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Q92608

- DOCK2_HUMAN

UniProt

Q92608 - DOCK2_HUMAN

Protein

Dedicator of cytokinesis protein 2

Gene

DOCK2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 2 (03 Jul 2003)
      Previous versions | rss
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    Functioni

    Involved in cytoskeletal rearrangements required for lymphocyte migration in response of chemokines. Activates RAC1 and RAC2, but not CDC42, by functioning as a guanine nucleotide exchange factor (GEF), which exchanges bound GDP for free GTP. May also participate in IL2 transcriptional activation via the activation of RAC2.1 Publication

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. Rac GTPase activator activity Source: Ensembl
    3. Rac guanyl-nucleotide exchange factor activity Source: UniProtKB
    4. T cell receptor binding Source: UniProtKB

    GO - Biological processi

    1. actin cytoskeleton organization Source: UniProtKB
    2. alpha-beta T cell proliferation Source: Ensembl
    3. chemotaxis Source: Ensembl
    4. establishment of T cell polarity Source: Ensembl
    5. immunological synapse formation Source: Ensembl
    6. macropinocytosis Source: UniProtKB
    7. membrane raft polarization Source: Ensembl
    8. myeloid dendritic cell activation involved in immune response Source: UniProtKB
    9. negative thymic T cell selection Source: Ensembl
    10. positive regulation of phagocytosis Source: UniProtKB
    11. positive thymic T cell selection Source: Ensembl
    12. regulation of defense response to virus by virus Source: Reactome
    13. small GTPase mediated signal transduction Source: InterPro
    14. viral process Source: Reactome

    Keywords - Molecular functioni

    Guanine-nucleotide releasing factor

    Enzyme and pathway databases

    ReactomeiREACT_11068. Nef and signal transduction.
    REACT_24970. Factors involved in megakaryocyte development and platelet production.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dedicator of cytokinesis protein 2
    Gene namesi
    Name:DOCK2
    Synonyms:KIAA0209
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:2988. DOCK2.

    Subcellular locationi

    Endomembrane system 1 Publication; Peripheral membrane protein 1 Publication. Cytoplasmcytoskeleton 1 Publication
    Note: Colocalizes with F-actin.

    GO - Cellular componenti

    1. cytoskeleton Source: UniProtKB-SubCell
    2. cytosol Source: Reactome
    3. endomembrane system Source: UniProtKB-SubCell
    4. extracellular vesicular exosome Source: UniProt
    5. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA27454.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 18301830Dedicator of cytokinesis protein 2PRO_0000189986Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei304 – 3041N6-acetyllysine1 Publication
    Modified residuei588 – 5881Phosphoserine1 Publication
    Modified residuei593 – 5931Phosphoserine1 Publication
    Modified residuei738 – 7381N6-acetyllysine1 Publication
    Modified residuei1685 – 16851Phosphoserine3 Publications
    Modified residuei1731 – 17311Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ92608.
    PaxDbiQ92608.
    PeptideAtlasiQ92608.
    PRIDEiQ92608.

    PTM databases

    PhosphoSiteiQ92608.

    Expressioni

    Tissue specificityi

    Specifically expressed in hematopoietic cells. Highly expressed in peripheral blood leukocytes, and expressed at intermediate level in thymus and spleen. Expressed at very low level in the small intestine and colon.1 Publication

    Gene expression databases

    ArrayExpressiQ92608.
    BgeeiQ92608.
    CleanExiHS_DOCK2.
    GenevestigatoriQ92608.

    Organism-specific databases

    HPAiHPA036468.
    HPA036469.

    Interactioni

    Subunit structurei

    Homodimer Probable. Interacts with RAC1 and RAC2. Interacts with CRKL and VAV. Interacts with CD3Z.4 PublicationsCurated

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    RAC1P630003EBI-448771,EBI-413628

    Protein-protein interaction databases

    BioGridi108129. 9 interactions.
    DIPiDIP-31791N.
    IntActiQ92608. 4 interactions.
    MINTiMINT-2813049.
    STRINGi9606.ENSP00000256935.

    Structurei

    Secondary structure

    1
    1830
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi12 – 176
    Beta strandi34 – 418
    Beta strandi44 – 496
    Beta strandi52 – 609
    Helixi61 – 633
    Beta strandi64 – 674
    Helixi84 – 10724
    Helixi111 – 13323
    Helixi138 – 15821
    Helixi1197 – 121418
    Helixi1217 – 123317
    Helixi1237 – 124812
    Turni1265 – 12673
    Helixi1273 – 129119
    Helixi1294 – 131017
    Helixi1315 – 133420
    Beta strandi1342 – 13498
    Turni1354 – 13585
    Beta strandi1359 – 13646
    Helixi1371 – 138111
    Beta strandi1385 – 13873
    Helixi1396 – 14005
    Beta strandi1405 – 141410
    Helixi1419 – 14213
    Beta strandi1422 – 14243
    Helixi1428 – 14369
    Beta strandi1437 – 144913
    Helixi1458 – 14614
    Beta strandi1462 – 149231
    Helixi1494 – 151825
    Beta strandi1520 – 15223
    Helixi1525 – 153511
    Beta strandi1538 – 15403
    Helixi1544 – 15507
    Helixi1553 – 15586
    Helixi1560 – 15623
    Helixi1563 – 158927
    Helixi1593 – 15953
    Helixi1596 – 161722

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2RQRNMR-A8-70[»]
    2YINX-ray2.70A/B1192-1622[»]
    3A98X-ray2.10A/C1-177[»]
    3B13X-ray3.01A/C1196-1622[»]
    ProteinModelPortaliQ92608.
    SMRiQ92608. Positions 1-167, 423-609, 1196-1622.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini8 – 6962SH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini423 – 607185DHR-1Add
    BLAST
    Domaini1211 – 1622412DHR-2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni939 – 1476538Interaction with CRKLAdd
    BLAST

    Domaini

    The DHR-2 domain may mediate the GEF activity.By similarity

    Sequence similaritiesi

    Belongs to the DOCK family.Curated
    Contains 1 DHR-1 domain.Curated
    Contains 1 DHR-2 domain.Curated
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH3 domain

    Phylogenomic databases

    eggNOGiNOG289808.
    HOGENOMiHOG000006631.
    HOVERGENiHBG051389.
    InParanoidiQ92608.
    KOiK12367.
    OMAiGDWMAMS.
    OrthoDBiEOG7QNVK8.
    PhylomeDBiQ92608.
    TreeFamiTF300423.

    Family and domain databases

    InterProiIPR016024. ARM-type_fold.
    IPR027007. DHR-1_domain.
    IPR027357. DHR-2.
    IPR026791. DOCK.
    IPR026799. DOCK_2.
    IPR010703. DOCK_C.
    IPR011511. SH3_2.
    IPR001452. SH3_domain.
    [Graphical view]
    PANTHERiPTHR23317. PTHR23317. 1 hit.
    PTHR23317:SF73. PTHR23317:SF73. 1 hit.
    PfamiPF06920. Ded_cyto. 1 hit.
    PF14429. DOCK-C2. 1 hit.
    PF07653. SH3_2. 1 hit.
    [Graphical view]
    SMARTiSM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 3 hits.
    SSF50044. SSF50044. 1 hit.
    PROSITEiPS51650. DHR_1. 1 hit.
    PS51651. DHR_2. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q92608-1) [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

    MAPWRKADKE RHGVAIYNFQ GSGAPQLSLQ IGDVVRIQET CGDWYRGYLI     50
    KHKMLQGIFP KSFIHIKEVT VEKRRNTENI IPAEIPLAQE VTTTLWEWGS 100
    IWKQLYVASK KERFLQVQSM MYDLMEWRSQ LLSGTLPKDE LKELKQKVTS 150
    KIDYGNKILE LDLIVRDEDG NILDPDNTSV ISLFHAHEEA TDKITERIKE 200
    EMSKDQPDYA MYSRISSSPT HSLYVFVRNF VCRIGEDAEL FMSLYDPNKQ 250
    TVISENYLVR WGSRGFPKEI EMLNNLKVVF TDLGNKDLNR DKIYLICQIV 300
    RVGKMDLKDT GAKKCTQGLR RPFGVAVMDI TDIIKGKAES DEEKQHFIPF 350
    HPVTAENDFL HSLLGKVIAS KGDSGGQGLW VTMKMLVGDI IQIRKDYPHL 400
    VDRTTVVARK LGFPEIIMPG DVRNDIYITL LQGDFDKYNK TTQRNVEVIM 450
    CVCAEDGKTL PNAICVGAGD KPMNEYRSVV YYQVKQPRWM ETVKVAVPIE 500
    DMQRIHLRFM FRHRSSLESK DKGEKNFAMS YVKLMKEDGT TLHDGFHDLV 550
    VLKGDSKKME DASAYLTLPS YRHHVENKGA TLSRSSSSVG GLSVSSRDVF 600
    SISTLVCSTK LTQNVGLLGL LKWRMKPQLL QENLEKLKIV DGEEVVKFLQ 650
    DTLDALFNIM MEHSQSDEYD ILVFDALIYI IGLIADRKFQ HFNTVLEAYI 700
    QQHFSATLAY KKLMTVLKTY LDTSSRGEQC EPILRTLKAL EYVFKFIVRS 750
    RTLFSQLYEG KEQMEFEESM RRLFESINNL MKSQYKTTIL LQVAALKYIP 800
    SVLHDVEMVF DAKLLSQLLY EFYTCIPPVK LQKQKVQSMN EIVQSNLFKK 850
    QECRDILLPV ITKELKELLE QKDDMQHQVL ERKYCVELLN SILEVLSYQD 900
    AAFTYHHIQE IMVQLLRTVN RTVITMGRDH ILISHFVACM TAILNQMGDQ 950
    HYSFYIETFQ TSSELVDFLM ETFIMFKDLI GKNVYPGDWM AMSMVQNRVF 1000
    LRAINKFAET MNQKFLEHTN FEFQLWNNYF HLAVAFITQD SLQLEQFSHA 1050
    KYNKILNKYG DMRRLIGFSI RDMWYKLGQN KICFIPGMVG PILEMTLIPE 1100
    AELRKATIPI FFDMMLCEYQ RSGDFKKFEN EIILKLDHEV EGGRGDEQYM 1150
    QLLESILMEC AAEHPTIAKS VENFVNLVKG LLEKLLDYRG VMTDESKDNR 1200
    MSCTVNLLNF YKDNNREEMY IRYLYKLRDL HLDCDNYTEA AYTLLLHTWL 1250
    LKWSDEQCAS QVMQTGQQHP QTHRQLKETL YETIIGYFDK GKMWEEAISL 1300
    CKELAEQYEM EIFDYELLSQ NLIQQAKFYE SIMKILRPKP DYFAVGYYGQ 1350
    GFPSFLRNKV FIYRGKEYER REDFQMQLMT QFPNAEKMNT TSAPGDDVKN 1400
    APGQYIQCFT VQPVLDEHPR FKNKPVPDQI INFYKSNYVQ RFHYSRPVRR 1450
    GTVDPENEFA SMWIERTSFV TAYKLPGILR WFEVVHMSQT TISPLENAIE 1500
    TMSTANEKIL MMINQYQSDE TLPINPLSML LNGIVDPAVM GGFAKYEKAF 1550
    FTEEYVRDHP EDQDKLTHLK DLIAWQIPFL GAGIKIHEKR VSDNLRPFHD 1600
    RMEECFKNLK MKVEKEYGVR EMPDFDDRRV GRPRSMLRSY RQMSIISLAS 1650
    MNSDCSTPSK PTSESFDLEL ASPKTPRVEQ EEPISPGSTL PEVKLRRSKK 1700
    RTKRSSVVFA DEKAAAESDL KRLSRKHEFM SDTNLSEHAA IPLKASVLSQ 1750
    MSFASQSMPT IPALALSVAG IPGLDEANTS PRLSQTFLQL SDGDKKTLTR 1800
    KKVNQFFKTM LASKSAEEGK QIPDSLSTDL 1830
    Length:1,830
    Mass (Da):211,948
    Last modified:July 3, 2003 - v2
    Checksum:i18568D3322DAA92A
    GO
    Isoform 2 (identifier: Q92608-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-449: Missing.
         462-494: Missing.
         630-766: Missing.
         934-955: SHFVACMTAILNQMGDQHYSFY → GACCNCGFPSSTPHSLIQWLWG
         956-1830: Missing.

    Note: Splicing donor and acceptor sites between exon 6 and exon 7 are not canonical. No experimental confirmation available.

    Show »
    Length:336
    Mass (Da):38,461
    Checksum:iC5D6CAAB1C3A3490
    GO

    Sequence cautioni

    The sequence BAA13200.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1558 – 15581D → A.
    Corresponds to variant rs13179480 [ dbSNP | Ensembl ].
    VAR_053064
    Natural varianti1746 – 17461S → T.
    Corresponds to variant rs2270898 [ dbSNP | Ensembl ].
    VAR_015822
    Natural varianti1779 – 17791T → S.
    Corresponds to variant rs2270898 [ dbSNP | Ensembl ].
    VAR_022137

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 449449Missing in isoform 2. 1 PublicationVSP_007696Add
    BLAST
    Alternative sequencei462 – 49433Missing in isoform 2. 1 PublicationVSP_007697Add
    BLAST
    Alternative sequencei630 – 766137Missing in isoform 2. 1 PublicationVSP_007698Add
    BLAST
    Alternative sequencei934 – 95522SHFVA…HYSFY → GACCNCGFPSSTPHSLIQWL WG in isoform 2. 1 PublicationVSP_007699Add
    BLAST
    Alternative sequencei956 – 1830875Missing in isoform 2. 1 PublicationVSP_007700Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D86964 mRNA. Translation: BAA13200.1. Different initiation.
    BC016996 mRNA. Translation: AAH16996.1.
    BC104900 mRNA. Translation: AAI04901.1.
    BC113457 mRNA. Translation: AAI13458.1.
    CCDSiCCDS4371.1. [Q92608-1]
    RefSeqiNP_004937.1. NM_004946.2. [Q92608-1]
    UniGeneiHs.586174.

    Genome annotation databases

    EnsembliENST00000256935; ENSP00000256935; ENSG00000134516. [Q92608-1]
    GeneIDi1794.
    KEGGihsa:1794.
    UCSCiuc003maf.3. human. [Q92608-1]

    Polymorphism databases

    DMDMi32469765.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D86964 mRNA. Translation: BAA13200.1 . Different initiation.
    BC016996 mRNA. Translation: AAH16996.1 .
    BC104900 mRNA. Translation: AAI04901.1 .
    BC113457 mRNA. Translation: AAI13458.1 .
    CCDSi CCDS4371.1. [Q92608-1 ]
    RefSeqi NP_004937.1. NM_004946.2. [Q92608-1 ]
    UniGenei Hs.586174.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2RQR NMR - A 8-70 [» ]
    2YIN X-ray 2.70 A/B 1192-1622 [» ]
    3A98 X-ray 2.10 A/C 1-177 [» ]
    3B13 X-ray 3.01 A/C 1196-1622 [» ]
    ProteinModelPortali Q92608.
    SMRi Q92608. Positions 1-167, 423-609, 1196-1622.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108129. 9 interactions.
    DIPi DIP-31791N.
    IntActi Q92608. 4 interactions.
    MINTi MINT-2813049.
    STRINGi 9606.ENSP00000256935.

    PTM databases

    PhosphoSitei Q92608.

    Polymorphism databases

    DMDMi 32469765.

    Proteomic databases

    MaxQBi Q92608.
    PaxDbi Q92608.
    PeptideAtlasi Q92608.
    PRIDEi Q92608.

    Protocols and materials databases

    DNASUi 1794.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000256935 ; ENSP00000256935 ; ENSG00000134516 . [Q92608-1 ]
    GeneIDi 1794.
    KEGGi hsa:1794.
    UCSCi uc003maf.3. human. [Q92608-1 ]

    Organism-specific databases

    CTDi 1794.
    GeneCardsi GC05P169064.
    HGNCi HGNC:2988. DOCK2.
    HPAi HPA036468.
    HPA036469.
    MIMi 603122. gene.
    neXtProti NX_Q92608.
    PharmGKBi PA27454.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG289808.
    HOGENOMi HOG000006631.
    HOVERGENi HBG051389.
    InParanoidi Q92608.
    KOi K12367.
    OMAi GDWMAMS.
    OrthoDBi EOG7QNVK8.
    PhylomeDBi Q92608.
    TreeFami TF300423.

    Enzyme and pathway databases

    Reactomei REACT_11068. Nef and signal transduction.
    REACT_24970. Factors involved in megakaryocyte development and platelet production.

    Miscellaneous databases

    ChiTaRSi DOCK2. human.
    GeneWikii Dock2.
    GenomeRNAii 1794.
    NextBioi 7309.
    PROi Q92608.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92608.
    Bgeei Q92608.
    CleanExi HS_DOCK2.
    Genevestigatori Q92608.

    Family and domain databases

    InterProi IPR016024. ARM-type_fold.
    IPR027007. DHR-1_domain.
    IPR027357. DHR-2.
    IPR026791. DOCK.
    IPR026799. DOCK_2.
    IPR010703. DOCK_C.
    IPR011511. SH3_2.
    IPR001452. SH3_domain.
    [Graphical view ]
    PANTHERi PTHR23317. PTHR23317. 1 hit.
    PTHR23317:SF73. PTHR23317:SF73. 1 hit.
    Pfami PF06920. Ded_cyto. 1 hit.
    PF14429. DOCK-C2. 1 hit.
    PF07653. SH3_2. 1 hit.
    [Graphical view ]
    SMARTi SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 3 hits.
    SSF50044. SSF50044. 1 hit.
    PROSITEi PS51650. DHR_1. 1 hit.
    PS51651. DHR_2. 1 hit.
    PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. VI. The coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of cDNA clones from cell line KG-1 and brain."
      Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., Tanaka A., Kotani H., Miyajima N., Nomura N.
      DNA Res. 3:321-329(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Bone marrow.
    2. "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] (ISOFORMS 1 AND 2).
      Tissue: Colon and Liver.
    3. "Non-adherent cell-specific expression of DOCK2, a member of the human CDM-family proteins."
      Nishihara H., Kobayashi S., Hashimoto Y., Ohba F., Mochizuki N., Kurata T., Nagashima K., Matsuda M.
      Biochim. Biophys. Acta 1452:179-187(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, RAC1 ACTIVATION, INTERACTION WITH RAC1 AND RAC2.
    4. "DOCK2 associates with CrkL and regulates Rac1 in human leukemia cell lines."
      Nishihara H., Maeda M., Oda A., Tsuda M., Sawa H., Nagashima K., Tanaka S.
      Blood 100:3968-3974(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CRKL AND VAV.
    5. "DOCK2 mediates T cell receptor-induced activation of Rac2 and IL-2 transcription."
      Nishihara H., Maeda M., Tsuda M., Makino Y., Sawa H., Nagashima K., Tanaka S.
      Biochem. Biophys. Res. Commun. 296:716-720(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CD3Z.
    6. "Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity."
      Cote J.-F., Vuori K.
      J. Cell Sci. 115:4901-4913(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NOMENCLATURE.
    7. "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
      Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
      Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    8. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1685, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1685, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-588; SER-593; SER-1685 AND SER-1731, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    11. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-304 AND LYS-738, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "The solution structure of human DOCK2 SH3 domain - ELMO1 peptide chimera complex."
      RIKEN structural genomics initiative (RSGI)
      Submitted (OCT-2010) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 8-70.
    14. "Multiple factors confer specific Cdc42 and Rac protein activation by dedicator of cytokinesis (DOCK) nucleotide exchange factors."
      Kulkarni K., Yang J., Zhang Z., Barford D.
      J. Biol. Chem. 286:25341-25351(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1192-1622 IN COMPLEX WITH RAC1, INTERACTION WITH RAC1, SUBUNIT, FUNCTION.

    Entry informationi

    Entry nameiDOCK2_HUMAN
    AccessioniPrimary (citable) accession number: Q92608
    Secondary accession number(s): Q2M3I0, Q96AK7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 3, 2003
    Last sequence update: July 3, 2003
    Last modified: October 1, 2014
    This is version 135 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 5
      Human chromosome 5: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3