DIAPH1
entrez
1729
canonical
uniprot
O60610
canonical
ensembl
ENSG00000131504
resolver
ensp
ENSP00000373706
resolver
ensp
ENSP00000428268
resolver
ensp
ENSP00000494675
resolver
enst
ENST00000647433
resolver
genesymbol
DIAPH1
resolver
genesymbol_syn
DIAP1
resolver
hgnc
HGNC:2876
resolver
uniprot
A0A2R8Y5N1
resolver
uniprot
A6NF18
resolver
uniprot
B7ZKW2
resolver
uniprot
E9PEZ2
resolver
uniprot
Q17RN4
resolver
uniprot
Q59FH8
resolver
uniprot
Q6URC4
resolver
uniprot
Q9UC76
resolver
uniprot_entry
A0A2R8Y5N1_HUMAN
resolver
uniprot_entry
DIAP1_HUMAN
resolver
uniprot_entry
Q6URC4_HUMAN
resolver
uniprot_sec
A6NF18
resolver
uniprot_sec
B7ZKW2
resolver
uniprot_sec
E9PEZ2
resolver
uniprot_sec
Q17RN4
resolver
uniprot_sec
Q59FH8
resolver
uniprot_sec
Q9UC76
resolver
amino_acid_sequence
MEPPGGSLGPGRGTRDKKKGRSPDELPSAGGDGGKSKKFTLKRLMADELERFTSMRIKKEKEKPNSAHRNSSASYGDDPTAQSLQDVSDEQVLVLFEQMLLDMNLNEEKQQPLREKDIIIKREMVSQYLYTSKAGMSQKESSKSAMMYIQELRSGLRDMPLLSCLESLRVSLNNNPVSWVQTFGAEGLASLLDILKRLHDEKEETAGSYDSRNKHEIIRCLKAFMNNKFGIKTMLETEEGILLLVRAMDPAVPNMMIDAAKLLSALCILPQPEDMNERVLEAMTERAEMDEVERFQPLLDGLKSGTTIALKVGCLQLINALITPAEELDFRVHIRSELMRLGLHQVLQDLREIENEDMRVQLNVFDEQGEEDSYDLKGRLDDIRMEMDDFNEVFQILLNTVKDSKAEPHFLSILQHLLLVRNDYEARPQYYKLIEECISQIVLHKNGADPDFKCRHLQIEIEGLIDQMIDKTKVEKSEAKAAELEKKLDSELTARHELQVEMKKMESDFEQKLQDLQGEKDALHSEKQQIATEKQDLEAEVSQLTGEVAKLTKELEDAKKEMASLSAAAITVPPSVPSRAPVPPAPPLPGDSGTIIPPPPAPGDSTTPPPPPPPPPPPPPLPGGVCISSPPSLPGGTAISPPPPLSGDATIPPPPPLPEGVGIPSPSSLPGGTAIPPPPPLPGSARIPPPPPPLPGSAGIPPPPPPLPGEAGMPPPPPPLPGGPGIPPPPPFPGGPGIPPPPPGMGMPPPPPFGFGVPAAPVLPFGLTPKKLYKPEVQLRRPNWSKLVAEDLSQDCFWTKVKEDRFENNELFAKLTLTFSAQTKTSKAKKDQEGGEEKKSVQKKKVKELKVLDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKDEYDDLAESEQFGVVMGTVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSESFSNLLEITLLVGNYMNAGSRNAGAFGFNISFLCKLRDTKSTDQKMTLLHFLAELCENDYPDVLKFPDELAHVEKASRVSAENLQKNLDQMKKQISDVERDVQNFPAATDEKDKFVEKMTSFVKDAQEQYNKLRMMHSNMETLYKELGEYFLFDPKKLSVEEFFMDLHNFRNMFLQAVKENQKRRETEEKMRRAKLAKEKAEKERLEKQQKREQLIDMNAEGDETGVMDSLLEALQSGAAFRRKRGPRQANRKAGCAVTSLLASELTKDDAMAAVPAKVSKNSETFPTILEEAKELVGRAS
uniprot
proteins
disease_involvement
DISEASE: Deafness, autosomal dominant 1, with or without thrombocytopenia (DFNA1) [MIM:124900]: A form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information. Patients may have mild thrombocytopenia and enlarged platelets, although most of DFNA1 affected individuals do not have significant bleeding tendencies. {ECO:0000269|PubMed:22938506, ECO:0000269|PubMed:26912466, ECO:0000269|PubMed:27808407, ECO:0000269|PubMed:9360932}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Seizures, cortical blindness, and microcephaly syndrome (SCBMS) [MIM:616632]: A severe autosomal recessive neurodevelopmental disorder characterized by microcephaly, early-onset seizures, severely delayed psychomotor development, short stature, and cortical blindness. {ECO:0000269|PubMed:24781755, ECO:0000269|PubMed:26463574}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Actin nucleation and elongation factor required for the assembly of F-actin structures, such as actin cables and stress fibers (By similarity). Binds to the barbed end of the actin filament and slows down actin polymerization and depolymerization (By similarity). Required for cytokinesis, and transcriptional activation of the serum response factor (By similarity). DFR proteins couple Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics (By similarity). Functions as a scaffold protein for MAPRE1 and APC to stabilize microtubules and promote cell migration (By similarity). Has neurite outgrowth promoting activity. Acts in a Rho-dependent manner to recruit PFY1 to the membrane (By similarity). In hear cells, it may play a role in the regulation of actin polymerization in hair cells (PubMed:20937854, PubMed:21834987, PubMed:26912466). The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex (PubMed:20937854, PubMed:21834987). It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity (PubMed:20937854, PubMed:21834987). In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization (PubMed:20937854, PubMed:21834987). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape (PubMed:20937854, PubMed:21834987). Plays a role in brain development (PubMed:24781755). Also acts as an actin nucleation and elongation factor in the nucleus by promoting nuclear actin polymerization inside the nucleus to drive serum-dependent SRF-MRTFA activity (By similarity). {ECO:0000250|UniProtKB:O08808, ECO:0000269|PubMed:20937854, ECO:0000269|PubMed:21834987, ECO:0000269|PubMed:24781755, ECO:0000269|PubMed:26912466}.
uniprot
proteins
mass_dalton
141347
uniprot
proteins
mutagenesis
MUTAGEN 154; /note="S->A: Partial decrease of phosphorylation."; /evidence="ECO:0000269|PubMed:23325789"; MUTAGEN 768; /note="T->A: Substantial loss of phosphorylation, no increase of phosphorylation in response to cAMP, increased stability, reduced interaction with OSBPL2 and OSBPL10 and reduced mitochondrial movement."; /evidence="ECO:0000269|PubMed:23325789"; MUTAGEN 1091; /note="T->A: Substantial loss of phosphorylation."; /evidence="ECO:0000269|PubMed:23325789"; MUTAGEN 1238; /note="T->A: Substantial loss of phosphorylation."; /evidence="ECO:0000269|PubMed:23325789
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Thr-768 is stimulated by cAMP and regulates stability, complex formation and mitochondrial movement. {ECO:0000269|PubMed:23325789}.
uniprot
proteins
protein_family
Diaphanous subfamily
uniprot
proteins
protein_family
Formin homology family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16887337
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20937854
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21834987
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
22938506
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23325789
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24781755
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26463574
uniprot
proteins
pubmed
26912466
uniprot
proteins
pubmed
27808407
uniprot
proteins
pubmed
7737110
uniprot
proteins
pubmed
9360932
uniprot
proteins
sequence_length
1272
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O08808}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:O08808}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:24781755}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:24781755}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:24781755}. Cytoplasm {ECO:0000250|UniProtKB:O08808}. Nucleus {ECO:0000250|UniProtKB:O08808}. Note=Membrane ruffles, especially at the tip of ruffles, of motile cells. {ECO:0000250|UniProtKB:O08808}.
uniprot
proteins