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Q9Y463

- DYR1B_HUMAN

UniProt

Q9Y463 - DYR1B_HUMAN

Protein

Dual specificity tyrosine-phosphorylation-regulated kinase 1B

Gene

DYRK1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Dual-specificity kinase which possesses both serine/ threonine and tyrosine kinase activities. Enhances the transcriptional activity of TCF1/HNF1A and FOXO1. Inhibits epithelial cell migration. Mediates colon carcinoma cell survival in mitogen-poor environments.3 Publications

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.1 Publication

    Enzyme regulationi

    Inhibited by RANBP9.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei140 – 1401ATPPROSITE-ProRule annotation
    Active sitei239 – 2391Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi117 – 1259ATPPROSITE-ProRule annotation
    Nucleotide bindingi190 – 1934ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. protein kinase activity Source: UniProtKB
    4. protein serine/threonine/tyrosine kinase activity Source: UniProtKB-EC
    5. protein serine/threonine kinase activity Source: UniProtKB-KW
    6. protein tyrosine kinase activity Source: UniProtKB-KW
    7. transcription coactivator activity Source: UniProtKB

    GO - Biological processi

    1. myoblast fusion Source: Ensembl
    2. positive regulation of transcription, DNA-templated Source: UniProtKB
    3. protein phosphorylation Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS02690-MONOMER.
    BRENDAi2.7.12.1. 2681.
    SignaLinkiQ9Y463.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dual specificity tyrosine-phosphorylation-regulated kinase 1B (EC:2.7.12.1)
    Alternative name(s):
    Minibrain-related kinase
    Mirk protein kinase
    Gene namesi
    Name:DYRK1B
    Synonyms:MIRK
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:3092. DYRK1B.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: ProtInc

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi140 – 1401K → R: Abolishes kinase activity. 1 Publication
    Mutagenesisi271 – 2711Y → F: Abolishes kinase activity; when associated with F-273. 1 Publication
    Mutagenesisi273 – 2731Y → F: Abolishes kinase activity; when associated with F-271. 1 Publication

    Organism-specific databases

    PharmGKBiPA27549.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 629629Dual specificity tyrosine-phosphorylation-regulated kinase 1BPRO_0000085934Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei271 – 2711Phosphotyrosine; by autocatalysis1 Publication
    Modified residuei273 – 2731Phosphotyrosine; by autocatalysis1 Publication

    Post-translational modificationi

    Autophosphorylated on tyrosine residues. Phosphorylated by MAP kinase. Tyrosine phosphorylation may be required for dimerization.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9Y463.
    PaxDbiQ9Y463.
    PRIDEiQ9Y463.

    PTM databases

    PhosphoSiteiQ9Y463.

    Expressioni

    Tissue specificityi

    Highest expression in skeletal muscle, testis, heart and brain with little expression in colon or lung. Expressed in a variety of tumor cell lines.1 Publication

    Gene expression databases

    ArrayExpressiQ9Y463.
    BgeeiQ9Y463.
    CleanExiHS_DYRK1B.
    GenevestigatoriQ9Y463.

    Organism-specific databases

    HPAiHPA028786.

    Interactioni

    Subunit structurei

    Dimer. Interacts with DCOHM, MAP2K3/MKK3, RANBP9 and TCF1/HNF1A. Part of a complex consisting of RANBP9, RAN, DYRK1B and COPS5. Interacts with DCAF7.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DCAF7P619622EBI-634187,EBI-359808
    HNF1AP208234EBI-634187,EBI-636034
    LZTS2Q9BRK43EBI-634187,EBI-741037
    MAP2K3P467342EBI-634187,EBI-602462
    PCBD2Q9H0N52EBI-634187,EBI-634289
    RANBP9Q96S594EBI-634187,EBI-636085
    RB1P064003EBI-634187,EBI-491274
    RBL1P287493EBI-634187,EBI-971402
    TROAPQ128153EBI-634187,EBI-2349743

    Protein-protein interaction databases

    BioGridi114596. 58 interactions.
    IntActiQ9Y463. 54 interactions.
    MINTiMINT-2790122.
    STRINGi9606.ENSP00000312789.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y463.
    SMRiQ9Y463. Positions 100-432.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini111 – 431321Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni480 – 52041Interaction with RANBP9Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi69 – 8618Bipartite nuclear localization signalSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi558 – 5614Poly-Pro

    Sequence similaritiesi

    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000220863.
    HOVERGENiHBG051425.
    InParanoidiQ9Y463.
    KOiK08825.
    OMAiNYRYSNR.
    OrthoDBiEOG77127N.
    PhylomeDBiQ9Y463.
    TreeFamiTF314624.

    Family and domain databases

    InterProiIPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    [Graphical view]
    SMARTiSM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y463-1) [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

    MAVPPGHGPF SGFPGPQEHT QVLPDVRLLP RRLPLAFRDA TSAPLRKLSV    50
    DLIKTYKHIN EVYYAKKKRR AQQAPPQDSS NKKEKKVLNH GYDDDNHDYI 100
    VRSGERWLER YEIDSLIGKG SFGQVVKAYD HQTQELVAIK IIKNKKAFLN 150
    QAQIELRLLE LMNQHDTEMK YYIVHLKRHF MFRNHLCLVF ELLSYNLYDL 200
    LRNTHFRGVS LNLTRKLAQQ LCTALLFLAT PELSIIHCDL KPENILLCNP 250
    KRSAIKIVDF GSSCQLGQRI YQYIQSRFYR SPEVLLGTPY DLAIDMWSLG 300
    CILVEMHTGE PLFSGSNEVD QMNRIVEVLG IPPAAMLDQA PKARKYFERL 350
    PGGGWTLRRT KELRKDYQGP GTRRLQEVLG VQTGGPGGRR AGEPGHSPAD 400
    YLRFQDLVLR MLEYEPAARI SPLGALQHGF FRRTADEATN TGPAGSSAST 450
    SPAPLDTCPS SSTASSISSS GGSSGSSSDN RTYRYSNRYC GGPGPPITDC 500
    EMNSPQVPPS QPLRPWAGGD VPHKTHQAPA SASSLPGTGA QLPPQPRYLG 550
    RPPSPTSPPP PELMDVSLVG GPADCSPPHP APAPQHPAAS ALRTRMTGGR 600
    PPLPPPDDPA TLGPHLGLRG VPQSTAASS 629
    Length:629
    Mass (Da):69,198
    Last modified:November 1, 1999 - v1
    Checksum:iD7C354AC55943A8B
    GO
    Isoform 2 (identifier: Q9Y463-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         366-405: Missing.

    Show »
    Length:589
    Mass (Da):64,934
    Checksum:iE98BF9B257237A9D
    GO
    Isoform 3 (identifier: Q9Y463-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         378-405: Missing.

    Show »
    Length:601
    Mass (Da):66,336
    Checksum:i8601907D9652274B
    GO

    Sequence cautioni

    The sequence AAC28914.1 differs from that shown. Reason: Erroneous gene model prediction.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti28 – 281L → P.1 Publication
    Corresponds to variant rs34587974 [ dbSNP | Ensembl ].
    VAR_040454
    Natural varianti102 – 1021R → H.1 Publication
    Corresponds to variant rs55687541 [ dbSNP | Ensembl ].
    VAR_040455
    Natural varianti234 – 2341S → G.1 Publication
    Corresponds to variant rs35858874 [ dbSNP | Ensembl ].
    VAR_040456
    Natural varianti275 – 2751Q → R in a metastatic melanoma sample; somatic mutation. 1 Publication
    VAR_040457

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei366 – 40540Missing in isoform 2. 1 PublicationVSP_004925Add
    BLAST
    Alternative sequencei378 – 40528Missing in isoform 3. 1 PublicationVSP_004926Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y17999 mRNA. Translation: CAA76991.1.
    Y17999 mRNA. Translation: CAA76990.1.
    Y17999 mRNA. Translation: CAA76989.1.
    AF205861 mRNA. Translation: AAF15893.1.
    AC005393 Genomic DNA. Translation: AAC28914.1. Sequence problems.
    BC018751 mRNA. Translation: AAH18751.1.
    BC025291 mRNA. Translation: AAH25291.1.
    CCDSiCCDS12543.1. [Q9Y463-1]
    CCDS12544.1. [Q9Y463-3]
    CCDS46075.1. [Q9Y463-2]
    PIRiJG0195.
    RefSeqiNP_004705.1. NM_004714.2. [Q9Y463-1]
    NP_006474.1. NM_006483.2. [Q9Y463-2]
    NP_006475.1. NM_006484.2. [Q9Y463-3]
    XP_005259455.1. XM_005259398.2. [Q9Y463-1]
    UniGeneiHs.130988.

    Genome annotation databases

    EnsembliENST00000323039; ENSP00000312789; ENSG00000105204. [Q9Y463-1]
    ENST00000348817; ENSP00000221803; ENSG00000105204. [Q9Y463-3]
    ENST00000430012; ENSP00000403182; ENSG00000105204. [Q9Y463-2]
    ENST00000593685; ENSP00000469863; ENSG00000105204. [Q9Y463-1]
    ENST00000597639; ENSP00000472941; ENSG00000105204. [Q9Y463-3]
    GeneIDi9149.
    KEGGihsa:9149.
    UCSCiuc002omi.3. human. [Q9Y463-3]
    uc002omj.3. human. [Q9Y463-1]
    uc002omk.3. human. [Q9Y463-2]

    Polymorphism databases

    DMDMi9296963.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y17999 mRNA. Translation: CAA76991.1 .
    Y17999 mRNA. Translation: CAA76990.1 .
    Y17999 mRNA. Translation: CAA76989.1 .
    AF205861 mRNA. Translation: AAF15893.1 .
    AC005393 Genomic DNA. Translation: AAC28914.1 . Sequence problems.
    BC018751 mRNA. Translation: AAH18751.1 .
    BC025291 mRNA. Translation: AAH25291.1 .
    CCDSi CCDS12543.1. [Q9Y463-1 ]
    CCDS12544.1. [Q9Y463-3 ]
    CCDS46075.1. [Q9Y463-2 ]
    PIRi JG0195.
    RefSeqi NP_004705.1. NM_004714.2. [Q9Y463-1 ]
    NP_006474.1. NM_006483.2. [Q9Y463-2 ]
    NP_006475.1. NM_006484.2. [Q9Y463-3 ]
    XP_005259455.1. XM_005259398.2. [Q9Y463-1 ]
    UniGenei Hs.130988.

    3D structure databases

    ProteinModelPortali Q9Y463.
    SMRi Q9Y463. Positions 100-432.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114596. 58 interactions.
    IntActi Q9Y463. 54 interactions.
    MINTi MINT-2790122.
    STRINGi 9606.ENSP00000312789.

    Chemistry

    BindingDBi Q9Y463.
    ChEMBLi CHEMBL5543.
    GuidetoPHARMACOLOGYi 2010.

    PTM databases

    PhosphoSitei Q9Y463.

    Polymorphism databases

    DMDMi 9296963.

    Proteomic databases

    MaxQBi Q9Y463.
    PaxDbi Q9Y463.
    PRIDEi Q9Y463.

    Protocols and materials databases

    DNASUi 9149.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000323039 ; ENSP00000312789 ; ENSG00000105204 . [Q9Y463-1 ]
    ENST00000348817 ; ENSP00000221803 ; ENSG00000105204 . [Q9Y463-3 ]
    ENST00000430012 ; ENSP00000403182 ; ENSG00000105204 . [Q9Y463-2 ]
    ENST00000593685 ; ENSP00000469863 ; ENSG00000105204 . [Q9Y463-1 ]
    ENST00000597639 ; ENSP00000472941 ; ENSG00000105204 . [Q9Y463-3 ]
    GeneIDi 9149.
    KEGGi hsa:9149.
    UCSCi uc002omi.3. human. [Q9Y463-3 ]
    uc002omj.3. human. [Q9Y463-1 ]
    uc002omk.3. human. [Q9Y463-2 ]

    Organism-specific databases

    CTDi 9149.
    GeneCardsi GC19M040316.
    HGNCi HGNC:3092. DYRK1B.
    HPAi HPA028786.
    MIMi 604556. gene.
    neXtProti NX_Q9Y463.
    PharmGKBi PA27549.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000220863.
    HOVERGENi HBG051425.
    InParanoidi Q9Y463.
    KOi K08825.
    OMAi NYRYSNR.
    OrthoDBi EOG77127N.
    PhylomeDBi Q9Y463.
    TreeFami TF314624.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS02690-MONOMER.
    BRENDAi 2.7.12.1. 2681.
    SignaLinki Q9Y463.

    Miscellaneous databases

    ChiTaRSi DYRK1B. human.
    GeneWikii DYRK1B.
    GenomeRNAii 9149.
    NextBioi 34319.
    PROi Q9Y463.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y463.
    Bgeei Q9Y463.
    CleanExi HS_DYRK1B.
    Genevestigatori Q9Y463.

    Family and domain databases

    InterProi IPR011009. Kinase-like_dom.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    [Graphical view ]
    SMARTi SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of DYRK1B, a novel member of the DYRK family of protein kinases."
      Leder S., Weber Y., Altafaj X., Estivill X., Joost H.-G., Becker W.
      Biochem. Biophys. Res. Commun. 254:474-479(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
      Tissue: Testis.
    2. "Mirk protein kinase is a mitogen-activated protein kinase substrate that mediates survival of colon cancer cells."
      Lee K., Deng X., Friedman E.
      Cancer Res. 60:3631-3637(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION AT TYR-271 AND TYR-273, MUTAGENESIS OF LYS-140; TYR-271 AND TYR-273.
      Tissue: Colon carcinoma.
    3. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: Pancreas.
    5. "Mirk protein kinase is activated by MKK3 and functions as a transcriptional activator of HNF1alpha."
      Lim S., Jin K., Friedman E.
      J. Biol. Chem. 277:25040-25046(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DCOHM; MAP2K3 AND TCF1.
      Tissue: Muscle.
    6. "Serine/threonine kinase Mirk/Dyrk1B is an inhibitor of epithelial cell migration and is negatively regulated by the Met adaptor Ran-binding protein M."
      Zou Y., Lim S., Lee K., Deng X., Friedman E.
      J. Biol. Chem. 278:49573-49581(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DIMERIZATION, INTERACTION WITH RANBP9, IDENTIFICATION IN A COMPLEX WITH RAN; RANBP9 AND COPS5.
    7. "Phosphorylation of Ser640 in muscle glycogen synthase by DYRK family protein kinases."
      Skurat A.V., Dietrich A.D.
      J. Biol. Chem. 279:2490-2498(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DCAF7.
    8. "Selectivity, cocrystal structures, and neuroprotective properties of leucettines, a family of protein kinase inhibitors derived from the marine sponge alkaloid leucettamine B."
      Tahtouh T., Elkins J.M., Filippakopoulos P., Soundararajan M., Burgy G., Durieu E., Cochet C., Schmid R.S., Lo D.C., Delhommel F., Oberholzer A.E., Pearl L.H., Carreaux F., Bazureau J.P., Knapp S., Meijer L.
      J. Med. Chem. 55:9312-9330(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY.
    9. "Patterns of somatic mutation in human cancer genomes."
      Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
      , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
      Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS [LARGE SCALE ANALYSIS] PRO-28; HIS-102; GLY-234 AND ARG-275.

    Entry informationi

    Entry nameiDYR1B_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y463
    Secondary accession number(s): O75258, O75788, O75789
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 148 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: 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. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3