(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-386 AND SER-391.
    9. "Differential regulation of MAP kinase activation by a novel splice variant of human MAP kinase phosphatase-2."
      Cadalbert L.C., Sloss C.M., Cunningham M.R., Al-Mutairi M., McIntire A., Shipley J., Plevin R.
      Cell. Signal. 22:357-365(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Crystal structure of the catalytic domain of human MKP-2 reveals a 24-mer assembly."
      Jeong D.G., Jung S.K., Yoon T.S., Woo E.J., Kim J.H., Park B.C., Ryu S.E., Kim S.J.
      Proteins 76:763-767(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 194-336, SUBUNIT.

    Entry informationi

    Entry nameiDUS4_HUMAN
    AccessioniPrimary (citable) accession number: Q13115
    Secondary accession number(s): B2RBU5
    , D3DSU4, G5E930, Q13524
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 140 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3