CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000967
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein diaphanous homolog 1 
Protein Synonyms/Alias
 Diaphanous-related formin-1; DRF1 
Gene Name
 DIAPH1 
Gene Synonyms/Alias
 DIAP1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
193LKRLHDEKEETAGSYubiquitination[1]
368EEDSYDLKGRLDDIRubiquitination[1]
494HELQVEMKKMESDFEubiquitination[1]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 
Functional Description
 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 (By similarity). Has neurite outgrowth promoting activity (By similarity). 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. 
Sequence Annotation
 DOMAIN 84 449 GBD/FH3.
 DOMAIN 583 764 FH1.
 DOMAIN 769 1171 FH2.
 DOMAIN 1194 1222 DAD.
 MOD_RES 22 22 Phosphoserine.
 MOD_RES 1057 1057 N6-acetyllysine.
 MOD_RES 1103 1103 N6-acetyllysine.
 MOD_RES 1121 1121 Phosphotyrosine (By similarity).
 CROSSLNK 486 486 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Acetylation; Actin-binding; Alternative splicing; Cell membrane; Cell projection; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Deafness; Direct protein sequencing; Hearing; Isopeptide bond; Membrane; Non-syndromic deafness; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1272 AA 
Protein Sequence
MEPPGGSLGP GRGTRDKKKG RSPDELPSAG GDGGKSKKFL ERFTSMRIKK EKEKPNSAHR 60
NSSASYGDDP TAQSLQDVSD EQVLVLFEQM LLDMNLNEEK QQPLREKDII IKREMVSQYL 120
YTSKAGMSQK ESSKSAMMYI QELRSGLRDM PLLSCLESLR VSLNNNPVSW VQTFGAEGLA 180
SLLDILKRLH DEKEETAGSY DSRNKHEIIR CLKAFMNNKF GIKTMLETEE GILLLVRAMD 240
PAVPNMMIDA AKLLSALCIL PQPEDMNERV LEAMTERAEM DEVERFQPLL DGLKSGTTIA 300
LKVGCLQLIN ALITPAEELD FRVHIRSELM RLGLHQVLQD LREIENEDMR VQLNVFDEQG 360
EEDSYDLKGR LDDIRMEMDD FNEVFQILLN TVKDSKAEPH FLSILQHLLL VRNDYEARPQ 420
YYKLIEECIS QIVLHKNGAD PDFKCRHLQI EIEGLIDQMI DKTKVEKSEA KAAELEKKLD 480
SELTARHELQ VEMKKMESDF EQKLQDLQGE KDALHSEKQQ IATEKQDLEA EVSQLTGEVA 540
KLTKELEDAK KEMASLSAAA ITVPPSVPSR APVPPAPPLP GDSGTIIPPP PAPGDSTTPP 600
PPPPPPPPPP PLPGGTAISP PPPLSGDATI PPPPPLPEGV GIPSPSSLPG GTAIPPPPPL 660
PGSARIPPPP PPLPGSAGIP PPPPPLPGEA GMPPPPPPLP GGPGIPPPPP FPGGPGIPPP 720
PPGMGMPPPP PFGFGVPAAP VLPFGLTPKK LYKPEVQLRR PNWSKLVAED LSQDCFWTKV 780
KEDRFENNEL FAKLTLTFSA QTKTKKDQEG GEEKKSVQKK KVKELKVLDS KTAQNLSIFL 840
GSFRMPYQEI KNVILEVNEA VLTESMIQNL IKQMPEPEQL KMLSELKDEY DDLAESEQFG 900
VVMGTVPRLR PRLNAILFKL QFSEQVENIK PEIVSVTAAC EELRKSESFS NLLEITLLVG 960
NYMNAGSRNA GAFGFNISFL CKLRDTKSTD QKMTLLHFLA ELCENDYPDV LKFPDELAHV 1020
EKASRVSAEN LQKNLDQMKK QISDVERDVQ NFPAATDEKD KFVEKMTSFV KDAQEQYNKL 1080
RMMHSNMETL YKELGEYFLF DPKKLSVEEF FMDLHNFRNM FLQAVKENQK RRETEEKMRR 1140
AKLAKEKAEK ERLEKQQKRE QLIDMNAEGD ETGVMDSLLE ALQSGAAFRR KRGPRQANRK 1200
AGCAVTSLLA SELTKDDAMA AVPAKVSKNS ETFPTILEEA KELVGRAS 1248 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0072686; C:mitotic spindle; IDA:BHF-UCL.
 GO:0043005; C:neuron projection; IEA:Compara.
 GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
 GO:0005102; F:receptor binding; NAS:ProtInc.
 GO:0030041; P:actin filament polymerization; IEA:Compara.
 GO:0071420; P:cellular response to histamine; IMP:BHF-UCL.
 GO:0007010; P:cytoskeleton organization; IMP:UniProtKB.
 GO:0031175; P:neuron projection development; IEA:Compara.
 GO:0035372; P:protein localization to microtubule; IMP:BHF-UCL.
 GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
 GO:0032886; P:regulation of microtubule-based process; IMP:UniProtKB.
 GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IMP:BHF-UCL.
 GO:0007605; P:sensory perception of sound; TAS:ProtInc. 
Interpro
 IPR003104; Actin-bd_FH2/DRF_autoreg.
 IPR016024; ARM-type_fold.
 IPR014767; Diaphanous_autoregulatory.
 IPR010465; Drf_DAD.
 IPR010472; Drf_FH3.
 IPR010473; Drf_GTPase-bd.
 IPR015425; FH2_actin-bd.
 IPR009408; Formin_homology_1.
 IPR014768; GTPase-bd/formin_homology_3. 
Pfam
 PF06345; Drf_DAD
 PF06346; Drf_FH1
 PF06367; Drf_FH3
 PF06371; Drf_GBD
 PF02181; FH2 
SMART
 SM00498; FH2 
PROSITE
 PS51231; DAD
 PS51444; FH2
 PS51232; GBD_FH3 
PRINTS