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O08808

- DIAP1_MOUSE

UniProt

O08808 - DIAP1_MOUSE

Protein

Protein diaphanous homolog 1

Gene

Diaph1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Acts in a Rho-dependent manner to recruit PFY1 to the membrane. Required for the assembly of F-actin structures, such as actin cables and stress fibers. Nucleates actin filaments. Binds to the barbed end of the actin filament and slows down actin polymerization and depolymerization. Required for cytokinesis, and transcriptional activation of the serum response factor. DFR proteins couple Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics. Functions as a scaffold protein for MAPRE1 and APC to stabilize microtubules and promote cell migration. Has neurite outgrowth promoting activity. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape By similarity.By similarity

    GO - Molecular functioni

    1. actin binding Source: MGI
    2. identical protein binding Source: IntAct
    3. ion channel binding Source: BHF-UCL
    4. profilin binding Source: MGI
    5. protein binding Source: UniProtKB
    6. Rho GTPase binding Source: MGI

    GO - Biological processi

    1. actin cytoskeleton organization Source: MGI
    2. actin filament polymerization Source: MGI
    3. cellular response to histamine Source: Ensembl
    4. cytoskeleton organization Source: UniProtKB
    5. neuron projection development Source: UniProtKB
    6. positive regulation of cell migration Source: Ensembl
    7. protein localization to microtubule Source: Ensembl
    8. regulation of cell shape Source: UniProtKB
    9. regulation of microtubule-based process Source: UniProtKB
    10. regulation of release of sequestered calcium ion into cytosol Source: Ensembl
    11. sensory perception of sound Source: UniProtKB-KW

    Keywords - Biological processi

    Hearing

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein diaphanous homolog 1
    Alternative name(s):
    Diaphanous-related formin-1
    Short name:
    DRF1
    p140mDIA
    Short name:
    mDIA1
    Gene namesi
    Name:Diaph1
    Synonyms:Diap1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:1194490. Diap1.

    Subcellular locationi

    Cell membrane 1 Publication. Cell projectionruffle membrane 1 Publication. Cytoplasmcytoskeleton 1 Publication
    Note: Membrane ruffles, especially at the tip of ruffles, of motile cells.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-KW
    2. mitotic spindle Source: Ensembl
    3. neuron projection Source: UniProtKB
    4. ruffle membrane Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12551255Protein diaphanous homolog 1PRO_0000194894Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei22 – 221PhosphoserineBy similarity
    Cross-linki477 – 477Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei1040 – 10401N6-acetyllysineBy similarity
    Modified residuei1086 – 10861N6-acetyllysineBy similarity
    Modified residuei1104 – 11041Phosphotyrosine1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO08808.
    PaxDbiO08808.
    PRIDEiO08808.

    PTM databases

    PhosphoSiteiO08808.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiO08808.
    BgeeiO08808.
    CleanExiMM_DIAP1.
    GenevestigatoriO08808.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with the GTP-bound form of RHOA. Interacts with RHOC, PFY1, MAPRE1, BAIAP2 and APC. Interacts with SCAI. Interacts with DCAF7, via FH2 domain By similarity. Interacts with NCDN.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-1026445,EBI-1026445
    Baiap2Q8BKX13EBI-1026445,EBI-771498
    IQGAP1P469408EBI-1026445,EBI-297509From a different organism.
    RHOAP615863EBI-1026445,EBI-446668From a different organism.

    Protein-protein interaction databases

    BioGridi199221. 6 interactions.
    DIPiDIP-29028N.
    IntActiO08808. 13 interactions.
    MINTiMINT-4093098.

    Structurei

    Secondary structure

    1
    1255
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi85 – 939
    Helixi98 – 1058
    Helixi109 – 12214
    Helixi136 – 1438
    Turni144 – 1463
    Helixi149 – 16517
    Helixi168 – 19023
    Turni194 – 1963
    Helixi201 – 21515
    Helixi219 – 2279
    Beta strandi228 – 2303
    Helixi231 – 2377
    Helixi244 – 25815
    Beta strandi261 – 2633
    Helixi266 – 28116
    Helixi287 – 2926
    Helixi299 – 31315
    Helixi319 – 33113
    Helixi334 – 3418
    Helixi347 – 37731
    Helixi381 – 39212
    Beta strandi393 – 3953
    Helixi397 – 40812
    Turni415 – 4173
    Helixi418 – 43316
    Helixi436 – 4383
    Beta strandi447 – 4515
    Turni453 – 4553
    Helixi464 – 4696
    Turni470 – 4723
    Beta strandi748 – 7503
    Turni772 – 7754
    Beta strandi777 – 7804
    Helixi781 – 7833
    Helixi786 – 7894
    Helixi794 – 8018
    Beta strandi833 – 8353
    Helixi837 – 85014
    Helixi854 – 86310
    Turni866 – 8683
    Helixi871 – 88010
    Helixi884 – 8918
    Helixi894 – 8996
    Helixi902 – 91110
    Helixi916 – 93419
    Helixi937 – 95115
    Helixi954 – 9585
    Turni971 – 9733
    Beta strandi974 – 9763
    Beta strandi980 – 9823
    Helixi984 – 9863
    Helixi987 – 9926
    Helixi1002 – 101211
    Helixi1015 – 10195
    Helixi1020 – 10234
    Helixi1027 – 10326
    Helixi1035 – 105723
    Beta strandi1063 – 10664
    Helixi1069 – 110436
    Turni1109 – 11113
    Helixi1114 – 115946
    Helixi1181 – 119111

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1V9DX-ray2.60A/B/C/D826-1163[»]
    1Z2CX-ray3.00B/D69-451[»]
    2BAPX-ray3.30A/B135-451[»]
    C/D1145-1200[»]
    2BNXX-ray2.40A/B131-516[»]
    2F31X-ray2.10A135-367[»]
    B1177-1196[»]
    2V8FX-ray1.10C635-655[»]
    3EG5X-ray2.70B/D69-451[»]
    3O4XX-ray3.20A/B/C/D131-458[»]
    E/F/G/H736-1200[»]
    3OBVX-ray2.75A/B/C/D131-457[»]
    E/F/G/H753-1209[»]
    ProteinModelPortaliO08808.
    SMRiO08808. Positions 83-457, 745-1198.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO08808.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini75 – 440366GBD/FH3PROSITE-ProRule annotationAdd
    BLAST
    Domaini586 – 747162FH1Add
    BLAST
    Domaini752 – 1154403FH2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1177 – 120529DADPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili460 – 562103Sequence AnalysisAdd
    BLAST
    Coiled coili1027 – 1179153Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1196 – 11994Arg/Lys-rich (basic)

    Domaini

    The DAD domain regulates activation via by an autoinhibitory interaction with the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments.1 Publication

    Sequence similaritiesi

    Contains 1 DAD (diaphanous autoregulatory) domain.PROSITE-ProRule annotation
    Contains 1 FH2 (formin homology 2) domain.PROSITE-ProRule annotation
    Contains 1 GBD/FH3 (Rho GTPase-binding/formin homology 3) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG149898.
    GeneTreeiENSGT00730000110702.
    HOGENOMiHOG000293231.
    HOVERGENiHBG051357.
    KOiK05740.
    OrthoDBiEOG7G1V5D.
    PhylomeDBiO08808.

    Family and domain databases

    InterProiIPR016024. ARM-type_fold.
    IPR014767. Diaphanous_autoregulatory.
    IPR010465. Drf_DAD.
    IPR015425. FH2_Formin.
    IPR010472. FH3_dom.
    IPR027653. Formin_Diaph1.
    IPR009408. Formin_homology_1.
    IPR010473. GTPase-bd.
    IPR014768. GTPase-bd/formin_homology_3.
    [Graphical view]
    PANTHERiPTHR23213:SF17. PTHR23213:SF17. 1 hit.
    PfamiPF06345. Drf_DAD. 1 hit.
    PF06346. Drf_FH1. 1 hit.
    PF06367. Drf_FH3. 1 hit.
    PF06371. Drf_GBD. 1 hit.
    PF02181. FH2. 1 hit.
    [Graphical view]
    SMARTiSM00498. FH2. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 1 hit.
    PROSITEiPS51231. DAD. 1 hit.
    PS51444. FH2. 1 hit.
    PS51232. GBD_FH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O08808-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEPSGGGLGP GRGTRDKKKG RSPDELPATG GDGGKHKKFL ERFTSMRIKK     50
    EKEKPNSAHR NSSASYGDDP TAQSLQDISD EQVLVLFEQM LVDMNLNEEK 100
    QQPLREKDIV IKREMVSQYL HTSKAGMNQK ESSRSAMMYI QELRSGLRDM 150
    HLLSCLESLR VSLNNNPVSW VQTFGAEGLA SLLDILKRLH DEKEETSGNY 200
    DSRNQHEIIR CLKAFMNNKF GIKTMLETEE GILLLVRAMD PAVPNMMIDA 250
    AKLLSALCIL PQPEDMNERV LEAMTERAEM DEVERFQPLL DGLKSGTSIA 300
    LKVGCLQLIN ALITPAEELD FRVHIRSELM RLGLHQVLQE LREIENEDMK 350
    VQLCVFDEQG DEDFFDLKGR LDDIRMEMDD FGEVFQIILN TVKDSKAEPH 400
    FLSILQHLLL VRNDYEARPQ YYKLIEECVS QIVLHKNGTD PDFKCRHLQI 450
    DIERLVDQMI DKTKVEKSEA KATELEKKLD SELTARHELQ VEMKKMENDF 500
    EQKLQDLQGE KDALDSEKQQ ITAQKQDLEA EVSKLTGEVA KLSKELEDAK 550
    NEMASLSAVV VAPSVSSSAA VPPAPPLPGD SGTVIPPPPP PPPLPGGVVP 600
    PSPPLPPGTC IPPPPPLPGG ACIPPPPQLP GSAAIPPPPP LPGVASIPPP 650
    PPLPGATAIP PPPPLPGATA IPPPPPLPGG TGIPPPPPPL PGSVGVPPPP 700
    PLPGGPGLPP PPPPFPGAPG IPPPPPGMGV PPPPPFGFGV PAAPVLPFGL 750
    TPKKVYKPEV QLRRPNWSKF VAEDLSQDCF WTKVKEDRFE NNELFAKLTL 800
    AFSAQTKTSK AKKDQEGGEE KKSVQKKKVK ELKVLDSKTA QNLSIFLGSF 850
    RMPYQEIKNV ILEVNEAVLT ESMIQNLIKQ MPEPEQLKML SELKEEYDDL 900
    AESEQFGVVM GTVPRLRPRL NAILFKLQFS EQVENIKPEI VSVTAACEEL 950
    RKSENFSSLL ELTLLVGNYM NAGSRNAGAF GFNISFLCKL RDTKSADQKM 1000
    TLLHFLAELC ENDHPEVLKF PDELAHVEKA SRVSAENLQK SLDQMKKQIA 1050
    DVERDVQNFP AATDEKDKFV EKMTSFVKDA QEQYNKLRMM HSNMETLYKE 1100
    LGDYFVFDPK KLSVEEFFMD LHNFRNMFLQ AVKENQKRRE TEEKMRRAKL 1150
    AKEKAEKERL EKQQKREQLI DMNAEGDETG VMDSLLEALQ SGAAFRRKRG 1200
    PRQVNRKAGC AVTSLLASEL TKDDAMAPGP VKVPKKSEGV PTILEEAKEL 1250
    VGRAS 1255
    Length:1,255
    Mass (Da):139,343
    Last modified:July 1, 1997 - v1
    Checksum:i09404164873CA7C1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U96963 mRNA. Translation: AAC53280.1.
    CCDSiCCDS57121.1.
    PIRiT31065.
    RefSeqiNP_031884.1. NM_007858.2.
    UniGeneiMm.195916.

    Genome annotation databases

    EnsembliENSMUST00000115634; ENSMUSP00000111297; ENSMUSG00000024456.
    GeneIDi13367.
    KEGGimmu:13367.
    UCSCiuc008erj.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U96963 mRNA. Translation: AAC53280.1 .
    CCDSi CCDS57121.1.
    PIRi T31065.
    RefSeqi NP_031884.1. NM_007858.2.
    UniGenei Mm.195916.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1V9D X-ray 2.60 A/B/C/D 826-1163 [» ]
    1Z2C X-ray 3.00 B/D 69-451 [» ]
    2BAP X-ray 3.30 A/B 135-451 [» ]
    C/D 1145-1200 [» ]
    2BNX X-ray 2.40 A/B 131-516 [» ]
    2F31 X-ray 2.10 A 135-367 [» ]
    B 1177-1196 [» ]
    2V8F X-ray 1.10 C 635-655 [» ]
    3EG5 X-ray 2.70 B/D 69-451 [» ]
    3O4X X-ray 3.20 A/B/C/D 131-458 [» ]
    E/F/G/H 736-1200 [» ]
    3OBV X-ray 2.75 A/B/C/D 131-457 [» ]
    E/F/G/H 753-1209 [» ]
    ProteinModelPortali O08808.
    SMRi O08808. Positions 83-457, 745-1198.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199221. 6 interactions.
    DIPi DIP-29028N.
    IntActi O08808. 13 interactions.
    MINTi MINT-4093098.

    PTM databases

    PhosphoSitei O08808.

    Proteomic databases

    MaxQBi O08808.
    PaxDbi O08808.
    PRIDEi O08808.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000115634 ; ENSMUSP00000111297 ; ENSMUSG00000024456 .
    GeneIDi 13367.
    KEGGi mmu:13367.
    UCSCi uc008erj.1. mouse.

    Organism-specific databases

    CTDi 13367.
    MGIi MGI:1194490. Diap1.

    Phylogenomic databases

    eggNOGi NOG149898.
    GeneTreei ENSGT00730000110702.
    HOGENOMi HOG000293231.
    HOVERGENi HBG051357.
    KOi K05740.
    OrthoDBi EOG7G1V5D.
    PhylomeDBi O08808.

    Miscellaneous databases

    EvolutionaryTracei O08808.
    NextBioi 283706.
    PROi O08808.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O08808.
    Bgeei O08808.
    CleanExi MM_DIAP1.
    Genevestigatori O08808.

    Family and domain databases

    InterProi IPR016024. ARM-type_fold.
    IPR014767. Diaphanous_autoregulatory.
    IPR010465. Drf_DAD.
    IPR015425. FH2_Formin.
    IPR010472. FH3_dom.
    IPR027653. Formin_Diaph1.
    IPR009408. Formin_homology_1.
    IPR010473. GTPase-bd.
    IPR014768. GTPase-bd/formin_homology_3.
    [Graphical view ]
    PANTHERi PTHR23213:SF17. PTHR23213:SF17. 1 hit.
    Pfami PF06345. Drf_DAD. 1 hit.
    PF06346. Drf_FH1. 1 hit.
    PF06367. Drf_FH3. 1 hit.
    PF06371. Drf_GBD. 1 hit.
    PF02181. FH2. 1 hit.
    [Graphical view ]
    SMARTi SM00498. FH2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    PROSITEi PS51231. DAD. 1 hit.
    PS51444. FH2. 1 hit.
    PS51232. GBD_FH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin."
      Watanabe N., Madaule P., Reid T., Ishizaki T., Watanabe G., Kakizuka A., Saito Y., Nakao K., Jockusch B.M., Narumiya S.
      EMBO J. 16:3044-3056(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH RHOA, SUBCELLULAR LOCATION.
    2. "Rho small G-protein-dependent binding of mDia to an Src homology 3 domain-containing IRSp53/BAIAP2."
      Fujiwara T., Mammoto A., Kim Y., Takai Y.
      Biochem. Biophys. Res. Commun. 271:626-629(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH BAIAP2.
    3. "Diaphanous-related formins bridge Rho GTPase and Src tyrosine kinase signaling."
      Tominaga T., Sahai E., Chardin P., McCormick F., Courtneidge S.A., Alberts A.S.
      Mol. Cell 5:13-25(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    4. "EB1 and APC bind to mDia to stabilize microtubules downstream of Rho and promote cell migration."
      Wen Y., Eng C.H., Schmoranzer J., Cabrera-Poch N., Morris E.J.S., Chen M., Wallar B.J., Alberts A.S., Gundersen G.G.
      Nat. Cell Biol. 6:820-830(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APC AND MAPRE1.
    5. "Actin polymerization-driven molecular movement of mDia1 in living cells."
      Higashida C., Miyoshi T., Fujita A., Oceguera-Yanez F., Monypenny J., Andou Y., Narumiya S., Watanabe N.
      Science 303:2007-2010(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ACTIN.
    6. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
      Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    7. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
      Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
      J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1104, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Mast cell.
    8. "Identification of Neurochondrin as a new interaction partner of the FH3 domain of the Diaphanous-related formin Dia1."
      Schwaibold E.M., Brandt D.T.
      Biochem. Biophys. Res. Commun. 373:366-372(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH NCDN.
    9. "SCAI acts as a suppressor of cancer cell invasion through the transcriptional control of beta1-integrin."
      Brandt D.T., Baarlink C., Kitzing T.M., Kremmer E., Ivaska J., Nollau P., Grosse R.
      Nat. Cell Biol. 11:557-568(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SCAI.
    10. "The core FH2 domain of diaphanous-related formins is an elongated actin binding protein that inhibits polymerization."
      Shimada A., Nyitrai M., Vetter I.R., Kuehlmann D., Bugyi B., Narumiya S., Geeves M.A., Wittinghofer A.
      Mol. Cell 13:511-522(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 826-1163, OLIGOMERIZATION, INTERACTION WITH ACTIN.
    11. "The regulation of mDia1 by autoinhibition and its release by Rho*GTP."
      Lammers M., Rose R., Scrima A., Wittinghofer A.
      EMBO J. 24:4176-4187(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 135-451 AND 1145-1200, DOMAIN DAD, AUTOINHIBITION.
    12. "Structural and mechanistic insights into the interaction between Rho and mammalian Dia."
      Rose R., Weyand M., Lammers M., Ishizaki T., Ahmadian M.R., Wittinghofer A.
      Nature 435:513-518(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 69-451 IN COMPLEX WITH RHOC, HOMODIMERIZATION.

    Entry informationi

    Entry nameiDIAP1_MOUSE
    AccessioniPrimary (citable) accession number: O08808
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 137 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3