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Protein Page:
Diaphanous-1 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

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; Adaptor/scaffold; Motility/polarity/chemotaxis
Chromosomal Location of Human Ortholog: 5q31
Cellular Component: cytosol; microtubule organizing center
Molecular Function: actin binding; protein binding; receptor binding; Rho GTPase binding
Biological Process: actin filament polymerization; cytoskeleton organization and biogenesis; positive regulation of cell migration; regulation of cell shape; regulation of microtubule-based process; regulation of release of sequestered calcium ion into cytosol; sensory perception of sound
Disease: Deafness, Autosomal Dominant 1
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-ß Signaling
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Diaphanous-1

Protein Structure Not Found.
Download PyMol Script
Download ChimeraX Script


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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


 LTP 

LTP: 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.


 HTP 

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


       human

► Hide Isoforms
 
0 2 S7‑p _MEPPGGsLGPGRGt
0 1 T14‑p sLGPGRGtRDKKKGR
0 22 S22‑p RDKKKGRsPDELPsA
0 2 S28‑p RsPDELPsAGGDGGk
0 1 K35‑ac sAGGDGGkskkFtLK
0 1 K35‑ub sAGGDGGkskkFtLK
0 2 S36‑p AGGDGGkskkFtLKR
0 1 K37‑ac GGDGGkskkFtLKRL
0 1 K38‑ac GDGGkskkFtLKRLM
0 1 T40‑p GGkskkFtLKRLMAD
0 3 S54‑p DELERFTsMRIKKEK
0 1 S71‑p PNSAHRNsSASyGDD
0 6 Y75‑p HRNsSASyGDDPTAQ
0 9 Y128‑p KREMVSQyLytsKAG
0 172 Y130‑p EMVSQyLytsKAGMS
0 3 T131‑p MVSQyLytsKAGMSQ
0 3 S132‑p VSQyLytsKAGMSQK
1 1 S154‑p MYIQELRsGLRDMPL
0 1 K202‑ub LKRLHDEkEETAGSy
0 1 Y209‑p kEETAGSyDSRNKHE
0 3 K222‑ub HEIIRCLkAFMNNKF
0 4 K311‑ub SGTTIALkVGCLQLI
0 3 S373‑p DEQGEEDsyDLkGRL
0 39 Y374‑p EQGEEDsyDLkGRLD
0 2 K377‑ub EEDsyDLkGRLDDIR
0 132 Y424‑p LLLVRNDyEARPQYY
0 1 K453‑ub NGADPDFkCRHLQIE
0 1 K473‑ac DQMIDKTkVEkSEAk
0 1 K476‑ac IDKTkVEkSEAkAAE
0 1 K480‑ac kVEkSEAkAAELEkk
1 1 K486‑ub AkAAELEkkLDSELT
0 1 K487‑ub kAAELEkkLDSELTA
0 15 K503‑ub HELQVEMkKMEsDFE
0 1 S507‑p VEMkKMEsDFEQKLQ
0 1 K520‑ac LQDLQGEkDALHSEk
0 1 K527‑ub kDALHSEkQQIATEK
0 2 S542‑p QDLEAEVsQLTGEVA
0 1 K550 QLTGEVAKLTKELED
2 1 T768‑p PVLPFGLtPKkLykP
0 2 K771‑ub PFGLtPKkLykPEVQ
0 20 Y773‑p GLtPKkLykPEVQLR
0 12 K774‑ub LtPKkLykPEVQLRR
0 1 K800‑ub SQDCFWTkVkEDRFE
0 1 K802‑ub DCFWTkVkEDRFENN
0 1 K814‑ac ENNELFAkLTLTFSA
0 2 K824‑ac LTFSAQTkTSKAKkD
0 1 K824‑ub LTFSAQTkTSKAKkD
0 1 K829 QTkTSKAKkDQEGGE
0 2 K830‑ac TkTSKAKkDQEGGEE
0 2 K855‑ub ELKVLDSkTAQNLSI
0 1 S866‑p NLSIFLGsFRMPyQE
0 1 Y871‑p LGsFRMPyQEIKNVI
0 1 S974 LRKSESFSNLLEITL
0 1 Y986 ITLLVGNYMNAGSRN
0 1 S1051‑p VEKASRVsAENLQkN
0 1 K1057‑ac VsAENLQkNLDQMKK
0 1 K1057‑ub VsAENLQkNLDQMKK
1 0 T1091‑p DKFVEKMtSFVKDAQ
0 2 K1103‑ac DAQEQYNkLRMMHSN
0 1 Y1115 HSNMETLYKELGEyF
0 4 Y1121‑p LYKELGEyFLFDPKK
0 1 K1224‑ub GPRQANRkAGCAVTS
1 0 T1238‑p SLLASELtkDDAMAA
0 1 K1239‑ub LLASELtkDDAMAAV
0 1 S1251‑p AAVPAKVsKNsEtFP
0 3 S1254‑p PAKVsKNsEtFPTIL
0 1 T1256‑p KVsKNsEtFPTILEE
0 3 S1272‑p KELVGRAs_______
  Diaphanous-1 iso2  
S7 _MEPPGGSLGPGRGT
T14 SLGPGRGTRDKKKGR
S22 RDKKKGRSPDELPSA
S28 RSPDELPSAGGDGGK
K35 SAGGDGGKSKKFLER
K35 SAGGDGGKSKKFLER
S36 AGGDGGKSKKFLERF
K37 GGDGGKSKKFLERFT
K38 GDGGKSKKFLERFTS
- gap
S45 KFLERFTSMRIKKEK
S62 PNSAHRNSSASYGDD
Y66 HRNSSASYGDDPTAQ
Y119 KREMVSQYLYTSKAG
Y121 EMVSQYLYTSKAGMS
T122 MVSQYLYTSKAGMSQ
S123 VSQYLYTSKAGMSQK
S145 MYIQELRSGLRDMPL
K193 LKRLHDEKEETAGSY
Y200 KEETAGSYDSRNKHE
K213 HEIIRCLKAFMNNKF
K302 SGTTIALKVGCLQLI
S364 DEQGEEDSYDLKGRL
Y365 EQGEEDSYDLKGRLD
K368 EEDSYDLKGRLDDIR
Y415 LLLVRNDYEARPQYY
K444 NGADPDFKCRHLQIE
K464 DQMIDKTKVEKSEAK
K467 IDKTKVEKSEAKAAE
K471 KVEKSEAKAAELEKK
K477 AKAAELEKKLDSELT
K478 KAAELEKKLDSELTA
K494 HELQVEMKKMESDFE
S498 VEMKKMESDFEQKLQ
K511 LQDLQGEKDALHSEK
K518 KDALHSEKQQIATEK
S533 QDLEAEVSQLTGEVA
K541 QLTGEVAKLTKELED
T747 PVLPFGLTPKKLYKP
K750 PFGLTPKKLYKPEVQ
Y752 GLTPKKLYKPEVQLR
K753 LTPKKLYKPEVQLRR
K779 SQDCFWTKVKEDRFE
K781 DCFWTKVKEDRFENN
K793 ENNELFAKLTLTFSA
K803‑ac LTFSAQTkTkkDQEG
K803 LTFSAQTKTkkDQEG
K805‑ac FSAQTkTkkDQEGGE
K806‑ac SAQTkTkkDQEGGEE
K831 ELKVLDSKTAQNLSI
S842 NLSIFLGSFRMPYQE
Y847 LGSFRMPYQEIKNVI
S950 LRKSESFSNLLEITL
Y962 ITLLVGNYMNAGSRN
S1027 VEKASRVSAENLQKN
K1033 VSAENLQKNLDQMKK
K1033 VSAENLQKNLDQMKK
T1067 DKFVEKMTSFVKDAQ
K1079 DAQEQYNKLRMMHSN
Y1091 HSNMETLYKELGEYF
Y1097 LYKELGEYFLFDPKK
K1200 GPRQANRKAGCAVTS
T1214 SLLASELTKDDAMAA
K1215 LLASELTKDDAMAAV
S1227 AAVPAKVSKNSETFP
S1230 PAKVSKNSETFPTIL
T1232 KVSKNSETFPTILEE
S1248 KELVGRAS_______
  mouse

 
G7 _MEPSGGGLGPGRGT
T14 GLGPGRGTRDKKKGR
S22‑p RDKKKGRsPDELPAT
A28 RsPDELPATGGDGGK
K35 ATGGDGGKHKKFLER
K35 ATGGDGGKHKKFLER
H36 TGGDGGKHKKFLERF
K37 GGDGGKHKKFLERFT
K38 GDGGKHKKFLERFTS
- gap
S45 KFLERFTSMRIKKEK
S62 PNSAHRNSSASYGDD
Y66 HRNSSASYGDDPTAQ
Y119 KREMVSQYLHTSKAG
H121 EMVSQYLHTSKAGMN
T122 MVSQYLHTSKAGMNQ
S123 VSQYLHTSKAGMNQK
S145 MYIQELRSGLRDMHL
K193 LKRLHDEKEETSGNY
Y200 KEETSGNYDSRNQHE
K213 HEIIRCLKAFMNNKF
K302 SGTSIALKVGCLQLI
F364 DEQGDEDFFDLKGRL
F365 EQGDEDFFDLKGRLD
K368 DEDFFDLKGRLDDIR
Y415‑p LLLVRNDyEARPQYY
K444 NGTDPDFKCRHLQID
K464 DQMIDKTKVEKSEAK
K467 IDKTKVEKSEAKATE
K471 KVEKSEAKATELEKK
K477 AKATELEKKLDSELT
K478 KATELEKKLDSELTA
K494‑ub HELQVEMkKMENDFE
N498 VEMkKMENDFEQKLQ
K511 LQDLQGEKDALDSEK
K518 KDALDSEKQQITAQK
S533 QDLEAEVSKLTGEVA
K541‑ub KLTGEVAkLSKELED
T751 PVLPFGLTPKKVYKP
K754 PFGLTPKKVYKPEVQ
Y756 GLTPKKVYKPEVQLR
K757 LTPKKVYKPEVQLRR
K783 SQDCFWTKVKEDRFE
K785 DCFWTKVKEDRFENN
K797 ENNELFAKLTLAFSA
K807 LAFSAQTKTSKAKKD
K807 LAFSAQTKTSKAKKD
K812 QTKTSKAKKDQEGGE
K813 TKTSKAKKDQEGGEE
K838 ELKVLDSKTAQNLSI
S849 NLSIFLGSFRMPYQE
Y854 LGSFRMPYQEIKNVI
S957‑p LRKSENFsSLLELTL
Y969‑p LTLLVGNyMNAGSRN
S1034 VEKASRVSAENLQKS
K1040 VSAENLQKSLDQMKK
K1040 VSAENLQKSLDQMKK
T1074 DKFVEKMTSFVKDAQ
K1086 DAQEQYNKLRMMHSN
Y1098 HSNMETLYKELGDyF
Y1104‑p LYKELGDyFVFDPKK
K1207 GPRQVNRKAGCAVTS
T1221 SLLASELTKDDAMAP
K1222 LLASELTKDDAMAPG
P1234 APGPVKVPKKSEGVP
S1237 PVKVPKKSEGVPTIL
G1239 KVPKKSEGVPTILEE
S1255‑p KELVGRAs_______
  rat

 
G7 _MEPSGGGLGPGRGT
T14 GLGPGRGTRDKKKGR
S22 RDKKKGRSPDELPAT
A28 RSPDELPATGGDGGK
K35 ATGGDGGKHKKFTLK
K35 ATGGDGGKHKKFTLK
H36 TGGDGGKHKKFTLKR
K37 GGDGGKHKKFTLKRL
K38 GDGGKHKKFTLKRLM
T40 GGKHKKFTLKRLMAD
S54 DELERFTSMRIKKEK
S71 PNSAHRNSSASYGDD
Y75 HRNSSASYGDDPTAQ
Y128 KREMVSQYLHTSKAG
H130 EMVSQYLHTSKAGMN
T131 MVSQYLHTSKAGMNQ
S132 VSQYLHTSKAGMNQK
S154 MYIQELRSGLRDMHL
K202 LKRLHDEKEETSGNY
Y209 KEETSGNYDSRNQHE
K222 HEIIRCLKAFMNNKF
K311 SGTSIALKVGCLQLI
F373 DEQGDEDFFDLKGRL
F374 EQGDEDFFDLKGRLD
K377 DEDFFDLKGRLDDIR
Y424 LLLVRNDYEARPQYY
K453 NGTDPDFKCRHLQID
K473 DQMIDKTKVEKSEAK
K476 IDKTKVEKSEAKATE
K480 KVEKSEAKATELEKK
K486 AKATELEKKLDSELT
K487 KATELEKKLDSELTA
K503 HELQVEMKKMENDFE
N507 VEMKKMENDFEQKLQ
K520 LQDLQGEKDALDSEK
K527 KDALDSEKQQITTQK
S542 QDLEAEVSKLTGEVA
K550 KLTGEVAKLSKELED
T761 PVLPFGLTPKKVYKP
K764 PFGLTPKKVYKPEVQ
Y766 GLTPKKVYKPEVQLR
K767 LTPKKVYKPEVQLRR
K793 SQDCFWTKVKEDRFE
K795 DCFWTKVKEDRFENN
K807 ENNELFAKLTLAFSA
K817 LAFSAQTKTSKAKKD
K817 LAFSAQTKTSKAKKD
K822 QTKTSKAKKDQEGGE
K823 TKTSKAKKDQEGGEE
K848 ELKVLDSKTAQNLSI
S859 NLSIFLGSFRMPYQE
Y864 LGSFRMPYQEIKNVI
S967 LRKSENFSSLLELTL
Y979 LTLLVGNYMNAGSRN
S1044 VEKASRVSAENLQKN
K1050 VSAENLQKNLDQMKK
K1050 VSAENLQKNLDQMKK
T1084 DKFVEKMTSFVKDAQ
K1096 DAQEQYNKLRMMHSN
Y1108‑p HSNMETLyKELGDYF
Y1114 LyKELGDYFVFDPKK
K1217 GPRQVNRKAGCAVTS
T1231 SLLASELTKDDAVAA
K1232 LLASELTKDDAVAAS
P1244 AASSAKVPKKSEGVT
S1247 SAKVPKKSEGVTTIL
G1249 KVPKKSEGVTTILEE
S1265 KELVGRAS_______
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