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Q9NRW4

- DUS22_HUMAN

UniProt

Q9NRW4 - DUS22_HUMAN

Protein

Dual specificity protein phosphatase 22

Gene

DUSP22

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    Functioni

    Activates the Jnk signaling pathway. Dephosphorylates and deactivates p38 and stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK) By similarity.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 sitei88 – 881Phosphocysteine intermediateBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. apoptotic process Source: ProtInc
    2. cell proliferation Source: ProtInc
    3. inactivation of MAPK activity Source: ProtInc
    4. multicellular organismal development Source: ProtInc
    5. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    6. positive regulation of JNK cascade Source: RefGenome
    7. protein dephosphorylation Source: RefGenome
    8. regulation of cell proliferation Source: RefGenome
    9. transforming growth factor beta receptor signaling pathway Source: RefGenome

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Enzyme and pathway databases

    SABIO-RKQ9NRW4.
    SignaLinkiQ9NRW4.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity protein phosphatase 22 (EC:3.1.3.16, EC:3.1.3.48)
    Alternative name(s):
    JNK-stimulatory phosphatase-1
    Short name:
    JSP-1
    Low molecular weight dual specificity phosphatase 2
    Short name:
    LMW-DSP2
    Mitogen-activated protein kinase phosphatase x
    Short name:
    MAP kinase phosphatase x
    Short name:
    MKP-x
    Gene namesi
    Name:DUSP22
    Synonyms:JSP1, LMWDSP2, MKPX
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:16077. DUSP22.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134991025.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 184183Dual specificity protein phosphatase 22PRO_0000244751Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi2 – 21N-myristoyl glycine1 Publication

    Post-translational modificationi

    Myristoylation regulates subcellular location, and is necessary for activation of JNK.1 Publication

    Keywords - PTMi

    Lipoprotein, Myristate

    Proteomic databases

    MaxQBiQ9NRW4.
    PaxDbiQ9NRW4.
    PRIDEiQ9NRW4.

    Expressioni

    Tissue specificityi

    Ubiquitous. Highest expression seen in heart, placenta, lung, liver, kidney and pancreas.1 Publication

    Gene expression databases

    ArrayExpressiQ9NRW4.
    BgeeiQ9NRW4.
    CleanExiHS_DUSP22.
    GenevestigatoriQ9NRW4.

    Organism-specific databases

    HPAiHPA031394.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Protein-protein interaction databases

    BioGridi121264. 5 interactions.
    IntActiQ9NRW4. 1 interaction.
    STRINGi9606.ENSP00000345281.

    Structurei

    Secondary structure

    1
    184
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 94
    Beta strandi12 – 154
    Helixi19 – 213
    Helixi23 – 286
    Beta strandi31 – 366
    Beta strandi49 – 524
    Helixi64 – 663
    Helixi67 – 7913
    Beta strandi83 – 875
    Beta strandi89 – 935
    Helixi94 – 10512
    Helixi111 – 12111
    Helixi129 – 14113
    Helixi143 – 15311

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WRMX-ray1.50A1-163[»]
    ProteinModelPortaliQ9NRW4.
    SMRiQ9NRW4. Positions 1-154.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NRW4.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini65 – 13369Tyrosine-protein phosphataseAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG2453.
    HOGENOMiHOG000007880.
    HOVERGENiHBG054344.
    InParanoidiQ9NRW4.
    KOiK14165.
    OMAiLFIGNFK.
    OrthoDBiEOG7966HM.
    PhylomeDBiQ9NRW4.
    TreeFamiTF105126.

    Family and domain databases

    Gene3Di3.90.190.10. 1 hit.
    InterProiIPR020417. Atypical_DUSP.
    IPR000340. Dual-sp_phosphatase_cat-dom.
    IPR020422. Dual-sp_phosphatase_subgr_cat.
    IPR024950. DUSP.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    [Graphical view]
    PANTHERiPTHR10159. PTHR10159. 1 hit.
    PfamiPF00782. DSPc. 1 hit.
    [Graphical view]
    PRINTSiPR01908. ADSPHPHTASE.
    SMARTiSM00195. DSPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52799. SSF52799. 1 hit.
    PROSITEiPS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NRW4-1) [UniParc]FASTAAdd to Basket

    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

    MGNGMNKILP GLYIGNFKDA RDAEQLSKNK VTHILSVHDS ARPMLEGVKY    50
    LCIPAADSPS QNLTRHFKES IKFIHECRLR GESCLVHCLA GVSRSVTLVI 100
    AYIMTVTDFG WEDALHTVRA GRSCANPNVG FQRQLQEFEK HEVHQYRQWL 150
    KEEYGESPLQ DAEEAKNILA APGILKFWAF LRRL 184
    Length:184
    Mass (Da):20,910
    Last modified:October 1, 2000 - v1
    Checksum:iB3F962A087C2BA20
    GO
    Isoform 2 (identifier: Q9NRW4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         170-184: AAPGILKFWAFLRRL → GKYKEQGRTEPQPGARRWSSFPALAPLTYDNYTTET

    Show »
    Length:205
    Mass (Da):23,268
    Checksum:i48334A97991FCFF8
    GO

    Sequence cautioni

    The sequence AAH16844.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti119 – 1191R → H.
    Corresponds to variant rs7768224 [ dbSNP | Ensembl ].
    VAR_026912

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei170 – 18415AAPGI…FLRRL → GKYKEQGRTEPQPGARRWSS FPALAPLTYDNYTTET in isoform 2. 2 PublicationsVSP_019614Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF424702 mRNA. Translation: AAL18850.1.
    AF165519 mRNA. Translation: AAF86649.1.
    AY249859 mRNA. Translation: AAP76376.1.
    AK296402 mRNA. Translation: BAG59068.1.
    AL365272 Genomic DNA. Translation: CAH72534.1.
    AL365272 Genomic DNA. Translation: CAH72535.1.
    BC016844 mRNA. Translation: AAH16844.1. Different initiation.
    BC022847 mRNA. Translation: AAH22847.1.
    AB208997 mRNA. Translation: BAD92234.1.
    CCDSiCCDS4468.1. [Q9NRW4-1]
    CCDS69035.1. [Q9NRW4-2]
    RefSeqiNP_001273484.1. NM_001286555.1. [Q9NRW4-2]
    NP_064570.1. NM_020185.4. [Q9NRW4-1]
    UniGeneiHs.29106.

    Genome annotation databases

    EnsembliENST00000344450; ENSP00000345281; ENSG00000112679. [Q9NRW4-1]
    ENST00000419235; ENSP00000397459; ENSG00000112679. [Q9NRW4-2]
    GeneIDi56940.
    KEGGihsa:56940.
    UCSCiuc003msx.3. human. [Q9NRW4-1]
    uc011dhn.1. human. [Q9NRW4-2]

    Polymorphism databases

    DMDMi74752929.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF424702 mRNA. Translation: AAL18850.1 .
    AF165519 mRNA. Translation: AAF86649.1 .
    AY249859 mRNA. Translation: AAP76376.1 .
    AK296402 mRNA. Translation: BAG59068.1 .
    AL365272 Genomic DNA. Translation: CAH72534.1 .
    AL365272 Genomic DNA. Translation: CAH72535.1 .
    BC016844 mRNA. Translation: AAH16844.1 . Different initiation.
    BC022847 mRNA. Translation: AAH22847.1 .
    AB208997 mRNA. Translation: BAD92234.1 .
    CCDSi CCDS4468.1. [Q9NRW4-1 ]
    CCDS69035.1. [Q9NRW4-2 ]
    RefSeqi NP_001273484.1. NM_001286555.1. [Q9NRW4-2 ]
    NP_064570.1. NM_020185.4. [Q9NRW4-1 ]
    UniGenei Hs.29106.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WRM X-ray 1.50 A 1-163 [» ]
    ProteinModelPortali Q9NRW4.
    SMRi Q9NRW4. Positions 1-154.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121264. 5 interactions.
    IntActi Q9NRW4. 1 interaction.
    STRINGi 9606.ENSP00000345281.

    Chemistry

    BindingDBi Q9NRW4.
    ChEMBLi CHEMBL3924.

    Polymorphism databases

    DMDMi 74752929.

    Proteomic databases

    MaxQBi Q9NRW4.
    PaxDbi Q9NRW4.
    PRIDEi Q9NRW4.

    Protocols and materials databases

    DNASUi 56940.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000344450 ; ENSP00000345281 ; ENSG00000112679 . [Q9NRW4-1 ]
    ENST00000419235 ; ENSP00000397459 ; ENSG00000112679 . [Q9NRW4-2 ]
    GeneIDi 56940.
    KEGGi hsa:56940.
    UCSCi uc003msx.3. human. [Q9NRW4-1 ]
    uc011dhn.1. human. [Q9NRW4-2 ]

    Organism-specific databases

    CTDi 56940.
    GeneCardsi GC06P000292.
    HGNCi HGNC:16077. DUSP22.
    HPAi HPA031394.
    neXtProti NX_Q9NRW4.
    PharmGKBi PA134991025.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2453.
    HOGENOMi HOG000007880.
    HOVERGENi HBG054344.
    InParanoidi Q9NRW4.
    KOi K14165.
    OMAi LFIGNFK.
    OrthoDBi EOG7966HM.
    PhylomeDBi Q9NRW4.
    TreeFami TF105126.

    Enzyme and pathway databases

    SABIO-RK Q9NRW4.
    SignaLinki Q9NRW4.

    Miscellaneous databases

    ChiTaRSi DUSP22. human.
    EvolutionaryTracei Q9NRW4.
    GeneWikii DUSP22.
    GenomeRNAii 56940.
    NextBioi 62505.
    PROi Q9NRW4.

    Gene expression databases

    ArrayExpressi Q9NRW4.
    Bgeei Q9NRW4.
    CleanExi HS_DUSP22.
    Genevestigatori Q9NRW4.

    Family and domain databases

    Gene3Di 3.90.190.10. 1 hit.
    InterProi IPR020417. Atypical_DUSP.
    IPR000340. Dual-sp_phosphatase_cat-dom.
    IPR020422. Dual-sp_phosphatase_subgr_cat.
    IPR024950. DUSP.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    [Graphical view ]
    PANTHERi PTHR10159. PTHR10159. 1 hit.
    Pfami PF00782. DSPc. 1 hit.
    [Graphical view ]
    PRINTSi PR01908. ADSPHPHTASE.
    SMARTi SM00195. DSPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52799. SSF52799. 1 hit.
    PROSITEi PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50054. TYR_PHOSPHATASE_DUAL. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Activation of the Jnk signaling pathway by a dual-specificity phosphatase, JSP-1."
      Shen Y., Luche R., Wei B., Gordon M.L., Diltz C.D., Tonks N.K.
      Proc. Natl. Acad. Sci. U.S.A. 98:13613-13618(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY.
    2. "Novel genes expressed in hematopoietic stem/progenitor cells from myelodysplastic syndromes patient."
      Gu J., Huang Q., Yu Y., Xu S., Wang Y., Han Z., Chen Z., Zhou J., Tu Y., Gu W., Fu G., Huang C.
      Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Hematopoietic stem cell.
    3. "Cloning and characterization of human LMW-DSP2 gene."
      Mao Y., Xie Y., Cheng H.
      Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "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 2).
      Tissue: Thalamus.
    5. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Lung and Pancreas.
    7. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 56-184 (ISOFORM 2).
      Tissue: Myeloid.
    8. "Myristoylation of the dual-specificity phosphatase c-JUN N-terminal kinase (JNK) stimulatory phosphatase 1 is necessary for its activation of JNK signaling and apoptosis."
      Schwertassek U., Buckley D.A., Xu C.F., Lindsay A.J., McCaffrey M.W., Neubert T.A., Tonks N.K.
      FEBS J. 277:2463-2473(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: MYRISTOYLATION AT GLY-2.
    9. "Crystal structure of human dual specificity phosphatase, JNK stimulatory phosphatase-1, at 1.5 A resolution."
      Yokota T., Nara Y., Kashima A., Matsubara K., Misawa S., Kato R., Sugio S.
      Proteins 66:272-278(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1-163, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiDUS22_HUMAN
    AccessioniPrimary (citable) accession number: Q9NRW4
    Secondary accession number(s): B4DK56
    , Q59GW2, Q5VWR2, Q96AR1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 27, 2006
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 120 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 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3