Search Results

Overview

Uniprot IDO60610
Protein NameProtein diaphanous homolog 1
Gene NameDIAPH1
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1224 GPRQANRKAGCAVTS
1249 AMAAVPAKVSKNSET
1252 AVPAKVSKNSETFPT
133 SQYLYTSKAGMSQKE
35 SAGGDGGKSKKFTLK
37 GGDGGKSKKFTLKRL
527 KDALHSEKQQIATEK

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)

Protein Sequence

10 MEPPGGSLGP 20 GRGTRDKKKG 30 RSPDELPSAG 40 GDGGKSKKFT 50 LKRLMADELE 60 RFTSMRIKKE 70 KEKPNSAHRN 80 SSASYGDDPT 90 AQSLQDVSDE 100 QVLVLFEQML 110 LDMNLNEEKQ 120 QPLREKDIII 130 KREMVSQYLY 140 TSKAGMSQKE 150 SSKSAMMYIQ 160 ELRSGLRDMP 170 LLSCLESLRV 180 SLNNNPVSWV 190 QTFGAEGLAS 200 LLDILKRLHD 210 EKEETAGSYD 220 SRNKHEIIRC 230 LKAFMNNKFG 240 IKTMLETEEG 250 ILLLVRAMDP 260 AVPNMMIDAA 270 KLLSALCILP 280 QPEDMNERVL 290 EAMTERAEMD 300 EVERFQPLLD 310 GLKSGTTIAL 320 KVGCLQLINA 330 LITPAEELDF 340 RVHIRSELMR 350 LGLHQVLQDL 360 REIENEDMRV 370 QLNVFDEQGE 380 EDSYDLKGRL 390 DDIRMEMDDF 400 NEVFQILLNT 410 VKDSKAEPHF 420 LSILQHLLLV 430 RNDYEARPQY 440 YKLIEECISQ 450 IVLHKNGADP 460 DFKCRHLQIE 470 IEGLIDQMID 480 KTKVEKSEAK 490 AAELEKKLDS 500 ELTARHELQV 510 EMKKMESDFE 520 QKLQDLQGEK 530 DALHSEKQQI 540 ATEKQDLEAE 550 VSQLTGEVAK 560 LTKELEDAKK 570 EMASLSAAAI 580 TVPPSVPSRA 590 PVPPAPPLPG 600 DSGTIIPPPP 610 APGDSTTPPP 620 PPPPPPPPPP 630 LPGGVCISSP 640 PSLPGGTAIS 650 PPPPLSGDAT 660 IPPPPPLPEG 670 VGIPSPSSLP 680 GGTAIPPPPP 690 LPGSARIPPP 700 PPPLPGSAGI 710 PPPPPPLPGE 720 AGMPPPPPPL 730 PGGPGIPPPP 740 PFPGGPGIPP 750 PPPGMGMPPP 760 PPFGFGVPAA 770 PVLPFGLTPK 780 KLYKPEVQLR 790 RPNWSKLVAE 800 DLSQDCFWTK 810 VKEDRFENNE 820 LFAKLTLTFS 830 AQTKTSKAKK 840 DQEGGEEKKS 850 VQKKKVKELK 860 VLDSKTAQNL 870 SIFLGSFRMP 880 YQEIKNVILE 890 VNEAVLTESM 900 IQNLIKQMPE 910 PEQLKMLSEL 920 KDEYDDLAES 930 EQFGVVMGTV 940 PRLRPRLNAI 950 LFKLQFSEQV 960 ENIKPEIVSV 970 TAACEELRKS 980 ESFSNLLEIT 990 LLVGNYMNAG 1000 SRNAGAFGFN 1010 ISFLCKLRDT 1020 KSTDQKMTLL 1030 HFLAELCEND 1040 YPDVLKFPDE 1050 LAHVEKASRV 1060 SAENLQKNLD 1070 QMKKQISDVE 1080 RDVQNFPAAT 1090 DEKDKFVEKM 1100 TSFVKDAQEQ 1110 YNKLRMMHSN 1120 METLYKELGE 1130 YFLFDPKKLS 1140 VEEFFMDLHN 1150 FRNMFLQAVK 1160 ENQKRRETEE 1170 KMRRAKLAKE 1180 KAEKERLEKQ 1190 QKREQLIDMN 1200 AEGDETGVMD 1210 SLLEALQSGA 1220 AFRRKRGPRQ 1230 ANRKAGCAVT 1240 SLLASELTKD 1250 DAMAAVPAKV 1260 SKNSETFPTI 1270 LEEAKELVGR AS

Gene Ontology

Classification GO ID Description
Cellular Component GO:0005884 actin filament
Cellular Component GO:0005634 nucleus
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0032587 ruffle membrane
Cellular Component GO:0030667 secretory granule membrane
Molecular Function GO:0003779 actin binding
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0005102 signaling receptor binding
Molecular Function GO:0031267 small GTPase binding
Molecular Function GO:0044325 transmembrane transporter binding
Biological Process GO:0030036 actin cytoskeleton organization
Biological Process GO:0030041 actin filament polymerization
Biological Process GO:0071420 cellular response to histamine
Biological Process GO:0007010 cytoskeleton organization
Biological Process GO:0035372 protein localization to microtubule
Biological Process GO:0051493 regulation of cytoskeleton organization
Biological Process GO:0032886 regulation of microtubule-based process
Biological Process GO:0051279 regulation of release of sequestered calcium ion into cytosol
Biological Process GO:0007605 sensory perception of sound
Cellular Component GO:0005813 centrosome
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0101003 ficolin-1-rich granule membrane
Cellular Component GO:0072686 mitotic spindle

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[3] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[4] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[5] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[6] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.