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Overview

Uniprot IDP06396
Protein NameGelsolin
Gene NameGSN
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
239 SNRYERLKATQVSKG

Function

Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed (PubMed:19666512). Plays a role in ciliogenesis (PubMed:20393563)

Protein Sequence

10 MAPHRPAPAL 20 LCALSLALCA 30 LSLPVRAATA 40 SRGASQAGAP 50 QGRVPEARPN 60 SMVVEHPEFL 70 KAGKEPGLQI 80 WRVEKFDLVP 90 VPTNLYGDFF 100 TGDAYVILKT 110 VQLRNGNLQY 120 DLHYWLGNEC 130 SQDESGAAAI 140 FTVQLDDYLN 150 GRAVQHREVQ 160 GFESATFLGY 170 FKSGLKYKKG 180 GVASGFKHVV 190 PNEVVVQRLF 200 QVKGRRVVRA 210 TEVPVSWESF 220 NNGDCFILDL 230 GNNIHQWCGS 240 NSNRYERLKA 250 TQVSKGIRDN 260 ERSGRARVHV 270 SEEGTEPEAM 280 LQVLGPKPAL 290 PAGTEDTAKE 300 DAANRKLAKL 310 YKVSNGAGTM 320 SVSLVADENP 330 FAQGALKSED 340 CFILDHGKDG 350 KIFVWKGKQA 360 NTEERKAALK 370 TASDFITKMD 380 YPKQTQVSVL 390 PEGGETPLFK 400 QFFKNWRDPD 410 QTDGLGLSYL 420 SSHIANVERV 430 PFDAATLHTS 440 TAMAAQHGMD 450 DDGTGQKQIW 460 RIEGSNKVPV 470 DPATYGQFYG 480 GDSYIILYNY 490 RHGGRQGQII 500 YNWQGAQSTQ 510 DEVAASAILT 520 AQLDEELGGT 530 PVQSRVVQGK 540 EPAHLMSLFG 550 GKPMIIYKGG 560 TSREGGQTAP 570 ASTRLFQVRA 580 NSAGATRAVE 590 VLPKAGALNS 600 NDAFVLKTPS 610 AAYLWVGTGA 620 SEAEKTGAQE 630 LLRVLRAQPV 640 QVAEGSEPDG 650 FWEALGGKAA 660 YRTSPRLKDK 670 KMDAHPPRLF 680 ACSNKIGRFV 690 IEEVPGELMQ 700 EDLATDDVML 710 LDTWDQVFVW 720 VGKDSQEEEK 730 TEALTSAKRY 740 IETDPANRDR 750 RTPITVVKQG 760 FEPPSFVGWF 770 LGWDDDYWSV 780 DPLDRAMAEL AA

Gene Ontology

Classification GO ID Description
Cellular Component GO:0030478 actin cap
Cellular Component GO:0015629 actin cytoskeleton
Cellular Component GO:0072562 blood microparticle
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005576 extracellular region
Cellular Component GO:0005615 extracellular space
Cellular Component GO:1904813 ficolin-1-rich granule lumen
Cellular Component GO:0005925 focal adhesion
Cellular Component GO:0030027 lamellipodium
Cellular Component GO:0045335 phagocytic vesicle
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0016528 sarcoplasm
Cellular Component GO:0034774 secretory granule lumen
Molecular Function GO:0003779 actin binding
Molecular Function GO:0051015 actin filament binding
Molecular Function GO:0005509 calcium ion binding
Molecular Function GO:0045159 myosin II binding
Molecular Function GO:0036313 phosphatidylinositol 3-kinase catalytic subunit binding
Molecular Function GO:0005546 phosphatidylinositol-4,5-bisphosphate binding
Biological Process GO:0051693 actin filament capping
Biological Process GO:0030042 actin filament depolymerization
Biological Process GO:0007015 actin filament organization
Biological Process GO:0030041 actin filament polymerization
Biological Process GO:0051014 actin filament severing
Biological Process GO:0008154 actin polymerization or depolymerization
Biological Process GO:1990000 amyloid fibril formation
Biological Process GO:0051016 barbed-end actin filament capping
Biological Process GO:0086003 cardiac muscle cell contraction
Biological Process GO:0030031 cell projection assembly
Biological Process GO:0007417 central nervous system development
Biological Process GO:0060271 cilium assembly
Biological Process GO:0097284 hepatocyte apoptotic process
Biological Process GO:0046597 host-mediated suppression of symbiont invasion
Biological Process GO:0006911 phagocytosis, engulfment
Biological Process GO:0051127 positive regulation of actin nucleation
Biological Process GO:0010628 positive regulation of gene expression
Biological Process GO:1902174 positive regulation of keratinocyte apoptotic process
Biological Process GO:1903923 positive regulation of protein processing in phagocytic vesicle
Biological Process GO:0031648 protein destabilization
Biological Process GO:1903903 regulation of establishment of T cell polarity
Biological Process GO:1903906 regulation of plasma membrane raft polarization
Biological Process GO:1903909 regulation of receptor clustering
Biological Process GO:0055119 relaxation of cardiac muscle
Biological Process GO:0097017 renal protein absorption
Biological Process GO:0035994 response to muscle stretch
Biological Process GO:0014891 striated muscle atrophy

Reference

[1] 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.