Search Results

Overview

Uniprot IDP21333
Protein NameFilamin-A
Gene NameFLNA
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
1007 GQGKVASKIVGPSGA
1019 SGAAVPCKVEPGLGA
1071 PTKPSKVKAFGPGLQ
1162 VPCFDASKVKCSGPG
1164 CFDASKVKCSGPGLE
120 FLDRESIKLVSIDSK
127 KLVSIDSKAIVDGNL
1294 QTGGPHVKARVANPS
1372 IQSGTTNKPNKFTVE
1450 HDVTDASKVKCSGPG
1452 VTDASKVKCSGPGLS
1486 GVAPLQVKVQGPKGL
1491 QVKVQGPKGLVEPVD
1538 PRSPFKVKVLPTHDA
1547 LPTHDASKVKASGPG
1549 THDASKVKASGPGLN
1593 DPEGKPKKTHIQDNH
1801 VIPFTIKKGEITGEV
1814 EVRMPSGKVAQPTIT
1824 QPTITDNKDGTVTVR
2000 REEPCLLKRLRNGHV
2024 GEHLVHVKKNGQHVA
2133 PGSPFSVKVTGEGRV
2141 VTGEGRVKESITRRR
2165 SHCDLSLKIPEISIQ
220 WDSWDASKPVTNARE
2215 GTHTVSVKYKGQHVP
2289 EISFEDRKDGSCGVA
2387 VTEIDQDKYAVRFIP
2473 IDGPSKVKMDCQECP
2515 GGSPFKAKVTGPRLV
2559 PGPADASKVVAKGLG
2563 DASKVVAKGLGLSKA
2569 AKGLGLSKAYVGQKS
2575 SKAYVGQKSSFTVDC
2607 PCEEILVKHVGSRLY
2621 YSVSYLLKDKGEYTL
2623 VSYLLKDKGEYTLVV
268 LSQFPKAKLKPGAPL
299 EPTGNMVKKRAEFTV
300 PTGNMVKKRAEFTVE
376 PFEVYVDKSQGDASK
383 KSQGDASKVTAQGPG
42 LAEDAPWKKIQQNTF
43 AEDAPWKKIQQNTFT
493 VGRGLQPKGVRVKET
498 QPKGVRVKETADFKV
504 VKETADFKVYTKGAG
508 ADFKVYTKGAGSGEL
516 GAGSGELKVTVKGPK
520 GELKVTVKGPKGEER
578 GTECGNQKVRAWGPG
626 AKIECDDKGDGSCDV
684 ARGPGLEKTGVAVNK
700 AEFTVDAKHGGKAPL
771 GAGSHPNKVKVYGPG
773 GSHPNKVKVYGPGVA
781 VYGPGVAKTGLKAHE
837 DNDTFTVKYTPRGAG
865 PTSPIRVKVEPSHDA
87 LLEVLSQKKMHRKHN
874 EPSHDASKVKAEGPG
876 SHDASKVKAEGPGLS
906 AKAAGKGKLDVQFSG
916 VQFSGLTKGDAVRDV
975 SLDLSKIKVSGLGEK
982 KVSGLGEKVDVGKDQ
994 KDQEFTVKSKGAGGQ
996 QEFTVKSKGAGGQGK

Function

Promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. Anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. Interaction with FLNB may allow neuroblast migration from the ventricular zone into the cortical plate. Tethers cell surface-localized furin, modulates its rate of internalization and directs its intracellular trafficking (By similarity). Involved in ciliogenesis. Plays a role in cell-cell contacts and adherens junctions during the development of blood vessels, heart and brain organs. Plays a role in platelets morphology through interaction with SYK that regulates ITAM- and ITAM-like-containing receptor signaling, resulting in by platelet cytoskeleton organization maintenance (By similarity). During the axon guidance process, required for growth cone collapse induced by SEMA3A-mediated stimulation of neurons (PubMed:25358863)

Protein Sequence

10 MSSSHSRAGQ 20 SAAGAAPGGG 30 VDTRDAEMPA 40 TEKDLAEDAP 50 WKKIQQNTFT 60 RWCNEHLKCV 70 SKRIANLQTD 80 LSDGLRLIAL 90 LEVLSQKKMH 100 RKHNQRPTFR 110 QMQLENVSVA 120 LEFLDRESIK 130 LVSIDSKAIV 140 DGNLKLILGL 150 IWTLILHYSI 160 SMPMWDEEED 170 EEAKKQTPKQ 180 RLLGWIQNKL 190 PQLPITNFSR 200 DWQSGRALGA 210 LVDSCAPGLC 220 PDWDSWDASK 230 PVTNAREAMQ 240 QADDWLGIPQ 250 VITPEEIVDP 260 NVDEHSVMTY 270 LSQFPKAKLK 280 PGAPLRPKLN 290 PKKARAYGPG 300 IEPTGNMVKK 310 RAEFTVETRS 320 AGQGEVLVYV 330 EDPAGHQEEA 340 KVTANNDKNR 350 TFSVWYVPEV 360 TGTHKVTVLF 370 AGQHIAKSPF 380 EVYVDKSQGD 390 ASKVTAQGPG 400 LEPSGNIANK 410 TTYFEIFTAG 420 AGTGEVEVVI 430 QDPMGQKGTV 440 EPQLEARGDS 450 TYRCSYQPTM 460 EGVHTVHVTF 470 AGVPIPRSPY 480 TVTVGQACNP 490 SACRAVGRGL 500 QPKGVRVKET 510 ADFKVYTKGA 520 GSGELKVTVK 530 GPKGEERVKQ 540 KDLGDGVYGF 550 EYYPMVPGTY 560 IVTITWGGQN 570 IGRSPFEVKV 580 GTECGNQKVR 590 AWGPGLEGGV 600 VGKSADFVVE 610 AIGDDVGTLG 620 FSVEGPSQAK 630 IECDDKGDGS 640 CDVRYWPQEA 650 GEYAVHVLCN 660 SEDIRLSPFM 670 ADIRDAPQDF 680 HPDRVKARGP 690 GLEKTGVAVN 700 KPAEFTVDAK 710 HGGKAPLRVQ 720 VQDNEGCPVE 730 ALVKDNGNGT 740 YSCSYVPRKP 750 VKHTAMVSWG 760 GVSIPNSPFR 770 VNVGAGSHPN 780 KVKVYGPGVA 790 KTGLKAHEPT 800 YFTVDCAEAG 810 QGDVSIGIKC 820 APGVVGPAEA 830 DIDFDIIRND 840 NDTFTVKYTP 850 RGAGSYTIMV 860 LFADQATPTS 870 PIRVKVEPSH 880 DASKVKAEGP 890 GLSRTGVELG 900 KPTHFTVNAK 910 AAGKGKLDVQ 920 FSGLTKGDAV 930 RDVDIIDHHD 940 NTYTVKYTPV 950 QQGPVGVNVT 960 YGGDPIPKSP 970 FSVAVSPSLD 980 LSKIKVSGLG 990 EKVDVGKDQE 1000 FTVKSKGAGG 1010 QGKVASKIVG 1020 PSGAAVPCKV 1030 EPGLGADNSV 1040 VRFLPREEGP 1050 YEVEVTYDGV 1060 PVPGSPFPLE 1070 AVAPTKPSKV 1080 KAFGPGLQGG 1090 SAGSPARFTI 1100 DTKGAGTGGL 1110 GLTVEGPCEA 1120 QLECLDNGDG 1130 TCSVSYVPTE 1140 PGDYNINILF 1150 ADTHIPGSPF 1160 KAHVVPCFDA 1170 SKVKCSGPGL 1180 ERATAGEVGQ 1190 FQVDCSSAGS 1200 AELTIEICSE 1210 AGLPAEVYIQ 1220 DHGDGTHTIT 1230 YIPLCPGAYT 1240 VTIKYGGQPV 1250 PNFPSKLQVE 1260 PAVDTSGVQC 1270 YGPGIEGQGV 1280 FREATTEFSV 1290 DARALTQTGG 1300 PHVKARVANP 1310 SGNLTETYVQ 1320 DRGDGMYKVE 1330 YTPYEEGLHS 1340 VDVTYDGSPV 1350 PSSPFQVPVT 1360 EGCDPSRVRV 1370 HGPGIQSGTT 1380 NKPNKFTVET 1390 RGAGTGGLGL 1400 AVEGPSEAKM 1410 SCMDNKDGSC 1420 SVEYIPYEAG 1430 TYSLNVTYGG 1440 HQVPGSPFKV 1450 PVHDVTDASK 1460 VKCSGPGLSP 1470 GMVRANLPQS 1480 FQVDTSKAGV 1490 APLQVKVQGP 1500 KGLVEPVDVV 1510 DNADGTQTVN 1520 YVPSREGPYS 1530 ISVLYGDEEV 1540 PRSPFKVKVL 1550 PTHDASKVKA 1560 SGPGLNTTGV 1570 PASLPVEFTI 1580 DAKDAGEGLL 1590 AVQITDPEGK 1600 PKKTHIQDNH 1610 DGTYTVAYVP 1620 DVTGRYTILI 1630 KYGGDEIPFS 1640 PYRVRAVPTG 1650 DASKCTVTVS 1660 IGGHGLGAGI 1670 GPTIQIGEET 1680 VITVDTKAAG 1690 KGKVTCTVCT 1700 PDGSEVDVDV 1710 VENEDGTFDI 1720 FYTAPQPGKY 1730 VICVRFGGEH 1740 VPNSPFQVTA 1750 LAGDQPSVQP 1760 PLRSQQLAPQ 1770 YTYAQGGQQT 1780 WAPERPLVGV 1790 NGLDVTSLRP 1800 FDLVIPFTIK 1810 KGEITGEVRM 1820 PSGKVAQPTI 1830 TDNKDGTVTV 1840 RYAPSEAGLH 1850 EMDIRYDNMH 1860 IPGSPLQFYV 1870 DYVNCGHVTA 1880 YGPGLTHGVV 1890 NKPATFTVNT 1900 KDAGEGGLSL 1910 AIEGPSKAEI 1920 SCTDNQDGTC 1930 SVSYLPVLPG 1940 DYSILVKYNE 1950 QHVPGSPFTA 1960 RVTGDDSMRM 1970 SHLKVGSAAD 1980 IPINISETDL 1990 SLLTATVVPP 2000 SGREEPCLLK 2010 RLRNGHVGIS 2020 FVPKETGEHL 2030 VHVKKNGQHV 2040 ASSPIPVVIS 2050 QSEIGDASRV 2060 RVSGQGLHEG 2070 HTFEPAEFII 2080 DTRDAGYGGL 2090 SLSIEGPSKV 2100 DINTEDLEDG 2110 TCRVTYCPTE 2120 PGNYIINIKF 2130 ADQHVPGSPF 2140 SVKVTGEGRV 2150 KESITRRRRA 2160 PSVANVGSHC 2170 DLSLKIPEIS 2180 IQDMTAQVTS 2190 PSGKTHEAEI 2200 VEGENHTYCI 2210 RFVPAEMGTH 2220 TVSVKYKGQH 2230 VPGSPFQFTV 2240 GPLGEGGAHK 2250 VRAGGPGLER 2260 AEAGVPAEFS 2270 IWTREAGAGG 2280 LAIAVEGPSK 2290 AEISFEDRKD 2300 GSCGVAYVVQ 2310 EPGDYEVSVK 2320 FNEEHIPDSP 2330 FVVPVASPSG 2340 DARRLTVSSL 2350 QESGLKVNQP 2360 ASFAVSLNGA 2370 KGAIDAKVHS 2380 PSGALEECYV 2390 TEIDQDKYAV 2400 RFIPRENGVY 2410 LIDVKFNGTH 2420 IPGSPFKIRV 2430 GEPGHGGDPG 2440 LVSAYGAGLE 2450 GGVTGNPAEF 2460 VVNTSNAGAG 2470 ALSVTIDGPS 2480 KVKMDCQECP 2490 EGYRVTYTPM 2500 APGSYLISIK 2510 YGGPYHIGGS 2520 PFKAKVTGPR 2530 LVSNHSLHET 2540 SSVFVDSLTK 2550 ATCAPQHGAP 2560 GPGPADASKV 2570 VAKGLGLSKA 2580 YVGQKSSFTV 2590 DCSKAGNNML 2600 LVGVHGPRTP 2610 CEEILVKHVG 2620 SRLYSVSYLL 2630 KDKGEYTLVV 2640 KWGDEHIPGS PYRVVVP

Gene Ontology

Classification GO ID Description
Cellular Component GO:0015629 actin cytoskeleton
Cellular Component GO:0005884 actin filament
Cellular Component GO:0097440 apical dendrite
Cellular Component GO:0005911 cell-cell junction
Cellular Component GO:0030863 cortical cytoskeleton
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0043198 dendritic shaft
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005576 extracellular region
Cellular Component GO:0005925 focal adhesion
Cellular Component GO:0098978 glutamatergic synapse
Cellular Component GO:0030426 growth cone
Cellular Component GO:0016020 membrane
Cellular Component GO:0031523 Myb complex
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005634 nucleus
Cellular Component GO:0043204 perikaryon
Cellular Component GO:0048471 perinuclear region of cytoplasm
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0002102 podosome
Cellular Component GO:0098794 postsynapse
Cellular Component GO:0030018 Z disc
Molecular Function GO:0051015 actin filament binding
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0140297 DNA-binding transcription factor binding
Molecular Function GO:0034988 Fc-gamma receptor I complex binding
Molecular Function GO:0001664 G protein-coupled receptor binding
Molecular Function GO:0051020 GTPase binding
Molecular Function GO:0019900 kinase binding
Molecular Function GO:0015459 potassium channel regulator activity
Molecular Function GO:0042803 protein homodimerization activity
Molecular Function GO:0140311 protein sequestering activity
Molecular Function GO:0003723 RNA binding
Molecular Function GO:0046332 SMAD binding
Molecular Function GO:0031267 small GTPase binding
Molecular Function GO:0044325 transmembrane transporter binding
Biological Process GO:0051764 actin crosslink formation
Biological Process GO:0030036 actin cytoskeleton organization
Biological Process GO:0007195 adenylate cyclase-inhibiting dopamine receptor signaling pathway
Biological Process GO:0007597 blood coagulation, intrinsic pathway
Biological Process GO:0021987 cerebral cortex development
Biological Process GO:0060271 cilium assembly
Biological Process GO:0045184 establishment of protein localization
Biological Process GO:0097368 establishment of Sertoli cell barrier
Biological Process GO:0021943 formation of radial glial scaffolds
Biological Process GO:0035855 megakaryocyte development
Biological Process GO:0090307 mitotic spindle assembly
Biological Process GO:0042789 mRNA transcription by RNA polymerase II
Biological Process GO:0043066 negative regulation of apoptotic process
Biological Process GO:0042177 negative regulation of protein catabolic process
Biological Process GO:0016479 negative regulation of transcription by RNA polymerase I
Biological Process GO:0070527 platelet aggregation
Biological Process GO:0032233 positive regulation of actin filament bundle assembly
Biological Process GO:0043123 positive regulation of canonical NF-kappaB signal transduction
Biological Process GO:2001046 positive regulation of integrin-mediated signaling pathway
Biological Process GO:2000179 positive regulation of neural precursor cell proliferation
Biological Process GO:2001224 positive regulation of neuron migration
Biological Process GO:0010572 positive regulation of platelet activation
Biological Process GO:1901381 positive regulation of potassium ion transmembrane transport
Biological Process GO:0042307 positive regulation of protein import into nucleus
Biological Process GO:1900026 positive regulation of substrate adhesion-dependent cell spreading
Biological Process GO:1902396 protein localization to bicellular tight junction
Biological Process GO:0034394 protein localization to cell surface
Biological Process GO:0072659 protein localization to plasma membrane
Biological Process GO:0050821 protein stabilization
Biological Process GO:0043113 receptor clustering
Biological Process GO:0030334 regulation of cell migration
Biological Process GO:1905000 regulation of membrane repolarization during atrial cardiac muscle cell action potential
Biological Process GO:1905031 regulation of membrane repolarization during cardiac muscle cell action potential
Biological Process GO:0051209 release of sequestered calcium ion into cytosol
Biological Process GO:0071526 semaphorin-plexin signaling pathway
Biological Process GO:0090042 tubulin deacetylation
Biological Process GO:0044319 wound healing, spreading of cells

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] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[4] 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.

[5] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[6] 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.

[7] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[8] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[9] 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.