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Q5VWQ8

- DAB2P_HUMAN

UniProt

Q5VWQ8 - DAB2P_HUMAN

Protein

Disabled homolog 2-interacting protein

Gene

DAB2IP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 2 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Functions as a scaffold protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Involved in several processes such as innate immune response, inflammation and cell growth inhibition, apoptosis, cell survival, angiogenesis, cell migration and maturation. Plays also a role in cell cycle checkpoint control; reduces G1 phase cyclin levels resulting in G0/G1 cell cycle arrest. Mediates signal transduction by receptor-mediated inflammatory signals, such as the tumor necrosis factor (TNF), interferon (IFN) or lipopolysaccharide (LPS). Modulates the balance between phosphatidylinositol 3-kinase (PI3K)-AKT-mediated cell survival and apoptosis stimulated kinase (MAP3K5)-JNK signaling pathways; sequesters both AKT1 and MAP3K5 and counterbalances the activity of each kinase by modulating their phosphorylation status in response to proinflammatory stimuli. Acts as a regulator of the endoplasmic reticulum (ER) unfolded protein response (UPR) pathway; specifically involved in transduction of the ER stress-response to the JNK cascade through ERN1. Mediates TNF-alpha-induced apoptosis activation by facilitating dissociation of inhibitor 14-3-3 from MAP3K5; recruits the PP2A phosphatase complex which dephosphorylates MAP3K5 on 'Ser-966', leading to the dissociation of 13-3-3 proteins and activation of the MAP3K5-JNK signaling pathway in endothelial cells. Mediates also TNF/TRAF2-induced MAP3K5-JNK activation, while it inhibits CHUK-NF-kappa-B signaling. Acts a negative regulator in the IFN-gamma-mediated JAK-STAT signaling cascade by inhibiting smooth muscle cell (VSMCs) proliferation and intimal expansion, and thus, prevents graft arteriosclerosis (GA). Acts as a GTPase-activating protein (GAP) for the ADP ribosylation factor 6 (ARF6) and Ras. Promotes hydrolysis of the ARF6-bound GTP and thus, negatively regulates phosphatidylinositol 4,5-bisphosphate (PIP2)-dependent TLR4-TIRAP-MyD88 and NF-kappa-B signaling pathways in endothelial cells in response to lipopolysaccharides (LPS). Binds specifically to phosphatidylinositol 4-phosphate (PtdIns4P) and phosphatidylinositol 3-phosphate (PtdIns3P). In response to vascular endothelial growth factor (VEGFA), acts as a negative regulator of the VEGFR2-PI3K-mediated angiogenic signaling pathway by inhibiting endothelial cell migration and tube formation. In the developing brain, promotes both the transition from the multipolar to the bipolar stage and the radial migration of cortical neurons from the ventricular zone toward the superficial layer of the neocortex in a glial-dependent locomotion process. Probable downstream effector of the Reelin signaling pathway; promotes Purkinje cell (PC) dendrites development and formation of cerebellar synapses. Functions also as a tumor suppressor protein in prostate cancer progression; prevents cell proliferation and epithelial-to-mesenchymal transition (EMT) through activation of the glycogen synthase kinase-3 beta (GSK3B)-induced beta-catenin and inhibition of PI3K-AKT and Ras-MAPK survival downstream signaling cascades, respectively.10 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei172 – 1732Breakpoint for translocation to form KMT2A/MLL1-DAB2IP

    GO - Molecular functioni

    1. 14-3-3 protein binding Source: BHF-UCL
    2. death receptor binding Source: BHF-UCL
    3. identical protein binding Source: IntAct
    4. kinase binding Source: UniProtKB
    5. mitogen-activated protein kinase kinase binding Source: UniProtKB
    6. mitogen-activated protein kinase kinase kinase binding Source: BHF-UCL
    7. phosphatidylinositol 3-kinase binding Source: UniProtKB
    8. phosphatidylinositol 3-kinase regulatory subunit binding Source: UniProtKB
    9. phosphatidylinositol-3-phosphate binding Source: UniProtKB
    10. phosphatidylinositol-4-phosphate binding Source: UniProtKB
    11. protein binding Source: UniProtKB
    12. protein complex binding Source: UniProtKB
    13. protein homodimerization activity Source: BHF-UCL
    14. protein kinase binding Source: BHF-UCL
    15. protein phosphatase 2A binding Source: BHF-UCL
    16. Ras GTPase activator activity Source: BHF-UCL
    17. SH3 domain binding Source: UniProtKB
    18. signaling adaptor activity Source: BHF-UCL
    19. vascular endothelial growth factor receptor 2 binding Source: UniProtKB

    GO - Biological processi

    1. activation of JUN kinase activity Source: BHF-UCL
    2. activation of MAPKKK activity Source: UniProtKB
    3. angiogenesis Source: UniProtKB-KW
    4. cell cycle Source: UniProtKB-KW
    5. cell motility involved in cerebral cortex radial glia guided migration Source: UniProtKB
    6. cellular protein catabolic process Source: UniProtKB
    7. cellular response to epidermal growth factor stimulus Source: BHF-UCL
    8. cellular response to interleukin-1 Source: UniProtKB
    9. cellular response to lipopolysaccharide Source: UniProtKB
    10. cellular response to tumor necrosis factor Source: UniProtKB
    11. cellular response to vascular endothelial growth factor stimulus Source: UniProtKB
    12. endothelial cell apoptotic process Source: BHF-UCL
    13. extrinsic apoptotic signaling pathway via death domain receptors Source: BHF-UCL
    14. I-kappaB phosphorylation Source: UniProtKB
    15. inflammatory response Source: UniProtKB-KW
    16. innate immune response Source: UniProtKB-KW
    17. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: BHF-UCL
    18. layer formation in cerebral cortex Source: UniProtKB
    19. negative regulation of angiogenesis Source: UniProtKB
    20. negative regulation of canonical Wnt signaling pathway Source: BHF-UCL
    21. negative regulation of catenin import into nucleus Source: BHF-UCL
    22. negative regulation of cell growth Source: Ensembl
    23. negative regulation of cell proliferation Source: UniProtKB
    24. negative regulation of cyclin catabolic process Source: UniProtKB
    25. negative regulation of endothelial cell migration Source: UniProtKB
    26. negative regulation of epidermal growth factor receptor signaling pathway Source: BHF-UCL
    27. negative regulation of epithelial cell migration Source: UniProtKB
    28. negative regulation of epithelial cell proliferation Source: BHF-UCL
    29. negative regulation of epithelial to mesenchymal transition Source: UniProtKB
    30. negative regulation of ERK1 and ERK2 cascade Source: UniProtKB
    31. negative regulation of fibroblast proliferation Source: BHF-UCL
    32. negative regulation of G0 to G1 transition Source: UniProtKB
    33. negative regulation of GTPase activity Source: UniProtKB
    34. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    35. negative regulation of MAP kinase activity Source: BHF-UCL
    36. negative regulation of NF-kappaB transcription factor activity Source: BHF-UCL
    37. negative regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
    38. negative regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
    39. negative regulation of protein phosphorylation Source: UniProtKB
    40. negative regulation of protein serine/threonine kinase activity Source: UniProtKB
    41. negative regulation of Ras GTPase activity Source: BHF-UCL
    42. negative regulation of Ras protein signal transduction Source: BHF-UCL
    43. negative regulation of toll-like receptor 4 signaling pathway Source: UniProtKB
    44. negative regulation of transcription, DNA-templated Source: UniProtKB
    45. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    46. negative regulation of vascular endothelial growth factor receptor signaling pathway Source: UniProtKB
    47. negative regulation of vascular endothelial growth factor signaling pathway Source: UniProtKB
    48. neuron projection morphogenesis Source: UniProtKB
    49. positive regulation of apoptotic process Source: UniProtKB
    50. positive regulation of apoptotic signaling pathway Source: UniProtKB
    51. positive regulation of cell cycle arrest Source: UniProtKB
    52. positive regulation of dendrite development Source: UniProtKB
    53. positive regulation of JNK cascade Source: UniProtKB
    54. positive regulation of JUN kinase activity Source: BHF-UCL
    55. positive regulation of MAPK cascade Source: UniProtKB
    56. positive regulation of neuron migration Source: UniProtKB
    57. positive regulation of neuron projection development Source: UniProtKB
    58. positive regulation of proteasomal protein catabolic process Source: UniProtKB
    59. positive regulation of protein catabolic process Source: UniProtKB
    60. positive regulation of protein serine/threonine kinase activity Source: UniProtKB
    61. positive regulation of Ras GTPase activity Source: RefGenome
    62. positive regulation of synapse maturation Source: UniProtKB
    63. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    64. regulation of ARF GTPase activity Source: UniProtKB
    65. regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
    66. regulation of p38MAPK cascade Source: UniProtKB
    67. regulation of protein complex assembly Source: UniProtKB
    68. response to unfolded protein Source: UniProtKB-KW
    69. transformed cell apoptotic process Source: BHF-UCL
    70. tube formation Source: UniProtKB
    71. vascular endothelial growth factor receptor-2 signaling pathway Source: UniProtKB

    Keywords - Molecular functioni

    Developmental protein, GTPase activation

    Keywords - Biological processi

    Angiogenesis, Apoptosis, Cell cycle, Growth regulation, Immunity, Inflammatory response, Innate immunity, Stress response, Unfolded protein response

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Disabled homolog 2-interacting protein
    Short name:
    DAB2 interaction protein
    Short name:
    DAB2-interacting protein
    Alternative name(s):
    ASK-interacting protein 1
    Short name:
    AIP-1
    DOC-2/DAB-2 interactive protein
    Gene namesi
    Name:DAB2IP
    Synonyms:AF9Q34, AIP1, KIAA1743
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:17294. DAB2IP.

    Subcellular locationi

    Cytoplasm. Cell membrane Curated; Peripheral membrane protein Curated. Membrane. Cell projectiondendrite By similarity
    Note: Localized in soma and dendrites of Purkinje cells as well as in scattered cell bodies in the molecular layer of the cerebellum By similarity. Colocalizes with TIRAP at the plasma membrane. Colocalizes with ARF6 at the plasma membrane and endocytic vesicles. Translocates from the plasma membrane to the cytoplasm in response to TNF-alpha. Phosphatidylinositol 4-phosphate (PtdIns4P) binding is essential for plasma membrane localization.By similarity

    GO - Cellular componenti

    1. axon Source: UniProtKB
    2. cerebellar mossy fiber Source: UniProtKB
    3. climbing fiber Source: UniProtKB
    4. cytoplasm Source: UniProtKB
    5. dendrite Source: UniProtKB-SubCell
    6. endocytic vesicle Source: UniProtKB
    7. extracellular vesicular exosome Source: UniProt
    8. intrinsic component of the cytoplasmic side of the plasma membrane Source: RefGenome
    9. neuronal cell body Source: UniProtKB
    10. neuronal cell body membrane Source: UniProtKB
    11. parallel fiber Source: UniProtKB
    12. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    A chromosomal aberration involving DAB2IP is found in a patient with acute myeloid leukemia (AML). Translocation t(9;11)(q34;q23) with KMT2A/MLL1. May give rise to a KMT2A/MLL1-DAB2IP fusion protein lacking the PH domain.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi228 – 2303KKK → AAA: Reduces interaction with KDR/VEGFR2. Does not inhibit interaction with MAP3K5. 1 Publication
    Mutagenesisi281 – 2844KKKK → AAAA: Significantly reduces interaction with MAP3K5. Does not reduce interaction with KDR/VEGFR2. 1 Publication
    Mutagenesisi413 – 4131R → L: Does not inhibit interaction with MAP3K5. Does not reduce GSK3B-induced beta-catenin transcription activity, TNF-alpha-induced apoptosis, ARF6-mediated TLR4-TIRAP-MyD88 signaling inhibition, Ras and NF-kappa-B activities and tumor development. Does not suppress tumor development; when associated with A-728. 5 Publications
    Mutagenesisi728 – 7281S → A: Inhibits phosphorylation and TNF-alpha-induced MAP3K5 dephosphorylation. Reduces interaction with 14-3-3 proteins, AKT1, a regulatory p85 subunit, MAP3K5, RIPK1, TRAF2 and TNF-alpha-induced MAP3K5-JNK signaling and apoptosis. Reduces RAS activity. Does not reduce GSK3B-induced beta catenin-mediated transcription activity. Does not reduce NF-kappa-B activity, cell invasion, epithelial-to-mesenchymal transition (EMT) and tumor development. Does not suppress tumor development; when associated with R-413. 5 Publications
    Mutagenesisi920 – 92910PPPPPPPPPP → AAAAAAAAAA: Reduces interaction with a regulatory p85 subunit of the PI3K complex. Inhibits MAP3K5 active form increase, AKT1 active form decrease, PI3K-p85 complex activity inhibition and TNF-induced apoptosis. 1 Publication
    Mutagenesisi935 – 9351T → A: Does not reduce interaction with 14-3-3 proteins. 2 Publications

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA27133.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11891189Disabled homolog 2-interacting proteinPRO_0000252407Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei728 – 7281Phosphoserine; by MAP3K5 and RIPK12 Publications
    Modified residuei978 – 9781Phosphoserine1 Publication

    Post-translational modificationi

    In response to TNF-alpha-induction, phosphorylated at Ser-728; phosphorylation leads to a conformational change, and thus, increases its association with 14-3-3 proteins, MAP3K5, RIPK1 and TRAF2 in endothelial cells; also stimulates regulatory p85 subunit sequestring and PI3K-p85 complex activity inhibition.3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ5VWQ8.
    PaxDbiQ5VWQ8.
    PRIDEiQ5VWQ8.

    PTM databases

    PhosphoSiteiQ5VWQ8.

    Expressioni

    Tissue specificityi

    Expressed in endothelial and vascular smooth muscle cells (VSMCs). Expressed in prostate epithelial but poorly in prostate cancer cells. Poorly expressed in medulloblastoma cells compared to cerebellar precursor proliferating progenitor cells (at protein level). Low expression in prostate. Down-regulated in prostate cancer.4 Publications

    Inductioni

    Down-regulated in prostate cancer and medulloblastoma.2 Publications

    Gene expression databases

    ArrayExpressiQ5VWQ8.
    BgeeiQ5VWQ8.
    CleanExiHS_DAB2IP.
    GenevestigatoriQ5VWQ8.

    Organism-specific databases

    HPAiHPA036977.

    Interactioni

    Subunit structurei

    On plasma membrane, exists in an inactive form complexed with TNFR1; in response to TNF-alpha, dissociates from TNFR1 complex, tranlocates to cytoplasm and forms part of an intracellular signaling complex comprising TRADD, RALBP1, TRAF2 and MAP3K5. Interacts with DAB1. Interacts (via NPXY motif) with DAB2 (via PID domain). Interacts (via PH domain) with ERN1 By similarity. Part of a cytoplasmic complex made of HIPK1, DAB2IP and MAP3K5 in response to TNF-alpha; this complex formation promotes MAP3K5-JNK activation and subsequent apoptosis. Interacts (via N-terminal domain) with JAK2; the interaction occurs in a IFNG/IFN-gamma-dependent manner and inhibits JAK2 autophosphorylation activity. Interacts (via C2 domain) with GSK3B; the interaction stimulates GSK3B kinase activation. Interacts (via C2 domain) with PPP2CA. Interacts (via proline-rich motif) with a regulatory p85 subunit (via SH3 domain) of the PI3K complex; the interaction inhibits the PI3K-AKT complex activity in a TNF-alpha-dependent manner in prostate cancer (PCa) cells. Interacts with AKT1; the interaction is increased in a TNF-alpha-induced manner. Interacts (via C2 domain and active form preferentially) with KDR/VEGFR2 (tyrosine-phosphorylated active form preferentially); the interaction occurs at the late phase of VEGFA response and inhibits KDR/VEGFR2 activity. Interacts (via N-terminus C2 domain) with MAP3K5 ('Ser-966' dephosphorylated form preferentially); the interaction occurs in a TNF-alpha-induced manner. Interacts (via Ras-GAP domain) with the catalytic subunit of protein phosphatase PP2A; the interaction occurs in resting endothelial cells, is further enhanced by TNF-alpha stimulation and is required to bridge PP2A to MAP3K5. Interacts (via C-terminus PER domain) with TRAF2 (via zinc fingers); the interaction occurs in a TNF-alpha-dependent manner. Interacts with 14-3-3 proteins; the interaction occurs in a TNF-alpha-dependent manner. Interacts (via Ras-GAP domain) with RIPK1 (via kinase domain); the interaction occurs in a TNF-alpha-dependent manner.By similarity9 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-2871881,EBI-2871881
    AXIN1O151692EBI-9543020,EBI-710484
    GSK3BP498412EBI-9543020,EBI-373586
    MAP3K5Q996832EBI-2871881,EBI-476263

    Protein-protein interaction databases

    BioGridi127478. 13 interactions.
    DIPiDIP-41721N.
    IntActiQ5VWQ8. 5 interactions.
    MINTiMINT-268247.
    STRINGi9606.ENSP00000259371.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5VWQ8.
    SMRiQ5VWQ8. Positions 329-662.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini101 – 202102PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini200 – 29596C2Add
    BLAST
    Domaini371 – 563193Ras-GAPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni646 – 943298Necessary for interaction with AKT1Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1026 – 1159134Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi8 – 5245Arg-richAdd
    BLAST
    Compositional biasi112 – 1176Poly-Ala
    Compositional biasi867 – 8704Poly-Ala
    Compositional biasi903 – 94846Pro-richAdd
    BLAST

    Domaini

    The C2 and Ras-GAP domains constitutively bind to MAP3K5 and facilitate the release of 14-3-3 proteins from MAP3K5. The PH and Ras-GAP domains, but not the NPXY motif, are crucial for its cell membrane localization and neuronal migration function. The PH domain is necessary but not sufficient to activate the JNK signaling pathway through ERN1 By similarity. Exists in a closed inactive form by an intramolecular interaction between the N- and the C-terminal domains. The proline-rich motif is critical both for PI3K-AKT activity inhibition and MAP3K5 activation. The PH and C2 domains are necessary for the binding to phosphatidylinositol phosphate. The Ras-GAP domain is necessary for its tumor-suppressive function.By similarity

    Sequence similaritiesi

    Contains 1 C2 domain.Curated
    Contains 1 PH domain.PROSITE-ProRule annotation
    Contains 1 Ras-GAP domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG245428.
    HOVERGENiHBG006492.
    InParanoidiQ5VWQ8.
    OMAiEKGGQPT.
    OrthoDBiEOG74XS5P.
    PhylomeDBiQ5VWQ8.
    TreeFamiTF105303.

    Family and domain databases

    Gene3Di1.10.506.10. 1 hit.
    2.30.29.30. 1 hit.
    2.60.40.150. 1 hit.
    InterProiIPR000008. C2_dom.
    IPR021887. DUF3498.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR001936. RasGAP.
    IPR023152. RasGAP_CS.
    IPR008936. Rho_GTPase_activation_prot.
    [Graphical view]
    PfamiPF00168. C2. 1 hit.
    PF12004. DUF3498. 1 hit.
    PF00616. RasGAP. 1 hit.
    [Graphical view]
    SMARTiSM00239. C2. 1 hit.
    SM00233. PH. 1 hit.
    SM00323. RasGAP. 1 hit.
    [Graphical view]
    SUPFAMiSSF48350. SSF48350. 1 hit.
    SSF49562. SSF49562. 1 hit.
    PROSITEiPS50003. PH_DOMAIN. 1 hit.
    PS00509. RAS_GTPASE_ACTIV_1. 1 hit.
    PS50018. RAS_GTPASE_ACTIV_2. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q5VWQ8-1) [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

    MSAGGSARKS TGRSSYYYRL LRRPRLQRQR SRSRSRTRPA RESPQERPGS     50
    RRSLPGSLSE KSPSMEPSAA TPFRVTGFLS RRLKGSIKRT KSQPKLDRNH 100
    SFRHILPGFR SAAAAAADNE RSHLMPRLKE SRSHESLLSP SSAVEALDLS 150
    MEEEVVIKPV HSSILGQDYC FEVTTSSGSK CFSCRSAAER DKWMENLRRA 200
    VHPNKDNSRR VEHILKLWVI EAKDLPAKKK YLCELCLDDV LYARTTGKLK 250
    TDNVFWGEHF EFHNLPPLRT VTVHLYRETD KKKKKERNSY LGLVSLPAAS 300
    VAGRQFVEKW YPVVTPNPKG GKGPGPMIRI KARYQTITIL PMEMYKEFAE 350
    HITNHYLGLC AALEPILSAK TKEEMASALV HILQSTGKVK DFLTDLMMSE 400
    VDRCGDNEHL IFRENTLATK AIEEYLKLVG QKYLQDALGE FIKALYESDE 450
    NCEVDPSKCS AADLPEHQGN LKMCCELAFC KIINSYCVFP RELKEVFASW 500
    RQECSSRGRP DISERLISAS LFLRFLCPAI MSPSLFNLLQ EYPDDRTART 550
    LTLIAKVTQN LANFAKFGSK EEYMSFMNQF LEHEWTNMQR FLLEISNPET 600
    LSNTAGFEGY IDLGRELSSL HSLLWEAVSQ LEQSIVSKLG PLPRILRDVH 650
    TALSTPGSGQ LPGTNDLAST PGSGSSSISA GLQKMVIEND LSGLIDFTRL 700
    PSPTPENKDL FFVTRSSGVQ PSPARSSSYS EANEPDLQMA NGGKSLSMVD 750
    LQDARTLDGE AGSPAGPDVL PTDGQAAAAQ LVAGWPARAT PVNLAGLATV 800
    RRAGQTPTTP GTSEGAPGRP QLLAPLSFQN PVYQMAAGLP LSPRGLGDSG 850
    SEGHSSLSSH SNSEELAAAA KLGSFSTAAE ELARRPGELA RRQMSLTEKG 900
    GQPTVPRQNS AGPQRRIDQP PPPPPPPPPA PRGRTPPNLL STLQYPRPSS 950
    GTLASASPDW VGPSTRLRQQ SSSSKGDSPE LKPRAVHKQG PSPVSPNALD 1000
    RTAAWLLTMN AQLLEDEGLG PDPPHRDRLR SKDELSQAEK DLAVLQDKLR 1050
    ISTKKLEEYE TLFKCQEETT QKLVLEYQAR LEEGEERLRR QQEDKDIQMK 1100
    GIISRLMSVE EELKKDHAEM QAAVDSKQKI IDAQEKRIAS LDAANARLMS 1150
    ALTQLKERYS MQARNGISPT NPTKLQITEN GEFRNSSNC 1189

    Note: Gene prediction based on EST data.

    Length:1,189
    Mass (Da):131,625
    Last modified:October 17, 2006 - v2
    Checksum:i7494FF05AACF3320
    GO
    Isoform 2 (identifier: Q5VWQ8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-124: Missing.

    Show »
    Length:1,065
    Mass (Da):117,651
    Checksum:i4787F41F02108AA3
    GO
    Isoform 3 (identifier: Q5VWQ8-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-193: Missing.
         1158-1189: RYSMQARNGISPTNPTKLQITENGEFRNSSNC → SMH

    Show »
    Length:967
    Mass (Da):106,764
    Checksum:iE69CEB1FB00A2219
    GO
    Isoform 4 (identifier: Q5VWQ8-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-124: Missing.
         1158-1189: RYSMQARNGISPTNPTKLQITENGEFRNSSNC → SMH

    Show »
    Length:1,036
    Mass (Da):114,410
    Checksum:i1B07D8D3B9DEA76A
    GO
    Isoform 5 (identifier: Q5VWQ8-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2-41: SAGGSARKSTGRSSYYYRLLRRPRLQRQRSRSRSRTRPAR → EPDSLLDQDDSY
         1158-1189: RYSMQARNGISPTNPTKLQITENGEFRNSSNC → SMH

    Note: Gene prediction based on EST data.

    Show »
    Length:1,132
    Mass (Da):125,041
    Checksum:i85C487CD98660B19
    GO

    Sequence cautioni

    The sequence CAH72155.3 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti482 – 4821I → T in AAM00371. (PubMed:11944990)Curated
    Sequence conflicti921 – 9211P → S in AAM00371. (PubMed:11944990)Curated
    Sequence conflicti1091 – 10922QQ → HE in AAM00371. (PubMed:11944990)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti59 – 591S → F.
    Corresponds to variant rs7027492 [ dbSNP | Ensembl ].
    VAR_056858

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 193193Missing in isoform 3. 1 PublicationVSP_020952Add
    BLAST
    Alternative sequencei1 – 124124Missing in isoform 2 and isoform 4. 3 PublicationsVSP_020953Add
    BLAST
    Alternative sequencei2 – 4140SAGGS…TRPAR → EPDSLLDQDDSY in isoform 5. CuratedVSP_047361Add
    BLAST
    Alternative sequencei1158 – 118932RYSMQ…NSSNC → SMH in isoform 3, isoform 4 and isoform 5. 3 PublicationsVSP_020954Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF367051 mRNA. Translation: AAM00371.1.
    AY032952 mRNA. Translation: AAK50336.1.
    AB051530 mRNA. Translation: BAB21834.2.
    AL357936 Genomic DNA. No translation available.
    AL365274 Genomic DNA. Translation: CAH72155.3. Sequence problems.
    AL365274 Genomic DNA. Translation: CAQ10385.1.
    AL365274 Genomic DNA. Translation: CAH72158.1.
    CH471090 Genomic DNA. Translation: EAW87503.1.
    CH471090 Genomic DNA. Translation: EAW87504.1.
    BC146762 mRNA. Translation: AAI46763.1.
    CCDSiCCDS6832.1. [Q5VWQ8-2]
    CCDS6833.2. [Q5VWQ8-5]
    RefSeqiNP_115941.2. NM_032552.3. [Q5VWQ8-5]
    NP_619723.1. NM_138709.2. [Q5VWQ8-2]
    XP_005251776.1. XM_005251719.2. [Q5VWQ8-1]
    UniGeneiHs.522378.

    Genome annotation databases

    EnsembliENST00000259371; ENSP00000259371; ENSG00000136848. [Q5VWQ8-5]
    ENST00000309989; ENSP00000310827; ENSG00000136848. [Q5VWQ8-2]
    ENST00000408936; ENSP00000386183; ENSG00000136848. [Q5VWQ8-1]
    GeneIDi153090.
    KEGGihsa:153090.
    UCSCiuc004bln.3. human.
    uc004blo.3. human. [Q5VWQ8-1]

    Polymorphism databases

    DMDMi116247768.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement, 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
    AF367051 mRNA. Translation: AAM00371.1 .
    AY032952 mRNA. Translation: AAK50336.1 .
    AB051530 mRNA. Translation: BAB21834.2 .
    AL357936 Genomic DNA. No translation available.
    AL365274 Genomic DNA. Translation: CAH72155.3 . Sequence problems.
    AL365274 Genomic DNA. Translation: CAQ10385.1 .
    AL365274 Genomic DNA. Translation: CAH72158.1 .
    CH471090 Genomic DNA. Translation: EAW87503.1 .
    CH471090 Genomic DNA. Translation: EAW87504.1 .
    BC146762 mRNA. Translation: AAI46763.1 .
    CCDSi CCDS6832.1. [Q5VWQ8-2 ]
    CCDS6833.2. [Q5VWQ8-5 ]
    RefSeqi NP_115941.2. NM_032552.3. [Q5VWQ8-5 ]
    NP_619723.1. NM_138709.2. [Q5VWQ8-2 ]
    XP_005251776.1. XM_005251719.2. [Q5VWQ8-1 ]
    UniGenei Hs.522378.

    3D structure databases

    ProteinModelPortali Q5VWQ8.
    SMRi Q5VWQ8. Positions 329-662.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 127478. 13 interactions.
    DIPi DIP-41721N.
    IntActi Q5VWQ8. 5 interactions.
    MINTi MINT-268247.
    STRINGi 9606.ENSP00000259371.

    PTM databases

    PhosphoSitei Q5VWQ8.

    Polymorphism databases

    DMDMi 116247768.

    Proteomic databases

    MaxQBi Q5VWQ8.
    PaxDbi Q5VWQ8.
    PRIDEi Q5VWQ8.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000259371 ; ENSP00000259371 ; ENSG00000136848 . [Q5VWQ8-5 ]
    ENST00000309989 ; ENSP00000310827 ; ENSG00000136848 . [Q5VWQ8-2 ]
    ENST00000408936 ; ENSP00000386183 ; ENSG00000136848 . [Q5VWQ8-1 ]
    GeneIDi 153090.
    KEGGi hsa:153090.
    UCSCi uc004bln.3. human.
    uc004blo.3. human. [Q5VWQ8-1 ]

    Organism-specific databases

    CTDi 153090.
    GeneCardsi GC09P124329.
    HGNCi HGNC:17294. DAB2IP.
    HPAi HPA036977.
    MIMi 609205. gene.
    neXtProti NX_Q5VWQ8.
    PharmGKBi PA27133.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG245428.
    HOVERGENi HBG006492.
    InParanoidi Q5VWQ8.
    OMAi EKGGQPT.
    OrthoDBi EOG74XS5P.
    PhylomeDBi Q5VWQ8.
    TreeFami TF105303.

    Miscellaneous databases

    ChiTaRSi DAB2IP. human.
    GeneWikii DAB2IP.
    GenomeRNAii 153090.
    NextBioi 87071.
    PROi Q5VWQ8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q5VWQ8.
    Bgeei Q5VWQ8.
    CleanExi HS_DAB2IP.
    Genevestigatori Q5VWQ8.

    Family and domain databases

    Gene3Di 1.10.506.10. 1 hit.
    2.30.29.30. 1 hit.
    2.60.40.150. 1 hit.
    InterProi IPR000008. C2_dom.
    IPR021887. DUF3498.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR001936. RasGAP.
    IPR023152. RasGAP_CS.
    IPR008936. Rho_GTPase_activation_prot.
    [Graphical view ]
    Pfami PF00168. C2. 1 hit.
    PF12004. DUF3498. 1 hit.
    PF00616. RasGAP. 1 hit.
    [Graphical view ]
    SMARTi SM00239. C2. 1 hit.
    SM00233. PH. 1 hit.
    SM00323. RasGAP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48350. SSF48350. 1 hit.
    SSF49562. SSF49562. 1 hit.
    PROSITEi PS50003. PH_DOMAIN. 1 hit.
    PS00509. RAS_GTPASE_ACTIV_1. 1 hit.
    PS50018. RAS_GTPASE_ACTIV_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Differential regulation of the human gene DAB2IP in normal and malignant prostatic epithelia: cloning and characterization."
      Chen H., Pong R.-C., Wang Z., Hsieh J.-T.
      Genomics 79:573-581(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY.
    2. "Identification of a novel RAS GTPase-activating protein (RASGAP) gene at 9q34 as an MLL fusion partner in a patient with de novo acute myeloid leukemia."
      von Bergh A.R.M., Wijers P.M., Groot A.J., van Zelderen-Bhola S., Falkenburg J.H.F., Kluin P.M., Schuuring E.
      Genes Chromosomes Cancer 39:324-334(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CHROMOSOMAL TRANSLOCATION WITH KMT2A/MLL1.
    3. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
      DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Brain.
    4. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    5. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [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 4).
    8. "AIP1 mediates TNF-alpha-induced ASK1 activation by facilitating dissociation of ASK1 from its inhibitor 14-3-3."
      Zhang R., He X., Liu W., Lu M., Hsieh J.-T., Min W.
      J. Clin. Invest. 111:1933-1943(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MAP3K5, MUTAGENESIS OF 228-LYS--LYS-230; 281-LYS--LYS-284 AND ARG-413.
    9. "AIP1/DAB2IP, a novel member of the Ras-GAP family, transduces TRAF2-induced ASK1-JNK activation."
      Zhang H., Zhang R., Luo Y., D'Alessio A., Pober J.S., Min W.
      J. Biol. Chem. 279:44955-44965(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH TNFR1; MAP3K5; TRADD; RALBP1 AND TRAF2.
    10. "Tumor necrosis factor alpha-induced desumoylation and cytoplasmic translocation of homeodomain-interacting protein kinase 1 are critical for apoptosis signal-regulating kinase 1-JNK/p38 activation."
      Li X., Zhang R., Luo D., Park S.-J., Wang Q., Kim Y., Min W.
      J. Biol. Chem. 280:15061-15070(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIPK1, SUBCELLULAR LOCATION.
    11. "RIP1-mediated AIP1 phosphorylation at a 14-3-3-binding site is critical for tumor necrosis factor-induced ASK1-JNK/p38 activation."
      Zhang H., Zhang H., Lin Y., Li J., Pober J.S., Min W.
      J. Biol. Chem. 282:14788-14796(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH 14-3-3 PROTEINS; MAP3K5; RIPK1 AND TRAF2, PHOSPHORYLATION AT SER-728, MUTAGENESIS OF SER-728 AND THR-935, TISSUE SPECIFICITY.
    12. "AIP1 recruits phosphatase PP2A to ASK1 in tumor necrosis factor-induced ASK1-JNK activation."
      Min W., Lin Y., Tang S., Yu L., Zhang H., Wan T., Luhn T., Fu H., Chen H.
      Circ. Res. 102:840-848(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF SER-728.
    13. "AIP1 functions as an endogenous inhibitor of VEGFR2-mediated signaling and inflammatory angiogenesis in mice."
      Zhang H., He Y., Dai S., Xu Z., Luo Y., Wan T., Luo D., Jones D., Tang S., Chen H., Sessa W.C., Min W.
      J. Clin. Invest. 118:3904-3916(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH KDR AND P85 SUBUNIT OF PI3K, MUTAGENESIS OF 228-LYS--LYS-230 AND 281-LYS--LYS-284.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "DAB2IP coordinates both PI3K-Akt and ASK1 pathways for cell survival and apoptosis."
      Xie D., Gore C., Zhou J., Pong R.C., Zhang H., Yu L., Vessella R.L., Min W., Hsieh J.T.
      Proc. Natl. Acad. Sci. U.S.A. 106:19878-19883(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH AKT1 AND P85 SUBUNIT OF PI3K, PHOSPHORYLATION AT SER-728, MUTAGENESIS OF ARG-413; SER-728 AND 920-PRO--PRO-929.
    16. "AIP1 functions as Arf6-GAP to negatively regulate TLR4 signaling."
      Wan T., Liu T., Zhang H., Tang S., Min W.
      J. Biol. Chem. 285:3750-3757(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PHOSPHATIDYLINOSITOL, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-413.
    17. "An oncogene-tumor suppressor cascade drives metastatic prostate cancer by coordinately activating Ras and nuclear factor-kappaB."
      Min J., Zaslavsky A., Fedele G., McLaughlin S.K., Reczek E.E., De Raedt T., Guney I., Strochlic D.E., Macconaill L.E., Beroukhim R., Bronson R.T., Ryeom S., Hahn W.C., Loda M., Cichowski K.
      Nat. Med. 16:286-294(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PROSTATE CANCER, INDUCTION, MUTAGENESIS OF ARG-413 AND SER-728.
    18. "Role of DAB2IP in modulating epithelial-to-mesenchymal transition and prostate cancer metastasis."
      Xie D., Gore C., Liu J., Pong R.C., Mason R., Hao G., Long M., Kabbani W., Yu L., Zhang H., Chen H., Sun X., Boothman D.A., Min W., Hsieh J.T.
      Proc. Natl. Acad. Sci. U.S.A. 107:2485-2490(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PROSTATE CANCER, INTERACTION WITH GSK3B AND PPP2CA.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "AIP1 prevents graft arteriosclerosis by inhibiting interferon-gamma-dependent smooth muscle cell proliferation and intimal expansion."
      Yu L., Qin L., Zhang H., He Y., Chen H., Pober J.S., Tellides G., Min W.
      Circ. Res. 109:418-427(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH JAK2, TISSUE SPECIFICITY.
    21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-978, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "EZH2-regulated DAB2IP is a medulloblastoma tumor suppressor and a positive marker for survival."
      Smits M., van Rijn S., Hulleman E., Biesmans D., van Vuurden D.G., Kool M., Haberler C., Aronica E., Vandertop W.P., Noske D.P., Wurdinger T.
      Clin. Cancer Res. 18:4048-4058(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MEDULLOBLASTOMA DEVELOPMENT, INDUCTION, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiDAB2P_HUMAN
    AccessioniPrimary (citable) accession number: Q5VWQ8
    Secondary accession number(s): A6H8V2
    , A6NHI9, B0QZB1, G3XA90, Q8TDL2, Q96SE1, Q9C0C0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 17, 2006
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 103 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

    Miscellaneous

    The DAB2IP gene is found epigenetically silenced in numerous aggressive cancers, like prostate cancers and medulloblastoma tumors. Epigenetic suppression of DAB2IP by EZH2 is a major mechanism of DAB2IP inactivation in human prostate cancer and increases metastatic potential (PubMed:20154697, PubMed:22696229).2 Publications

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3