Objective　Human　secretory　phospholipase　A2group　IIA(sPLA2-IIA)plays　an　important　role　in　the　regulation　of　cellular　lipid　metabolism　and　signal　transmission,　and　participates　in　a　variety　of　acute　and　chronicinflammatory　responses.　Investigating　the　relationship　between　their　dynamics,　allostery　and　functions　is　of　important　significance.　Methods　The　elastic　network　model(ENM),perturbation-response　scanning(PRS)and　protein　structure　network(PSN)methods　are　utilized　to　analyze　the　structural　dynamics　and　allostery　of31human　sPLA2-IIA　members,　and　explore　the　relationship　between　their　shared/specific　dynamics　and　functions.　Results　The　results　show　that　the　catalytic　residues　and　cysteine　residues　involved　in　disulfide　bond　formation,　important　for　the　enzyme＇s　catalysis　and　structural　stability　respectively,are　of　minimal　mobility,which　are　therequirements　for　the　enzyme＇s　shared　functions;however,the5regions　involved　in　the　association　with　calciumion/membrane　are　of　high　mobility,which　embody　the　specificity　of　sPLA2-IIA　members.Additionally,the　PRSanalysis　reveals　that　the　above　five　regions　have　a　high　sensitivity　to　external　perturbations,suggesting　theirimportant　roles　in　allosteric　modulation,while　those　residues　with　a　low　sensitivity　play　an　important　role　inmaintaining　structural　stability.　Finally,the　ANM　analysis　indicates　that　the　strong　correlation　movements　around　the　catalytic　sites　of　sPLA2,are　helpful　for　the　enzyme＇s　catalytic　function　exertion.　Conclusion　This　study　is　helpful　for　the　deep　understanding　of　the　dynamics　and　functionally　allosteric　mechanism　of　human　sPLA2-IIA,and　can　provide　a　guide　for　drug　design　and　accurate　design　of　proteins　with　finely　tuned　activities.