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Protein Page:
Diaphanous-1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
Diaphanous-1 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. In hear cells, it may play a role in the regulation of actin polymerization in hair cells. 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. 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. Interacts with NCDN. Expressed in brain, heart, placenta, lung, kidney, pancreas, liver, skeletal muscle and cochlea. Belongs to the formin homology family. Diaphanous subfamily. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Actin binding protein; Adaptor/scaffold; Motility/polarity/chemotaxis
Cellular Component: neuron projection; cytoplasm
Molecular Function: identical protein binding; protein binding; Rho GTPase binding; actin binding; receptor binding; profilin binding
Biological Process: regulation of cell shape; regulation of microtubule-based process; sensory perception of sound; actin filament polymerization; cytoskeleton organization and biogenesis; regulation of release of sequestered calcium ion into cytosol; neurite development; positive regulation of cell migration
Reference #:  O60610 (UniProtKB)
Alt. Names/Synonyms: DFNA1; DIA1; DIAP1; DIAPH1; diaphanous homolog 1 (Drosophila); diaphanous-related formin 1; Diaphanous-related formin-1; DRF1; FLJ25265; hDIA1; LFHL1; Protein diaphanous homolog 1
Gene Symbols: DIAPH1
Molecular weight: 141,347 Da
Basal Isoelectric point: 5.31  Predict pI for various phosphorylation states
CST Pathways:  Actin Dynamics  |  Adherens Junction Dynamics  |  Microtubule Dynamics  |  TGF-├č Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Diaphanous-1

Protein Structure Not Found.


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Sites Implicated In
molecular association, regulation: T768‑p
protein degradation: T768‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

► Hide Isoforms
 
0 1 S7-p _MEPPGGsLGPGRGT
0 10 S22-p RDKKKGRsPDELPsA
0 2 S28-p RsPDELPsAGGDGGk
0 1 K35-u sAGGDGGksKKFTLK
0 1 S36-p AGGDGGksKKFTLKR
0 3 S54-p DELERFTsMRIKKEK
0 6 Y75-p HRNSSASyGDDPTAQ
0 9 Y128-p KREMVSQyLytsKAG
0 172 Y130-p EMVSQyLytsKAGMS
0 2 T131-p MVSQyLytsKAGMSQ
0 2 S132-p VSQyLytsKAGMSQK
1 0 S154-p MYIQELRsGLRDMPL
0 2 K222-u HEIIRCLkAFMNNKF
0 4 K311-u SGTTIALkVGCLQLI
0 2 S373-p DEQGEEDsyDLkGRL
0 39 Y374-p EQGEEDsyDLkGRLD
0 1 K377-u EEDsyDLkGRLDDIR
0 133 Y424-p LLLVRNDyEARPQYY
1 1 K486-u AKAAELEkKLDSELT
0 14 K503-u HELQVEMkKMESDFE
0 1 K527-u KDALHSEkQQIATEK
0 1 K550 QLTGEVAKLTKELED
2 1 T768-p PVLPFGLtPKKLykP
0 20 Y773-p GLtPKKLykPEVQLR
0 11 K774-u LtPKKLykPEVQLRR
0 2 K824-a LTFSAQTkTSKAKkD
0 2 K830-a TkTSKAKkDQEGGEE
0 2 K855-u ELKVLDSkTAQNLSI
0 1 S974 LRKSESFSNLLEITL
0 1 Y986 ITLLVGNYMNAGSRN
0 1 S1051-p VEKASRVsAENLQkN
0 1 K1057-a VsAENLQkNLDQMKK
0 1 K1057-u VsAENLQkNLDQMKK
1 0 T1091-p DKFVEKMtSFVKDAQ
0 1 K1103-a DAQEQYNkLRMMHSN
0 3 Y1121-p LYKELGEyFLFDPKK
1 0 T1238-p SLLASELtKDDAMAA
0 1 S1251-p AAVPAKVsKNsEtFP
0 1 S1254-p PAKVsKNsEtFPTIL
0 1 T1256-p KVsKNsEtFPTILEE
0 1 S1272-p KELVGRAs_______
  Diaphanous-1 iso2  
S7 _MEPPGGSLGPGRGT
S22 RDKKKGRSPDELPSA
S28 RSPDELPSAGGDGGK
K35 SAGGDGGKSKKFLER
S36 AGGDGGKSKKFLERF
S45 KFLERFTSMRIKKEK
Y66 HRNSSASYGDDPTAQ
Y119 KREMVSQYLYTSKAG
Y121 EMVSQYLYTSKAGMS
T122 MVSQYLYTSKAGMSQ
S123 VSQYLYTSKAGMSQK
S145 MYIQELRSGLRDMPL
K213 HEIIRCLKAFMNNKF
K302 SGTTIALKVGCLQLI
S364 DEQGEEDSYDLKGRL
Y365 EQGEEDSYDLKGRLD
K368 EEDSYDLKGRLDDIR
Y415 LLLVRNDYEARPQYY
K477 AKAAELEKKLDSELT
K494 HELQVEMKKMESDFE
K518 KDALHSEKQQIATEK
K541 QLTGEVAKLTKELED
T747 PVLPFGLTPKKLYKP
Y752 GLTPKKLYKPEVQLR
K753 LTPKKLYKPEVQLRR
K803-a LTFSAQTkTKkDQEG
K806-a SAQTkTKkDQEGGEE
K831 ELKVLDSKTAQNLSI
S950 LRKSESFSNLLEITL
Y962 ITLLVGNYMNAGSRN
S1027 VEKASRVSAENLQKN
K1033 VSAENLQKNLDQMKK
K1033 VSAENLQKNLDQMKK
T1067 DKFVEKMTSFVKDAQ
K1079 DAQEQYNKLRMMHSN
Y1097 LYKELGEYFLFDPKK
T1214 SLLASELTKDDAMAA
S1227 AAVPAKVSKNSETFP
S1230 PAKVSKNSETFPTIL
T1232 KVSKNSETFPTILEE
S1248 KELVGRAS_______
  mouse

 
G7 _MEPSGGGLGPGRGT
S22-p RDKKKGRsPDELPAT
A28 RsPDELPATGGDGGK
K35 ATGGDGGKHKKFLER
H36 TGGDGGKHKKFLERF
S45 KFLERFTSMRIKKEK
Y66 HRNSSASYGDDPTAQ
Y119 KREMVSQYLHTSKAG
H121 EMVSQYLHTSKAGMN
T122 MVSQYLHTSKAGMNQ
S123 VSQYLHTSKAGMNQK
S145 MYIQELRSGLRDMHL
K213 HEIIRCLKAFMNNKF
K302 SGTSIALKVGCLQLI
F364 DEQGDEDFFDLKGRL
F365 EQGDEDFFDLKGRLD
K368 DEDFFDLKGRLDDIR
Y415-p LLLVRNDyEARPQYY
K477 AKATELEKKLDSELT
K494-u HELQVEMkKMENDFE
K518 KDALDSEKQQITAQK
K541-u KLTGEVAkLSKELED
T751 PVLPFGLTPKKVYKP
Y756 GLTPKKVYKPEVQLR
K757 LTPKKVYKPEVQLRR
K807 LAFSAQTKTSKAKKD
K813 TKTSKAKKDQEGGEE
K838 ELKVLDSKTAQNLSI
S957-p LRKSENFsSLLELTL
Y969-p LTLLVGNyMNAGSRN
S1034 VEKASRVSAENLQKS
K1040 VSAENLQKSLDQMKK
K1040 VSAENLQKSLDQMKK
T1074 DKFVEKMTSFVKDAQ
K1086 DAQEQYNKLRMMHSN
Y1104-p LYKELGDyFVFDPKK
T1221 SLLASELTKDDAMAP
P1234 APGPVKVPKKSEGVP
S1237 PVKVPKKSEGVPTIL
G1239 KVPKKSEGVPTILEE
S1255 KELVGRAS_______
  rat

 
G7 _MEPSGGGLGPGRGT
S22 RDKKKGRSPDELPAT
A28 RSPDELPATGGDGGK
K35 ATGGDGGKHKKFTLK
H36 TGGDGGKHKKFTLKR
S54 DELERFTSMRIKKEK
Y75 HRNSSASYGDDPTAQ
Y128 KREMVSQYLHTSKAG
H130 EMVSQYLHTSKAGMN
T131 MVSQYLHTSKAGMNQ
S132 VSQYLHTSKAGMNQK
S154 MYIQELRSGLRDMHL
K222 HEIIRCLKAFMNNKF
K311 SGTSIALKVGCLQLI
F373 DEQGDEDFFDLKGRL
F374 EQGDEDFFDLKGRLD
K377 DEDFFDLKGRLDDIR
Y424 LLLVRNDYEARPQYY
K486 AKATELEKKLDSELT
K503 HELQVEMKKMENDFE
K527 KDALDSEKQQITTQK
K550 KLTGEVAKLSKELED
T761 PVLPFGLTPKKVYKP
Y766 GLTPKKVYKPEVQLR
K767 LTPKKVYKPEVQLRR
K817 LAFSAQTKTSKAKKD
K823 TKTSKAKKDQEGGEE
K848 ELKVLDSKTAQNLSI
S967 LRKSENFSSLLELTL
Y979 LTLLVGNYMNAGSRN
S1044 VEKASRVSAENLQKN
K1050 VSAENLQKNLDQMKK
K1050 VSAENLQKNLDQMKK
T1084 DKFVEKMTSFVKDAQ
K1096 DAQEQYNKLRMMHSN
Y1114 LYKELGDYFVFDPKK
T1231 SLLASELTKDDAVAA
- under review  
S1247 SAKVPKKSEGVTTIL
G1249 KVPKKSEGVTTILEE
S1265 KELVGRAS_______
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