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Q9P104

- DOK5_HUMAN

UniProt

Q9P104 - DOK5_HUMAN

Protein

Docking protein 5

Gene

DOK5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 2 (06 Dec 2002)
      Previous versions | rss
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    Functioni

    DOK proteins are enzymatically inert adaptor or scaffolding proteins. They provide a docking platform for the assembly of multimolecular signaling complexes. DOK5 functions in RET-mediated neurite outgrowth and plays a positive role in activation of the MAP kinase pathway. Putative link with downstream effectors of RET in neuronal differentiation.

    GO - Molecular functioni

    1. receptor signaling protein activity Source: Ensembl

    GO - Biological processi

    1. MAPK cascade Source: Ensembl
    2. nervous system development Source: Ensembl
    3. transmembrane receptor protein tyrosine kinase signaling pathway Source: Ensembl

    Enzyme and pathway databases

    SignaLinkiQ9P104.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Docking protein 5
    Alternative name(s):
    Downstream of tyrosine kinase 5
    Insulin receptor substrate 6
    Short name:
    IRS-6
    Short name:
    IRS6
    Gene namesi
    Name:DOK5
    Synonyms:C20orf180
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:16173. DOK5.

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25724.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 306306Docking protein 5PRO_0000187277Add
    BLAST

    Post-translational modificationi

    Phosphorylated on tyrosine residues in response to insulin, IGF1 and GDNF.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9P104.
    PRIDEiQ9P104.

    PTM databases

    PhosphoSiteiQ9P104.

    Expressioni

    Tissue specificityi

    Highest expression in skeletal muscle, lower in brain, heart and kidney. Also detected in activated peripheral blood T-lymphocytes.2 Publications

    Gene expression databases

    BgeeiQ9P104.
    CleanExiHS_DOK5.
    GenevestigatoriQ9P104.

    Interactioni

    Subunit structurei

    Interacts with phosphorylated RET. In contrast to other DOK proteins, it does not interact with RASGAP By similarity.By similarity

    Protein-protein interaction databases

    BioGridi120926. 4 interactions.
    IntActiQ9P104. 4 interactions.
    MINTiMINT-1435904.
    STRINGi9606.ENSP00000262593.

    Structurei

    Secondary structure

    1
    306
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi137 – 1437
    Beta strandi153 – 1597
    Beta strandi161 – 17111
    Beta strandi174 – 1807
    Helixi181 – 1833
    Beta strandi184 – 1896
    Beta strandi191 – 1988
    Beta strandi200 – 2045
    Beta strandi206 – 2127
    Helixi216 – 22914

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1J0WX-ray2.50A/B133-232[»]
    ProteinModelPortaliQ9P104.
    SMRiQ9P104. Positions 133-232.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9P104.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini8 – 112105PHAdd
    BLAST
    Domaini132 – 237106IRS-type PTBPROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi263 – 27311DKFBH motifAdd
    BLAST

    Domaini

    PTB domain mediates receptor interaction.By similarity

    Sequence similaritiesi

    Belongs to the DOK family. Type B subfamily.Curated
    Contains 1 IRS-type PTB domain.PROSITE-ProRule annotation
    Contains 1 PH domain.Curated

    Phylogenomic databases

    eggNOGiNOG256436.
    HOVERGENiHBG002356.
    InParanoidiQ9P104.
    OMAiHAVGIYF.
    OrthoDBiEOG7GTT3W.
    PhylomeDBiQ9P104.
    TreeFamiTF324994.

    Family and domain databases

    Gene3Di2.30.29.30. 2 hits.
    InterProiIPR002404. Insln_rcpt_S1.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view]
    PfamiPF02174. IRS. 1 hit.
    [Graphical view]
    SMARTiSM00233. PH. 1 hit.
    SM00310. PTBI. 1 hit.
    [Graphical view]
    PROSITEiPS51064. IRS_PTB. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9P104-1) [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

    MASNFNDIVK QGYVRIRSRR LGIYQRCWLV FKKASSKGPK RLEKFSDERA    50
    AYFRCYHKVT ELNNVKNVAR LPKSTKKHAI GIYFNDDTSK TFACESDLEA 100
    DEWCKVLQME CVGTRINDIS LGEPDLLATG VEREQSERFN VYLMPSPNLD 150
    VHGECALQIT YEYICLWDVQ NPRVKLISWP LSALRRYGRD TTWFTFEAGR 200
    MCETGEGLFI FQTRDGEAIY QKVHSAALAI AEQHERLLQS VKNSMLQMKM 250
    SERAASLSTM VPLPRSAYWQ HITRQHSTGQ LYRLQDVSSP LKLHRTETFP 300
    AYRSEH 306
    Length:306
    Mass (Da):35,464
    Last modified:December 6, 2002 - v2
    Checksum:i2F259529E8B068DB
    GO
    Isoform 2 (identifier: Q9P104-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-108: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:198
    Mass (Da):22,824
    Checksum:i291F9F2A419FE062
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti225 – 23410SAALAIAEQH → LLQMKMSERA in AAF66443. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 108108Missing in isoform 2. 1 PublicationVSP_003854Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF132732 mRNA. Translation: AAF66443.1.
    AF466368 mRNA. Translation: AAL74194.1.
    AL118501, AL162292 Genomic DNA. Translation: CAI19415.1.
    AL118501 Genomic DNA. Translation: CAI19416.1.
    AL162292, AL118501 Genomic DNA. Translation: CAI16465.1.
    BC008992 mRNA. Translation: AAH08992.1.
    AL050069 mRNA. Translation: CAB43255.3.
    CCDSiCCDS13446.1. [Q9P104-1]
    PIRiT08731.
    RefSeqiNP_060901.2. NM_018431.3. [Q9P104-1]
    XP_005260508.1. XM_005260451.1. [Q9P104-2]
    UniGeneiHs.656582.

    Genome annotation databases

    EnsembliENST00000262593; ENSP00000262593; ENSG00000101134. [Q9P104-1]
    ENST00000395939; ENSP00000379270; ENSG00000101134. [Q9P104-2]
    GeneIDi55816.
    KEGGihsa:55816.
    UCSCiuc002xwy.3. human. [Q9P104-1]

    Polymorphism databases

    DMDMi26393190.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF132732 mRNA. Translation: AAF66443.1 .
    AF466368 mRNA. Translation: AAL74194.1 .
    AL118501 , AL162292 Genomic DNA. Translation: CAI19415.1 .
    AL118501 Genomic DNA. Translation: CAI19416.1 .
    AL162292 , AL118501 Genomic DNA. Translation: CAI16465.1 .
    BC008992 mRNA. Translation: AAH08992.1 .
    AL050069 mRNA. Translation: CAB43255.3 .
    CCDSi CCDS13446.1. [Q9P104-1 ]
    PIRi T08731.
    RefSeqi NP_060901.2. NM_018431.3. [Q9P104-1 ]
    XP_005260508.1. XM_005260451.1. [Q9P104-2 ]
    UniGenei Hs.656582.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1J0W X-ray 2.50 A/B 133-232 [» ]
    ProteinModelPortali Q9P104.
    SMRi Q9P104. Positions 133-232.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120926. 4 interactions.
    IntActi Q9P104. 4 interactions.
    MINTi MINT-1435904.
    STRINGi 9606.ENSP00000262593.

    PTM databases

    PhosphoSitei Q9P104.

    Polymorphism databases

    DMDMi 26393190.

    Proteomic databases

    PaxDbi Q9P104.
    PRIDEi Q9P104.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262593 ; ENSP00000262593 ; ENSG00000101134 . [Q9P104-1 ]
    ENST00000395939 ; ENSP00000379270 ; ENSG00000101134 . [Q9P104-2 ]
    GeneIDi 55816.
    KEGGi hsa:55816.
    UCSCi uc002xwy.3. human. [Q9P104-1 ]

    Organism-specific databases

    CTDi 55816.
    GeneCardsi GC20P053092.
    HGNCi HGNC:16173. DOK5.
    MIMi 608334. gene.
    neXtProti NX_Q9P104.
    PharmGKBi PA25724.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG256436.
    HOVERGENi HBG002356.
    InParanoidi Q9P104.
    OMAi HAVGIYF.
    OrthoDBi EOG7GTT3W.
    PhylomeDBi Q9P104.
    TreeFami TF324994.

    Enzyme and pathway databases

    SignaLinki Q9P104.

    Miscellaneous databases

    EvolutionaryTracei Q9P104.
    GeneWikii DOK5.
    GenomeRNAii 55816.
    NextBioi 60998.
    PROi Q9P104.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9P104.
    CleanExi HS_DOK5.
    Genevestigatori Q9P104.

    Family and domain databases

    Gene3Di 2.30.29.30. 2 hits.
    InterProi IPR002404. Insln_rcpt_S1.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view ]
    Pfami PF02174. IRS. 1 hit.
    [Graphical view ]
    SMARTi SM00233. PH. 1 hit.
    SM00310. PTBI. 1 hit.
    [Graphical view ]
    PROSITEi PS51064. IRS_PTB. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Luo W.Q., Chen J.H., Huang X.W., Zhou Y., Zhou H.J., Hu S.N., Yuan J.G.
      Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "DOK4 and DOK5: new Dok-related genes expressed in human T cells."
      Favre C., Gerard A., Clauzier E., Pontarotti P., Olive D., Nunes J.A.
      Genes Immun. 4:40-45(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    3. "Two new substrates in insulin signaling, IRS5/DOK4 and IRS6/DOK5."
      Cai D., Dhe-Paganon S., Melendez P.A., Lee J., Shoelson S.E.
      J. Biol. Chem. 278:25323-25330(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, PHOSPHORYLATION AT TYROSINE RESIDUES.
      Tissue: Skeletal muscle.
    4. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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 2).
      Tissue: Brain.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 42-306 (ISOFORM 1).
      Tissue: Kidney.
    7. "Expression, crystallization and preliminary X-ray studies of the recombinant PTB domain of human dok-5 protein."
      Shi N., Zhou W., Tang K., Gao Y., Jin J., Gao F., Peng X., Bartlam M., Qiang B., Yuan J., Rao Z.
      Acta Crystallogr. D 58:2170-2172(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: CRYSTALLIZATION.

    Entry informationi

    Entry nameiDOK5_HUMAN
    AccessioniPrimary (citable) accession number: Q9P104
    Secondary accession number(s): Q5T7Y0
    , Q5TE53, Q8TEW7, Q96H13, Q9BZ24, Q9NQF4, Q9Y411
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 6, 2002
    Last sequence update: December 6, 2002
    Last modified: October 1, 2014
    This is version 122 of the entry and version 2 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 20
      Human chromosome 20: 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