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O08808

- DIAP1_MOUSE

UniProt

O08808 - DIAP1_MOUSE

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Protein

Protein diaphanous homolog 1

Gene

Diaph1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. Rho GTPase binding Source: MGI

GO - Biological processi

  1. actin cytoskeleton organization Source: MGI
  2. actin filament polymerization Source: MGI
  3. cytoskeleton organization Source: UniProtKB
  4. neuron projection development Source: UniProtKB
  5. regulation of cell shape Source: UniProtKB
  6. regulation of microtubule-based process Source: UniProtKB
  7. sensory perception of sound Source: UniProtKB-KW
Complete GO annotation...

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. cytoskeleton Source: UniProtKB-KW
  3. neuron projection Source: UniProtKB
  4. ruffle membrane Source: MGI
Complete GO annotation...

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

BgeeiO08808.
CleanExiMM_DIAP1.
ExpressionAtlasiO08808. baseline and differential.
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 – 939Combined sources
Helixi98 – 1058Combined sources
Helixi109 – 12214Combined sources
Helixi136 – 1438Combined sources
Turni144 – 1463Combined sources
Helixi149 – 16517Combined sources
Helixi168 – 19023Combined sources
Turni194 – 1963Combined sources
Helixi201 – 21515Combined sources
Helixi219 – 2279Combined sources
Beta strandi228 – 2303Combined sources
Helixi231 – 2377Combined sources
Helixi244 – 25815Combined sources
Beta strandi261 – 2633Combined sources
Helixi266 – 28116Combined sources
Helixi287 – 2926Combined sources
Helixi299 – 31315Combined sources
Helixi319 – 33113Combined sources
Helixi334 – 3418Combined sources
Helixi347 – 37731Combined sources
Helixi381 – 39212Combined sources
Beta strandi393 – 3953Combined sources
Helixi397 – 40812Combined sources
Turni415 – 4173Combined sources
Helixi418 – 43316Combined sources
Helixi436 – 4383Combined sources
Beta strandi447 – 4515Combined sources
Turni453 – 4553Combined sources
Helixi464 – 4696Combined sources
Turni470 – 4723Combined sources
Beta strandi748 – 7503Combined sources
Turni772 – 7754Combined sources
Beta strandi777 – 7804Combined sources
Helixi781 – 7833Combined sources
Helixi786 – 7894Combined sources
Helixi794 – 8018Combined sources
Beta strandi833 – 8353Combined sources
Helixi837 – 85014Combined sources
Helixi854 – 86310Combined sources
Turni866 – 8683Combined sources
Helixi871 – 88010Combined sources
Helixi884 – 8918Combined sources
Helixi894 – 8996Combined sources
Helixi902 – 91110Combined sources
Helixi916 – 93419Combined sources
Helixi937 – 95115Combined sources
Helixi954 – 9585Combined sources
Turni971 – 9733Combined sources
Beta strandi974 – 9763Combined sources
Beta strandi980 – 9823Combined sources
Helixi984 – 9863Combined sources
Helixi987 – 9926Combined sources
Helixi1002 – 101211Combined sources
Helixi1015 – 10195Combined sources
Helixi1020 – 10234Combined sources
Helixi1027 – 10326Combined sources
Helixi1035 – 105723Combined sources
Beta strandi1063 – 10664Combined sources
Helixi1069 – 110436Combined sources
Turni1109 – 11113Combined sources
Helixi1114 – 115946Combined sources
Helixi1181 – 119111Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000118986.
HOGENOMiHOG000293231.
HOVERGENiHBG051357.
InParanoidiO08808.
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

        10         20         30         40         50
MEPSGGGLGP GRGTRDKKKG RSPDELPATG GDGGKHKKFL ERFTSMRIKK
60 70 80 90 100
EKEKPNSAHR NSSASYGDDP TAQSLQDISD EQVLVLFEQM LVDMNLNEEK
110 120 130 140 150
QQPLREKDIV IKREMVSQYL HTSKAGMNQK ESSRSAMMYI QELRSGLRDM
160 170 180 190 200
HLLSCLESLR VSLNNNPVSW VQTFGAEGLA SLLDILKRLH DEKEETSGNY
210 220 230 240 250
DSRNQHEIIR CLKAFMNNKF GIKTMLETEE GILLLVRAMD PAVPNMMIDA
260 270 280 290 300
AKLLSALCIL PQPEDMNERV LEAMTERAEM DEVERFQPLL DGLKSGTSIA
310 320 330 340 350
LKVGCLQLIN ALITPAEELD FRVHIRSELM RLGLHQVLQE LREIENEDMK
360 370 380 390 400
VQLCVFDEQG DEDFFDLKGR LDDIRMEMDD FGEVFQIILN TVKDSKAEPH
410 420 430 440 450
FLSILQHLLL VRNDYEARPQ YYKLIEECVS QIVLHKNGTD PDFKCRHLQI
460 470 480 490 500
DIERLVDQMI DKTKVEKSEA KATELEKKLD SELTARHELQ VEMKKMENDF
510 520 530 540 550
EQKLQDLQGE KDALDSEKQQ ITAQKQDLEA EVSKLTGEVA KLSKELEDAK
560 570 580 590 600
NEMASLSAVV VAPSVSSSAA VPPAPPLPGD SGTVIPPPPP PPPLPGGVVP
610 620 630 640 650
PSPPLPPGTC IPPPPPLPGG ACIPPPPQLP GSAAIPPPPP LPGVASIPPP
660 670 680 690 700
PPLPGATAIP PPPPLPGATA IPPPPPLPGG TGIPPPPPPL PGSVGVPPPP
710 720 730 740 750
PLPGGPGLPP PPPPFPGAPG IPPPPPGMGV PPPPPFGFGV PAAPVLPFGL
760 770 780 790 800
TPKKVYKPEV QLRRPNWSKF VAEDLSQDCF WTKVKEDRFE NNELFAKLTL
810 820 830 840 850
AFSAQTKTSK AKKDQEGGEE KKSVQKKKVK ELKVLDSKTA QNLSIFLGSF
860 870 880 890 900
RMPYQEIKNV ILEVNEAVLT ESMIQNLIKQ MPEPEQLKML SELKEEYDDL
910 920 930 940 950
AESEQFGVVM GTVPRLRPRL NAILFKLQFS EQVENIKPEI VSVTAACEEL
960 970 980 990 1000
RKSENFSSLL ELTLLVGNYM NAGSRNAGAF GFNISFLCKL RDTKSADQKM
1010 1020 1030 1040 1050
TLLHFLAELC ENDHPEVLKF PDELAHVEKA SRVSAENLQK SLDQMKKQIA
1060 1070 1080 1090 1100
DVERDVQNFP AATDEKDKFV EKMTSFVKDA QEQYNKLRMM HSNMETLYKE
1110 1120 1130 1140 1150
LGDYFVFDPK KLSVEEFFMD LHNFRNMFLQ AVKENQKRRE TEEKMRRAKL
1160 1170 1180 1190 1200
AKEKAEKERL EKQQKREQLI DMNAEGDETG VMDSLLEALQ SGAAFRRKRG
1210 1220 1230 1240 1250
PRQVNRKAGC AVTSLLASEL TKDDAMAPGP VKVPKKSEGV PTILEEAKEL

VGRAS
Length:1,255
Mass (Da):139,343
Last modified:July 1, 1997 - v1
Checksum:i09404164873CA7C1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 ENSGT00760000118986.
HOGENOMi HOG000293231.
HOVERGENi HBG051357.
InParanoidi O08808.
KOi K05740.
OrthoDBi EOG7G1V5D.
PhylomeDBi O08808.

Miscellaneous databases

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

Gene expression databases

Bgeei O08808.
CleanExi MM_DIAP1.
ExpressionAtlasi O08808. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 138 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